|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-483 |
3.95e-136 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 402.52 E-value: 3.95e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 9 AENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVS--SNC-------IPFFFEQ----- 74
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSipKGLrigylpqEPPLDDDltvld 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 75 --FGSDSEYFE--------------------------TDYAEAG-------------KMGVADHIWQENV---SGGEDTR 110
Cdd:COG0488 81 tvLDGDAELRAleaeleeleaklaepdedlerlaelqEEFEALGgweaearaeeilsGLGFPEEDLDRPVselSGGWRRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 111 IRLAQLFSSPHAVAFLDEPTSNLDYNGVEMLKKRLNEIE-TLVVISHDRSVLNEICDRIVEISFGKLQNYSGNYDEYVVQ 189
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPgTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 190 KEEQRKTQQAEYENYQAEKKRLQsvyvekkakaktvdkkpknmsaseakvrAFIgnRKPEDKARGIERsATNVLKRLEHM 269
Cdd:COG0488 241 RAERLEQEAAAYAKQQKKIAKEE----------------------------EFI--RRFRAKARKAKQ-AQSRIKALEKL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 270 EIKEKPKEELTVRpdFRLTNPPR-NPIVIRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREK- 347
Cdd:COG0488 290 EREEPPRRDKTVE--IRFPPPERlGKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEp 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 348 ----VYVVPGAKIGYARQNMSQIDLSQTVLVNVRRVSIQ-SESISRIVLARLLLSERDMNKKASELSGGERMKLSFAMLF 422
Cdd:COG0488 368 dsgtVKLGETVKIGYFDQHQEELDPDKTVLDELRDGAPGgTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLL 447
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1124469102 423 VSDVNLLILDEPTNYLDIPSVEALEKMLVEYEGTLIFTSHDKVFVDRIATDRLYIGDGKIR 483
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
31-482 |
1.04e-78 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 254.82 E-value: 1.04e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 31 EGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNciP-----------FFFEQFG----------------------- 76
Cdd:PRK15064 26 GGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD--PnerlgklrqdqFAFEEFTvldtvimghtelwevkqerdriy 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 77 -----SDSEYF-----ETDYAE---------AGK--MGVADHIWQEN-----VSGGEDTRIRLAQ-LFSSPHaVAFLDEP 129
Cdd:PRK15064 104 alpemSEEDGMkvadlEVKFAEmdgytaearAGEllLGVGIPEEQHYglmseVAPGWKLRVLLAQaLFSNPD-ILLLDEP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 130 TSNLDYNGVEMLKKRLNEIE-TLVVISHDRSVLNEICDRIVEISFGKLQNYSGNYDEYVVQKEEQRKTQQAEYENYQAEK 208
Cdd:PRK15064 183 TNNLDINTIRWLEDVLNERNsTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYMTAATQARERLLADNAKKKAQI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 209 KRLQSVyvekkakaktvdkkpknmsaseakVRAFIGNRKpedKARgierSATNVLKRLEHMEIKEkpkeeltVRPDFRLt 288
Cdd:PRK15064 263 AELQSF------------------------VSRFSANAS---KAK----QATSRAKQIDKIKLEE-------VKPSSRQ- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 289 NP----------PRNPIVIrgEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLL-----ELINNREKVYVVPG 353
Cdd:PRK15064 304 NPfirfeqdkklHRNALEV--ENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLrtlvgELEPDSGTVKWSEN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 354 AKIGYARQNMS---QIDLSQTVLVNVRRVSIQSESISRIVLARLLLSERDMNKKASELSGGERMKLSFAMLFVSDVNLLI 430
Cdd:PRK15064 382 ANIGYYAQDHAydfENDLTLFDWMSQWRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLV 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1124469102 431 LDEPTNYLDIPSVEALEKMLVEYEGTLIFTSHDKVFVDRIATDRLYIGDGKI 482
Cdd:PRK15064 462 MDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGV 513
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-482 |
1.55e-63 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 217.13 E-value: 1.55e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGEL--------------------EPTK---GT 62
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVllddgriiyeqdlivarlqqDPPRnveGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 63 VSSncipFFFEQFGSDSEYF----------ETDYAE------AGKMGVADH--IWQ-EN-------------------VS 104
Cdd:PRK11147 83 VYD----FVAEGIEEQAEYLkryhdishlvETDPSEknlnelAKLQEQLDHhnLWQlENrinevlaqlgldpdaalssLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 105 GGEDTRIRLAQ-LFSSPHaVAFLDEPTSNLDYNGVEMLKKRLNEIE-TLVVISHDRSVLNEICDRIVEISFGKLQNYSGN 182
Cdd:PRK11147 159 GGWLRKAALGRaLVSNPD-VLLLDEPTNHLDIETIEWLEGFLKTFQgSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 183 YDEYVVQKEEQRKTQqaEYENYQAEKKRLQS-VYVEKKAKAKtvdkKPKNmsasEAKVRAFignrkpedKARGIERSAtn 261
Cdd:PRK11147 238 YDQYLLEKEEALRVE--ELQNAEFDRKLAQEeVWIRQGIKAR----RTRN----EGRVRAL--------KALRRERSE-- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 262 vlkRLEHMEiKEKPKEELTVRpdfrltnppRNPIVIRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLEL 341
Cdd:PRK11147 298 ---RREVMG-TAKMQVEEASR---------SGKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKL 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 342 I-----NNREKVYVvpGAK--IGYARQNMSQIDLSQTVLVNV----RRVSIQSesISRIVLARL---LLS-ERDMNK-KA 405
Cdd:PRK11147 365 MlgqlqADSGRIHC--GTKleVAYFDQHRAELDPEKTVMDNLaegkQEVMVNG--RPRHVLGYLqdfLFHpKRAMTPvKA 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1124469102 406 seLSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIPSVEALEKMLVEYEGTLIFTSHDKVFVDRIATDR-LYIGDGKI 482
Cdd:PRK11147 441 --LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECwIFEGNGKI 516
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
30-483 |
3.29e-63 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 214.41 E-value: 3.29e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 30 YEGEKVGLVGMNGAGKSTLLKILAG------------------------ELEPTKgTVSSNCIPF-------------FF 72
Cdd:TIGR03719 29 FPGAKIGVLGLNGAGKSTLLRIMAGvdkdfngearpqpgikvgylpqepQLDPTK-TVRENVEEGvaeikdaldrfneIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 73 EQFGSDSEYFETDYAEAGKMgvADHI-----WQ---------------------ENVSGGEDTRIRLAQLFSSPHAVAFL 126
Cdd:TIGR03719 108 AKYAEPDADFDKLAAEQAEL--QEIIdaadaWDldsqleiamdalrcppwdadvTKLSGGERRRVALCRLLLSKPDMLLL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 127 DEPTSNLDYNGVEMLKKRLNEIE-TLVVISHDRSVLNEICDRIVEISFGKLQNYSGNYDEYVVQKEEqRKTQQAEYEnyQ 205
Cdd:TIGR03719 186 DEPTNHLDAESVAWLERHLQEYPgTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKQK-RLEQEEKEE--S 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 206 AEKKRLQSV--YVEKKAKAktvdkkpknmsaseakvrafignRKPEDKARgiersatnvLKRLEHMEIKEKPK----EEL 279
Cdd:TIGR03719 263 ARQKTLKREleWVRQSPKG-----------------------RQAKSKAR---------LARYEELLSQEFQKrnetAEI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 280 TVRPDFRLTNpprnpIVIRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREK-----VYVVPGA 354
Cdd:TIGR03719 311 YIPPGPRLGD-----KVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQpdsgtIEIGETV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 355 KIGYARQNMSQIDLSQTV---------LVNVRRVSIQSesisRIVLARLLLSERDMNKKASELSGGERMKLSFAMLFVSD 425
Cdd:TIGR03719 386 KLAYVDQSRDALDPNKTVweeisggldIIKLGKREIPS----RAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSG 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1124469102 426 VNLLILDEPTNYLDIPSVEALEKMLVEYEGTLIFTSHDKVFVDRIATDRL-YIGDGKIR 483
Cdd:TIGR03719 462 GNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILaFEGDSHVE 520
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
30-482 |
3.42e-57 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 198.42 E-value: 3.42e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 30 YEGEKVGLVGMNGAGKSTLLKILAG------------------------ELEPTKgTVSSNCIPFF-------------F 72
Cdd:PRK11819 31 FPGAKIGVLGLNGAGKSTLLRIMAGvdkefegearpapgikvgylpqepQLDPEK-TVRENVEEGVaevkaaldrfneiY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 73 EQFGSDSEYFETDYAEAGKM-GVADHI--------------------WQENV---SGGEDTRIRLAQLFSSPHAVAFLDE 128
Cdd:PRK11819 110 AAYAEPDADFDALAAEQGELqEIIDAAdawdldsqleiamdalrcppWDAKVtklSGGERRRVALCRLLLEKPDMLLLDE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 129 PTSNLDYNGVEMLKKRLNEIE-TLVVISHDRSVLNEICDRIVEISFGKLQNYSGNYDEYVVQKEEQRKTQQAEyenyqaE 207
Cdd:PRK11819 190 PTNHLDAESVAWLEQFLHDYPgTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKAKRLAQEEKQ------E 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 208 KKRlqsvyveKKAKAKT---VDKKPKnmsASEAKvrafignrkpeDKARgiersatnvLKRLEHM---EIKEKP-KEELT 280
Cdd:PRK11819 264 AAR-------QKALKRElewVRQSPK---ARQAK-----------SKAR---------LARYEELlseEYQKRNeTNEIF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 281 VRPDFRLTNpprnpIVIRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREK-----VYVVPGAK 355
Cdd:PRK11819 314 IPPGPRLGD-----KVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQpdsgtIKIGETVK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 356 IGYARQNMSQIDLSQTV---------LVNVRRVSIQSesisRIVLARLLLSERDMNKKASELSGGERMKLSFAMLFVSDV 426
Cdd:PRK11819 389 LAYVDQSRDALDPNKTVweeisggldIIKVGNREIPS----RAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGG 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1124469102 427 NLLILDEPTNYLDIPSVEALEKMLVEYEGTLIFTSHDKVFVDRIATDRL-YIGDGKI 482
Cdd:PRK11819 465 NVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILaFEGDSQV 521
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
32-482 |
1.31e-51 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 184.99 E-value: 1.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 32 GEKVGLVGMNGAGKSTLLKILAGELEPTKGTVS--SNCIPFFFEQ-------------FGSDSEY--FETDYAEA----- 89
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLALLKNEISADGGSYTfpGNWQLAWVNQetpalpqpaleyvIDGDREYrqLEAQLHDAnernd 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 90 --------GKMGvADHIW----------------QENV-------SGGEDTRIRLAQLFSSPHAVAFLDEPTSNLDYNGV 138
Cdd:PRK10636 107 ghaiatihGKLD-AIDAWtirsraasllhglgfsNEQLerpvsdfSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 139 EMLKKRLNEIE-TLVVISHDRSVLNEICDRIVEISFGKLQNYSGNYDEYVVQKEEQRKTQQAEYENYQAEKKRLQSvYVE 217
Cdd:PRK10636 186 IWLEKWLKSYQgTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRATRLAQQQAMYESQQERVAHLQS-YID 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 218 K-KAKAktvdkkpknmsaSEAKvrafignrkpedkargierSATNVLKRLEHMEIKEKPKEELTVRPDFRLTNPPRNPIv 296
Cdd:PRK10636 265 RfRAKA------------TKAK-------------------QAQSRIKMLERMELIAPAHVDNPFHFSFRAPESLPNPL- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINN-----REKVYVVPGAKIGY-ARQNMSQIDLSQ 370
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGelapvSGEIGLAKGIKLGYfAQHQLEFLRADE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 371 TVLVNVRRVSIQ-SESISRIVLARLLLSERDMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIPSVEALEKM 449
Cdd:PRK10636 393 SPLQHLARLAPQeLEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEA 472
|
490 500 510
....*....|....*....|....*....|....
gi 1124469102 450 LVEYEGTLIFTSHDKVFVdRIATDRLY-IGDGKI 482
Cdd:PRK10636 473 LIDFEGALVVVSHDRHLL-RSTTDDLYlVHDGKV 505
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
297-481 |
5.35e-50 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 167.24 E-value: 5.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREKVY-----VVPGAKIGYARQnmsqidlsqt 371
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDegivtWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 372 vlvnvrrvsiqsesisrivlarlllserdmnkkaseLSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIPSVEALEKMLV 451
Cdd:cd03221 71 ------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALK 114
|
170 180 190
....*....|....*....|....*....|
gi 1124469102 452 EYEGTLIFTSHDKVFVDRIATDRLYIGDGK 481
Cdd:cd03221 115 EYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-175 |
9.92e-41 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 142.97 E-value: 9.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTV--SSNCIPFFFEQFgsdseyfet 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVtwGSTVKIGYFEQL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 85 dyaeagkmgvadhiwqenvSGGEDTRIRLAQLFSSPHAVAFLDEPTSNLDYNGVEMLKKRLNEIE-TLVVISHDRSVLNE 163
Cdd:cd03221 72 -------------------SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPgTVILVSHDRYFLDQ 132
|
170
....*....|..
gi 1124469102 164 ICDRIVEISFGK 175
Cdd:cd03221 133 VATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-186 |
4.65e-40 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 150.99 E-value: 4.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 5 LLIKAENIVHSYGEQTVL-DFDrFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTV--SSNCIPFFFEQfgsDSEY 81
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLdDLS-LRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVklGETVKIGYFDQ---HQEE 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 82 FETDyaeagkMGVADHIWQENV----------------------------SGGEDTRIRLAQLFSSPHAVAFLDEPTSNL 133
Cdd:COG0488 390 LDPD------KTVLDELRDGAPggteqevrgylgrflfsgddafkpvgvlSGGEKARLALAKLLLSPPNVLLLDEPTNHL 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1124469102 134 DYNGVEMLKKRLNEIE-TLVVISHDRSVLNEICDRIVEISFGKLQNYSGNYDEY 186
Cdd:COG0488 464 DIETLEALEEALDDFPgTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDY 517
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
104-482 |
2.45e-32 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 130.75 E-value: 2.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 104 SGGEDTRIRLAQ-LFSSPHaVAFLDEPTSNLDYNGVEMLKKRLNEI-ETLVVISHDRSVLNEICDRIVEISFGKLQNYSG 181
Cdd:PLN03073 346 SGGWRMRIALARaLFIEPD-LLLLDEPTNHLDLHAVLWLETYLLKWpKTFIVVSHAREFLNTVVTDILHLHGQKLVTYKG 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 182 NYDEYVVQKEEQRKTQQAEYENyqAEKKRlqsvyvekkakaktvdkkpknmsaseAKVRAFIGNRKPEDKARGIERSATN 261
Cdd:PLN03073 425 DYDTFERTREEQLKNQQKAFES--NERSR--------------------------SHMQAFIDKFRYNAKRASLVQSRIK 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 262 VLKRLEHMEikekpkeELTVRPDFRLTNP-----PRNPIvIRGEHISFAY-DDHVIFDDADFMIKNGSKVALLGGNGAGK 335
Cdd:PLN03073 477 ALDRLGHVD-------AVVNDPDYKFEFPtpddrPGPPI-ISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGK 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 336 TTLLELINNREK-----VYVVPGAKIG-YARQNMSQIDLSQTVLVNVRRVSIQS-ESISRIVLARLLLSERDMNKKASEL 408
Cdd:PLN03073 549 STILKLISGELQpssgtVFRSAKVRMAvFSQHHVDGLDLSSNPLLYMMRCFPGVpEQKLRAHLGSFGVTGNLALQPMYTL 628
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1124469102 409 SGGERMKLSFAMLFVSDVNLLILDEPTNYLDIPSVEALEKMLVEYEGTLIFTSHDKVFVDRIATDRLYIGDGKI 482
Cdd:PLN03073 629 SGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-175 |
2.35e-30 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 115.42 E-value: 2.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 8 KAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVssncipfffeqfgsdsEYFETDYA 87
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI----------------LIDGKDIA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 88 EAGKMGVADHI---WQenVSGGEDTRIRLAQLFSSPHAVAFLDEPTSNLDYNGVEMLKKRLNEI----ETLVVISHDRSV 160
Cdd:cd00267 65 KLPLEELRRRIgyvPQ--LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELaeegRTVIIVTHDPEL 142
|
170
....*....|....*
gi 1124469102 161 LNEICDRIVEISFGK 175
Cdd:cd00267 143 AELAADRVIVLKDGK 157
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
296-483 |
1.42e-29 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 116.11 E-value: 1.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 296 VIRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINN-----------------------REKVYVVP 352
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGllkpdsgsilidgedvrkepreaRRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 353 GAKIGYARQnmsqidlsqTVLVNVRRVS----IQSESISRIV--LARLLLSERDMNKKASELSGGERMKLSFAMLFVSDV 426
Cdd:COG4555 81 DERGLYDRL---------TVRENIRYFAelygLFDEELKKRIeeLIELLGLEEFLDRRVGELSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 427 NLLILDEPTNYLDIPSVEALEKMLVEY---EGTLIFTSHDKVFVDRIATDRLYIGDGKIR 483
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKGKVV 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
297-482 |
9.44e-29 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 112.60 E-value: 9.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREKVYvvpGAKIGYARQNMSQID--------- 367
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPT---SGEIYLDGKPLSAMPppewrrqva 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 368 -LSQ-------TVLVNVRRV-SIQSESISRI----VLARLLLSERDMNKKASELSGGERMKLSF--AMLFVSDVnlLILD 432
Cdd:COG4619 78 yVPQepalwggTVRDNLPFPfQLRERKFDREraleLLERLGLPPDILDKPVERLSGGERQRLALirALLLQPDV--LLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1124469102 433 EPTNYLDIPSVEALEKMLVEY----EGTLIFTSHDKVFVDRIATDRLYIGDGKI 482
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
297-482 |
1.56e-28 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 110.95 E-value: 1.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREKVYvvpgakigyarqnmsqidlSQTVLVNV 376
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPD-------------------SGEIKVLG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 377 RRVSIQSESISRIVLarlLLSERDM---NKKASE---LSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIPSVEALEKML 450
Cdd:cd03230 62 KDIKKEPEEVKRRIG---YLPEEPSlyeNLTVREnlkLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELL 138
|
170 180 190
....*....|....*....|....*....|....*
gi 1124469102 451 VEY---EGTLIFTSHDKVFVDRIATDRLYIGDGKI 482
Cdd:cd03230 139 RELkkeGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
300-481 |
4.47e-28 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 109.26 E-value: 4.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 300 EHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREKVYvvpgakigyarqnmsqidlSQTVLVNVRRV 379
Cdd:cd00267 3 ENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT-------------------SGEILIDGKDI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 380 SIQSESISRIVLARLllserdmnkkaSELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIPSVEALEKMLVEY--EG-T 456
Cdd:cd00267 64 AKLPLEELRRRIGYV-----------PQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELaeEGrT 132
|
170 180
....*....|....*....|....*
gi 1124469102 457 LIFTSHDKVFVDRIATDRLYIGDGK 481
Cdd:cd00267 133 VIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-176 |
1.53e-27 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 108.25 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPFF------FEQFGSDSE 80
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKkepeevKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 81 YFETDyaeaGKMGVADHIwqeNVSGGEDTRIRLAQ-LFSSPHaVAFLDEPTSNLDYNGVEMLKKRLNEIE----TLVVIS 155
Cdd:cd03230 81 EPSLY----ENLTVRENL---KLSGGMKQRLALAQaLLHDPE-LLILDEPTSGLDPESRREFWELLRELKkegkTILLSS 152
|
170 180
....*....|....*....|.
gi 1124469102 156 HDRSVLNEICDRIVEISFGKL 176
Cdd:cd03230 153 HILEEAERLCDRVAILNNGRI 173
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
296-481 |
2.98e-27 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 108.34 E-value: 2.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 296 VIRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELI---------------NNREKVYVVPGAKIGYAR 360
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILagllppsagevlwngEPIRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 361 QNmSQIDLSQTVLVNVR------RVSIQSESISRiVLARLLLSERdMNKKASELSGGERMKLSFAMLFVSDVNLLILDEP 434
Cdd:COG4133 82 HA-DGLKPELTVRENLRfwaalyGLRADREAIDE-ALEAVGLAGL-ADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1124469102 435 TNYLDIPSVEALEKMLVEY---EGTLIFTSHDKVFVDriATDRLYIGDGK 481
Cdd:COG4133 159 FTALDAAGVALLAELIAAHlarGGAVLLTTHQPLELA--AARVLDLGDFK 206
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
300-482 |
5.17e-27 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 106.75 E-value: 5.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 300 EHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREKVYvvpGAKIGYARQNMSQIDLSQTvlvnVRRV 379
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPS---SGEILLDGKDLASLSPKEL----ARKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 380 SIQSESISRIVLARllLSERDMNkkasELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIP-SVEALE--KMLVEYEG- 455
Cdd:cd03214 76 AYVPQALELLGLAH--LADRPFN----ELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAhQIELLEllRRLARERGk 149
|
170 180
....*....|....*....|....*...
gi 1124469102 456 TLIFTSHDKVFVDRIAtDRLY-IGDGKI 482
Cdd:cd03214 150 TVVMVLHDLNLAARYA-DRVIlLKDGRI 176
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
297-482 |
6.91e-27 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 108.23 E-value: 6.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELI-------------------NNREKVYvvpgAKIG 357
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLlgllrptsgevrvlgedvaRDPAEVR----RRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 358 YARQNMSqIDLSQTVLVNVRRVSI-----QSESISRI--VLARLLLSERdMNKKASELSGGERMKLSFAMLFVSDVNLLI 430
Cdd:COG1131 77 YVPQEPA-LYPDLTVRENLRFFARlyglpRKEARERIdeLLELFGLTDA-ADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1124469102 431 LDEPTNYLDIPSVEALEKMLVEY--EG-TLIFTSHDKVFVDRIATDRLYIGDGKI 482
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELaaEGkTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-482 |
9.05e-26 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 109.99 E-value: 9.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 1 MERHLLIKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPT---KGTV-------------- 63
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVlldgrdllelseal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 64 --------------SSNC------IPFFFEQFGSDSEYFETDYAEAGKMGVADHIWQEN---VSGGEDTRIRLAQLFSSP 120
Cdd:COG1123 81 rgrrigmvfqdpmtQLNPvtvgdqIAEALENLGLSRAEARARVLELLEAVGLERRLDRYphqLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 121 HAVAFLDEPTSNLDYNG---VEMLKKRLNEIE--TLVVISHDRSVLNEICDRIVEISFGKLQnysgnydeyvvqkeEQRK 195
Cdd:COG1123 161 PDLLIADEPTTALDVTTqaeILDLLRELQRERgtTVLLITHDLGVVAEIADRVVVMDDGRIV--------------EDGP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 196 TQQaeyenyqaekkrlqsvyvekkakaktVDKKPKNMSASEAKvrafignRKPEDKARGIERSATNVLkRLEHmeikekp 275
Cdd:COG1123 227 PEE--------------------------ILAAPQALAAVPRL-------GAARGRAAPAAAAAEPLL-EVRN------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 276 keeLTVRpdFRLTNPPRNPIVirgehisfayddhvifDDADFMIKNGSKVALLGGNGAGKTTLLELINNREK-----VYV 350
Cdd:COG1123 266 ---LSKR--YPVRGKGGVRAV----------------DDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRptsgsILF 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 351 ----VPGA----------KIGYARQN-MSQIDLSQTV-------LVNVRRVSiQSESISRI--VLARLLLSERDMNKKAS 406
Cdd:COG1123 325 dgkdLTKLsrrslrelrrRVQMVFQDpYSSLNPRMTVgdiiaepLRLHGLLS-RAERRERVaeLLERVGLPPDLADRYPH 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 407 ELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDiPSVEA-----LEKMLVEYEGTLIFTSHDKVFVDRIAtDRLYI-GDG 480
Cdd:COG1123 404 ELSGGQRQRVAIARALALEPKLLILDEPTSALD-VSVQAqilnlLRDLQRELGLTYLFISHDLAVVRYIA-DRVAVmYDG 481
|
..
gi 1124469102 481 KI 482
Cdd:COG1123 482 RI 483
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
293-483 |
1.60e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 104.79 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 293 NPIVIRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINN-----------REKVYVVPGAKIGYARQ 361
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGllpptsgtvrlFGKPPRRARRRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 362 NmSQIDLSQTVLVN-------------VRRVSIQSESISRIVLARLLLSERdMNKKASELSGGERMKLSFAMLFVSDVNL 428
Cdd:COG1121 83 R-AEVDWDFPITVRdvvlmgrygrrglFRRPSRADREAVDEALERVGLEDL-ADRPIGELSGGQQQRVLLARALAQDPDL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1124469102 429 LILDEPTNYLDIPSVEALEKMLVEY--EG-TLIFTSHDKVFVDRIATDRLYIGDGKIR 483
Cdd:COG1121 161 LLLDEPFAGVDAATEEALYELLRELrrEGkTILVVTHDLGAVREYFDRVLLLNRGLVA 218
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
300-471 |
2.52e-25 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 103.38 E-value: 2.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 300 EHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELI-----NNREKVYVVP------GAKIGYARQnmsQIDL 368
Cdd:cd03235 3 EDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAIlgllkPTSGSIRVFGkplekeRKRIGYVPQ---RRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 369 SQTVLVNVRRV------------SIQSESISRIVLArlLLSERDMNKKA----SELSGGERMKLSFAMLFVSDVNLLILD 432
Cdd:cd03235 80 DRDFPISVRDVvlmglyghkglfRRLSKADKAKVDE--ALERVGLSELAdrqiGELSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1124469102 433 EPTNYLDIPSVEALEKMLVEY--EG-TLIFTSHD----KVFVDRIA 471
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELrrEGmTILVVTHDlglvLEYFDRVL 203
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-190 |
3.79e-25 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 108.44 E-value: 3.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 1 MERHLLIkAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTV--SSNCIPFFFEQfgsD 78
Cdd:PRK15064 315 LHRNALE-VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwSENANIGYYAQ---D 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 79 SEY-FETDyaeagkMGVADHIWQ-----------------------------ENVSGGEDTRIRLAQLFSSPHAVAFLDE 128
Cdd:PRK15064 391 HAYdFEND------LTLFDWMSQwrqegddeqavrgtlgrllfsqddikksvKVLSGGEKGRMLFGKLMMQKPNVLVMDE 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1124469102 129 PTSNLDYNGVEMLKKRLNEIE-TLVVISHDRSVLNEICDRIVEISFGKLQNYSGNYDEYVVQK 190
Cdd:PRK15064 465 PTNHMDMESIESLNMALEKYEgTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRSQ 527
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
300-481 |
3.92e-25 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 102.55 E-value: 3.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 300 EHISFAYDDH--VIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREKVY----VVPG------------AKIGYARQ 361
Cdd:cd03225 3 KNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTsgevLVDGkdltklslkelrRKVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 362 NM-SQIdLSQTV-------LVNvRRVSiQSESISRI--VLARLLLSERdMNKKASELSGGERMKLSFAMLFVSDVNLLIL 431
Cdd:cd03225 83 NPdDQF-FGPTVeeevafgLEN-LGLP-EEEIEERVeeALELVGLEGL-RDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1124469102 432 DEPTNYLDIPSVEALEKMLVEY--EG-TLIFTSHDKVFVDRIATDRLYIGDGK 481
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLkaEGkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-185 |
6.28e-25 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 103.01 E-value: 6.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSN------------------- 66
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDgedvrkeprearrqigvlp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 67 -------------CIPFFFEQFGSDSEYFETDYAE-AGKMG---VADHIWQEnVSGGEDTRIRLAQLFSSPHAVAFLDEP 129
Cdd:COG4555 81 derglydrltvreNIRYFAELYGLFDEELKKRIEElIELLGleeFLDRRVGE-LSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 130 TSNLDYNGVEMLKKRLNEI---ETLVVIS-HDRSVLNEICDRIVEISFGKLQnYSGNYDE 185
Cdd:COG4555 160 TNGLDVMARRLLREILRALkkeGKTVLFSsHIMQEVEALCDRVVILHKGKVV-AQGSLDE 218
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
9-176 |
6.32e-25 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 101.95 E-value: 6.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 9 AENIVHSYGEQT-VLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSN-----------CIPFFFE--- 73
Cdd:cd03226 2 IENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNgkpikakerrkSIGYVMQdvd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 74 -QFGSDSEYFETDY---AEAGKMGVADHIWQE------------NVSGGEDTRIRLA-QLFSSPHAVaFLDEPTSNLDYN 136
Cdd:cd03226 82 yQLFTDSVREELLLglkELDAGNEQAETVLKDldlyalkerhplSLSGGQKQRLAIAaALLSGKDLL-IFDEPTSGLDYK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1124469102 137 GVEMLKKRLNEIE----TLVVISHDRSVLNEICDRIVEISFGKL 176
Cdd:cd03226 161 NMERVGELIRELAaqgkAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-176 |
4.94e-24 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 98.27 E-value: 4.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPFffeQFGSDseyfetdy 86
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV---SFASP-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 87 AEAGKMGVAdHIWQenVSGGEDTRIRLAQLFSSPHAVAFLDEPTSNLDYNGVEMLKKRLNEI----ETLVVISHDRSVLN 162
Cdd:cd03216 70 RDARRAGIA-MVYQ--LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLraqgVAVIFISHRLDEVF 146
|
170
....*....|....
gi 1124469102 163 EICDRIVEISFGKL 176
Cdd:cd03216 147 EIADRVTVLRDGRV 160
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
10-175 |
2.14e-23 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 97.92 E-value: 2.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 10 ENIVHSY--GEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTV-------SSNCIPFFFEQFG---- 76
Cdd:cd03225 3 KNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVlvdgkdlTKLSLKELRRKVGlvfq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 77 -SDSEYFETDYAE-----AGKMGVADHIWQENV--------------------SGGEDTRIRLAQLFSSPHAVAFLDEPT 130
Cdd:cd03225 83 nPDDQFFGPTVEEevafgLENLGLPEEEIEERVeealelvgleglrdrspftlSGGQKQRVAIAGVLAMDPDILLLDEPT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1124469102 131 SNLDYNG----VEMLKKRLNEIETLVVISHDRSVLNEICDRIVEISFGK 175
Cdd:cd03225 163 AGLDPAGrrelLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
296-463 |
1.00e-22 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 97.04 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 296 VIRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREK-----VYV-------VPGA----KIGYA 359
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKpssgeVLLdgrdlasLSRRelarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 360 RQNmSQIDLSQTV--LV---------NVRRVSIQSESISRIVLARL-L--LSERDMNkkasELSGGERMKLSFAMLFVSD 425
Cdd:COG1120 81 PQE-PPAPFGLTVreLValgryphlgLFGRPSAEDREAVEEALERTgLehLADRPVD----ELSGGERQRVLIARALAQE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1124469102 426 VNLLILDEPTNYLDIPS-VEALEKM--LVEYEG-TLIFTSHD 463
Cdd:COG1120 156 PPLLLLDEPTSHLDLAHqLEVLELLrrLARERGrTVVMVLHD 197
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-176 |
1.02e-22 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 94.81 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 8 KAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSsncipfffeqfgsdseYFETDYA 87
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL----------------LDGKDLA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 88 E------AGKMGV-------------ADHIWQEnVSGGEDTRIRLAQLFSSPHAVAFLDEPTSNLDYNG-VEMLK--KRL 145
Cdd:cd03214 65 SlspkelARKIAYvpqalellglahlADRPFNE-LSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHqIELLEllRRL 143
|
170 180 190
....*....|....*....|....*....|....*.
gi 1124469102 146 NEIE--TLVVISHDrsvLN---EICDRIVEISFGKL 176
Cdd:cd03214 144 ARERgkTVVMVLHD---LNlaaRYADRVILLKDGRI 176
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-171 |
1.27e-22 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 96.70 E-value: 1.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 1 MERHLLIKAENIVHSYGEQTVL---DFDrfyLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPFFFE---- 73
Cdd:COG1121 1 MMMMPAIELENLTVSYGGRPVLedvSLT---IPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRArrri 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 74 ----QFGSDSEYF-----------------------ETDYAEA----GKMGVAD----HIWQenVSGGEDTRIRLAQLFS 118
Cdd:COG1121 78 gyvpQRAEVDWDFpitvrdvvlmgrygrrglfrrpsRADREAVdealERVGLEDladrPIGE--LSGGQQQRVLLARALA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1124469102 119 SPHAVAFLDEPTSNLDYNGVEMLKKRLNEIE----TLVVISHDRSVLNEICDRIVEI 171
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYELLRELRregkTILVVTHDLGAVREYFDRVLLL 212
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
7-175 |
1.67e-22 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 94.18 E-value: 1.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIP-----FFFEQFGSDSEY 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDltdleDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 82 FETDYAEAGKMGVADHIwQENVSGGEDTRIRLAQ-LFSSPHaVAFLDEPTSNLD---YNGVEMLKKRLNEIE--TLVVIS 155
Cdd:cd03229 81 VFQDFALFPHLTVLENI-ALGLSGGQQQRVALARaLAMDPD-VLLLDEPTSALDpitRREVRALLKSLQAQLgiTVVLVT 158
|
170 180
....*....|....*....|
gi 1124469102 156 HDRSVLNEICDRIVEISFGK 175
Cdd:cd03229 159 HDLDEAARLADRVVVLRDGK 178
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
297-482 |
1.09e-21 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 93.55 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAY-DDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELIN-----------------NREKVYVVPgAKIGY 358
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNgllkptsgevlvdgkdiTKKNLRELR-RKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 359 ARQN-MSQIdLSQTV-------LVNvRRVSiQSESISRI--VLARLLLSERdMNKKASELSGGERMKLSFAMLFVSDVNL 428
Cdd:COG1122 80 VFQNpDDQL-FAPTVeedvafgPEN-LGLP-REEIRERVeeALELVGLEHL-ADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1124469102 429 LILDEPTNYLDIPSVEALEKMLVEY--EG-TLIFTSHDKVFVDRIAtDRLYI-GDGKI 482
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLnkEGkTVIIVTHDLDLVAELA-DRVIVlDDGRI 212
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
8-171 |
1.83e-21 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 92.21 E-value: 1.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 8 KAENIVHSYGEQTVL-DFDrFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSsncipFFFEQFGSD-------- 78
Cdd:cd03235 1 EVEDLTVSYGGHPVLeDVS-FEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIR-----VFGKPLEKErkrigyvp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 79 -SEYFETDY------------------------------AEAGKMGVADHIWQENV---SGGEDTRIRLAQLFSSPHAVA 124
Cdd:cd03235 75 qRRSIDRDFpisvrdvvlmglyghkglfrrlskadkakvDEALERVGLSELADRQIgelSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1124469102 125 FLDEPTSNLDYNGVEMLKKRLNEIE----TLVVISHDRSVLNEICDRIVEI 171
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRregmTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
7-169 |
1.97e-21 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 91.12 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYG--EQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPFF---FEQFG----- 76
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISqwdPNELGdhvgy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 77 --SDSEYFetdyaeAGKmgVADHIwqenVSGGEDTRIRLAQ-LFSSPHAVaFLDEPTSNLDYNG-------VEMLKKRLn 146
Cdd:cd03246 81 lpQDDELF------SGS--IAENI----LSGGQRQRLGLARaLYGNPRIL-VLDEPNSHLDVEGeralnqaIAALKAAG- 146
|
170 180
....*....|....*....|...
gi 1124469102 147 eiETLVVISHDRSVLnEICDRIV 169
Cdd:cd03246 147 --ATRIVIAHRPETL-ASADRIL 166
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
7-175 |
2.02e-21 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 90.91 E-value: 2.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYG--EQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNcipfffeqfGSD-SEYFE 83
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILID---------GVDlRDLDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 84 TDYAEagKMGVAD---HIWQ----ENV-SGGEDTRIRLAQLFSSPHAVAFLDEPTSNLDYNGVEMLKKRLNEIE---TLV 152
Cdd:cd03228 72 ESLRK--NIAYVPqdpFLFSgtirENIlSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAkgkTVI 149
|
170 180
....*....|....*....|...
gi 1124469102 153 VISHDRSVLnEICDRIVEISFGK 175
Cdd:cd03228 150 VIAHRLSTI-RDADRIIVLDDGR 171
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-195 |
2.78e-21 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 96.93 E-value: 2.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 5 LLIKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVS--SNCIPFFFEQF-----GS 77
Cdd:TIGR03719 321 KVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEigETVKLAYVDQSrdaldPN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 78 DSEYFE----TDYAEAGKMGV-------------ADHiwQENV---SGGEDTRIRLAQLFSSPHAVAFLDEPTSNLDyng 137
Cdd:TIGR03719 401 KTVWEEisggLDIIKLGKREIpsrayvgrfnfkgSDQ--QKKVgqlSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD--- 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1124469102 138 VEMLKKRLNEIETL----VVISHDRSVLNEICDRIveISF---GKLQNYSGNYDEYvvqkEEQRK 195
Cdd:TIGR03719 476 VETLRALEEALLNFagcaVVISHDRWFLDRIATHI--LAFegdSHVEWFEGNFSEY----EEDKK 534
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
7-195 |
2.89e-21 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 92.40 E-value: 2.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSY-GEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIP---------------- 69
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDitkknlrelrrkvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 70 -------FFF-----------EQFGSDSEYFETDYAEAGKM----GVADHIWQEnVSGGEDTRIRLA-QLFSSPhAVAFL 126
Cdd:COG1122 81 fqnpddqLFAptveedvafgpENLGLPREEIRERVEEALELvgleHLADRPPHE-LSGGQKQRVAIAgVLAMEP-EVLVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1124469102 127 DEPTSNLDYNGVEMLKKRLNEIE----TLVVISHDRSVLNEICDRIVEISFGKLQnYSGNYDEYVVQKEEQRK 195
Cdd:COG1122 159 DEPTAGLDPRGRRELLELLKRLNkegkTVIIVTHDLDLVAELADRVIVLDDGRIV-ADGTPREVFSDYELLEE 230
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
7-185 |
2.93e-21 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 97.21 E-value: 2.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQT--VLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIP--------------- 69
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDlrqidpaslrrqigv 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 70 -----FFFEqfGS--------DSEYFETDYAEAGKM-GVADHIWQ-------------ENVSGGEDTRIRLAQLFSSPHA 122
Cdd:COG2274 554 vlqdvFLFS--GTirenitlgDPDATDEEIIEAARLaGLHDFIEAlpmgydtvvgeggSNLSGGQRQRLAIARALLRNPR 631
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1124469102 123 VAFLDEPTSNLDYNGVEMLKKRLNEIE---TLVVISHDRSVLnEICDRIVEISFGKLQNySGNYDE 185
Cdd:COG2274 632 ILILDEATSALDAETEAIILENLRRLLkgrTVIIIAHRLSTI-RLADRIIVLDKGRIVE-DGTHEE 695
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
10-176 |
3.06e-21 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 91.88 E-value: 3.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 10 ENIVHSYGEQT--VLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSN-----------------CIP- 69
Cdd:cd03245 6 RNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDgtdirqldpadlrrnigYVPq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 70 ----FF---------FEQFGSDSEYFE-------TDYAEAGKMGVADHIWQ--ENVSGGEDTRIRLAQLFSSPHAVAFLD 127
Cdd:cd03245 86 dvtlFYgtlrdnitlGAPLADDERILRaaelagvTDFVNKHPNGLDLQIGErgRGLSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1124469102 128 EPTSNLDYNGVEMLKKRLNEI---ETLVVISHdRSVLNEICDRIVEISFGKL 176
Cdd:cd03245 166 EPTSAMDMNSEERLKERLRQLlgdKTLIIITH-RPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
7-176 |
3.17e-21 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 91.78 E-value: 3.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQ----TVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIP------------- 69
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDisklsekelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 70 -----FFFEQF-------------------GSDSEYFETDYAEA-GKMGVADHIWQ--ENVSGGEDTRIRLAQ-LFSSPh 121
Cdd:cd03255 81 rrhigFVFQSFnllpdltalenvelplllaGVPKKERRERAEELlERVGLGDRLNHypSELSGGQQQRVAIARaLANDP- 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 122 AVAFLDEPTSNLD-YNGVEMLK--KRLNEIE--TLVVISHDRSvLNEICDRIVEISFGKL 176
Cdd:cd03255 160 KIILADEPTGNLDsETGKEVMEllRELNKEAgtTIVVVTHDPE-LAEYADRIIELRDGKI 218
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
6-212 |
3.53e-21 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 96.78 E-value: 3.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVS-SNCIPF-FFEQfgSDSEYFE 83
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGlAKGIKLgYFAQ--HQLEFLR 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 84 TDYAEA-------------------GKMGV-ADHIWQ--ENVSGGEDTRIRLAQLFSSPHAVAFLDEPTSNLDYNGVEML 141
Cdd:PRK10636 390 ADESPLqhlarlapqeleqklrdylGGFGFqGDKVTEetRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQAL 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1124469102 142 KKRLNEIE-TLVVISHDRSVLNEICDRIVEISFGKLQNYSGNYDEYV-----VQKEE-QRKTQQAEYENYQAEKKRLQ 212
Cdd:PRK10636 470 TEALIDFEgALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQqwlsdVQKQEnQTDEAPKENNANSAQARKDQ 547
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
10-481 |
1.18e-20 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 94.85 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 10 ENIVHSYGEqtvldfDRFYLY------EGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSS-----NCIPFFfeqfgSD 78
Cdd:COG1245 77 EDPVHRYGE------NGFRLYglpvpkKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEepswdEVLKRF-----RG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 79 SE---YFE-------------------------------TDYAEAGKM-GVAD-----HIWQENV---SGGEDTRIRLAQ 115
Cdd:COG1245 146 TElqdYFKklangeikvahkpqyvdlipkvfkgtvrellEKVDERGKLdELAEklgleNILDRDIselSGGELQRVAIAA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 116 LFSSPHAVAFLDEPTSNLD----YNGVEMLKKRLNEIETLVVISHDRSVLNEICDrIVEISFGKlqnySGNYDeyVVQKE 191
Cdd:COG1245 226 ALLRDADFYFFDEPSSYLDiyqrLNVARLIRELAEEGKYVLVVEHDLAILDYLAD-YVHILYGE----PGVYG--VVSKP 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 192 EQRKTQQAEY-ENY-QAEKKRLQSVYVEKKAKAKTVDKKpknmsaSEAKVrafignrkpedkargierSATNVLKRLehm 269
Cdd:COG1245 299 KSVRVGINQYlDGYlPEENVRIRDEPIEFEVHAPRREKE------EETLV------------------EYPDLTKSY--- 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 270 eikekpkeeltvrPDFRLTnpprnpiVIRGEhisfayddhvifddadfmIKNGSKVALLGGNGAGKTTLLELINNREKV- 348
Cdd:COG1245 352 -------------GGFSLE-------VEGGE------------------IREGEVLGIVGPNGIGKTTFAKILAGVLKPd 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 349 --YVVPGAKIGYARQNMSqIDLSQTVLVNVRRVSIQ--SESISRIVLARLLLSERDMNKKASELSGGERMKLSFAMLFVS 424
Cdd:COG1245 394 egEVDEDLKISYKPQYIS-PDYDGTVEEFLRSANTDdfGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSR 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1124469102 425 DVNLLILDEPTNYLDipsVE-------ALEKMLVEYEGTLIFTSHDKVFVDRIAtDRLYIGDGK 481
Cdd:COG1245 473 DADLYLLDEPSAHLD---VEqrlavakAIRRFAENRGKTAMVVDHDIYLIDYIS-DRLMVFEGE 532
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-169 |
1.50e-20 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 90.87 E-value: 1.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVS--------------------- 64
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgrdlaslsrrelarriayv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 65 --SNCIPFFF--------------EQFGSDSeyfETDYAEAGK----MGV---ADHIWQEnVSGGEDTRIRLAQlfssph 121
Cdd:COG1120 81 pqEPPAPFGLtvrelvalgryphlGLFGRPS---AEDREAVEEalerTGLehlADRPVDE-LSGGERQRVLIAR------ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1124469102 122 AVA------FLDEPTSNLD-YNGVEMLK--KRLNEIE--TLVVISHDrsvLN---EICDRIV 169
Cdd:COG1120 151 ALAqeppllLLDEPTSHLDlAHQLEVLEllRRLARERgrTVVMVLHD---LNlaaRYADRLV 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
296-482 |
2.12e-20 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 89.87 E-value: 2.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 296 VIRGEHISFAYDD----HVIFDDADFMIKNGSKVALLGGNGAGKTTLL-------------------ELINNREKVYVVP 352
Cdd:cd03257 1 LLEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLArailgllkptsgsiifdgkDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 353 GAKIGYARQN-MSQIDLSQTV------LVNVRRVSIQSESISRIVLA---RLLLSERDMNKKASELSGGERMKLSFAMLF 422
Cdd:cd03257 81 RKEIQMVFQDpMSSLNPRMTIgeqiaePLRIHGKLSKKEARKEAVLLllvGVGLPEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1124469102 423 VSDVNLLILDEPTNYLDiPSVEA-----LEKMLVEYEGTLIFTSHDKVFVDRIAtDRLYI-GDGKI 482
Cdd:cd03257 161 ALNPKLLIADEPTSALD-VSVQAqildlLKKLQEELGLTLLFITHDLGVVAKIA-DRVAVmYAGKI 224
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
10-481 |
2.55e-20 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 94.10 E-value: 2.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 10 ENIVHSYGEqtvldfDRFYLY------EGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSS-----NCIPFFfeqfgSD 78
Cdd:PRK13409 77 EEPVHRYGV------NGFKLYglpipkEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEepswdEVLKRF-----RG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 79 SE---YFETDYAeaGKMGVA---------------------------------------DHIWQENV---SGGEDTRIRL 113
Cdd:PRK13409 146 TElqnYFKKLYN--GEIKVVhkpqyvdlipkvfkgkvrellkkvdergkldevverlglENILDRDIselSGGELQRVAI 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 114 AQLFSSPHAVAFLDEPTSNLD-YNGVEMLK--KRLNEIETLVVISHDRSVLNEICDrIVEISFGKlqnysgnydeyvvqk 190
Cdd:PRK13409 224 AAALLRDADFYFFDEPTSYLDiRQRLNVARliRELAEGKYVLVVEHDLAVLDYLAD-NVHIAYGE--------------- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 191 eeqrktqqaeyenyqaekkrlQSVYvekkakakTVDKKPKnmSASEAkVRAFIGNRKPEDkargiersatNVLKRLEHME 270
Cdd:PRK13409 288 ---------------------PGAY--------GVVSKPK--GVRVG-INEYLKGYLPEE----------NMRIRPEPIE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 271 IKEKPKEELTVRPdfrltnpprnpIVIRGEHISFAYDDHVIFDDADFmIKNGSKVALLGGNGAGKTTLLELINNREKV-- 348
Cdd:PRK13409 326 FEERPPRDESERE-----------TLVEYPDLTKKLGDFSLEVEGGE-IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPde 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 349 -YVVPGAKIGYARQNMSqIDLSQTVLVNVRRVS-------IQSESISRIVLARLLlsERDMNkkasELSGGERMKLSFAM 420
Cdd:PRK13409 394 gEVDPELKISYKPQYIK-PDYDGTVEDLLRSITddlgssyYKSEIIKPLQLERLL--DKNVK----DLSGGELQRVAIAA 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1124469102 421 LFVSDVNLLILDEPTNYLDipsVE-------ALEKMLVEYEGTLIFTSHDKVFVDRIAtDRLYIGDGK 481
Cdd:PRK13409 467 CLSRDADLYLLDEPSAHLD---VEqrlavakAIRRIAEEREATALVVDHDIYMIDYIS-DRLMVFEGE 530
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
312-436 |
3.42e-20 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 86.93 E-value: 3.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 312 FDDADFMIKNGSKVALLGGNGAGKTTLLELINNREK----------------VYVVPGAKIGYARQNmSQIDLSQTVLVN 375
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSptegtilldgqdltddERKSLRKEIGYVFQD-PQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1124469102 376 VRRV-------SIQSESISRIVLARL---LLSERDMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTN 436
Cdd:pfam00005 80 LRLGlllkglsKREKDARAEEALEKLglgDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
310-477 |
6.17e-20 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 92.93 E-value: 6.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 310 VIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREKV-----------------------------YVVPG------- 353
Cdd:PRK10636 15 VLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISAdggsytfpgnwqlawvnqetpalpqpaleYVIDGdreyrql 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 354 ---AKIGYARQNMSQIDLSQTVLVNVRRVSIQSESISriVLARLLLSERDMNKKASELSGGERMKLSFAMLFVSDVNLLI 430
Cdd:PRK10636 95 eaqLHDANERNDGHAIATIHGKLDAIDAWTIRSRAAS--LLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1124469102 431 LDEPTNYLDIPSVEALEKMLVEYEGTLIFTSHDKVFVDRIATDRLYI 477
Cdd:PRK10636 173 LDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHI 219
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
7-176 |
8.42e-20 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 88.20 E-value: 8.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSN-------------CIPFFFE 73
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLgedvardpaevrrRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 74 QFGSD------------SEYFETDYAEAGK--------MGVADHIWQ--ENVSGGEDTRIRLAQ-LFSSPhAVAFLDEPT 130
Cdd:COG1131 81 EPALYpdltvrenlrffARLYGLPRKEAREridellelFGLTDAADRkvGTLSGGMKQRLGLALaLLHDP-ELLILDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1124469102 131 SNLDYNGVEMLKKRLNEIE----TLVVISHDRSVLNEICDRIVEISFGKL 176
Cdd:COG1131 160 SGLDPEARRELWELLRELAaegkTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
295-483 |
2.14e-19 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 86.79 E-value: 2.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 295 IVIRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREK-----VYVvPGAKIGY----ARQNMS- 364
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRptsgtAYI-NGYSIRTdrkaARQSLGy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 365 --Q---IDLSQTVLVNVR--------RVSIQSESISRivLARLLLSERDMNKKASELSGGERMKLSFAMLFVSDVNLLIL 431
Cdd:cd03263 80 cpQfdaLFDELTVREHLRfyarlkglPKSEIKEEVEL--LLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1124469102 432 DEPTNYLDIPSVEALEKMLVEYEG--TLIFTSHDKVFVDRIAtDRLYI-GDGKIR 483
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVRKgrSIILTTHSMDEAEALC-DRIAImSDGKLR 211
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
297-482 |
3.57e-19 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 86.00 E-value: 3.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDD----HVIFDDADFMIKNGSKVALLGGNGAGKTTLLELI-------------NNREKVYVVPGAKIGYA 359
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILggldrptsgevrvDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 360 RQNMSQI--------DLsqTVLVNV-------RRVSIQSESISRIVLARLLLSERdMNKKASELSGGERMKLSFAMLFVS 424
Cdd:cd03255 81 RRHIGFVfqsfnllpDL--TALENVelplllaGVPKKERRERAEELLERVGLGDR-LNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1124469102 425 DVNLLILDEPTNYLDIPS----VEALEKMLVEYEGTLIFTSHDKVFVDRiaTDR-LYIGDGKI 482
Cdd:cd03255 158 DPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDPELAEY--ADRiIELRDGKI 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-172 |
4.44e-19 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 85.22 E-value: 4.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSYGEQTV---LDFDrfyLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIP------------- 69
Cdd:COG4133 2 MLEAENLSCRRGERLLfsgLSFT---LAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPirdaredyrrrla 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 70 -------------------FFFEQFGSDSEyfETDYAEA-GKMGVADHIWQE--NVSGGEDTRIRLAQLFSSPHAVAFLD 127
Cdd:COG4133 79 ylghadglkpeltvrenlrFWAALYGLRAD--REAIDEAlEAVGLAGLADLPvrQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1124469102 128 EPTSNLDYNGVEMLKKRLNE-IE---TLVVISHDRsvLNEICDRIVEIS 172
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAhLArggAVLLTTHQP--LELAAARVLDLG 203
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
294-462 |
5.45e-19 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 86.29 E-value: 5.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 294 PIVIRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNR------EKVYV---VPG--------AKI 356
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlpptygNDVRLfgeRRGgedvwelrKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 357 GYARQNMSQ-IDLSQTVLvNV------------RRVSIQSESISRIVLARLLLSERdMNKKASELSGGERMKLSFAMLFV 423
Cdd:COG1119 81 GLVSPALQLrFPRDETVL-DVvlsgffdsiglyREPTDEQRERARELLELLGLAHL-ADRPFGTLSQGEQRRVLIARALV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1124469102 424 SDVNLLILDEPTNYLDIPS----VEALEKMLVEYEGTLIFTSH 462
Cdd:COG1119 159 KDPELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVTH 201
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
9-241 |
6.34e-19 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 89.62 E-value: 6.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 9 AENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVssNC-----IPfFFEQFGS--DSEY 81
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI--HCgtkleVA-YFDQHRAelDPEK 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 82 FETDYAEAGKM-----GVADHI---WQE-------------NVSGGEDTRIRLAQLFSSPHAVAFLDEPTSNLDYNGVEM 140
Cdd:PRK11147 399 TVMDNLAEGKQevmvnGRPRHVlgyLQDflfhpkramtpvkALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLEL 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 141 LKKRLNEIE-TLVVISHDRsvlnEICDRIVEISF-----GKLQNYSGNYDEYVVQkeeqrktQQAEYENYQAEKKRLQSV 214
Cdd:PRK11147 479 LEELLDSYQgTVLLVSHDR----QFVDNTVTECWifegnGKIGRYVGGYHDARQQ-------QAQYLALKQPAVKKKEEA 547
|
250 260 270
....*....|....*....|....*....|....*....
gi 1124469102 215 YVEKKAKAKTVDKK------------PKNMSASEAKVRA 241
Cdd:PRK11147 548 AAPKAETVKRSSKKlsyklqreleqlPQLLEDLEAEIEA 586
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
6-176 |
1.04e-18 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 85.18 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSY----GEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVS----------------- 64
Cdd:COG4181 8 IIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRlagqdlfaldedararl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 65 -SNCIPFFFEQF------------------GSDSEYFETDYAEAGKMGV---ADHIWQEnVSGGEDTRIRLAQLFSSPHA 122
Cdd:COG4181 88 rARHVGFVFQSFqllptltalenvmlplelAGRRDARARARALLERVGLghrLDHYPAQ-LSGGEQQRVALARAFATEPA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1124469102 123 VAFLDEPTSNLDY-NG---VEMLkKRLNEiE---TLVVISHDRSvLNEICDRIVEISFGKL 176
Cdd:COG4181 167 ILFADEPTGNLDAaTGeqiIDLL-FELNR-ErgtTLVLVTHDPA-LAARCDRVLRLRAGRL 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
300-483 |
1.79e-18 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 83.87 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 300 EHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELIN------------NREKVYVVPGAKIGY---AR---Q 361
Cdd:cd03269 4 ENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILgiilpdsgevlfDGKPLDIAARNRIGYlpeERglyP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 362 NMSQID----LSQtvLVNVRRVSIQSEsiSRIVLARLLLSERDmNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNY 437
Cdd:cd03269 84 KMKVIDqlvyLAQ--LKGLKKEEARRR--IDEWLERLELSEYA-NKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1124469102 438 LDIPSVEALEKMLVEYEG---TLIFTSHDKVFVDRIATDRLYIGDGKIR 483
Cdd:cd03269 159 LDPVNVELLKDVIRELARagkTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
7-185 |
2.10e-18 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 87.90 E-value: 2.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSY--GEQTVL-DFDrFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPF------------- 70
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLdGLS-LTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLrdldeddlrrria 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 71 FFEQfgsDSEYFETDYAEA---GKMGVAD-HIWQ--------------------------ENVSGGEDTRIRLAQLFSSP 120
Cdd:COG4987 413 VVPQ---RPHLFDTTLRENlrlARPDATDeELWAalervglgdwlaalpdgldtwlgeggRRLSGGERRRLALARALLRD 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1124469102 121 HAVAFLDEPTSNLDYNGVEMLKKRLNEIE---TLVVISHDRSVLnEICDRIVEISFGKLQNySGNYDE 185
Cdd:COG4987 490 APILLLDEPTEGLDAATEQALLADLLEALagrTVLLITHRLAGL-ERMDRILVLEDGRIVE-QGTHEE 555
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
300-482 |
3.84e-18 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 82.95 E-value: 3.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 300 EHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREK-----VYV-------VPGAK--IGYARQNMSq 365
Cdd:cd03259 4 KGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERpdsgeILIdgrdvtgVPPERrnIGMVFQDYA- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 366 idL--SQTVLVNV----RRVSIQSESISRIV--LARLLLSERDMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNY 437
Cdd:cd03259 83 --LfpHLTVAENIafglKLRGVPKAEIRARVreLLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1124469102 438 LDIPSVEALEKMLVEY----EGTLIFTSHDKVFVDRIAtDRLYI-GDGKI 482
Cdd:cd03259 161 LDAKLREELREELKELqrelGITTIYVTHDQEEALALA-DRIAVmNEGRI 209
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
6-176 |
5.93e-18 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 82.78 E-value: 5.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSYG----EQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTV------------------ 63
Cdd:COG1136 4 LLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVlidgqdisslserelarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 64 ----------SSNCIPFF--FEQ-------FGSDSEYFETDYAEA-GKMGVADHIWQ--ENVSGGEDTRIRLAQ-LFSSP 120
Cdd:COG1136 84 rrrhigfvfqFFNLLPELtaLENvalplllAGVSRKERRERARELlERVGLGDRLDHrpSQLSGGQQQRVAIARaLVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1124469102 121 hAVAFLDEPTSNLDY-NGVEMLK--KRLNEIE--TLVVISHDRSVLnEICDRIVEISFGKL 176
Cdd:COG1136 164 -KLILADEPTGNLDSkTGEEVLEllRELNRELgtTIVMVTHDPELA-ARADRVIRLRDGRI 222
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
297-482 |
1.71e-17 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 81.39 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELI-----NNREKVYVvpgakIGYARQNMSQIDL--- 368
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIvgllrPDSGEVLI-----DGEDISGLSEAELyrl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 369 ---------------SQTVLVNV----RRVSIQSES-ISRIVLARLL---LSERDmNKKASELSGGERMKLSFAMLFVSD 425
Cdd:cd03261 76 rrrmgmlfqsgalfdSLTVFENVafplREHTRLSEEeIREIVLEKLEavgLRGAE-DLYPAELSGGMKKRVALARALALD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1124469102 426 VNLLILDEPTNYLDIPSVEALEKMLV----EYEGTLIFTSHDKVFVDRIAtDRLY-IGDGKI 482
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLIRslkkELGLTSIMVTHDLDTAFAIA-DRIAvLYDGKI 215
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
297-482 |
1.91e-17 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 80.05 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYD--DHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELInnrEKVYVVPGAKIGYARQNMS--QIDLSQTV 372
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLL---TGDLKPQQGEITLDGVPVSdlEKALSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 373 LVNVRRVSIQSESIsrivlarlllserdMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLD-IPSVEALEKMLV 451
Cdd:cd03247 78 SVLNQRPYLFDTTL--------------RNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDpITERQLLSLIFE 143
|
170 180 190
....*....|....*....|....*....|....*
gi 1124469102 452 EYEG-TLIFTSHDKV---FVDRIatdrLYIGDGKI 482
Cdd:cd03247 144 VLKDkTLIWITHHLTgieHMDKI----LFLENGKI 174
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
297-467 |
2.48e-17 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 79.35 E-value: 2.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDD--HVIFDDADFMIKNGSKVALLGGNGAGKTTLLELI-----NNREKVYV--VPGAKIGYA--RQNMSQ 365
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLlrlydPTSGEILIdgVDLRDLDLEslRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 366 ID-----LSQTVLVNVrrvsiqsesisrivlarlllserdmnkkaseLSGGERMKLSFAMLFVSDVNLLILDEPTNYLDI 440
Cdd:cd03228 81 VPqdpflFSGTIRENI-------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDP 129
|
170 180 190
....*....|....*....|....*....|....*..
gi 1124469102 441 PSVEALEKMLVEYEG--TLIFTSH--------DKVFV 467
Cdd:cd03228 130 ETEALILEALRALAKgkTVIVIAHrlstirdaDRIIV 166
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
263-482 |
2.55e-17 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 84.89 E-value: 2.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 263 LKRLEhmEIKEKPKEEltvRPDFRLTNPPRNPIVIRGEHISFAYDDHV--IFDDADFMIKNGSKVALLGGNGAGKTTLLE 340
Cdd:COG2274 445 LERLD--DILDLPPER---EEGRSKLSLPRLKGDIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLK 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 341 LINnreKVYVVPGAKIGYARQNMSQIDLSQtvlvnVRR--------VSIQSESISR-IVLARLLLSERDMNKKA------ 405
Cdd:COG2274 520 LLL---GLYEPTSGRILIDGIDLRQIDPAS-----LRRqigvvlqdVFLFSGTIREnITLGDPDATDEEIIEAArlaglh 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 406 ------------------SELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIPSVEALEKMLVEYEG--TLIFTSHDK- 464
Cdd:COG2274 592 dfiealpmgydtvvgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLs 671
|
250 260
....*....|....*....|
gi 1124469102 465 --VFVDRIatdrLYIGDGKI 482
Cdd:COG2274 672 tiRLADRI----IVLDKGRI 687
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
169-278 |
2.66e-17 |
|
ABC transporter; This domain is an extension of some members of pfam00005 and other ABC-transporter families.
Pssm-ID: 463731 [Multi-domain] Cd Length: 85 Bit Score: 76.46 E-value: 2.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 169 VEISFGKLQNYSGNYDEYVVQKEEQRKTQQAEYENYQAEKKRLQSvYVEK-KAKAKTvdkkpknmsASEAKVRafignrk 247
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEE-FIDRfRAKASK---------AKQAQSR------- 63
|
90 100 110
....*....|....*....|....*....|.
gi 1124469102 248 pedkargiersatnvLKRLEHMEIKEKPKEE 278
Cdd:pfam12848 64 ---------------IKALEKMERIEKPERD 79
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
297-482 |
4.54e-17 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 80.30 E-value: 4.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREKVYvvPGAKI-GYARQNMSQIDLSQTVLVN 375
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLI--PGAPDeGEVLLDGKDIYDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 376 VRR-------------VSIQ--------------SESISRIV---LARLLLSERDMNK-KASELSGGERMKLSFAMLFVS 424
Cdd:cd03260 79 LRRrvgmvfqkpnpfpGSIYdnvayglrlhgiklKEELDERVeeaLRKAALWDEVKDRlHALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 425 DVNLLILDEPTNYLDIPSVEALEKMLVEY--EGTLIFTSHDKVFVDRIATDRLYIGDGKI 482
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELkkEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-177 |
5.32e-17 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 80.54 E-value: 5.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVS--------------------- 64
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRlngrplaawspwelarrravl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 65 --SNCIPFFF----------EQFGSDSEYFETDYAEA----GKMGVADHIWQEnVSGGEDTRIRLA----QLFSSPHAVA 124
Cdd:COG4559 81 pqHSSLAFPFtveevvalgrAPHGSSAAQDRQIVREAlalvGLAHLAGRSYQT-LSGGEQQRVQLArvlaQLWEPVDGGP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1124469102 125 ---FLDEPTSNLD----YNGVEMLKKRLNEIETLVVISHDrsvLN---EICDRIVEISFGKLQ 177
Cdd:COG4559 160 rwlFLDEPTSALDlahqHAVLRLARQLARRGGGVVAVLHD---LNlaaQYADRILLLHQGRLV 219
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
305-463 |
8.94e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 78.43 E-value: 8.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 305 AYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREK-----VYVVPGAKIGYARQNMSQID-LSQTV--LVNV 376
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRptsgtVRRAGGARVAYVPQRSEVPDsLPLTVrdLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 377 ---------RRVSIQ-----SESISRIVLARLLlserdmNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIPS 442
Cdd:NF040873 81 grwarrglwRRLTRDdraavDDALERVGLADLA------GRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180
....*....|....*....|....
gi 1124469102 443 VEALEKMLVEYEG---TLIFTSHD 463
Cdd:NF040873 155 RERIIALLAEEHArgaTVVVVTHD 178
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
306-482 |
1.05e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 79.30 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 306 YDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELI-------NNREKVY-VVPG-------AKIGYARQNMSQI--DL 368
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILsgllqptSGEVRVAgLVPWkrrkkflRRIGVVFGQKTQLwwDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 369 S--QTVLVNVRRVSIQSESISRIV--LARLLLSERDMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIPSVE 444
Cdd:cd03267 111 PviDSFYLLAAIYDLPPARFKKRLdeLSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQE 190
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1124469102 445 ALEKMLVEY----EGTLIFTSHDKVFVDRIATDRLYIGDGKI 482
Cdd:cd03267 191 NIRNFLKEYnrerGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
7-169 |
1.95e-16 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 81.56 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSY-GEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPFffEQFGSDSEY---- 81
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPL--ADADADSWRdqia 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 82 --------FETDYAEA---GKMGVADHIWQENV---------------------------SGGEDTRIRLAQLFSSPHAV 123
Cdd:TIGR02857 400 wvpqhpflFAGTIAENirlARPDASDAEIREALeragldefvaalpqgldtpigeggaglSGGQAQRLALARAFLRDAPL 479
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1124469102 124 AFLDEPTSNLDYNGVEMLKKRLNEI---ETLVVISHDRSVLnEICDRIV 169
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALRALaqgRTVLLVTHRLALA-ALADRIV 527
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
297-483 |
2.69e-16 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 77.26 E-value: 2.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELI------------------NNREKVYVVPGAKIGY 358
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIIlglikpdsgeitfdgksyQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 359 --------ARQNmsqidlsqtvLVNVRRVSIQSESISRIVLARLLLSERDmNKKASELSGGERMKLSFAMLFVSDVNLLI 430
Cdd:cd03268 81 pgfypnltAREN----------LRLLARLLGIRKKRIDEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1124469102 431 LDEPTNYLD---IPSVEALEKMLVEYEGTLIFTSHDKVFVDRIATDRLYIGDGKIR 483
Cdd:cd03268 150 LDEPTNGLDpdgIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-177 |
2.78e-16 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 77.56 E-value: 2.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSN-----CIP-------FFFEq 74
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDgrdvtGVPperrnigMVFQ- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 75 fgsdseyfetDYAEAGKMGVADHI-------------WQENV--------------------SGGEDTRIRLAQ-LFSSP 120
Cdd:cd03259 80 ----------DYALFPHLTVAENIafglklrgvpkaeIRARVrellelvglegllnryphelSGGQQQRVALARaLAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1124469102 121 hAVAFLDEPTSNLDYNGVEMLKKRLNEIE-----TLVVISHDRSVLNEICDRIVEISFGKLQ 177
Cdd:cd03259 150 -SLLLLDEPLSALDAKLREELREELKELQrelgiTTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
9-145 |
3.38e-16 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 77.01 E-value: 3.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 9 AENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIP------------------- 69
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPlaeqrdephenilylghlp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 70 -------------FFFEQFGSDSEYFETDYAEAGKMGVADHIWQEnVSGGEDTRIRLAQLFSSPHAVAFLDEPTSNLDYN 136
Cdd:TIGR01189 83 glkpelsalenlhFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQ-LSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
....*....
gi 1124469102 137 GVEMLKKRL 145
Cdd:TIGR01189 162 GVALLAGLL 170
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
297-481 |
4.14e-16 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 76.07 E-value: 4.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREKVyvvPGAKIGYARQNMSqiDLSQTVLVNV 376
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEP---DSGSILIDGEDLT--DLEDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 377 RRVSI---QSESISRI-VLARLLLSerdmnkkaseLSGGERMKLSFAMLFVSDVNLLILDEPTNYLD---IPSVEALEKM 449
Cdd:cd03229 76 RRIGMvfqDFALFPHLtVLENIALG----------LSGGQQQRVALARALAMDPDVLLLDEPTSALDpitRREVRALLKS 145
|
170 180 190
....*....|....*....|....*....|...
gi 1124469102 450 LVEYEG-TLIFTSHDKVFVDRIATDRLYIGDGK 481
Cdd:cd03229 146 LQAQLGiTVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
302-482 |
4.23e-16 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 77.24 E-value: 4.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 302 ISFAYDDHVI--FDDADFMIKNGSKVALLGGNGAGKTTLLELInnrEKVYVVPGAKIGYARQNMSQID----------LS 369
Cdd:cd03245 8 VSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLL---AGLYKPTSGSVLLDGTDIRQLDpadlrrnigyVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 370 QTVL---------VNVRRVSIQSESISRIV-------LAR-------LLLSERDMNkkaseLSGGERMKLSFAMLFVSDV 426
Cdd:cd03245 85 QDVTlfygtlrdnITLGAPLADDERILRAAelagvtdFVNkhpngldLQIGERGRG-----LSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1124469102 427 NLLILDEPTNYLDIPSVEALEKMLVEYEG--TLIFTSHDKVF---VDRIatdrLYIGDGKI 482
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLldlVDRI----IVMDSGRI 216
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
27-131 |
4.44e-16 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 75.38 E-value: 4.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 27 FYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPFFFEQ----------------------------FGSD 78
Cdd:pfam00005 6 LTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDErkslrkeigyvfqdpqlfprltvrenlrLGLL 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1124469102 79 SEYFETDYAEA---------GKMGVADHIWQENV---SGGEDTRIRLAQLFSSPHAVAFLDEPTS 131
Cdd:pfam00005 86 LKGLSKREKDAraeealeklGLGDLADRPVGERPgtlSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
7-185 |
5.80e-16 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 76.77 E-value: 5.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYG--EQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTV--------------------- 63
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyingysirtdrkaarqslgyc 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 64 -SSNCIP---------FFFEQF--GSDSEYFETDYAEAGKMGVADHIWQE--NVSGGEDTRIRLAQLFSSPHAVAFLDEP 129
Cdd:cd03263 81 pQFDALFdeltvrehlRFYARLkgLPKSEIKEEVELLLRVLGLTDKANKRarTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1124469102 130 TSNLDYNGVEMLKKRLNEIE---TLVVISHDRSVLNEICDRIVEISFGKLQnYSGNYDE 185
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRkgrSIILTTHSMDEAEALCDRIAIMSDGKLR-CIGSPQE 218
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
290-483 |
5.80e-16 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 80.20 E-value: 5.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 290 PPRNPIVIRGEHISFAYDD--HVIFDDADFMIKNGSKVALLGGNGAGKTTLLEL-------------INNREkVYVVPGA 354
Cdd:COG4987 327 PAPGGPSLELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALllrfldpqsgsitLGGVD-LRDLDED 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 355 KIgyaRQNMS----QIDL-SQTVLVNVRrvsiqsesisrivLARLLLSERDMNK------------------------KA 405
Cdd:COG4987 406 DL---RRRIAvvpqRPHLfDTTLRENLR-------------LARPDATDEELWAalervglgdwlaalpdgldtwlgeGG 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 406 SELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIPSVEALEKMLVEY--EGTLIFTSHDKVFVDRIatDRLY-IGDGKI 482
Cdd:COG4987 470 RRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAlaGRTVLLITHRLAGLERM--DRILvLEDGRI 547
|
.
gi 1124469102 483 R 483
Cdd:COG4987 548 V 548
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
306-482 |
5.92e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 77.06 E-value: 5.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 306 YDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREKV----YVVPGAKIGYARQNMSQIDLSQ----------- 370
Cdd:PRK09493 11 FGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEItsgdLIVDGLKVNDPKVDERLIRQEAgmvfqqfylfp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 371 --TVLVNV----RRV----SIQSESISRIVLARLLLSERdMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDi 440
Cdd:PRK09493 91 hlTALENVmfgpLRVrgasKEEAEKQARELLAKVGLAER-AHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALD- 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1124469102 441 PSV--EALEKM--LVEyEG-TLIFTSHDKVFVDRIATDRLYIGDGKI 482
Cdd:PRK09493 169 PELrhEVLKVMqdLAE-EGmTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-176 |
5.99e-16 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 77.15 E-value: 5.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSYGE----QTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPFFFEQfgsDSEY 81
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRR---RKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 82 FET------DY--------------AEAGK-MGVADH---IWQ--ENV--------------SGGEDTRIRLAQ-LFSSP 120
Cdd:COG1124 78 RRRvqmvfqDPyaslhprhtvdrilAEPLRiHGLPDReerIAEllEQVglppsfldryphqlSGGQRQRVAIARaLILEP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1124469102 121 hAVAFLDEPTSNLD-YNGVEMLK--KRLNEIE--TLVVISHDRSVLNEICDRIVEISFGKL 176
Cdd:COG1124 158 -ELLLLDEPTSALDvSVQAEILNllKDLREERglTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
298-482 |
6.95e-16 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 76.14 E-value: 6.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 298 RGEHISFAYDDHV-IFDDADFMIKNGSKVALLGGNGAGKTTLLELI-------------NNREKVYVVPGAKIGYARQNM 363
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILaglikessgsillNGKPIKAKERRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 364 SQIDLSQTVLVNVRRVS-IQSESISRI--VLARLLLSERdMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDI 440
Cdd:cd03226 81 DYQLFTDSVREELLLGLkELDAGNEQAetVLKDLDLYAL-KERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDY 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1124469102 441 PSVEALEKMLVEY--EGTLIFT-SHDKVFVDRIATDRLYIGDGKI 482
Cdd:cd03226 160 KNMERVGELIRELaaQGKAVIViTHDYEFLAKVCDRVLLLANGAI 204
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
293-482 |
7.88e-16 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 76.94 E-value: 7.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 293 NPIVIRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELI--------------------NNREKVYVVP 352
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIigllrpdsgeilvdgqditgLSEKELYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 353 gAKIGYARQNMSQIDlSQTVLVNV----RRVSIQSES-ISRIVLARLLLSE-RDM-NKKASELSGGERMKLSFAMLFVSD 425
Cdd:COG1127 82 -RRIGMLFQGGALFD-SLTVFENVafplREHTDLSEAeIRELVLEKLELVGlPGAaDKMPSELSGGMRKRVALARALALD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1124469102 426 VNLLILDEPTNYLDIPSVEALEKMLVE----YEGTLIFTSHDKVFVDRIAtDRLY-IGDGKI 482
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRElrdeLGLTSVVVTHDLDSAFAIA-DRVAvLADGKI 220
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
7-176 |
8.10e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 79.12 E-value: 8.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPF-------FFEQFGS-- 77
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVealsaraASRRVASvp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 78 --DSEYFETDYAEAGKMGVADHI-----WQE------------------------NVSGGEDTRIRLAQLFSSPHAVAFL 126
Cdd:PRK09536 84 qdTSLSFEFDVRQVVEMGRTPHRsrfdtWTEtdraaveramertgvaqfadrpvtSLSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1124469102 127 DEPTSNLDYN----GVEMLKKRLNEIETLVVISHDRSVLNEICDRIVEISFGKL 176
Cdd:PRK09536 164 DEPTASLDINhqvrTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-195 |
1.06e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 79.39 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVS-------SncipfFFEQF--GS 77
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKigetvklA-----YVDQSrdAL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 78 DSE--YFE-----TDYAEAGKMGV-------------ADHiwQENV---SGGEDTRIRLAQLFSSPHAVAFLDEPTSNLD 134
Cdd:PRK11819 400 DPNktVWEeisggLDIIKVGNREIpsrayvgrfnfkgGDQ--QKKVgvlSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1124469102 135 yngVEMLKKRLNEIE----TLVVISHDRSVLNEICDRIveISF---GKLQNYSGNYDEYvvqkEEQRK 195
Cdd:PRK11819 478 ---VETLRALEEALLefpgCAVVISHDRWFLDRIATHI--LAFegdSQVEWFEGNFQEY----EEDKK 536
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
7-185 |
1.16e-15 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 79.42 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSY-GEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCI----------------- 68
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsdldpaswrrqiawv 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 69 ---PFFFE-------QFG----SDSEY-------------------FETDYAEAGKmgvadhiwqeNVSGGEDTRIRLAQ 115
Cdd:COG4988 417 pqnPYLFAgtirenlRLGrpdaSDEELeaaleaagldefvaalpdgLDTPLGEGGR----------GLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1124469102 116 LFSSPHAVAFLDEPTSNLDYNGVEMLKKRLNEI---ETLVVISHDRSVLNEiCDRIVEISFGKLQNySGNYDE 185
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLakgRTVILITHRLALLAQ-ADRILVLDDGRIVE-QGTHEE 557
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
300-483 |
1.24e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 77.46 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 300 EHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNR------------EKVYVVPGAKIGY---AR---Q 361
Cdd:COG4152 5 KGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGIlapdsgevlwdgEPLDPEDRRRIGYlpeERglyP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 362 NMSQID----LSQtvLVNVRRvsiqSESISRI--VLARLLLSERdMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPT 435
Cdd:COG4152 85 KMKVGEqlvyLAR--LKGLSK----AEAKRRAdeWLERLGLGDR-ANKKVEELSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1124469102 436 NYLDIPSVEALEKMLVEY--EG-TLIFTSHDKVFVDRIAtDRLY-IGDGKIR 483
Cdd:COG4152 158 SGLDPVNVELLKDVIRELaaKGtTVIFSSHQMELVEELC-DRIViINKGRKV 208
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
15-209 |
1.37e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 76.27 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 15 SYGEQTVLD---FDrfyLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNC-IPFFFEqFGS--DSE-------Y 81
Cdd:COG1134 35 RREEFWALKdvsFE---VERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGrVSALLE-LGAgfHPEltgreniY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 82 F----------ETDYAEagkmgvaDHIwqENVSG-GE--DT---------RIRLAqlFSSphAVAF------LDEPTSnl 133
Cdd:COG1134 111 LngrllglsrkEIDEKF-------DEI--VEFAElGDfiDQpvktyssgmRARLA--FAV--ATAVdpdillVDEVLA-- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 134 dyngV----------EMLKKRLNEIETLVVISHDRSVLNEICDRIVEISFGKLQnYSGNYDEyVVqkeeqrktqqAEYEN 203
Cdd:COG1134 176 ----VgdaafqkkclARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLV-MDGDPEE-VI----------AAYEA 239
|
....*.
gi 1124469102 204 YQAEKK 209
Cdd:COG1134 240 LLAGRE 245
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-176 |
1.84e-15 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 75.62 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSsncipFFFEQFGSDSEyfETDY 86
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVL-----IDGEDISGLSE--AELY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 87 AEAGKMGV-----------------------------------------------ADHIWQENVSGGEDTRIRLAQlfss 119
Cdd:cd03261 74 RLRRRMGMlfqsgalfdsltvfenvafplrehtrlseeeireivlekleavglrgAEDLYPAELSGGMKKRVALAR---- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1124469102 120 phAVA------FLDEPTSNLD---YNGVEMLKKRLNEIE--TLVVISHDRSVLNEICDRIVEISFGKL 176
Cdd:cd03261 150 --ALAldpellLYDEPTAGLDpiaSGVIDDLIRSLKKELglTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
297-483 |
2.11e-15 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 75.10 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDD----HVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINN-----------------------REKVY 349
Cdd:cd03266 2 ITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGllepdagfatvdgfdvvkepaeaRRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 350 VVPGAKIGYARQNMSQIDLSQTVLVNVRRvsiqSESISRI-VLARLLLSERDMNKKASELSGGERMKLSFAMLFVSDVNL 428
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKG----DELTARLeELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1124469102 429 LILDEPTNYLDIPSVEALEKMLVEY--EG-TLIFTSHDKVFVDRIATDRLYIGDGKIR 483
Cdd:cd03266 158 LLLDEPTTGLDVMATRALREFIRQLraLGkCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
297-467 |
2.18e-15 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 75.34 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDDHV-IFDDADFMIKNGSKVALLGGNGAGKTTLLEL-------------INN-----------REKVYVV 351
Cdd:cd03253 1 IEFENVTFAYDPGRpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLlfrfydvssgsilIDGqdirevtldslRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 352 P----------GAKIGYARQNMSQIDlsqtvLVNVRRVSIQSESISRIVLA-RLLLSERDMnkkasELSGGERMKLSFAM 420
Cdd:cd03253 81 PqdtvlfndtiGYNIRYGRPDATDEE-----VIEAAKAAQIHDKIMRFPDGyDTIVGERGL-----KLSGGEKQRVAIAR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1124469102 421 LFVSDVNLLILDEPTNYLDIPSVEALEKMLVEYEG--TLIFTSH--------DKVFV 467
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDVSKgrTTIVIAHrlstivnaDKIIV 207
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
6-177 |
2.34e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 75.96 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVS--------------------- 64
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRlngrpladwspaelarrravl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 65 --SNCIPFFF--------------EQFGSDSEYFETDYAEAGKMGVADHIWQEnVSGGEDTRIRLA----QLFSSPHA-- 122
Cdd:PRK13548 82 pqHSSLSFPFtveevvamgraphgLSRAEDDALVAAALAQVDLAHLAGRDYPQ-LSGGEQQRVQLArvlaQLWEPDGPpr 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1124469102 123 VAFLDEPTSNLDyngvemLKKRLNEIETL-----------VVISHDrsvLN---EICDRIVEISFGKLQ 177
Cdd:PRK13548 161 WLLLDEPTSALD------LAHQHHVLRLArqlaherglavIVVLHD---LNlaaRYADRIVLLHQGRLV 220
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
2-179 |
2.86e-15 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 78.16 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 2 ERHLLIKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPFF---FEQFG-- 76
Cdd:TIGR01842 314 EGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKqwdRETFGkh 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 77 -----SDSEYFE----------TDYAEAGKM-------GVADHIWQ-------------ENVSGGEDTRIRLAQ-LFSSP 120
Cdd:TIGR01842 394 igylpQDVELFPgtvaeniarfGENADPEKIieaaklaGVHELILRlpdgydtvigpggATLSGGQRQRIALARaLYGDP 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1124469102 121 HAVaFLDEPTSNLDYNGVEMLKKRLNEIE----TLVVISHDRSVLNEIcDRIVEISFGKLQNY 179
Cdd:TIGR01842 474 KLV-VLDEPNSNLDEEGEQALANAIKALKargiTVVVITHRPSLLGCV-DKILVLQDGRIARF 534
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
294-482 |
3.34e-15 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 74.69 E-value: 3.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 294 PIVIRGEHISFAYDD----HVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREKV----YVVPGAKIGyarqNMSQ 365
Cdd:COG1136 2 SPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPtsgeVLIDGQDIS----SLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 366 IDLSQ-------------------TVLVNV------RRVSiQSESISRI--VLARLLLSERdMNKKASELSGGERMKLSF 418
Cdd:COG1136 78 RELARlrrrhigfvfqffnllpelTALENValplllAGVS-RKERRERAreLLERVGLGDR-LDHRPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1124469102 419 AMLFVSDVNLLILDEPTNYLDIPS----VEALEKMLVEYEGTLIFTSHDKvFVDRIATDRLYIGDGKI 482
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRI 222
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
27-176 |
4.84e-15 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 73.35 E-value: 4.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 27 FYLYEGEKVGLVGMNGAGKSTLLKILAGELEP--TKGTVSSNCIPFFFEQFGSDSEYFETD--------YAEAgkMGVAD 96
Cdd:cd03213 30 GKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSFRKIIGYVPQDdilhptltVRET--LMFAA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 97 HIwqENVSGGEDTRIRLA-QLFSSPHaVAFLDEPTSNLD----YNGVEMLKKRLNEIETLVVISHD-RSVLNEICDRIVE 170
Cdd:cd03213 108 KL--RGLSGGERKRVSIAlELVSNPS-LLFLDEPTSGLDsssaLQVMSLLRRLADTGRTIICSIHQpSSEIFELFDKLLL 184
|
....*.
gi 1124469102 171 ISFGKL 176
Cdd:cd03213 185 LSQGRV 190
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-176 |
5.79e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 77.15 E-value: 5.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSY-----GEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTV----------------- 63
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmtkpgpd 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 64 ----SSNCIPFFFEQFG-----------SDS-------EY-------------FETDYAEAgkmgVADHIWQEnVSGGED 108
Cdd:TIGR03269 359 grgrAKRYIGILHQEYDlyphrtvldnlTEAiglelpdELarmkavitlkmvgFDEEKAEE----ILDKYPDE-LSEGER 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1124469102 109 TRIRLAQ-LFSSPHAVaFLDEPTSNLD---YNGV--EMLKKRLNEIETLVVISHDRSVLNEICDRIVEISFGKL 176
Cdd:TIGR03269 434 HRVALAQvLIKEPRIV-ILDEPTGTMDpitKVDVthSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-169 |
5.92e-15 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 77.13 E-value: 5.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 2 ERHLLIKAENIVHSYGEQTvLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSN--------------- 66
Cdd:COG1245 337 EEETLVEYPDLTKSYGGFS-LEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkisykpqyispdyd 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 67 --CIPFFFEQFGS--DSEYFETDYAEagKMGVaDHIWQENV---SGGEDTRIRLAQLFSSPHAVAFLDEPTSNLDYNG-V 138
Cdd:COG1245 416 gtVEEFLRSANTDdfGSSYYKTEIIK--PLGL-EKLLDKNVkdlSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQrL 492
|
170 180 190
....*....|....*....|....*....|....*
gi 1124469102 139 EMLK--KRLNEIE--TLVVISHDRSVLNEICDRIV 169
Cdd:COG1245 493 AVAKaiRRFAENRgkTAMVVDHDIYLIDYISDRLM 527
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
288-482 |
6.91e-15 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 77.11 E-value: 6.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 288 TNPPRNPIVIRGEHISFAYDD-HVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREKVY----VVPG--------- 353
Cdd:COG4988 328 PLPAAGPPSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYsgsiLINGvdlsdldpa 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 354 ---AKIGYARQNmSQIdLSQTVLVNVR--RVSIQSESISRI--------VLARL------LLSERdmnkkASELSGGERM 414
Cdd:COG4988 408 swrRQIAWVPQN-PYL-FAGTIRENLRlgRPDASDEELEAAleaagldeFVAALpdgldtPLGEG-----GRGLSGGQAQ 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1124469102 415 KLSFAMLFVSDVNLLILDEPTNYLDIPS----VEALEKMLveyEG-TLIFTSHD---KVFVDRIatdrLYIGDGKI 482
Cdd:COG4988 481 RLALARALLRDAPLLLLDEPTAHLDAETeaeiLQALRRLA---KGrTVILITHRlalLAQADRI----LVLDDGRI 549
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-175 |
9.47e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 73.08 E-value: 9.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPFFFE---QFGSDSE--- 80
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAarnRIGYLPEerg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 81 ------------YFE--------------TDYAEagKMGVADHIWQ--ENVSGGEDTRIRL-AQLFSSPhAVAFLDEPTS 131
Cdd:cd03269 81 lypkmkvidqlvYLAqlkglkkeearrriDEWLE--RLELSEYANKrvEELSKGNQQKVQFiAAVIHDP-ELLILDEPFS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1124469102 132 NLDYNGVEMLKKRLNEIE----TLVVISHDRSVLNEICDRIVEISFGK 175
Cdd:cd03269 158 GLDPVNVELLKDVIRELAragkTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
9-145 |
9.90e-15 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 72.91 E-value: 9.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 9 AENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPF------------------ 70
Cdd:cd03231 3 ADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLdfqrdsiargllylghap 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 71 -------------FFEQFGSDSEYFETdYAEAGKMGVaDHIWQENVSGGEDTRIRLAQLFSSPHAVAFLDEPTSNLDYNG 137
Cdd:cd03231 83 gikttlsvlenlrFWHADHSDEQVEEA-LARVGLNGF-EDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
....*...
gi 1124469102 138 VEMLKKRL 145
Cdd:cd03231 161 VARFAEAM 168
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
300-476 |
1.05e-14 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 73.63 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 300 EHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELIN-----------------NREKVYVVpgAKIGYAR-- 360
Cdd:cd03219 4 RGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISgflrptsgsvlfdgediTGLPPHEI--ARLGIGRtf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 361 QNmSQIDLSQTVLVNVRrVSIQSESISRIVLARLLLSERDMNKK-----------------ASELSGGERMKLSFAMLFV 423
Cdd:cd03219 82 QI-PRLFPELTVLENVM-VAAQARTGSGLLLARARREEREARERaeellervgladladrpAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1124469102 424 SDVNLLILDEPTNYLDIPSVEALEKMLVE--YEG-TLIFTSHDKVFVDRIAtDRLY 476
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRElrERGiTVLLVEHDMDVVMSLA-DRVT 214
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
296-482 |
1.13e-14 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 73.16 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 296 VIRGEHISFAY-DDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREK-----VYV-------VPGAKIGYARQN 362
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERptsgqVLVngqdlsrLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 363 MSQI--------DLsqTVLVNVR---RVSIQSESI--SRI--VLARLLLSERdMNKKASELSGGERMKLSFAMLFVSDVN 427
Cdd:COG2884 81 IGVVfqdfrllpDR--TVYENVAlplRVTGKSRKEirRRVreVLDLVGLSDK-AKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1124469102 428 LLILDEPTNYLDIPSVEALEKMLVEY--EG-TLIFTSHDKVFVDRIATDRLYIGDGKI 482
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEInrRGtTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
6-185 |
1.24e-14 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 73.48 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSYGEQTVL-DFDrFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVssncipFFFEQ-FGSDSEyfE 83
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLdGVS-LDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEI------LVDGQdITGLSE--K 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 84 TDYAEAGKMGVadhIWQ-----------ENV---------------------------------------SGGEDTRIRL 113
Cdd:COG1127 76 ELYELRRRIGM---LFQggalfdsltvfENVafplrehtdlseaeirelvleklelvglpgaadkmpselSGGMRKRVAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 114 AQlfssphAVA------FLDEPTSNLDYNGVEM-------LKKRLNeiETLVVISHDRSVLNEICDRIVEISFGKLQnYS 180
Cdd:COG1127 153 AR------ALAldpeilLYDEPTAGLDPITSAVidelireLRDELG--LTSVVVTHDLDSAFAIADRVAVLADGKII-AE 223
|
....*
gi 1124469102 181 GNYDE 185
Cdd:COG1127 224 GTPEE 228
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
314-483 |
1.77e-14 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 72.33 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 314 DADFMIkNGSKVALLGGNGAGKTTLLELINNREKVY----VVPGA----------------KIGYARQNMS---QIDLSQ 370
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDggtiVLNGTvlfdsrkkinlppqqrKIGLVFQQYAlfpHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 371 TVLVNVRRVSIQSESIS-RIVLARLLLSERdMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIPSVEA---- 445
Cdd:cd03297 95 NLAFGLKRKRNREDRISvDELLDLLGLDHL-LNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQllpe 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 1124469102 446 LEKMLVEYEGTLIFTSHDKVFVDRIATDRLYIGDGKIR 483
Cdd:cd03297 174 LKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-169 |
2.30e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 75.23 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 2 ERHLLIKAENIVHSYGEQTvLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNC-------------- 67
Cdd:PRK13409 336 ERETLVEYPDLTKKLGDFS-LEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELkisykpqyikpdyd 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 68 --IPFFFEQFGS--DSEYFETDYAEagKMGVaDHIWQENV---SGGEDTRIRLAQLFSSPHAVAFLDEPTSNLDyngVE- 139
Cdd:PRK13409 415 gtVEDLLRSITDdlGSSYYKSEIIK--PLQL-ERLLDKNVkdlSGGELQRVAIAACLSRDADLYLLDEPSAHLD---VEq 488
|
170 180 190
....*....|....*....|....*....|....*..
gi 1124469102 140 ------MLKKRLNEIE-TLVVISHDRSVLNEICDRIV 169
Cdd:PRK13409 489 rlavakAIRRIAEEREaTALVVDHDIYMIDYISDRLM 525
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
7-177 |
2.38e-14 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 72.01 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSY-GEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTV----------SSNCIPFF---- 71
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVlvngqdlsrlKRREIPYLrrri 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 72 ---FEQF-------------------GSDSEYFETDYAEA-GKMGVADHIWQ--ENVSGGEDTRIRLAQ-LFSSPhAVAF 125
Cdd:COG2884 82 gvvFQDFrllpdrtvyenvalplrvtGKSRKEIRRRVREVlDLVGLSDKAKAlpHELSGGEQQRVAIARaLVNRP-ELLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1124469102 126 LDEPTSNLD-YNGVEMLK--KRLNEIETLVVI-SHDRSVLNEICDRIVEISFGKLQ 177
Cdd:COG2884 161 ADEPTGNLDpETSWEIMEllEEINRRGTTVLIaTHDLELVDRMPKRVLELEDGRLV 216
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
276-482 |
2.48e-14 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 75.20 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 276 KEELTVRPDFRLTNPPRNPIVIrgEHISFAYD-DHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINnreKVYVVPGA 354
Cdd:COG1132 321 PPEIPDPPGAVPLPPVRGEIEF--ENVSFSYPgDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLL---RFYDPTSG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 355 KIGYARQNMSQIDLSQ-----------------TVLVNVR--RVSIQSESISRI--------VLARL------LLSERDM 401
Cdd:COG1132 396 RILIDGVDIRDLTLESlrrqigvvpqdtflfsgTIRENIRygRPDATDEEVEEAakaaqaheFIEALpdgydtVVGERGV 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 402 NkkaseLSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIPS----VEALEKMLveyEG-TLIFTSHdkvfvdRIAT---- 472
Cdd:COG1132 476 N-----LSGGQRQRIAIARALLKDPPILILDEATSALDTETealiQEALERLM---KGrTTIVIAH------RLSTirna 541
|
250
....*....|.
gi 1124469102 473 DR-LYIGDGKI 482
Cdd:COG1132 542 DRiLVLDDGRI 552
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
287-470 |
3.08e-14 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 75.02 E-value: 3.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 287 LTNPPRNPIVIRGehISFAYDDH-VIFDDADFMIKNGSKVALLGGNGAGKTTLLEL-------------INNREKVYVVP 352
Cdd:TIGR02857 314 VTAAPASSLEFSG--VSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLllgfvdptegsiaVNGVPLADADA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 353 ---GAKIGYARQNmSQIdLSQTVLVNVR-------RVSIQsESISRIVLARLLLSERDM-----NKKASELSGGERMKLS 417
Cdd:TIGR02857 392 dswRDQIAWVPQH-PFL-FAGTIAENIRlarpdasDAEIR-EALERAGLDEFVAALPQGldtpiGEGGAGLSGGQAQRLA 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1124469102 418 FAMLFVSDVNLLILDEPTNYLDIPSVEALEKMLVEYEG--TLIFTSHDKVFV---DRI 470
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRLALAalaDRI 526
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
27-141 |
3.16e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.44 E-value: 3.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 27 FYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPFFFEQFGSDSEY------------------------- 81
Cdd:PRK13539 23 FTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYlghrnamkpaltvaenlefwaaflg 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1124469102 82 -FETDYAEAGK-MGVAD--HIWQENVSGGEDTRIRLAQLFSSPHAVAFLDEPTSNLDYNGVEML 141
Cdd:PRK13539 103 gEELDIAAALEaVGLAPlaHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALF 166
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-176 |
3.85e-14 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 71.63 E-value: 3.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSN-------------CIPFFFE 73
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAghdvvreprevrrRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 74 QFGSDSEY--FETDYAEAGKMGVADHIWQENV--------------------SGGEDTRIRLAQ-LFSSPHaVAFLDEPT 130
Cdd:cd03265 81 DLSVDDELtgWENLYIHARLYGVPGAERRERIdelldfvglleaadrlvktySGGMRRRLEIARsLVHRPE-VLFLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1124469102 131 SNLD-------YNGVEMLKKRLNeiETLVVISHDRSVLNEICDRIVEISFGKL 176
Cdd:cd03265 160 IGLDpqtrahvWEYIEKLKEEFG--MTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
34-186 |
4.00e-14 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 74.90 E-value: 4.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 34 KVGLVGMNGAGKSTLLKILAGELEPTKGTV---------------------SSN-------CIPFFFEQfgsdseyfeTD 85
Cdd:PLN03073 537 RIAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmavfsqhhvdgldlSSNpllymmrCFPGVPEQ---------KL 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 86 YAEAGKMGVADHIWQE---NVSGGEDTRIRLAQL-FSSPHaVAFLDEPTSNLDYNGVEMLKKRLNEIE-TLVVISHDRSV 160
Cdd:PLN03073 608 RAHLGSFGVTGNLALQpmyTLSGGQKSRVAFAKItFKKPH-ILLLDEPSNHLDLDAVEALIQGLVLFQgGVLMVSHDEHL 686
|
170 180
....*....|....*....|....*.
gi 1124469102 161 LNEICDRIVEISFGKLQNYSGNYDEY 186
Cdd:PLN03073 687 ISGSVDELWVVSEGKVTPFHGTFHDY 712
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-176 |
4.51e-14 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 71.09 E-value: 4.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVssncipfffEQFGSDseyFETDY 86
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEI---------TFDGKS---YQKNI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 87 AEAGKMG--VADHIWQENVSGGEDTRIrLAQLFSSPH---------------------------------AVAF------ 125
Cdd:cd03268 69 EALRRIGalIEAPGFYPNLTARENLRL-LARLLGIRKkridevldvvglkdsakkkvkgfslgmkqrlgiALALlgnpdl 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1124469102 126 --LDEPTSNLDYNGVEMLKK---RLNEIETLVVI-SHDRSVLNEICDRIVEISFGKL 176
Cdd:cd03268 148 liLDEPTNGLDPDGIKELRElilSLRDQGITVLIsSHLLSEIQKVADRIGIINKGKL 204
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
7-197 |
4.82e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 72.33 E-value: 4.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQT--VLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKG-------TVSSNCIPFFFEQFG- 76
Cdd:PRK13632 8 IKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGeikidgiTISKENLKEIRKKIGi 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 77 ----SDSEYF----ETDYA-------------------EAGKMGVADHIWQE--NVSGGEDTRIRLAQLFSSPHAVAFLD 127
Cdd:PRK13632 88 ifqnPDNQFIgatvEDDIAfglenkkvppkkmkdiiddLAKKVGMEDYLDKEpqNLSGGQKQRVAIASVLALNPEIIIFD 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1124469102 128 EPTSNLDYNGVEMLKKRLNEI-----ETLVVISHDrsvLNEI--CDRIVEISFGKLQnYSGNYDEYVVQKEEQRKTQ 197
Cdd:PRK13632 168 ESTSMLDPKGKREIKKIMVDLrktrkKTLISITHD---MDEAilADKVIVFSEGKLI-AQGKPKEILNNKEILEKAK 240
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
297-482 |
5.36e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 71.32 E-value: 5.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDDHVIfdDADFMIKNGSKVALLGGNGAGKTTLLELINNrekvYVVPGA-KIGYARQNMSQID-------- 367
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAG----FLPPDSgRILWNGQDLTALPpaerpvsm 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 368 LSQ--------TVLVNV--------RRVSIQSESISRIvLARLLLSERdMNKKASELSGGERMKLSFAMLFVSDVNLLIL 431
Cdd:COG3840 76 LFQennlfphlTVAQNIglglrpglKLTAEQRAQVEQA-LERVGLAGL-LDRLPGQLSGGQRQRVALARCLVRKRPILLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1124469102 432 DEPTNYLDIpsveAL-EKMLV-------EYEGTLIFTSHDKVFVDRIATDRLYIGDGKI 482
Cdd:COG3840 154 DEPFSALDP----ALrQEMLDlvdelcrERGLTVLMVTHDPEDAARIADRVLLVADGRI 208
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
297-483 |
5.82e-14 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 70.75 E-value: 5.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNRE-----KVYV-------VPGAK--IGYARQN 362
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEeptsgRIYIggrdvtdLPPKDrdIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 363 MSqIDLSQTVLVN------VRRVSiqSESISRIVL--ARLLLSERDMNKKASELSGGERMKLSFAMLFVSDVNLLILDEP 434
Cdd:cd03301 81 YA-LYPHMTVYDNiafglkLRKVP--KDEIDERVRevAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1124469102 435 TNYLD----IPSVEALEKMLVEYEGTLIFTSHDKV----FVDRIATdrlyIGDGKIR 483
Cdd:cd03301 158 LSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQVeamtMADRIAV----MNDGQIQ 210
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
259-475 |
6.47e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 72.94 E-value: 6.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 259 ATNVLKRLEHMEIKEKPKEELTVrpdfrLTNPPRN--PIVIRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKT 336
Cdd:PRK13536 7 AEEAPRRLELSPIERKHQGISEA-----KASIPGSmsTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 337 TLLELI-----NNREKVYV----VPG------AKIGYARQnMSQIDLSQTV----LVNVRRVSIQSESISRIV-----LA 392
Cdd:PRK13536 82 TIARMIlgmtsPDAGKITVlgvpVPArarlarARIGVVPQ-FDNLDLEFTVrenlLVFGRYFGMSTREIEAVIpslleFA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 393 RLllsERDMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDiPSVEAL--EKM--LVEYEGTLIFTSHDKVFVD 468
Cdd:PRK13536 161 RL---ESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD-PHARHLiwERLrsLLARGKTILLTTHFMEEAE 236
|
....*..
gi 1124469102 469 RIAtDRL 475
Cdd:PRK13536 237 RLC-DRL 242
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
16-181 |
6.92e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 71.21 E-value: 6.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 16 YGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSN-CIPF-----FFEQFG------------- 76
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAgLVPWkrrkkFLRRIGvvfgqktqlwwdl 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 77 --SDSEYF-----ETDYAEAGK--------MGVADHIWQ--ENVSGGEDTRIRL-AQLFSSPHaVAFLDEPTSNLDYNGV 138
Cdd:cd03267 111 pvIDSFYLlaaiyDLPPARFKKrldelselLDLEELLDTpvRQLSLGQRMRAEIaAALLHEPE-ILFLDEPTIGLDVVAQ 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1124469102 139 EMLKKRLNEIE-----TLVVISHDRSVLNEICDRIVEISFGKLQnYSG 181
Cdd:cd03267 190 ENIRNFLKEYNrergtTVLLTSHYMKDIEALARRVLVIDKGRLL-YDG 236
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
7-176 |
9.46e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 71.20 E-value: 9.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPffFEQFGSDS------- 79
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKP--ISMLSSRQlarrlal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 80 -----------------EYFETDYAEA-GKMGVADH--IWQ---------------ENVSGGEDTRIRLAQLFSSPHAVA 124
Cdd:PRK11231 81 lpqhhltpegitvrelvAYGRSPWLSLwGRLSAEDNarVNQameqtrinhladrrlTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1124469102 125 FLDEPTSNLDYN-GVE---MLKKRLNEIETLVVISHDrsvLNEI---CDRIVEISFGKL 176
Cdd:PRK11231 161 LLDEPTTYLDINhQVElmrLMRELNTQGKTVVTVLHD---LNQAsryCDHLVVLANGHV 216
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-169 |
1.09e-13 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 70.23 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSY----GEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVssncipfffeqfgsdsEY 81
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSI----------------IF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 82 FETDYAEAGK------------------------MGVADHIW-----QENVSGGEDTRIRLAQLFSS-----------PH 121
Cdd:cd03257 65 DGKDLLKLSRrlrkirrkeiqmvfqdpmsslnprMTIGEQIAeplriHGKLSKKEARKEAVLLLLVGvglpeevlnryPH 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1124469102 122 --------------AVA------FLDEPTSNLD-YNGVEMLK--KRLNEIE--TLVVISHDRSVLNEICDRIV 169
Cdd:cd03257 145 elsggqrqrvaiarALAlnpkllIADEPTSALDvSVQAQILDllKKLQEELglTLLFITHDLGVVAKIADRVA 217
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-176 |
1.10e-13 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 70.13 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQTV-LDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSN----------CIPFFFEQF 75
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNgqdvsdlrgrAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 76 G---------SDSEYFETDYAEAGKMGVADHIWQENV--------------------SGGEDTRIRLAQLFSSPHAVAFL 126
Cdd:cd03292 81 GvvfqdfrllPDRNVYENVAFALEVTGVPPREIRKRVpaalelvglshkhralpaelSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1124469102 127 DEPTSNLD---YNGVEMLKKRLNEIETLVVIS-HDRSVLNEICDRIVEISFGKL 176
Cdd:cd03292 161 DEPTGNLDpdtTWEIMNLLKKINKAGTTVVVAtHAKELVDTTRHRVIALERGKL 214
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-169 |
1.17e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 72.74 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSYGEQTVLD---FDrfyLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVssncipfFFEqfgsDSEYF 82
Cdd:COG1129 4 LLEMRGISKSFGGVKALDgvsLE---LRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEI-------LLD----GEPVR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 83 ETDYAEAGKMG---------------VADHIW--QENVSGG----EDTRIRLAQLFS------SPH-------------- 121
Cdd:COG1129 70 FRSPRDAQAAGiaiihqelnlvpnlsVAENIFlgREPRRGGlidwRAMRRRARELLArlgldiDPDtpvgdlsvaqqqlv 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1124469102 122 ----AVAF------LDEPTSNLDYNGVEMLKKRLNEIE----TLVVISHDrsvLNE---ICDRIV 169
Cdd:COG1129 150 eiarALSRdarvliLDEPTASLTEREVERLFRIIRRLKaqgvAIIYISHR---LDEvfeIADRVT 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
297-482 |
1.32e-13 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 69.87 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREKV----YVVPGAKIGYARQNMSQIDLS--- 369
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPdsgtIIIDGLKLTDDKKNINELRQKvgm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 370 ----------QTVLVN-------VRRVS-IQSESISRIVLARLLLSERdMNKKASELSGGERMKLSFAMLFVSDVNLLIL 431
Cdd:cd03262 81 vfqqfnlfphLTVLENitlapikVKGMSkAEAEERALELLEKVGLADK-ADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1124469102 432 DEPTNYLDIPSV-EALEKM--LVEyEG-TLIFTSHDKVFVDRIATDRLYIGDGKI 482
Cdd:cd03262 160 DEPTSALDPELVgEVLDVMkdLAE-EGmTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
27-172 |
1.38e-13 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 70.16 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 27 FYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGT------------------------------VSS--NCIPF---- 70
Cdd:COG4778 32 FSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSilvrhdggwvdlaqaspreilalrrrtigyVSQflRVIPRvsal 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 71 ------FFEQfGSDSEyfeTDYAEAGKM----GVADHIWQ---ENVSGGEDTRIRLAQLFSSPHAVAFLDEPTSNLDYNG 137
Cdd:COG4778 112 dvvaepLLER-GVDRE---EARARARELlarlNLPERLWDlppATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAAN 187
|
170 180 190
....*....|....*....|....*....|....*....
gi 1124469102 138 ----VEMLKKRLNEIETLVVISHDRSVLNEICDRIVEIS 172
Cdd:COG4778 188 ravvVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVT 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
311-462 |
1.67e-13 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 69.12 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 311 IFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREKVYVVPGakigyarqnmsqidlsqTVLVNVRRVSIQS-ESISR- 388
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSG-----------------EVLINGRPLDKRSfRKIIGy 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 389 -----IVLARLLLSER-DMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIPSVEALEKMLVEY--EG-TLIF 459
Cdd:cd03213 87 vpqddILHPTLTVRETlMFAAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLadTGrTIIC 166
|
...
gi 1124469102 460 TSH 462
Cdd:cd03213 167 SIH 169
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
297-482 |
1.85e-13 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 69.90 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAY-DDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELIN------------NREKVYVVPGAKIGYARQNM 363
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNglveptsgsvliDGTDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 364 SQI--DLS----QTVLVNV---------------RRVSIQSESISRIVLARLLLSERdMNKKASELSGGERMKLSFAMLF 422
Cdd:cd03256 81 GMIfqQFNlierLSVLENVlsgrlgrrstwrslfGLFPKEEKQRALAALERVGLLDK-AYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 423 VSDVNLLILDEPTNYLDIPS----VEALEKMLVEYEGTLIFTSHD----KVFVDRIatdrlyIG--DGKI 482
Cdd:cd03256 160 MQQPKLILADEPVASLDPASsrqvMDLLKRINREEGITVIVSLHQvdlaREYADRI------VGlkDGRI 223
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
297-482 |
1.88e-13 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 69.56 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYD-DHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINnreKVYVVPGAKIGYARQNMSQIDLSQ----- 370
Cdd:cd03254 3 IEFENVNFSYDeKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLM---RFYDPQKGQILIDGIDIRDISRKSlrsmi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 371 ------------TVLVNVR--RVSIQSESI---SRIVLARLLLS------ERDMNKKASELSGGERMKLSFAMLFVSDVN 427
Cdd:cd03254 80 gvvlqdtflfsgTIMENIRlgRPNATDEEVieaAKEAGAHDFIMklpngyDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1124469102 428 LLILDEPTNYLDiPSVEAL--EKMLVEYEG-TLIFTSH---DKVFVDRIatdrLYIGDGKI 482
Cdd:cd03254 160 ILILDEATSNID-TETEKLiqEALEKLMKGrTSIIIAHrlsTIKNADKI----LVLDDGKI 215
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
15-176 |
1.92e-13 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 69.48 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 15 SYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNC--IPFFFEQFGSDSE-------YF--- 82
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrvSSLLGLGGGFNPEltgreniYLngr 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 83 --------------ET-DYAEAGkmgvaDHIWQ--ENVSGGedTRIRLAqlFS----SPHAVAFLDEPTSNLDYNGVEML 141
Cdd:cd03220 111 llglsrkeidekidEIiEFSELG-----DFIDLpvKTYSSG--MKARLA--FAiataLEPDILLIDEVLAVGDAAFQEKC 181
|
170 180 190
....*....|....*....|....*....|....*....
gi 1124469102 142 KKRLNEI----ETLVVISHDRSVLNEICDRIVEISFGKL 176
Cdd:cd03220 182 QRRLRELlkqgKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
300-483 |
2.28e-13 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 69.14 E-value: 2.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 300 EHISFAYDDHVIFDDADFMIKNGSkVALLGGNGAGKTTLLELI-------------------NNREKVYvvpgAKIGYAR 360
Cdd:cd03264 4 ENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILatltppssgtiridgqdvlKQPQKLR----RRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 361 Q------NMSQIDLSQTVLVnVRRVSiQSESISRI--VLARLLLSERdMNKKASELSGGERMKLSFAMLFVSDVNLLILD 432
Cdd:cd03264 79 QefgvypNFTVREFLDYIAW-LKGIP-SKEVKARVdeVLELVNLGDR-AKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1124469102 433 EPTNYLDIPSVEALEKMLVEY--EGTLIFTSHDKVFVDRIATDRLYIGDGKIR 483
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELgeDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
311-483 |
2.60e-13 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 68.92 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 311 IFDDADFMIKNGSKVALLGGNGAGKTTLLELINNRE-----KVYVvpgakIGYARQNMSQIDLSQ--------------- 370
Cdd:TIGR02211 20 VLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDnptsgEVLF-----NGQSLSKLSSNERAKlrnkklgfiyqfhhl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 371 ----TVLVNV------RRVSIQ-SESISRIVLARLLLSERdMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLD 439
Cdd:TIGR02211 95 lpdfTALENVamplliGKKSVKeAKERAYEMLEKVGLEHR-INHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1124469102 440 IPSVEALEKML----VEYEGTLIFTSHDKVFVDRIATdRLYIGDGKIR 483
Cdd:TIGR02211 174 NNNAKIIFDLMlelnRELNTSFLVVTHDLELAKKLDR-VLEMKDGQLF 220
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
32-168 |
2.87e-13 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 72.09 E-value: 2.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 32 GEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPFFF---EQFGS-------DSEYFE-------------TDYA- 87
Cdd:COG4618 358 GEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwdrEELGRhigylpqDVELFDgtiaeniarfgdaDPEKv 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 88 -EAGKM-GVADHIWQ-------------ENVSGGEDTRIRLAQ-LFSSPHAVaFLDEPTSNLDYNGVEMLKKRLNEIE-- 149
Cdd:COG4618 438 vAAAKLaGVHEMILRlpdgydtrigeggARLSGGQRQRIGLARaLYGDPRLV-VLDEPNSNLDDEGEAALAAAIRALKar 516
|
170 180
....*....|....*....|.
gi 1124469102 150 --TLVVISHDRSVLNeICDRI 168
Cdd:COG4618 517 gaTVVVITHRPSLLA-AVDKL 536
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
17-157 |
3.52e-13 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 71.62 E-value: 3.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 17 GEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPF-------------FFEQfgsDSEYFE 83
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVssldqdevrrrvsVCAQ---DAHLFD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 84 TDY-------------AEAGKM----GVADHI----------WQEN---VSGGEDTRIRLAQLFSSPHAVAFLDEPTSNL 133
Cdd:TIGR02868 423 TTVrenlrlarpdatdEELWAAlervGLADWLralpdgldtvLGEGgarLSGGERQRLALARALLADAPILLLDEPTEHL 502
|
170 180
....*....|....*....|....*...
gi 1124469102 134 DYNG----VEMLKKRLNEiETLVVISHD 157
Cdd:TIGR02868 503 DAETadelLEDLLAALSG-RTVVLITHH 529
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
297-463 |
3.62e-13 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 71.62 E-value: 3.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAY-DDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLE----LINNREKVYVVPGAKIGYARQNMSQIDLS-- 369
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLAtlagLLDPLQGEVTLDGVPVSSLDQDEVRRRVSvc 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 370 --------QTVLVNVR----RVSIQ--SESISRIVLARLLLSERD-----MNKKASELSGGERMKLSFAMLFVSDVNLLI 430
Cdd:TIGR02868 415 aqdahlfdTTVRENLRlarpDATDEelWAALERVGLADWLRALPDgldtvLGEGGARLSGGERQRLALARALLADAPILL 494
|
170 180 190
....*....|....*....|....*....|....*
gi 1124469102 431 LDEPTNYLDIPSVEALEKML--VEYEGTLIFTSHD 463
Cdd:TIGR02868 495 LDEPTEHLDAETADELLEDLlaALSGRTVVLITHH 529
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
311-453 |
3.88e-13 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 68.84 E-value: 3.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 311 IFDDADFMIKNGSKVALLGGNGAGKTTLLELINNRekvyvVPGAK---------------------IGYARQ---NMSQI 366
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR-----VEGGGttsgqilfngqprkpdqfqkcVAYVRQddiLLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 367 DLSQTVL--VNVRRVSIQSESISRIVLARLLLSE----RDMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDI 440
Cdd:cd03234 97 TVRETLTytAILRLPRKSSDAIRKKRVEDVLLRDlaltRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170
....*....|...
gi 1124469102 441 PSVEALEKMLVEY 453
Cdd:cd03234 177 FTALNLVSTLSQL 189
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
7-176 |
5.80e-13 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 66.95 E-value: 5.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQ--TVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPFffeqfgsdSEYFEt 84
Cdd:cd03247 1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV--------SDLEK- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 85 dyAEAGKMGVAD---HIW----QENV----SGGEDTRIRLAQLFSSPHAVAFLDEPTSNLD----YNGVEMLKKRLNEiE 149
Cdd:cd03247 72 --ALSSLISVLNqrpYLFdttlRNNLgrrfSGGERQRLALARILLQDAPIVLLDEPTVGLDpiteRQLLSLIFEVLKD-K 148
|
170 180
....*....|....*....|....*..
gi 1124469102 150 TLVVISHDRSVLnEICDRIVEISFGKL 176
Cdd:cd03247 149 TLIWITHHLTGI-EHMDKILFLENGKI 174
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
297-463 |
6.89e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 68.50 E-value: 6.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREK-------VYVVPGAKIGyARQNMSQIDLS 369
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTpqsgtvfLGDKPISMLS-SRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 370 QTVL-----VNVR---------------RVSIQSESISRIVLARLLLSERdMNKKASELSGGERMKLSFAMLFVSDVNLL 429
Cdd:PRK11231 82 PQHHltpegITVRelvaygrspwlslwgRLSAEDNARVNQAMEQTRINHL-ADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1124469102 430 ILDEPTNYLDIPSVEALEKMLVEY--EG-TLIFTSHD 463
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELntQGkTVVTVLHD 197
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-180 |
7.92e-13 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 67.32 E-value: 7.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 22 LDFDrfylYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSN-----------CIP-------FFFEQ--------- 74
Cdd:cd03297 17 IDFD----LNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgtvlfdsrkkiNLPpqqrkigLVFQQyalfphlnv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 75 -----FG----SDSEyfETDYAEA--GKMGVaDHIWQENV---SGGEDTRIRLAQ-LFSSPhAVAFLDEPTSNLDYNGVE 139
Cdd:cd03297 93 renlaFGlkrkRNRE--DRISVDEllDLLGL-DHLLNRYPaqlSGGEKQRVALARaLAAQP-ELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1124469102 140 MLKKRLNEIET-----LVVISHDRSVLNEICDRIVEISFGKLQNYS 180
Cdd:cd03297 169 QLLPELKQIKKnlnipVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
296-462 |
8.43e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 69.06 E-value: 8.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 296 VIRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELI-----------------------NNREKVYVVP 352
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLlglthpdagsislcgepvpsrarHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 353 gakigyarqnmsQID-------LSQTVLVNVRRVSIQSESISRIV-----LARLllsERDMNKKASELSGGERMKLSFAM 420
Cdd:PRK13537 87 ------------QFDnldpdftVRENLLVFGRYFGLSAAAARALVpplleFAKL---ENKADAKVGELSGGMKRRLTLAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1124469102 421 LFVSDVNLLILDEPTNYLDiPSVEAL--EKM--LVEYEGTLIFTSH 462
Cdd:PRK13537 152 ALVNDPDVLVLDEPTTGLD-PQARHLmwERLrsLLARGKTILLTTH 196
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
27-185 |
8.56e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 68.96 E-value: 8.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 27 FYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSN-CIPF-----FFEQFG------------------------ 76
Cdd:COG4586 43 FTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLgYVPFkrrkeFARRIGvvfgqrsqlwwdlpaidsfrllka 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 77 ----SDSEYFET--DYAEAgkMGVADHIWQ--ENVSGGEdtRIR---LAQLFSSPhAVAFLDEPTSNLDYNGVEMLK--- 142
Cdd:COG4586 123 iyriPDAEYKKRldELVEL--LDLGELLDTpvRQLSLGQ--RMRcelAAALLHRP-KILFLDEPTIGLDVVSKEAIRefl 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1124469102 143 KRLNEIE--TLVVISHDRSVLNEICDRIVEISFGKLQnYSGNYDE 185
Cdd:COG4586 198 KEYNRERgtTILLTSHDMDDIEALCDRVIVIDHGRII-YDGSLEE 241
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
313-482 |
1.13e-12 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 67.05 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 313 DDADFMIKNGSKVALLGGNGAGKTTLLELINNREK------------VYVVPGAKIGYARQNM------SQIDLSQTVLV 374
Cdd:cd03292 18 DGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELptsgtirvngqdVSDLRGRAIPYLRRKIgvvfqdFRLLPDRNVYE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 375 NV----RRVSIQSESISRIV---LARLLLSERDmNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIPSVEALE 447
Cdd:cd03292 98 NVafalEVTGVPPREIRKRVpaaLELVGLSHKH-RALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIM 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 1124469102 448 KML--VEYEG-TLIFTSHDKVFVDRIATDRLYIGDGKI 482
Cdd:cd03292 177 NLLkkINKAGtTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
297-471 |
1.32e-12 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 67.26 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREKvyvVPGAKIGYARQNMSQIDLSQ------ 370
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFET---PTSGEILLDGKDITNLPPHKrpvntv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 371 ----------TVLVNV----RRVSIQSESISRIVLARLLLSERD--MNKKASELSGGERMKLSFAMLFVSDVNLLILDEP 434
Cdd:cd03300 78 fqnyalfphlTVFENIafglRLKKLPKAEIKERVAEALDLVQLEgyANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1124469102 435 TNYLDipsVEALEKMLVEYEG-------TLIFTSHDK----VFVDRIA 471
Cdd:cd03300 158 LGALD---LKLRKDMQLELKRlqkelgiTFVFVTHDQeealTMSDRIA 202
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
7-181 |
1.44e-12 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 66.83 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQTVLDFDRFYLYEGeKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIP-------------FFFE 73
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDvlkqpqklrrrigYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 74 QFGSDSEY--FE-TDYAEAGKmGVAD--------------HIWQEN------VSGGEDTRIRLAQLFSSPHAVAFLDEPT 130
Cdd:cd03264 80 EFGVYPNFtvREfLDYIAWLK-GIPSkevkarvdevlelvNLGDRAkkkigsLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1124469102 131 SNLD---YNGVEMLKKRLNEIETLVVISHDRSVLNEICDRIVEISFGKLQnYSG 181
Cdd:cd03264 159 AGLDpeeRIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLV-FEG 211
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-169 |
1.87e-12 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 67.05 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 29 LYEGEKVGLVGMNGAGKSTLLKILAGELEPTKG-------TVS-----------SNCIPFFFEQ---FGSDSeYFETDYA 87
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGdieieldTVSykpqyikadyeGTVRDLLSSItkdFYTHP-YFKTEIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 88 EAGKMgvaDHIWQENV---SGGEDTRIRLAQLFSSPHAVAFLDEPTSNLDYNGVEMLKK-----RLNEIETLVVISHDRS 159
Cdd:cd03237 101 KPLQI---EQILDREVpelSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKvirrfAENNEKTAFVVEHDII 177
|
170
....*....|
gi 1124469102 160 VLNEICDRIV 169
Cdd:cd03237 178 MIDYLADRLI 187
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
309-483 |
2.26e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.52 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 309 HVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREK------VYVVPGAKIGyarQNMSQIDlsqtvlvNVRRVSIQ 382
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtpvagCVDVPDNQFG---REASLID-------AIGRKGDF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 383 SESISriVLARLLLSER-DMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIPSVE----ALEKMLVEYEGTL 457
Cdd:COG2401 113 KDAVE--LLNAVGLSDAvLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKrvarNLQKLARRAGITL 190
|
170 180
....*....|....*....|....*.
gi 1124469102 458 IFTSHDKVFVDRIATDRLYIGDGKIR 483
Cdd:COG2401 191 VVATHHYDVIDDLQPDLLIFVGYGGV 216
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
297-482 |
3.33e-12 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 64.37 E-value: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINnrekvyvvpGAkigYARQnmsqidlSQTVLVNV 376
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILS---------GL---YKPD-------SGEILVDG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 377 RRVSIqsesisrivlarllLSERDMNKK----ASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIPSVEALEKMLVE 452
Cdd:cd03216 62 KEVSF--------------ASPRDARRAgiamVYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRR 127
|
170 180 190
....*....|....*....|....*....|....*.
gi 1124469102 453 Y--EG-TLIFTSH--DKVFvdRIAtDRLYI-GDGKI 482
Cdd:cd03216 128 LraQGvAVIFISHrlDEVF--EIA-DRVTVlRDGRV 160
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-176 |
3.49e-12 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 66.07 E-value: 3.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSYGEQ----TVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGeLE-PTKGTVSSNC------------- 67
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCING-LErPTSGSVLVDGtdltllsgkelrk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 68 ----IPFFFEQFG--SDSEYFE----------TDYAEAGK--------MGVAD--HIWQENVSGGEDTRIRLAQLFSSPH 121
Cdd:cd03258 80 arrrIGMIFQHFNllSSRTVFEnvalpleiagVPKAEIEErvlellelVGLEDkaDAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 122 AVAFLDEPTSNLDYNGVEMLKKRLNEIE-----TLVVISHDRSVLNEICDRIVEISFGKL 176
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINrelglTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
307-482 |
3.81e-12 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 65.24 E-value: 3.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 307 DDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREKvYVVPGAKIGYARQNMsqIDLSqtvlVNVRR-----VSI 381
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPK-YEVTEGEILFKGEDI--TDLP----PEERArlgifLAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 382 QS-ESISRIVLARLLlseRDMNKKaseLSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIPSV----EALEKMLVEYEGT 456
Cdd:cd03217 84 QYpPEIPGVKNADFL---RYVNEG---FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALrlvaEVINKLREEGKSV 157
|
170 180
....*....|....*....|....*..
gi 1124469102 457 LIFTSHDKVFvDRIATDRLYI-GDGKI 482
Cdd:cd03217 158 LIITHYQRLL-DYIKPDRVHVlYDGRI 183
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-482 |
4.07e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 68.29 E-value: 4.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAG--ELEPTKGTVSSN------C----IPFFFEQ 74
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHvalcekCgyveRPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 75 ----FGSDSEYFETDY----------------------------------------------AEAGKMGV---------- 94
Cdd:TIGR03269 81 pcpvCGGTLEPEEVDFwnlsdklrrrirkriaimlqrtfalygddtvldnvlealeeigyegKEAVGRAVdliemvqlsh 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 95 -ADHIWQEnVSGGEDTRIRLA-QLFSSPhAVAFLDEPTSNLDYNGVEMLKKRLNEIE-----TLVVISHDRSVLNEICDR 167
Cdd:TIGR03269 161 rITHIARD-LSGGEKQRVVLArQLAKEP-FLFLADEPTGTLDPQTAKLVHNALEEAVkasgiSMVLTSHWPEVIEDLSDK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 168 IVEISFGKLQNySGNYDEYVvqkeeqrktqqaeyenyqaekkrlqSVYVEkkakaktvdkkpknmSASEakvrafignrk 247
Cdd:TIGR03269 239 AIWLENGEIKE-EGTPDEVV-------------------------AVFME---------------GVSE----------- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 248 pedkargiersatnvLKRLEHMEIKEKpkeeltvrpdfrltnpprnpiVIRGEHISFAY---DDHVI--FDDADFMIKNG 322
Cdd:TIGR03269 267 ---------------VEKECEVEVGEP---------------------IIKVRNVSKRYisvDRGVVkaVDNVSLEVKEG 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 323 SKVALLGGNGAGKTTLLELIN-----NREKVYVVPGAKI-----------GYARQNM----SQIDL--SQTVLVNVrrvs 380
Cdd:TIGR03269 311 EIFGIVGTSGAGKTTLSKIIAgvlepTSGEVNVRVGDEWvdmtkpgpdgrGRAKRYIgilhQEYDLypHRTVLDNL---- 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 381 iqSESISR------------IVLARLLLSERD----MNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLD-IPSV 443
Cdd:TIGR03269 387 --TEAIGLelpdelarmkavITLKMVGFDEEKaeeiLDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpITKV 464
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1124469102 444 EALEKML---VEYEGTLIFTSHDKVFV----DRIATDRlyigDGKI 482
Cdd:TIGR03269 465 DVTHSILkarEEMEQTFIIVSHDMDFVldvcDRAALMR----DGKI 506
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
6-156 |
4.40e-12 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 65.88 E-value: 4.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGT----------------------- 62
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrlfgerrggedvwelrkrigl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 63 VSS---NCIPF-----------FFEQFGSDSEYFETDYAEAGK----MGV---ADHIWQEnVSGGEDTRIRLAQ-LFSSP 120
Cdd:COG1119 83 VSPalqLRFPRdetvldvvlsgFFDSIGLYREPTDEQRERAREllelLGLahlADRPFGT-LSQGEQRRVLIARaLVKDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1124469102 121 hAVAFLDEPTSNLDYNGVEMLKKRLNEI-----ETLVVISH 156
Cdd:COG1119 162 -ELLILDEPTAGLDLGARELLLALLDKLaaegaPTLVLVTH 201
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
297-483 |
6.16e-12 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 65.08 E-value: 6.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREKVY----VVPG-----------AKIGY--- 358
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTsgraTVAGhdvvreprevrRRIGIvfq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 359 ---------ARQNMsqidLSQTVLVNVRRvSIQSESISRIVLARLLLSERDmnKKASELSGGERMKLSFAMLFVSDVNLL 429
Cdd:cd03265 81 dlsvddeltGWENL----YIHARLYGVPG-AERRERIDELLDFVGLLEAAD--RLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1124469102 430 ILDEPTNYLDIPSV----EALEKMLVEYEGTLIFTSHDKVFVDRIAtDRLYIGD-GKIR 483
Cdd:cd03265 154 FLDEPTIGLDPQTRahvwEYIEKLKEEFGMTILLTTHYMEEAEQLC-DRVAIIDhGRII 211
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
300-435 |
6.45e-12 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 65.15 E-value: 6.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 300 EHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELIN-----------------NREKVYVVPGAKIGYARQN 362
Cdd:cd03224 4 ENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMgllpprsgsirfdgrdiTGLPPHERARAGIGYVPEG 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1124469102 363 MsQIDLSQTVLVNVRR-VSIQSESISRIVLARLL-----LSERdMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPT 435
Cdd:cd03224 84 R-RIFPELTVEENLLLgAYARRRAKRKARLERVYelfprLKER-RKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
7-179 |
6.49e-12 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 64.74 E-value: 6.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQ--TVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTV-----------------SSNC 67
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIeidgidistipledlrsSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 68 IP----FF----------FEQFgSDSEYFET-DYAEAGkmgvadhiwqENVSGGEDTRIRLAQLFSSPHAVAFLDEPTSN 132
Cdd:cd03369 87 IPqdptLFsgtirsnldpFDEY-SDEEIYGAlRVSEGG----------LNLSQGQRQLLCLARALLKRPRVLVLDEATAS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1124469102 133 LDYNGVEMLKKRLNEI---ETLVVISHD-RSVLNeiCDRIVEISFGKLQNY 179
Cdd:cd03369 156 IDYATDALIQKTIREEftnSTILTIAHRlRTIID--YDKILVMDAGEVKEY 204
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
9-168 |
7.09e-12 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 65.47 E-value: 7.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 9 AENIVHSYGEqtvldfDRFYLY------EGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSN-----CIPFFfeqFGS 77
Cdd:cd03236 3 EDEPVHRYGP------NSFKLHrlpvprEGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPpdwdeILDEF---RGS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 78 D-SEYFET----DYAEAGKMGVADHIWQ------------------------------------ENVSGGEDTRIRLAQL 116
Cdd:cd03236 74 ElQNYFTKllegDVKVIVKPQYVDLIPKavkgkvgellkkkdergkldelvdqlelrhvldrniDQLSGGELQRVAIAAA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1124469102 117 FSSPHAVAFLDEPTSNLD----YNGVEMLKKRLNEIETLVVISHDRSVLNEICDRI 168
Cdd:cd03236 154 LARDADFYFFDEPSSYLDikqrLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
6-169 |
7.50e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 65.33 E-value: 7.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSsncipfFFEQFGSDSEYFE-- 83
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH------YRMRDGQLRDLYAls 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 84 ---------TDY-------AEAGKMGV--------------ADHI---------WQENV--------------SGGEDTR 110
Cdd:PRK11701 80 eaerrrllrTEWgfvhqhpRDGLRMQVsaggnigerlmavgARHYgdiratagdWLERVeidaariddlpttfSGGMQQR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1124469102 111 IRLAQ-LFSSPHAVaFLDEPTSNLDyngVEMLKKRLNEIETLV--------VISHDRSVLNEICDRIV 169
Cdd:PRK11701 160 LQIARnLVTHPRLV-FMDEPTGGLD---VSVQARLLDLLRGLVrelglavvIVTHDLAVARLLAHRLL 223
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-168 |
7.92e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.38 E-value: 7.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 1 MERHLLIKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPfffeqfgsdse 80
Cdd:PRK15439 6 TTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNP----------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 81 YFETDYAEAGKMGV-----ADHIW-----QENV----SGGEDTRIRLAQLFS------SPHAVA---------------- 124
Cdd:PRK15439 75 CARLTPAKAHQLGIylvpqEPLLFpnlsvKENIlfglPKRQASMQKMKQLLAalgcqlDLDSSAgslevadrqiveilrg 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1124469102 125 --------FLDEPTSNLDYNGVEMLKKRLNEIET----LVVISHDRSVLNEICDRI 168
Cdd:PRK15439 155 lmrdsrilILDEPTASLTPAETERLFSRIRELLAqgvgIVFISHKLPEIRQLADRI 210
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-168 |
8.47e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.12 E-value: 8.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNcipfffeqfgsDSEYFETD 85
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN-----------NINYNKLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 86 YAEAGKMGVADhIWQE--------------------------------------------------------NVSGGEDT 109
Cdd:PRK09700 74 HKLAAQLGIGI-IYQElsvideltvlenlyigrhltkkvcgvniidwremrvraammllrvglkvdldekvaNLSISHKQ 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1124469102 110 RIRLAQLFSSPHAVAFLDEPTSNLDYNGVE---MLKKRL-NEIETLVVISHDRSVLNEICDRI 168
Cdd:PRK09700 153 MLEIAKTLMLDAKVIIMDEPTSSLTNKEVDylfLIMNQLrKEGTAIVYISHKLAEIRRICDRY 215
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
306-482 |
9.27e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 65.38 E-value: 9.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 306 YDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREK----VYVVPGAKIGYARQNMSQIDLSQ----------- 370
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKpsegSIVVNGQTINLVRDKDGQLKVADknqlrllrtrl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 371 -------------TVLVNVRRVSIQ------SESISRIV--LARLLLSERDMNKKASELSGGERMKLSFAMLFVSDVNLL 429
Cdd:PRK10619 95 tmvfqhfnlwshmTVLENVMEAPIQvlglskQEARERAVkyLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1124469102 430 ILDEPTNYLDIPSV-EALEKM--LVEYEGTLIFTSHDKVFVDRIATDRLYIGDGKI 482
Cdd:PRK10619 175 LFDEPTSALDPELVgEVLRIMqqLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
6-157 |
9.78e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 65.14 E-value: 9.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSN----------------CIP 69
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNgklrigyvpqklyldtTLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 70 FFFEQF-----GSDSEyfetDYAEAGKMGVADHIWQ---ENVSGGEDTRIRLAQ-LFSSPHAVAfLDEPTSNLDYNGVEM 140
Cdd:PRK09544 84 LTVNRFlrlrpGTKKE----DILPALKRVQAGHLIDapmQKLSGGETQRVLLARaLLNRPQLLV-LDEPTQGVDVNGQVA 158
|
170 180
....*....|....*....|..
gi 1124469102 141 LKKRLNEIET-----LVVISHD 157
Cdd:PRK09544 159 LYDLIDQLRReldcaVLMVSHD 180
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
289-483 |
1.09e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 66.77 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 289 NPPRNPIVIRGEHISFAYDD--HVIFDDADFMIKNGSKVALLGGNGAGKTTLLELInNREkvYVVPGAKI---GYARQNM 363
Cdd:PRK11160 331 TAAADQVSLTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL-TRA--WDPQQGEIllnGQPIADY 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 364 SQIDLSQTVLVNVRRVSIQSESI--------------------SRIVLARLLLSERDMNKKASE----LSGGERMKLSFA 419
Cdd:PRK11160 408 SEAALRQAISVVSQRVHLFSATLrdnlllaapnasdealievlQQVGLEKLLEDDKGLNAWLGEggrqLSGGEQRRLGIA 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1124469102 420 MLFVSDVNLLILDEPTNYLDIPSVEALEKMLVEY--EGTLIFTSHDKVFVDRIatDRLYIGD-GKIR 483
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLDAETERQILELLAEHaqNKTVLMITHRLTGLEQF--DRICVMDnGQII 552
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
297-471 |
1.12e-11 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 64.42 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDD----HVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREK-----VYV------VPGAKIGYarq 361
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERptsgeVLVdgepvtGPGPDRGY--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 362 nMSQIDLS---QTVLVNV------RRVS-IQSESISRIVLARLLLSERDmNKKASELSGGERMKLSFAMLFVSDVNLLIL 431
Cdd:cd03293 78 -VFQQDALlpwLTVLDNValglelQGVPkAEARERAEELLELVGLSGFE-NAYPHQLSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1124469102 432 DEPTNYLDIPSVEALE----KMLVEYEGTLIFTSHD---KVFV-DRIA 471
Cdd:cd03293 156 DEPFSALDALTREQLQeellDIWRETGKTVLLVTHDideAVFLaDRVV 203
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
313-471 |
1.22e-11 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 64.28 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 313 DDADFMIKNGSKVALLGGNGAGKTTLLELIN------------NREKVYVVPGAK--IGYARQNMS---QIDLSQTVLVN 375
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAgfikpdsgkillNGKDITNLPPEKrdISYVPQNYAlfpHMTVYKNIAYG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 376 VRRVSIQSESISRIVL--ARLLLSERDMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIPSVEALEKMLV-- 451
Cdd:cd03299 96 LKKRKVDKKEIERKVLeiAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKki 175
|
170 180
....*....|....*....|....*.
gi 1124469102 452 --EYEGTLIFTSHD----KVFVDRIA 471
Cdd:cd03299 176 rkEFGVTVLHVTHDfeeaWALADKVA 201
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
6-176 |
1.27e-11 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 64.83 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSY---------GEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPF------ 70
Cdd:TIGR02769 2 LLEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLyqldrk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 71 ------------FFEQFGS----------------------DSEYFETDYAEAGKMGVADHIWQE---NVSGGEDTRIRL 113
Cdd:TIGR02769 82 qrrafrrdvqlvFQDSPSAvnprmtvrqiigeplrhltsldESEQKARIAELLDMVGLRSEDADKlprQLSGGQLQRINI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1124469102 114 AQLFSSPHAVAFLDEPTSNLDY----NGVEMLKKRLNEIET-LVVISHDRSVLNEICDRIVEISFGKL 176
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMvlqaVILELLRKLQQAFGTaYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-177 |
1.42e-11 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 63.81 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKG------------------------- 61
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGriyiggrdvtdlppkdrdiamvfqn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 62 -------TVSSNcIPFFFEQFGSDSEYFETDYAEAGKMGVADHIWQENV---SGGEDTRIRLAQLFSSPHAVAFLDEPTS 131
Cdd:cd03301 81 yalyphmTVYDN-IAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPkqlSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1124469102 132 NLDYN-GVEM---LKKRLNEIE-TLVVISHDRSVLNEICDRIVEISFGKLQ 177
Cdd:cd03301 160 NLDAKlRVQMraeLKRLQQRLGtTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
383-482 |
1.44e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 66.81 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 383 SESISRIVLARLLLSERDMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIPSVEALEKMLVEYEGTLIFTSH 462
Cdd:PLN03073 320 AEARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSH 399
|
90 100
....*....|....*....|
gi 1124469102 463 DKVFVDRIATDRLYIGDGKI 482
Cdd:PLN03073 400 AREFLNTVVTDILHLHGQKL 419
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
7-176 |
1.53e-11 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 64.00 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKG------------------------- 61
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGsvlfdgeditglppheiarlgigrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 62 ----------TVSSNCI--------PFFFEQFGSDSEYFETDYAEA-----GKMGVADHIwQENVSGGEDTRIRLAQLFS 118
Cdd:cd03219 81 fqiprlfpelTVLENVMvaaqartgSGLLLARARREEREARERAEEllervGLADLADRP-AGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1124469102 119 SPHAVAFLDEPTSNLDYNGVEMLKKRLNEIE----TLVVISHDRSVLNEICDRIVEISFGKL 176
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRergiTVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
312-476 |
1.89e-11 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 63.61 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 312 FDDADFMIKNGSKVALLGGNGAGKTTLLELI--NnrekvYVVPGAKIGYARQNmSQIDLSQ----TVLvNVRRVSIQSES 385
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIygN-----YLPDSGSILVRHDG-GWVDLAQasprEIL-ALRRRTIGYVS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 386 -----ISRI----VLARLLL----SERDMNKKASEL------------------SGGERMKLSFAMLFVSDVNLLILDEP 434
Cdd:COG4778 100 qflrvIPRVsaldVVAEPLLergvDREEARARARELlarlnlperlwdlppatfSGGEQQRVNIARGFIADPPLLLLDEP 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1124469102 435 TNYLDIPSVEALEKMLVEY--EGTL---IFtsHDKVFVDRIAtDRLY 476
Cdd:COG4778 180 TASLDAANRAVVVELIEEAkaRGTAiigIF--HDEEVREAVA-DRVV 223
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
290-482 |
2.02e-11 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 63.61 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 290 PPRNPIVIRGEHISFAYDDH----VIFDDADFMIKNGSKVALLGGNGAGKTTLLELIN--------------------NR 345
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAgldrptsgtvrlagqdlfalDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 346 EKVYVVPGAKIGYARQNmSQIDLSQTVLVNV------RRVSiQSESISRIVLARLLLSERdMNKKASELSGGERMKLSFA 419
Cdd:COG4181 82 DARARLRARHVGFVFQS-FQLLPTLTALENVmlplelAGRR-DARARARALLERVGLGHR-LDHYPAQLSGGEQQRVALA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1124469102 420 MLFVSDVNLLILDEPTNYLDIPS----VEALEKMLVEYEGTLIFTSHDKVFVDRiaTDR-LYIGDGKI 482
Cdd:COG4181 159 RAFATEPAILFADEPTGNLDAATgeqiIDLLFELNRERGTTLVLVTHDPALAAR--CDRvLRLRAGRL 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
7-169 |
2.04e-11 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 63.32 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTV---------SSNCIP-------F 70
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIiidglkltdDKKNINelrqkvgM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 71 FFEQFG---------------------SDSEYFETDYAEAGKMGVADHI--WQENVSGGEDTRIRLAQ-LFSSPHAVAFl 126
Cdd:cd03262 81 VFQQFNlfphltvlenitlapikvkgmSKAEAEERALELLEKVGLADKAdaYPAQLSGGQQQRVAIARaLAMNPKVMLF- 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1124469102 127 DEPTSNLDyngVEMLKKRLNEIE-------TLVVISHDRSVLNEICDRIV 169
Cdd:cd03262 160 DEPTSALD---PELVGEVLDVMKdlaeegmTMVVVTHEMGFAREVADRVI 206
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
297-482 |
2.52e-11 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 63.47 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAY-DDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELIN------------NREKVYVVPGA----KIGYA 359
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINrlieptsgeifiDGEDIREQDPVelrrKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 360 RQnmsQIDL--SQTVLVNVRRV-SIQSESISRIVL-ARLLLSERDM------NKKASELSGGERMKLSFAMLFVSDVNLL 429
Cdd:cd03295 81 IQ---QIGLfpHMTVEENIALVpKLLKWPKEKIRErADELLALVGLdpaefaDRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1124469102 430 ILDEPTNYLDIPSVEALEKMLV----EYEGTLIFTSHDK----VFVDRIATdrlyIGDGKI 482
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKrlqqELGKTIVFVTHDIdeafRLADRIAI----MKNGEI 214
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
292-447 |
2.71e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.97 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 292 RNPIVIRGEHisfayddhVIFDDADFMIKNGSKVALLGGNGAGKTTLLELI-------------NNREKVYVVPGAKIGY 358
Cdd:PRK13539 6 EDLACVRGGR--------VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIagllppaagtiklDGGDIDDPDVAEACHY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 359 A-RQNMSQIDLsqTVLVNV---------RRVSIqSESISRIVLARLLlserdmNKKASELSGGERMKLSFAMLFVSDVNL 428
Cdd:PRK13539 78 LgHRNAMKPAL--TVAENLefwaaflggEELDI-AAALEAVGLAPLA------HLPFGYLSAGQKRRVALARLLVSNRPI 148
|
170
....*....|....*....
gi 1124469102 429 LILDEPTNYLDIPSVEALE 447
Cdd:PRK13539 149 WILDEPTAALDAAAVALFA 167
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-185 |
2.79e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 63.19 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 1 MERHLLIKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKG------------------- 61
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGtllfegedistlkpeiyrq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 62 --------------TVSSNCI-PFFFEQFGSDSEYFETDYAeagKMGVADHIWQENV---SGGEDTRIRLAQLFSSPHAV 123
Cdd:PRK10247 82 qvsycaqtptlfgdTVYDNLIfPWQIRNQQPDPAIFLDDLE---RFALPDTILTKNIaelSGGEKQRISLIRNLQFMPKV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 124 AFLDEPTSNLDyngvEMLKKRLNEIETLVVISHDRSVL------NEI--CDRIVeisfgKLQNYSGNYDE 185
Cdd:PRK10247 159 LLLDEITSALD----ESNKHNVNEIIHRYVREQNIAVLwvthdkDEInhADKVI-----TLQPHAGEMQE 219
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
319-481 |
2.92e-11 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 63.58 E-value: 2.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 319 IKNGSKVALLGGNGAGKTTLLELINNREKVYV----VPGAKIGYARQNMsQIDLSQTV----LVNVRRVSIQSESISRIv 390
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEgdieIELDTVSYKPQYI-KADYEGTVrdllSSITKDFYTHPYFKTEI- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 391 lARLLLSERDMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLD----IPSVEALEKMLVEYEGTLIFTSHDKVF 466
Cdd:cd03237 100 -AKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDveqrLMASKVIRRFAENNEKTAFVVEHDIIM 178
|
170
....*....|....*
gi 1124469102 467 VDRIAtDRLYIGDGK 481
Cdd:cd03237 179 IDYLA-DRLIVFEGE 192
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
294-483 |
3.17e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 64.86 E-value: 3.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 294 PIVIRGEHISFAydDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNrekvYVVPGAKI----GYARQNMSQIDLS 369
Cdd:PRK09536 3 MIDVSDLSVEFG--DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAING----TLTPTAGTvlvaGDDVEALSARAAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 370 QTVLVNVRRVSIQSE-SISRIV-------LARL--------LLSERDMN---------KKASELSGGERMKLSFAMLFVS 424
Cdd:PRK09536 77 RRVASVPQDTSLSFEfDVRQVVemgrtphRSRFdtwtetdrAAVERAMErtgvaqfadRPVTSLSGGERQRVLLARALAQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1124469102 425 DVNLLILDEPTNYLDIP-SVEALE--KMLVEYEGTLIFTSHDKVFVDRIATDRLYIGDGKIR 483
Cdd:PRK09536 157 ATPVLLLDEPTASLDINhQVRTLElvRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVR 218
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
19-172 |
4.78e-11 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 61.02 E-value: 4.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 19 QTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGeLEP-TKGTVSsncIP-----FFFEQfgsdseyfeTDYAEAGKM 92
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LWPwGSGRIG---MPegedlLFLPQ---------RPYLPLGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 93 gvADHI---WQENVSGGEDTRIRLAQLFSSPHAVAFLDEPTSNLD-------YngvEMLKKRLNeieTLVVISHdRSVLN 162
Cdd:cd03223 81 --REQLiypWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDeesedrlY---QLLKELGI---TVISVGH-RPSLW 151
|
170
....*....|
gi 1124469102 163 EICDRIVEIS 172
Cdd:cd03223 152 KFHDRVLDLD 161
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
6-201 |
4.94e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.13 E-value: 4.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSY--GEQT--VLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGT--VSSNCIP---------- 69
Cdd:PRK10535 4 LLELKDIRRSYpsGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTyrVAGQDVAtldadalaql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 70 ------FFFEQFG-----SDSEYFETD--YAEAGK-------------MGVADHI-WQEN-VSGGEDTRIRLAQLFSSPH 121
Cdd:PRK10535 84 rrehfgFIFQRYHllshlTAAQNVEVPavYAGLERkqrllraqellqrLGLEDRVeYQPSqLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 122 AVAFLDEPTSNLD-YNGVE---MLKKRLNEIETLVVISHDRSVLNEiCDRIVEISFGKLQNYSGNYDEYVVQKEEQRKTQ 197
Cdd:PRK10535 164 QVILADEPTGALDsHSGEEvmaILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPAQEKVNVAGGTEPVVN 242
|
....
gi 1124469102 198 QAEY 201
Cdd:PRK10535 243 TASG 246
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
297-464 |
5.08e-11 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 62.74 E-value: 5.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREKvyvVPGAKIGYARQNMSQIDLSQ------ 370
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLER---PDSGTILFGGEDATDVPVQErnvgfv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 371 ----------TVLVNV-------RRVSIQSES-ISRIVLARLLLSERD--MNKKASELSGGERMKLSFAMLFVSDVNLLI 430
Cdd:cd03296 80 fqhyalfrhmTVFDNVafglrvkPRSERPPEAeIRAKVHELLKLVQLDwlADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1124469102 431 LDEPTNYLDIPSVEALEKMLVEYEG----TLIFTSHDK 464
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDelhvTTVFVTHDQ 197
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
313-476 |
5.65e-11 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 62.75 E-value: 5.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 313 DDADFMIKNGSKVALLGGNGAGKTTLLELIN-----------------NREKVYVVpgAKIGYAR--QNmSQIDLSQTVL 373
Cdd:COG0411 21 DDVSLEVERGEIVGLIGPNGAGKTTLFNLITgfyrptsgrilfdgrdiTGLPPHRI--ARLGIARtfQN-PRLFPELTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 374 VNVR--RVSIQSESISRI--------------------VLARLLLSERdMNKKASELSGGERMKLSFAMLFVSDVNLLIL 431
Cdd:COG0411 98 ENVLvaAHARLGRGLLAAllrlprarreereareraeeLLERVGLADR-ADEPAGNLSYGQQRRLEIARALATEPKLLLL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1124469102 432 DEPT---NYLDIPSVEALEKMLVEYEG-TLIFTSHDKVFVDRIAtDRLY 476
Cdd:COG0411 177 DEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLVMGLA-DRIV 224
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
306-483 |
5.68e-11 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 62.16 E-value: 5.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 306 YDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINN-----------REKVYVVPGAKIGY-----ARQNmsqIDLS 369
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGiyppdsgtvtvRGRVSSLLGLGGGFnpeltGREN---IYLN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 370 QTVLvNVRRVSIQSESISRIVLARLllsERDMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIPSVE-ALEK 448
Cdd:cd03220 109 GRLL-GLSRKEIDEKIDEIIEFSEL---GDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEkCQRR 184
|
170 180 190
....*....|....*....|....*....|....*..
gi 1124469102 449 M--LVEYEGTLIFTSHDKVFVDRIATDRLYIGDGKIR 483
Cdd:cd03220 185 LreLLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
300-482 |
6.09e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 63.28 E-value: 6.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 300 EHISFAYDD--HVIFDDADFMIKNGSKVALLGGNGAGKTTLLELIN-------NREKVYVVPGA------------KIGY 358
Cdd:PRK13640 9 KHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINglllpddNPNSKITVDGItltaktvwdireKVGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 359 ARQNMSQIDLSQTVLVNVrRVSIQSESISR---IVLARLLLSERDM----NKKASELSGGERMKLSFAMLFVSDVNLLIL 431
Cdd:PRK13640 89 VFQNPDNQFVGATVGDDV-AFGLENRAVPRpemIKIVRDVLADVGMldyiDSEPANLSGGQKQRVAIAGILAVEPKIIIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1124469102 432 DEPTNYLDiPS-----VEALEKMLVEYEGTLIFTSHDkvfVDR--IATDRLYIGDGKI 482
Cdd:PRK13640 168 DESTSMLD-PAgkeqiLKLIRKLKKKNNLTVISITHD---IDEanMADQVLVLDDGKL 221
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
307-482 |
6.42e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 62.76 E-value: 6.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 307 DDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREKVY---VVPGAKIGYARQNMSQID---------------- 367
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYdskIKVDGKVLYFGKDIFQIDaiklrkevgmvfqqpn 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 368 --------------LSQTVLVNVRRVS-IQSESISRIVLARLLLSErdMNKKASELSGGERMKLSFAMLFVSDVNLLILD 432
Cdd:PRK14246 101 pfphlsiydniaypLKSHGIKEKREIKkIVEECLRKVGLWKEVYDR--LNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1124469102 433 EPTNYLDIPSVEALEKMLVEY--EGTLIFTSHDKVFVDRIATDRLYIGDGKI 482
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELknEIAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
297-482 |
7.78e-11 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 64.35 E-value: 7.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAY--DDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELInnrEKVYVVPGAKI---GYARQNMSQIDL--- 368
Cdd:TIGR02203 331 VEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLI---PRFYEPDSGQIlldGHDLADYTLASLrrq 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 369 ----SQ-------TVLVNV---RRVSIQSESISRIVLARLLLSERD---------MNKKASELSGGERMKLSFAMLFVSD 425
Cdd:TIGR02203 408 valvSQdvvlfndTIANNIaygRTEQADRAEIERALAAAYAQDFVDklplgldtpIGENGVLLSGGQRQRLAIARALLKD 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1124469102 426 VNLLILDEPTNYLDIPS---VEALEKMLVEYEGTLIFtSHdkvfvdRIAT----DR-LYIGDGKI 482
Cdd:TIGR02203 488 APILILDEATSALDNESerlVQAALERLMQGRTTLVI-AH------RLSTiekaDRiVVMDDGRI 545
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
6-64 |
7.81e-11 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 62.41 E-value: 7.81e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1124469102 6 LIKAENIVHSY----GEQTVL-DFDrFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVS 64
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALdDVS-LTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVL 69
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
6-176 |
8.69e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 62.73 E-value: 8.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSYGEQT--VLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIP-------------- 69
Cdd:PRK13635 5 IIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlseetvwdvrrqvg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 70 --------------------FFFEQFG-SDSEYFETDYAEAGKMGVADHIWQE--NVSGGEDTRIRLAQLFSSPHAVAFL 126
Cdd:PRK13635 85 mvfqnpdnqfvgatvqddvaFGLENIGvPREEMVERVDQALRQVGMEDFLNREphRLSGGQKQRVAIAGVLALQPDIIIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1124469102 127 DEPTSNLDYNG-VEMLK--KRLNEIETLVVIS--HDrsvLNEI--CDRIVEISFGKL 176
Cdd:PRK13635 165 DEATSMLDPRGrREVLEtvRQLKEQKGITVLSitHD---LDEAaqADRVIVMNKGEI 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
9-177 |
9.62e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 61.72 E-value: 9.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 9 AENI--VH------SYGEQ--TVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVS-------------- 64
Cdd:PRK10584 3 AENIveVHhlkksvGQGEHelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSlvgqplhqmdeear 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 65 ----SNCIPFFFEQF--------------------GSDSEYFETDYAEAGKMGVA---DHIwQENVSGGEDTRIRLAQLF 117
Cdd:PRK10584 83 aklrAKHVGFVFQSFmliptlnalenvelpallrgESSRQSRNGAKALLEQLGLGkrlDHL-PAQLSGGEQQRVALARAF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1124469102 118 SSPHAVAFLDEPTSNLDYNGVEMLKKRLNEIE-----TLVVISHDrSVLNEICDRIVEISFGKLQ 177
Cdd:PRK10584 162 NGRPDVLFADEPTGNLDRQTGDKIADLLFSLNrehgtTLILVTHD-LQLAARCDRRLRLVNGQLQ 225
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
316-482 |
1.01e-10 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 61.35 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 316 DFMIKNGSKVALLGGNGAGKTTLLELINNREK----VYVVPGAKIGYA-----------RQN--MSQIDLSQTVLV---- 374
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETpqsgRVLINGVDVTAAppadrpvsmlfQENnlFAHLTVEQNVGLglsp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 375 NVRRVSIQSESISRIvLARLLLSERDMnKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDiPSVEALEKMLV--- 451
Cdd:cd03298 98 GLKLTAEDRQAIEVA-LARVGLAGLEK-RLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALD-PALRAEMLDLVldl 174
|
170 180 190
....*....|....*....|....*....|...
gi 1124469102 452 --EYEGTLIFTSHDKVFVDRIATDRLYIGDGKI 482
Cdd:cd03298 175 haETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
27-164 |
1.02e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 61.00 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 27 FYLYEGEKVGLVGMNGAGKSTLLKILAG--ELEPTKGTVssncipfFFEqfGSDSEYFETDyaEAGKMG----------- 93
Cdd:cd03217 21 LTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEI-------LFK--GEDITDLPPE--ERARLGiflafqyppei 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 94 ----VADHIWQENV--SGGEDTRIRLAQLFSSPHAVAFLDEPTSNLDYNGVEMLKKRLNEI----ETLVVISHDRSVLNE 163
Cdd:cd03217 90 pgvkNADFLRYVNEgfSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLreegKSVLIITHYQRLLDY 169
|
.
gi 1124469102 164 I 164
Cdd:cd03217 170 I 170
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-176 |
1.02e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 62.40 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSY---------GEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPffFEQF- 75
Cdd:PRK10419 3 LLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEP--LAKLn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 76 GSDSEYFE-------------------------------TDYAEAGK----------MGVADHIWQE---NVSGGEDTRI 111
Cdd:PRK10419 81 RAQRKAFRrdiqmvfqdsisavnprktvreiireplrhlLSLDKAERlarasemlraVDLDDSVLDKrppQLSGGQLQRV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1124469102 112 RLAQ-LFSSPHAVaFLDEPTSNLDY----NGVEMLKKRLNEIET-LVVISHDRSVLNEICDRIVEISFGKL 176
Cdd:PRK10419 161 CLARaLAVEPKLL-ILDEAVSNLDLvlqaGVIRLLKKLQQQFGTaCLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-175 |
1.11e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 62.43 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQTVLD---FDrfyLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPFFFE---QFGsdse 80
Cdd:COG4152 2 LELKGLTKRFGDKTAVDdvsFT---VPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEdrrRIG---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 81 yfetdY--AEAG---KMGVADHI------------------------------WQENV---SGGEDTRIRLAQ-LFSSPH 121
Cdd:COG4152 75 -----YlpEERGlypKMKVGEQLvylarlkglskaeakrradewlerlglgdrANKKVeelSKGNQQKVQLIAaLLHDPE 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1124469102 122 AVaFLDEPTSNLDYNGVEMLK---KRLNEIETLVVIS-HDRSVLNEICDRIVEISFGK 175
Cdd:COG4152 150 LL-ILDEPFSGLDPVNVELLKdviRELAAKGTTVIFSsHQMELVEELCDRIVIINKGR 206
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-175 |
1.14e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 62.52 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVS---------------------- 64
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgepvpsrarharqrvgvvpq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 65 -SNCIPFF--FEQFGSDSEYFETDYAEAGKM--GVADHIWQEN--------VSGGEDTRIRLAQLFSSPHAVAFLDEPTS 131
Cdd:PRK13537 88 fDNLDPDFtvRENLLVFGRYFGLSAAAARALvpPLLEFAKLENkadakvgeLSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1124469102 132 NLDYNGVEMLKKRLNEI----ETLVVISHDRSVLNEICDRIVEISFGK 175
Cdd:PRK13537 168 GLDPQARHLMWERLRSLlargKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
314-483 |
1.25e-10 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 62.82 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 314 DADFMIKNGSKVALLGGNGAGKTTLLELINNREKVY----VVPGA----------------KIGYARQNMS---QIDLSQ 370
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDegeiVLNGRtlfdsrkgiflppekrRIGYVFQEARlfpHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 371 TVLVNVRRVSIQSESISRIVLARLLLSERDMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIPS----VEAL 446
Cdd:TIGR02142 95 NLRYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRkyeiLPYL 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 1124469102 447 EKMLVEYEGTLIFTSHDKVFVDRIATDRLYIGDGKIR 483
Cdd:TIGR02142 175 ERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVA 211
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
7-169 |
1.49e-10 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 59.89 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQTVLdFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCI-PFFFEQFGSdseyfetd 85
Cdd:cd03222 1 QLYPDCVKRYGVFFLL-VELGVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGItPVYKPQYID-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 86 yaeagkmgvadhiwqenVSGGEDTRIRLAQLFSSPHAVAFLDEPTSNLDYN---GVEMLKKRLNE--IETLVVISHDRSV 160
Cdd:cd03222 72 -----------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlNAARAIRRLSEegKKTALVVEHDLAV 134
|
....*....
gi 1124469102 161 LNEICDRIV 169
Cdd:cd03222 135 LDYLSDRIH 143
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
297-482 |
1.51e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 61.54 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLE----LINNREKVYVVPGA------------KIGYAR 360
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRtlsrLMTPAHGHVWLDGEhiqhyaskevarRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 361 QNMSQI-DLSQTVLVNVRRVSIQ----------SESISRIVLARLLLSERDMNkkASELSGGERMKLSFAMLFVSDVNLL 429
Cdd:PRK10253 88 QNATTPgDITVQELVARGRYPHQplftrwrkedEEAVTKAMQATGITHLADQS--VDTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1124469102 430 ILDEPTNYLDIPS----VEALEKMLVEYEGTLIFTSHDKVFVDRIATDRLYIGDGKI 482
Cdd:PRK10253 166 LLDEPTTWLDISHqidlLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKI 222
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-177 |
1.63e-10 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 61.20 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNC------------IPFFFEQ 74
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedatdvpvqernVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 75 fgsdseyfetdYAEAGKMGVADHI--------------------------------WQEN-----VSGGEDTRIRLAQLF 117
Cdd:cd03296 83 -----------YALFRHMTVFDNVafglrvkprserppeaeirakvhellklvqldWLADrypaqLSGGQRQRVALARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1124469102 118 SSPHAVAFLDEPTSNLDYNGVEMLKKRLNEIE-----TLVVISHDRSVLNEICDRIVEISFGKLQ 177
Cdd:cd03296 152 AVEPKVLLLDEPFGALDAKVRKELRRWLRRLHdelhvTTVFVTHDQEEALEVADRVVVMNKGRIE 216
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
32-176 |
1.80e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 61.34 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 32 GEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPFffEQFGSDSEYFETDY-------AEA--------------- 89
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPL--ESWSSKAFARKVAYlpqqlpaAEGmtvrelvaigrypwh 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 90 ---GKMGVAD-----------------HIWQENVSGGEDTRIRLAQLFSSPHAVAFLDEPTSNLDY-NGVEMLK--KRLN 146
Cdd:PRK10575 115 galGRFGAADrekveeaislvglkplaHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIaHQVDVLAlvHRLS 194
|
170 180 190
....*....|....*....|....*....|..
gi 1124469102 147 EIETLVVIS--HDRSVLNEICDRIVEISFGKL 176
Cdd:PRK10575 195 QERGLTVIAvlHDINMAARYCDYLVALRGGEM 226
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-175 |
2.74e-10 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 60.66 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQT-VLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIP---------------- 69
Cdd:cd03256 1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinklkgkalrqlrrqi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 70 -FFFEQFGSDSE------------------------YFETDYAEA----GKMGVADHIWQ--ENVSGGEDTRIRLAQLFS 118
Cdd:cd03256 81 gMIFQQFNLIERlsvlenvlsgrlgrrstwrslfglFPKEEKQRAlaalERVGLLDKAYQraDQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1124469102 119 SPHAVAFLDEPTSNLDYNG----VEMLKKRLNEIETLVVIS-HDRSVLNEICDRIVEISFGK 175
Cdd:cd03256 161 QQPKLILADEPVASLDPASsrqvMDLLKRINREEGITVIVSlHQVDLAREYADRIVGLKDGR 222
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
16-176 |
2.81e-10 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 61.25 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 16 YGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSN-------------CIPFFFEQFGSDS--- 79
Cdd:TIGR01188 3 YGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAgydvvreprkvrrSIGIVPQYASVDEdlt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 80 ---------------------------EYFETDYAEAGKMGvadhiwqeNVSGGEDTRIRLAQ-LFSSPhAVAFLDEPTS 131
Cdd:TIGR01188 83 grenlemmgrlyglpkdeaeeraeellELFELGEAADRPVG--------TYSGGMRRRLDIAAsLIHQP-DVLFLDEPTT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1124469102 132 NLD-------YNGVEMLKKrlnEIETLVVISHDRSVLNEICDRIVEISFGKL 176
Cdd:TIGR01188 154 GLDprtrraiWDYIRALKE---EGVTILLTTHYMEEADKLCDRIAIIDHGRI 202
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-64 |
3.09e-10 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 60.18 E-value: 3.09e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1124469102 7 IKAENIVHSYG----EQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVS 64
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVL 62
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
6-175 |
3.15e-10 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 59.95 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSYGEQT-VLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTV----------SSNCIPFF--- 71
Cdd:TIGR02673 1 MIEFHNVSKAYPGGVaALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVriagedvnrlRGRQLPLLrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 72 ----FEQF-------------------GSDS-EYFETDYAEAGKMGVADHIWQ--ENVSGGEDTRIRLAQ-LFSSPhAVA 124
Cdd:TIGR02673 81 igvvFQDFrllpdrtvyenvalplevrGKKErEIQRRVGAALRQVGLEHKADAfpEQLSGGEQQRVAIARaIVNSP-PLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1124469102 125 FLDEPTSNLD-YNGVEMLK--KRLNEIETLVVI-SHDRSVLNEICDRIVEISFGK 175
Cdd:TIGR02673 160 LADEPTGNLDpDLSERILDllKRLNKRGTTVIVaTHDLSLVDRVAHRVIILDDGR 214
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
294-463 |
3.33e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.51 E-value: 3.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 294 PIVIRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTL----LELINNRE-KVYVVPGAKIGYARQnmsQIDL 368
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLvrvvLGLVAPDEgVIKRNGKLRIGYVPQ---KLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 369 SQTVLVNVRRV-----SIQSESI----SRIVLARLLlsERDMNKkaseLSGGERMKLSFAMLFVSDVNLLILDEPTNYLD 439
Cdd:PRK09544 79 DTTLPLTVNRFlrlrpGTKKEDIlpalKRVQAGHLI--DAPMQK----LSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
170 180
....*....|....*....|....*...
gi 1124469102 440 IPSVEAL----EKMLVEYEGTLIFTSHD 463
Cdd:PRK09544 153 VNGQVALydliDQLRRELDCAVLMVSHD 180
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
301-469 |
3.99e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.19 E-value: 3.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 301 HISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNrekVYVVPGAKIGYARQNMSQiDLS----QTVLVNV 376
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAG---LLNPEKGEILFERQSIKK-DLCtyqkQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 377 RR---------------VSIQSESISRIVLARLLLSERDMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIP 441
Cdd:PRK13540 82 RSginpyltlrenclydIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL 161
|
170 180 190
....*....|....*....|....*....|.
gi 1124469102 442 SVEALEKMLVEYE---GTLIFTSHDKVFVDR 469
Cdd:PRK13540 162 SLLTIITKIQEHRakgGAVLLTSHQDLPLNK 192
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
306-483 |
3.99e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 60.10 E-value: 3.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 306 YDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELInnrekvyvvpgAKI-----GYARQNM---SQIDL------SQT 371
Cdd:COG1134 36 REEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLI-----------AGIleptsGRVEVNGrvsALLELgagfhpELT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 372 VLVNVRrvsiqsesisriVLARLL-LSERDMNKKA------SEL-----------SGGERMKLSFAMLFVSDVNLLILDE 433
Cdd:COG1134 105 GRENIY------------LNGRLLgLSRKEIDEKFdeivefAELgdfidqpvktySSGMRARLAFAVATAVDPDILLVDE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1124469102 434 PTNYLDIPSVE-ALEKM--LVEYEGTLIFTSHDKVFVDRIATDRLYIGDGKIR 483
Cdd:COG1134 173 VLAVGDAAFQKkCLARIreLRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLV 225
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
293-463 |
4.37e-10 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 60.10 E-value: 4.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 293 NPIVIRGEHISFAY----DDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELI------------NNREKVyVVPGAKI 356
Cdd:COG1116 4 AAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIaglekptsgevlVDGKPV-TGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 357 GYARQN------MsqidlsqTVLVNV------RRVSiQSESISRI--VLARLLLSERdMNKKASELSGGERMKLSFAMLF 422
Cdd:COG1116 83 GVVFQEpallpwL-------TVLDNValglelRGVP-KAERRERAreLLELVGLAGF-EDAYPHQLSGGMRQRVAIARAL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1124469102 423 VSDVNLLILDEPTNYLDIPSVEALEKMLVEY---EG-TLIFTSHD 463
Cdd:COG1116 154 ANDPEVLLMDEPFGALDALTRERLQDELLRLwqeTGkTVLFVTHD 198
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
297-482 |
4.52e-10 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 58.38 E-value: 4.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDD--HVIFDDADFMIKNGSKVALLGGNGAGKTTLLELI-----NNREKVYvVPGAKIgyarqnmSQIDLS 369
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLIlgllrPTSGRVR-LDGADI-------SQWDPN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 370 ---QTVLVNVRRVSIQSESISRIVlarlllserdmnkkaseLSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIPSVEAL 446
Cdd:cd03246 73 elgDHVGYLPQDDELFSGSIAENI-----------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERAL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1124469102 447 E---KMLVEYEGTLIFTSHDKVF---VDRIatdrLYIGDGKI 482
Cdd:cd03246 136 NqaiAALKAAGATRIVIAHRPETlasADRI----LVLEDGRV 173
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
307-468 |
4.85e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.05 E-value: 4.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 307 DDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELIN------------------------NREKVYvvpgakIGYArqn 362
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAglarpdagevlwqgepirrqrdeyHQDLLY------LGHQ--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 363 mSQIDLSQTVLVNVR---RVS-IQSESISRIVLARLLLSERdMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYL 438
Cdd:PRK13538 83 -PGIKTELTALENLRfyqRLHgPGDDEALWEALAQVGLAGF-EDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170 180 190
....*....|....*....|....*....|...
gi 1124469102 439 DIPSVEALEKML---VEYEGTLIFTSHDKVFVD 468
Cdd:PRK13538 161 DKQGVARLEALLaqhAEQGGMVILTTHQDLPVA 193
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
329-470 |
5.18e-10 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 59.16 E-value: 5.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 329 GGNGAGKTTLLE---------LINNREKVYVVPgaKIGYARQNMSQIDLSQTVLVNVRRVSIQSESISRIVL-------A 392
Cdd:cd03240 29 GQNGAGKTTIIEalkyaltgeLPPNSKGGAHDP--KLIREGEVRAQVKLAFENANGKKYTITRSLAILENVIfchqgesN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 393 RLLLSERDmnkkasELSGGERMKLSF------AMLFVSDVNLLILDEPTNYLDIPS-----VEALEKMLVEYEGTLIFTS 461
Cdd:cd03240 107 WPLLDMRG------RCSGGEKVLASLiirlalAETFGSNCGILALDEPTTNLDEENieeslAEIIEERKSQKNFQLIVIT 180
|
....*....
gi 1124469102 462 HDKVFVDRI 470
Cdd:cd03240 181 HDEELVDAA 189
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
295-440 |
6.43e-10 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 59.79 E-value: 6.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 295 IVIRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNrekvYVVPGA-KIGYARQNMSQIDLSQtvL 373
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSG----ELSPDSgEVRLNGRPLADWSPAE--L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 374 VNVRRVSIQSESIS------------------------RIVLARLL------LSERDMnkkaSELSGGERMKLSFAMLFV 423
Cdd:PRK13548 75 ARRRAVLPQHSSLSfpftveevvamgraphglsraeddALVAAALAqvdlahLAGRDY----PQLSGGEQQRVQLARVLA 150
|
170 180
....*....|....*....|...
gi 1124469102 424 ------SDVNLLILDEPTNYLDI 440
Cdd:PRK13548 151 qlwepdGPPRWLLLDEPTSALDL 173
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
7-190 |
6.50e-10 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 61.68 E-value: 6.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYG-EQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCI----------------- 68
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFslkdidrhtlrqfinyl 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 69 ---PFFF-------------EQFGSDSEYFETDYAEAGK------MGVADHIWQE--NVSGGEDTRIRLAQLFSSPHAVA 124
Cdd:TIGR01193 554 pqePYIFsgsilenlllgakENVSQDEIWAACEIAEIKDdienmpLGYQTELSEEgsSISGGQKQRIALARALLTDSKVL 633
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1124469102 125 FLDEPTSNLD-YNGVEMLKKRLNEIE-TLVVISHDRSVlNEICDRIVEISFGKLQNySGNYDEYVVQK 190
Cdd:TIGR01193 634 ILDESTSNLDtITEKKIVNNLLNLQDkTIIFVAHRLSV-AKQSDKIIVLDHGKIIE-QGSHDELLDRN 699
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
6-169 |
7.05e-10 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 60.50 E-value: 7.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSYGEQTVL-DFDrFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVS------SNCIP------FFF 72
Cdd:COG3842 5 ALELENVSKRYGDVTALdDVS-LSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILldgrdvTGLPPekrnvgMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 73 eQfgsdseyfetDYAEAGKMGVAdhiwqENV--------------------------------------SGGEDTRIRLA 114
Cdd:COG3842 84 -Q----------DYALFPHLTVA-----ENVafglrmrgvpkaeirarvaellelvglegladryphqlSGGQQQRVALA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1124469102 115 QlfssphAVAF------LDEPTSNLDYNG-VEM---LKKRLNEIE-TLVVISHDRSvlnE---ICDRIV 169
Cdd:COG3842 148 R------ALAPeprvllLDEPLSALDAKLrEEMreeLRRLQRELGiTFIYVTHDQE---EalaLADRIA 207
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
6-176 |
7.80e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 58.73 E-value: 7.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSY--GEQTVLDFDrFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTV----------SSNCIPFFFE 73
Cdd:PRK10908 1 MIRFEHVSKAYlgGRQALQGVT-FHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghditrlKNREVPFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 74 QFG---------------------------SDSEYFETDYAEAGKMGVADHI--WQENVSGGEDTRIRLAQLFSSPHAVA 124
Cdd:PRK10908 80 QIGmifqdhhllmdrtvydnvaipliiagaSGDDIRRRVSAALDKVGLLDKAknFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1124469102 125 FLDEPTSNLD---YNGVEMLKKRLNEIE-TLVVISHDRSVLNEICDRIVEISFGKL 176
Cdd:PRK10908 160 LADEPTGNLDdalSEGILRLFEEFNRVGvTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-168 |
9.49e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 57.00 E-value: 9.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 32 GEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPFFFEQfgsdseyfetdyAEAGKMGVADHIWQENVSGGEDTRI 111
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEE------------VLDQLLLIIVGGKKASGSGELRLRL 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1124469102 112 RLAQLFSSPHAVAFLDEPTSNLDYNGVEMLKKRLNEIE----------TLVVISHDRSVLNEICDRI 168
Cdd:smart00382 70 ALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLllllkseknlTVILTTNDEKDLGPALLRR 136
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
7-63 |
9.64e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 60.95 E-value: 9.64e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1124469102 7 IKAENIVHSY-GEQTVL-DFDrFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTV 63
Cdd:COG1132 340 IEFENVSFSYpGDRPVLkDIS-LTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRI 397
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
297-482 |
1.01e-09 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 58.71 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELIN-----NREKVYV-------VP-----GAKIGYA 359
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVglvkpDSGKILLdgqditkLPmhkraRLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 360 RQNMSqIDLSQTVLVNVRRVSIQSESISRIVLARL--LLSERDM----NKKASELSGGERMKLSFAMLFVSDVNLLILDE 433
Cdd:cd03218 81 PQEAS-IFRKLTVEENILAVLEIRGLSKKEREEKLeeLLEEFHIthlrKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1124469102 434 PTNYLDIPSVEALEKMLVEYE----GTLIfTSHDkvfVDRI--ATDRLYI-GDGKI 482
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKdrgiGVLI-TDHN---VRETlsITDRAYIiYEGKV 211
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
317-463 |
1.02e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 58.79 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 317 FMIKNGSKVALLGGNGAGKTTLLE----LINNREKVYV-------VPGAKIGYARQNMSQ-------------IDLSQTV 372
Cdd:PRK03695 17 AEVRAGEILHLVGPNGAGKSTLLArmagLLPGSGSIQFagqpleaWSAAELARHRAYLSQqqtppfampvfqyLTLHQPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 373 LVNVRrvsiQSESISRIVLARLLLSERdMNKKASELSGGE--RMKLSFAMLFV-SDVN----LLILDEPTNYLDIPSVEA 445
Cdd:PRK03695 97 KTRTE----AVASALNEVAEALGLDDK-LGRSVNQLSGGEwqRVRLAAVVLQVwPDINpagqLLLLDEPMNSLDVAQQAA 171
|
170 180
....*....|....*....|.
gi 1124469102 446 LEKMLVEYE---GTLIFTSHD 463
Cdd:PRK03695 172 LDRLLSELCqqgIAVVMSSHD 192
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
311-482 |
1.27e-09 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 59.05 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 311 IFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREKvyvvPG-AKIGYARQNMSQIDLS---------QTVL------V 374
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEK----PAqGTVSFRGQDLYQLDRKqrrafrrdvQLVFqdspsaV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 375 NVRRVSIQ--------------SESISRI--VLARLLLSERDMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYL 438
Cdd:TIGR02769 102 NPRMTVRQiigeplrhltsldeSEQKARIaeLLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1124469102 439 DI----PSVEALEKMLVEYEGTLIFTSHDKVFVDRIATDRLYIGDGKI 482
Cdd:TIGR02769 182 DMvlqaVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-177 |
1.42e-09 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 58.40 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTV-----SSNCIPFFFEQFGSdseY 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEIlldgkDITNLPPHKRPVNT---V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 82 FEtDYAEAGKMGVADHI-------------WQENV--------------------SGGEDTRIRLAQLFSSPHAVAFLDE 128
Cdd:cd03300 78 FQ-NYALFPHLTVFENIafglrlkklpkaeIKERVaealdlvqlegyanrkpsqlSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1124469102 129 PTSNLDYNGVEMLKKRLNEIE-----TLVVISHDRSVLNEICDRIVEISFGKLQ 177
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQkelgiTFVFVTHDQEEALTMSDRIAVMNKGKIQ 210
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
6-63 |
2.00e-09 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 58.13 E-value: 2.00e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1124469102 6 LIKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTV 63
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRI 61
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-176 |
2.01e-09 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 57.76 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSYG--EQTVLDFDR--FYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGT-------VSSNC------I 68
Cdd:cd03266 1 MITADALTKRFRdvKKTVQAVDGvsFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFatvdgfdVVKEPaearrrL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 69 PFFFEQFG--------SDSEYF------ETDYAEA------GKMGVADHIWQ--ENVSGGEDTRIRLAQ-LFSSPhAVAF 125
Cdd:cd03266 81 GFVSDSTGlydrltarENLEYFaglyglKGDELTArleelaDRLGMEELLDRrvGGFSTGMRQKVAIARaLVHDP-PVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1124469102 126 LDEPTSNLDYNGVEMLKKRLNEI----ETLVVISHDRSVLNEICDRIVEISFGKL 176
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLralgKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
300-471 |
2.01e-09 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 58.96 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 300 EHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELI-------------NNREKVYVVPGA-KIGYARQN--- 362
Cdd:COG3842 9 ENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIagfetpdsgrillDGRDVTGLPPEKrNVGMVFQDyal 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 363 ---MsqidlsqTVLVNV------RRVSiqSESISRIV---LARLLLSERDmNKKASELSGGERMKLSFAMLFVSDVNLLI 430
Cdd:COG3842 89 fphL-------TVAENVafglrmRGVP--KAEIRARVaelLELVGLEGLA-DRYPHQLSGGQQQRVALARALAPEPRVLL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1124469102 431 LDEPTNYLDIPSVEALEKMLV----EYEGTLIFTSHDK----VFVDRIA 471
Cdd:COG3842 159 LDEPLSALDAKLREEMREELRrlqrELGITFIYVTHDQeealALADRIA 207
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
6-176 |
2.02e-09 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 57.87 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSY---GEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTV--SSNCI------------ 68
Cdd:cd03248 11 IVKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVllDGKPIsqyehkylhskv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 69 ------PFFFEQ-------FGSDSEYFETDYAEAGK-------MGVADHIWQE------NVSGGEDTRIRLAQLFSSPHA 122
Cdd:cd03248 91 slvgqePVLFARslqdniaYGLQSCSFECVKEAAQKahahsfiSELASGYDTEvgekgsQLSGGQKQRVAIARALIRNPQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1124469102 123 VAFLDEPTSNLDYNGVEMLKKRL---NEIETLVVISHDRSVLnEICDRIVEISFGKL 176
Cdd:cd03248 171 VLILDEATSALDAESEQQVQQALydwPERRTVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-196 |
2.05e-09 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 57.94 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKG------------------------- 61
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGkilldgqditklpmhkrarlgigyl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 62 ----------TVSSNcIPFFFEQFGSDSEYFETDYAE----------AGKMGVAdhiwqenVSGGEDTRIRLAQLFSSPH 121
Cdd:cd03218 81 pqeasifrklTVEEN-ILAVLEIRGLSKKEREEKLEElleefhithlRKSKASS-------LSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 122 AVAFLDEPTSNLDYNGVEMLK---KRLNEIETLVVIS-HD-RSVLnEICDRIVEISFGKLQnYSGNYDEyVVQKEEQRKT 196
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQkiiKILKDRGIGVLITdHNvRETL-SITDRAYIIYEGKVL-AEGTPEE-IAANELVRKV 229
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
311-439 |
2.31e-09 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 56.87 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 311 IFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREKVYVVPGA--------------KIGYARQNMSQIDlSQTVlvnv 376
Cdd:cd03232 22 LLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGVITGEilingrpldknfqrSTGYVEQQDVHSP-NLTV---- 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1124469102 377 rRVSIQSESISRivlarlllserdmnkkasELSGGERMKLSFAMLFVSDVNLLILDEPTNYLD 439
Cdd:cd03232 97 -REALRFSALLR------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
7-64 |
2.48e-09 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 57.44 E-value: 2.48e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1124469102 7 IKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVS 64
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIR 58
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
6-63 |
2.49e-09 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 57.68 E-value: 2.49e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1124469102 6 LIKAENIVHSYGEQTVL---DFDrfyLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTV 63
Cdd:COG0410 3 MLEVENLHAGYGGIHVLhgvSLE---VEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSI 60
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
297-440 |
2.52e-09 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 57.79 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELInnrekvyvvpgakigyAR-QNMSQ-------IDL 368
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMI----------------SRlLPPDSgevlvdgLDV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 369 SQT---VLvnVRRVSI--QSESI-SRIVLARLL-----------LSERDMNK--KA--------------SELSGGERMK 415
Cdd:COG4604 66 ATTpsrEL--AKRLAIlrQENHInSRLTVRELVafgrfpyskgrLTAEDREIidEAiayldledladrylDELSGGQRQR 143
|
170 180
....*....|....*....|....*
gi 1124469102 416 LSFAMLFVSDVNLLILDEPTNYLDI 440
Cdd:COG4604 144 AFIAMVLAQDTDYVLLDEPLNNLDM 168
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
6-176 |
2.54e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 58.17 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSYGEQT-VLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPFFFEQFG-------- 76
Cdd:PRK13639 1 ILETRDLKYSYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllevrktv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 77 ------SDSEYF----ETDYAEAG-KMGVADHIWQENV--------------------SGGEDTRIRLAQLFSSPHAVAF 125
Cdd:PRK13639 81 givfqnPDDQLFaptvEEDVAFGPlNLGLSKEEVEKRVkealkavgmegfenkpphhlSGGQKKRVAIAGILAMKPEIIV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1124469102 126 LDEPTSNLDYNGVEMLKKRLNEIE----TLVVISHDRSVLNEICDRIVEISFGKL 176
Cdd:PRK13639 161 LDEPTSGLDPMGASQIMKLLYDLNkegiTIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
7-175 |
3.12e-09 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 57.07 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQTvLDFDrFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNcipfffeqfGSD-------- 78
Cdd:COG3840 2 LRLDDLTYRYGDFP-LRFD-LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWN---------GQDltalppae 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 79 ---SEYF--------------------------ETDYAE----AGKMGVADHIWQ--ENVSGGEDTRIRLAQLFSSPHAV 123
Cdd:COG3840 71 rpvSMLFqennlfphltvaqniglglrpglkltAEQRAQveqaLERVGLAGLLDRlpGQLSGGQRQRVALARCLVRKRPI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1124469102 124 AFLDEPTSNLDYN-GVEMLkKRLNEIE-----TLVVISHDrsvLNE---ICDRIVEISFGK 175
Cdd:COG3840 151 LLLDEPFSALDPAlRQEML-DLVDELCrerglTVLMVTHD---PEDaarIADRVLLVADGR 207
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
292-482 |
3.23e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 57.62 E-value: 3.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 292 RNPIVIRGEHISFAydDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREKVYvvPGAKI-GYAR---QNMSQID 367
Cdd:PRK14247 1 MNKIEIRDLKVSFG--QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELY--PEARVsGEVYldgQDIFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 368 LSQTvlvnVRRVS--------IQSESI----------SRIVLARLLLSER----------------DMNKKASELSGGER 413
Cdd:PRK14247 77 VIEL----RRRVQmvfqipnpIPNLSIfenvalglklNRLVKSKKELQERvrwalekaqlwdevkdRLDAPAGKLSGGQQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1124469102 414 MKLSFAMLFVSDVNLLILDEPTNYLDIPSVEALEKMLVEY--EGTLIFTSHDKVFVDRIATDRLYIGDGKI 482
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELkkDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
297-482 |
3.84e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 56.90 E-value: 3.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDD-HVIFDdadFMIKNGSKVALLGGNGAGKTTLLELI-------------NNREKVYVVPgakigyARQN 362
Cdd:PRK10771 2 LKLTDITWLYHHlPMRFD---LTVERGERVAILGPSGAGKSTLLNLIagfltpasgsltlNGQDHTTTPP------SRRP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 363 MSQidLSQ--------TVLVNV--------RRVSIQSESISRIvlARLLLSERDMNKKASELSGGERMKLSFAMLFVSDV 426
Cdd:PRK10771 73 VSM--LFQennlfshlTVAQNIglglnpglKLNAAQREKLHAI--ARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1124469102 427 NLLILDEPTNYLDiPsveAL-EKMLV-------EYEGTLIFTSHDKVFVDRIATDRLYIGDGKI 482
Cdd:PRK10771 149 PILLLDEPFSALD-P---ALrQEMLTlvsqvcqERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
7-190 |
3.97e-09 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 56.85 E-value: 3.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQT-VLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPF-------FFEQFG-- 76
Cdd:cd03254 3 IEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIrdisrksLRSMIGvv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 77 -----------------SDSEYFETDYAEAGKMGVADHIWQ--------------ENVSGGEDTRIRLAQLFSSPHAVAF 125
Cdd:cd03254 83 lqdtflfsgtimenirlGRPNATDEEVIEAAKEAGAHDFIMklpngydtvlgengGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1124469102 126 LDEPTSNLDYNGVEMLK---KRLNEIETLVVISHDRSVLNEiCDRIVEISFGKLQNySGNYDEYVVQK 190
Cdd:cd03254 163 LDEATSNIDTETEKLIQealEKLMKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIE-EGTHDELLAKK 228
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
296-482 |
4.72e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 57.44 E-value: 4.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 296 VIRGEHISFAY-DDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELIN-----NREKVYVVPGA-----------KIGY 358
Cdd:PRK13647 4 IIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNgiylpQRGRVKVMGREvnaenekwvrsKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 359 ARQNMSQIDLSQTVLVNVRRVSI-----QSESISRIVLARLLLSERDMNKKAS-ELSGGERMKLSFAMLFVSDVNLLILD 432
Cdd:PRK13647 84 VFQDPDDQVFSSTVWDDVAFGPVnmgldKDEVERRVEEALKAVRMWDFRDKPPyHLSYGQKKRVAIAGVLAMDPDVIVLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1124469102 433 EPTNYLDIPSVEALEKMLVEY--EG-TLIFTSHDKVFVDRIATDRLYIGDGKI 482
Cdd:PRK13647 164 EPMAYLDPRGQETLMEILDRLhnQGkTVIVATHDVDLAAEWADQVIVLKEGRV 216
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-157 |
5.00e-09 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 56.42 E-value: 5.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAG-----ELEPTKGTVssncipFFFEQ------- 74
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEV------LLDGKdiydldv 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 75 ----------------------------FG------SDSEYFETDYAEAGKMG-----VADHIWQENVSGGEDTRIRLAQ 115
Cdd:cd03260 75 dvlelrrrvgmvfqkpnpfpgsiydnvaYGlrlhgiKLKEELDERVEEALRKAalwdeVKDRLHALGLSGGQQQRLCLAR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1124469102 116 LFSSPHAVAFLDEPTSNLD---YNGVEMLKKRLNEIETLVVISHD 157
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDpisTAKIEELIAELKKEYTIVIVTHN 199
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-482 |
5.05e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.49 E-value: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 22 LDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSN---CIPFFFEQ----------------FGSDSEYF 82
Cdd:PRK10938 19 LQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQfshITRLSFEQlqklvsdewqrnntdmLSPGEDDT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 83 ETDYAEAGKMGVAD-----------HIWQ------ENVSGGEDTRIRLAQ-LFSSPHaVAFLDEPTSNLDYNGVEMLKKR 144
Cdd:PRK10938 99 GRTTAEIIQDEVKDparceqlaqqfGITAlldrrfKYLSTGETRKTLLCQaLMSEPD-LLILDEPFDGLDVASRQQLAEL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 145 LNEIE----TLVVIShDRsvLNEICDRIVEIsfGKLQNYsgnydEYVVQKEEQRKTQQAEYEnyqaekkrlQSVYVEKKA 220
Cdd:PRK10938 178 LASLHqsgiTLVLVL-NR--FDEIPDFVQFA--GVLADC-----TLAETGEREEILQQALVA---------QLAHSEQLE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 221 kaktvdkkpknmsaseakvrafiGNRKPEDKArgiersatnvlkrlehmeikekpkeeltvrPDFRLTNPP-RNPIVIRG 299
Cdd:PRK10938 239 -----------------------GVQLPEPDE------------------------------PSARHALPAnEPRIVLNN 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 300 EHISfaYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELI--------NNR-----------EKVYVVPgAKIGYAR 360
Cdd:PRK10938 266 GVVS--YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgySNDltlfgrrrgsgETIWDIK-KHIGYVS 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 361 qnmSQIDLSQTVLVNVRRVSIQ----SESISRIV-----------LARLLLSERDMNKKASELSGGERMKLSFAMLFVSD 425
Cdd:PRK10938 343 ---SSLHLDYRVSTSVRNVILSgffdSIGIYQAVsdrqqklaqqwLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKH 419
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1124469102 426 VNLLILDEPTNYLDiPSVEAL-----EKMLVEYEGTLIFTSHDKVFVDRIATDRL-YIGDGKI 482
Cdd:PRK10938 420 PTLLILDEPLQGLD-PLNRQLvrrfvDVLISEGETQLLFVSHHAEDAPACITHRLeFVPDGDI 481
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
307-462 |
5.11e-09 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 55.24 E-value: 5.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 307 DDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINN-----REKVYVVPGAKIGYarqnmsqidLSQT---VLVNVRR 378
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGlwpwgSGRIGMPEGEDLLF---------LPQRpylPLGTLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 379 VSIQSESisrivlarlllserdmnkkaSELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIPSVEALEKMLVEYEGTLI 458
Cdd:cd03223 83 QLIYPWD--------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVI 142
|
....
gi 1124469102 459 FTSH 462
Cdd:cd03223 143 SVGH 146
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
6-166 |
5.33e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 57.44 E-value: 5.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSY------GEQTVLDFDrFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCI----------- 68
Cdd:PRK13643 1 MIKFEKVNYTYqpnspfASRALFDID-LEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIvvsstskqkei 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 69 ---------------------------PFFFEQFGSDSEYFETDYAEAGKM-GVADHIWQEN---VSGGEDTRIRLAQLF 117
Cdd:PRK13643 80 kpvrkkvgvvfqfpesqlfeetvlkdvAFGPQNFGIPKEKAEKIAAEKLEMvGLADEFWEKSpfeLSGGQMRRVAIAGIL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1124469102 118 SSPHAVAFLDEPTSNLDYNG-VEMLK--KRLNEI-ETLVVISHdrsVLNEICD 166
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKArIEMMQlfESIHQSgQTVVLVTH---LMDDVAD 209
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
305-465 |
5.62e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 57.73 E-value: 5.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 305 AYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREKV-----YV-------VPGAKIG-------YA------ 359
Cdd:PRK11000 12 AYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDItsgdlFIgekrmndVPPAERGvgmvfqsYAlyphls 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 360 -RQNMSqIDLSqtvLVNVRRVSIQS--ESISRIV-LARLLlserdmNKKASELSGGERMKLSFAMLFVSDVNLLILDEPT 435
Cdd:PRK11000 92 vAENMS-FGLK---LAGAKKEEINQrvNQVAEVLqLAHLL------DRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 1124469102 436 NYLDipsvEALE-KMLVE-------YEGTLIFTSHDKV 465
Cdd:PRK11000 162 SNLD----AALRvQMRIEisrlhkrLGRTMIYVTHDQV 195
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
322-474 |
6.07e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 54.69 E-value: 6.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 322 GSKVALLGGNGAGKTTLLELInnrekvyvvpgakIGYARQNMSQIdlsqtvlvnvrrVSIQSESISRIVLARLLLSERDM 401
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARAL-------------ARELGPPGGGV------------IYIDGEDILEEVLDQLLLIIVGG 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 402 NKKasELSGGERMKLSFAMLFVSDVNLLILDEPTNYLD---------IPSVEALEKMLVEYEGTLIFTSHDKVFVDRIAT 472
Cdd:smart00382 57 KKA--SGSGELRLRLALALARKLKPDVLILDEITSLLDaeqeallllLEELRLLLLLKSEKNLTVILTTNDEKDLGPALL 134
|
..
gi 1124469102 473 DR 474
Cdd:smart00382 135 RR 136
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
297-451 |
6.16e-09 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 56.47 E-value: 6.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDDHV--IFDDADFMIKNGSKVALLGGNGAGKTTLLELI----------------NNREKVYVVPGAKIGY 358
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIprfydvdsgrilidghDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 359 ARQNMsqIDLSQTVLVNVR--RVSIQSESI---SRIVLARLLLSERD------MNKKASELSGGERMKLSFAMLFVSDVN 427
Cdd:cd03251 81 VSQDV--FLFNDTVAENIAygRPGATREEVeeaARAANAHEFIMELPegydtvIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180
....*....|....*....|....*...
gi 1124469102 428 LLILDEPTNYLDIPS----VEALEKMLV 451
Cdd:cd03251 159 ILILDEATSALDTESerlvQAALERLMK 186
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
300-471 |
6.24e-09 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 57.39 E-value: 6.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 300 EHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELI-------------NNREKVYVVPGA-KIG-----YA- 359
Cdd:COG3839 7 ENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIagledptsgeiliGGRDVTDLPPKDrNIAmvfqsYAl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 360 ------RQNMS-----------QIDlsqtvlvnvRRVsiqsESISRIV-LARLLlserdmNKKASELSGGERMKLSFAML 421
Cdd:COG3839 87 yphmtvYENIAfplklrkvpkaEID---------RRV----REAAELLgLEDLL------DRKPKQLSGGQRQRVALGRA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1124469102 422 FVSDVNLLILDEPTNYLDIPSVEALE----KMLVEYEGTLIFTSHDKV----FVDRIA 471
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDAKLRVEMRaeikRLHRRLGTTTIYVTHDQVeamtLADRIA 205
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
32-169 |
7.27e-09 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 55.55 E-value: 7.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 32 GEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPFFFEQ--------------FGS--DSEYFET----------- 84
Cdd:cd03250 31 GELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQepwiqngtirenilFGKpfDEERYEKvikacalepdl 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 85 ------DYAEAGKMGVadhiwqeNVSGGEDTRIRLAQLFSSPHAVAFLDEPTSNLD-------YNGVemLKKRLNEIETL 151
Cdd:cd03250 111 eilpdgDLTEIGEKGI-------NLSGGQKQRISLARAVYSDADIYLLDDPLSAVDahvgrhiFENC--ILGLLLNNKTR 181
|
170
....*....|....*...
gi 1124469102 152 VVISHDRSVLnEICDRIV 169
Cdd:cd03250 182 ILVTHQLQLL-PHADQIV 198
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
300-442 |
7.32e-09 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 56.34 E-value: 7.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 300 EHISFAY--DDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELInnrEKVYVVPGAKIGYARQNMSQID---------- 367
Cdd:cd03252 4 EHVRFRYkpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLI---QRFYVPENGRVLVDGHDLALADpawlrrqvgv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 368 -LSQTVLVN---VRRVSIQSE--SISRIVLARLLLSERD------------MNKKASELSGGERMKLSFAMLFVSDVNLL 429
Cdd:cd03252 81 vLQENVLFNrsiRDNIALADPgmSMERVIEAAKLAGAHDfiselpegydtiVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170
....*....|...
gi 1124469102 430 ILDEPTNYLDIPS 442
Cdd:cd03252 161 IFDEATSALDYES 173
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
296-483 |
7.37e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 55.94 E-value: 7.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 296 VIRGEH-ISfayddhvIFDDADFMIKNGSKVALLGGNGAGKTTLLELIN--------------------NREKVYVVPGA 354
Cdd:PRK10584 16 VGQGEHeLS-------ILTGVELVVKRGETIALIGESGSGKSTLLAILAglddgssgevslvgqplhqmDEEARAKLRAK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 355 KIGYARQNMSQIDlSQTVLVNVRRVSI-------QSESISRIVLARLLLSERdMNKKASELSGGERMKLSFAMLFVSDVN 427
Cdd:PRK10584 89 HVGFVFQSFMLIP-TLNALENVELPALlrgessrQSRNGAKALLEQLGLGKR-LDHLPAQLSGGEQQRVALARAFNGRPD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 428 LLILDEPTNYLDIPSVEALEKMLV----EYEGTLIFTSHDKVFVDRiATDRLYIGDGKIR 483
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIADLLFslnrEHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQ 225
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
6-145 |
7.42e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.01 E-value: 7.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPF-------FFEQFG-- 76
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAtrgdrsrFMAYLGhl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 77 ----SDSEYFETDY-------AEAGKM--------GVADH--IWQENVSGGEDTRIRLAQLFSSPHAVAFLDEPTSNLDY 135
Cdd:PRK13543 91 pglkADLSTLENLHflcglhgRRAKQMpgsalaivGLAGYedTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
170
....*....|
gi 1124469102 136 NGVEMLKKRL 145
Cdd:PRK13543 171 EGITLVNRMI 180
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
318-439 |
7.57e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 58.13 E-value: 7.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 318 MIKNGSKVALLGGNGAGKTTLLELINNR-------EKVYVVPGAKIGyaRQNMSQI-------DL---SQTVL------- 373
Cdd:TIGR00955 47 VAKPGELLAVMGSSGAGKTTLMNALAFRspkgvkgSGSVLLNGMPID--AKEMRAIsayvqqdDLfipTLTVRehlmfqa 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1124469102 374 -VNVRRVSIQSESISRI--VLARL-LLSERDM-----NKKASeLSGGERMKLSFAMLFVSDVNLLILDEPTNYLD 439
Cdd:TIGR00955 125 hLRMPRRVTKKEKRERVdeVLQALgLRKCANTrigvpGRVKG-LSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
300-435 |
7.76e-09 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 56.14 E-value: 7.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 300 EHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELI-------------NNRE----KVYVVPGAKIGYARQN 362
Cdd:COG0410 7 ENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAIsgllpprsgsirfDGEDitglPPHRIARLGIGYVPEG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 363 MsQIDLSQTVLVNVR---RVSIQSESISRIvLARLL-----LSERdMNKKASELSGGERMKLSFAMLFVSDVNLLILDEP 434
Cdd:COG0410 87 R-RIFPSLTVEENLLlgaYARRDRAEVRAD-LERVYelfprLKER-RRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEP 163
|
.
gi 1124469102 435 T 435
Cdd:COG0410 164 S 164
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
7-63 |
7.94e-09 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 57.39 E-value: 7.94e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQTVL---DFDrfyLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTV 63
Cdd:COG3839 4 LELENVSKSYGGVEALkdiDLD---IEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEI 60
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
7-175 |
8.10e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 56.59 E-value: 8.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQT-----VLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPF----------- 70
Cdd:PRK13637 3 IKIENLTHIYMEGTpfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkkvklsdir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 71 -------------FFEQ-------FG------SDSEYFETDYAEAGKMGVADHIWQE----NVSGGEDTRIRLAQLFSSP 120
Cdd:PRK13637 83 kkvglvfqypeyqLFEEtiekdiaFGpinlglSEEEIENRVKRAMNIVGLDYEDYKDkspfELSGGQKRRVAIAGVVAME 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1124469102 121 HAVAFLDEPTSNLDYNGVEMLkkrLNEIE--------TLVVISHDRSVLNEICDRIVEISFGK 175
Cdd:PRK13637 163 PKILILDEPTAGLDPKGRDEI---LNKIKelhkeynmTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-145 |
8.53e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.58 E-value: 8.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 22 LDFDrfyLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPFF--FEQFGSDSEY-------------FE--T 84
Cdd:PRK13538 20 LSFT---LNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRrqRDEYHQDLLYlghqpgikteltaLEnlR 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1124469102 85 DYAEAGKMGVADHIWQ----------ENV-----SGGEDTRIRLAQLFSSPHAVAFLDEPTSNLDYNGVEMLKKRL 145
Cdd:PRK13538 97 FYQRLHGPGDDEALWEalaqvglagfEDVpvrqlSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALL 172
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
6-197 |
9.96e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 56.35 E-value: 9.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSY-GEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTV--------SSNC--------- 67
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVlirgepitKENIrevrkfvgl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 68 -----------------IPFFFEQFGSDSEYFETDYAEAGKMGVADHIWQE---NVSGGEDTRIRLAQLFSSPHAVAFLD 127
Cdd:PRK13652 83 vfqnpddqifsptveqdIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRvphHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1124469102 128 EPTSNLDYNGVEMLKKRLNEIE-----TLVVISHDRSVLNEICDRIVEISFGKLQNYsGNYDEYVVQKEEQRKTQ 197
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLPetygmTVIFSTHQLDLVPEMADYIYVMDKGRIVAY-GTVEEIFLQPDLLARVH 236
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-175 |
1.04e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 56.76 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPF------------FFEQ 74
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpararlararigVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 75 FGS-DSE------------YF--ETDYAEAGKMGVADHIWQEN--------VSGGEDTRIRLAQ-LFSSPHaVAFLDEPT 130
Cdd:PRK13536 122 FDNlDLEftvrenllvfgrYFgmSTREIEAVIPSLLEFARLESkadarvsdLSGGMKRRLTLARaLINDPQ-LLILDEPT 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1124469102 131 SNLDYNGVEMLKKRLNEI----ETLVVISHDRSVLNEICDRIVEISFGK 175
Cdd:PRK13536 201 TGLDPHARHLIWERLRSLlargKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
6-197 |
1.04e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 56.39 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSYGEQT-VLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPFFFEQFG-------- 76
Cdd:PRK13636 5 ILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmklresv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 77 ------SDSEYFETDYAEAGKMGV-------------ADHIWQEN------------VSGGEDTRIRLAQLFSSPHAVAF 125
Cdd:PRK13636 85 gmvfqdPDNQLFSASVYQDVSFGAvnlklpedevrkrVDNALKRTgiehlkdkpthcLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1124469102 126 LDEPTSNLDYNGV----EMLKKRLNEIE-TLVVISHDRSVLNEICDRIVEISFGKLQnYSGNYDEYVVQKEEQRKTQ 197
Cdd:PRK13636 165 LDEPTAGLDPMGVseimKLLVEMQKELGlTIIIATHDIDIVPLYCDNVFVMKEGRVI-LQGNPKEVFAEKEMLRKVN 240
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
11-176 |
1.16e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 56.65 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 11 NIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKG---------TVSSN-----CIPF-----F 71
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGqifidgedvTHRSIqqrdiCMVFqsyalF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 72 ------------FEQFGSDSEYFETDYAEAGKM----GVADHiWQENVSGGEDTRIRLAQ-LFSSPHAVAFlDEPTSNLD 134
Cdd:PRK11432 91 phmslgenvgygLKMLGVPKEERKQRVKEALELvdlaGFEDR-YVDQISGGQQQRVALARaLILKPKVLLF-DEPLSNLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1124469102 135 YN-------GVEMLKKRLNeIETLVViSHDRSVLNEICDRIVEISFGKL 176
Cdd:PRK11432 169 ANlrrsmreKIRELQQQFN-ITSLYV-THDQSEAFAVSDTVIVMNKGKI 215
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
296-482 |
1.22e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 55.27 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 296 VIRGEHISFAY-DDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREKvyvvPGA-KIGYARQNMSQID------ 367
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIER----PSAgKIWFSGHDITRLKnrevpf 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 368 ---------------LSQTVLVNVRRVSI----QSESISRIVLARLllSERDMNKKAS----ELSGGERMKLSFAMLFVS 424
Cdd:PRK10908 77 lrrqigmifqdhhllMDRTVYDNVAIPLIiagaSGDDIRRRVSAAL--DKVGLLDKAKnfpiQLSGGEQQRVGIARAVVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1124469102 425 DVNLLILDEPTNYLDIPSVEALEKMLVEYEG---TLIFTSHDKVFVDRIATDRLYIGDGKI 482
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
296-482 |
1.34e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 55.85 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 296 VIRGEHISFAY-DDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINN----REKVYVVPGAKIGYarQNMSQIDLSQ 370
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGilkpTSGEVLIKGEPIKY--DKKSLLEVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 371 TVLVNVRRVSIQ--SESISRIVL---ARLLLSERDMNKKASE-----------------LSGGERMKLSFAMLFVSDVNL 428
Cdd:PRK13639 79 TVGIVFQNPDDQlfAPTVEEDVAfgpLNLGLSKEEVEKRVKEalkavgmegfenkpphhLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1124469102 429 LILDEPTNYLDIPSVEALEKMLVEY--EG-TLIFTSHDKVFVDRIATDRLYIGDGKI 482
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLnkEGiTIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
296-440 |
1.42e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 55.99 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 296 VIRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLL--------------------ELINNREKVYVVPGAK 355
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLkalagdltgggaprgarvtgDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 356 IGYARQNMSQ-------IDLSQTVLV----NVRR---VSIQSESISRIVLARL---LLSERDMnkkaSELSGGERMKLSF 418
Cdd:PRK13547 81 LARLRAVLPQaaqpafaFSAREIVLLgrypHARRagaLTHRDGEIAWQALALAgatALVGRDV----TTLSGGELARVQF 156
|
170 180 190
....*....|....*....|....*....|.
gi 1124469102 419 AMLF---------VSDVNLLILDEPTNYLDI 440
Cdd:PRK13547 157 ARVLaqlwpphdaAQPPRYLLLDEPTAALDL 187
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
322-463 |
1.67e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 55.23 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 322 GSKVALLGGNGAGKTTLLELINNrekvyVVPGA-KIGYARQNMSQIDLS-----------QTVLVNVRRV---------- 379
Cdd:COG4138 22 GELIHLIGPNGAGKSTLLARMAG-----LLPGQgEILLNGRPLSDWSAAelarhraylsqQQSPPFAMPVfqylalhqpa 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 380 SIQSESISRIV--LARLLLSERDMNKKASELSGGE--RMKLSFAMLFVS-DVN----LLILDEPTNYLDIPSVEALEKML 450
Cdd:COG4138 97 GASSEAVEQLLaqLAEALGLEDKLSRPLTQLSGGEwqRVRLAAVLLQVWpTINpegqLLLLDEPMNSLDVAQQAALDRLL 176
|
170
....*....|....*.
gi 1124469102 451 VEY---EGTLIFTSHD 463
Cdd:COG4138 177 RELcqqGITVVMSSHD 192
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
23-134 |
1.76e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 54.58 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 23 DFDrFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPT---KGTVSSNCIPF--FFEQFGSDSEYFETDYAEAGKMGVADH 97
Cdd:cd03233 25 DFS-GVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYkeFAEKYPGEIIYVSEEDVHFPTLTVRET 103
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1124469102 98 I-----WQEN-----VSGGEDTRIRLAQLFSSPHAVAFLDEPTSNLD 134
Cdd:cd03233 104 LdfalrCKGNefvrgISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-64 |
1.89e-08 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 55.09 E-value: 1.89e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1124469102 7 IKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVS 64
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVL 59
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
313-482 |
1.95e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 55.86 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 313 DDADFMIKNGSKVALLGGNGAGKTTLLELI------------------NNREKVY-----VVPGAKigyarqnmSQI--D 367
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLtgilvptsgevrvlgyvpFKRRKEFarrigVVFGQR--------SQLwwD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 368 L----SQTVLVNVRRVSiqsESISRIVLARL--LLSERD-MNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDI 440
Cdd:COG4586 111 LpaidSFRLLKAIYRIP---DAEYKKRLDELveLLDLGElLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1124469102 441 PSVEALEKMLVEY---EG-TLIFTSHDKVFVDRIAtDRLY-IGDGKI 482
Cdd:COG4586 188 VSKEAIREFLKEYnreRGtTILLTSHDMDDIEALC-DRVIvIDHGRI 233
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
296-482 |
2.09e-08 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 54.89 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 296 VIRGEHISFAYDDH----VIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREK-----VYV-------VPGAKIGYA 359
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERptsgsVLVdgtdltlLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 360 RQNMSQI----DL--SQTVLVNVR------RVSiQSESISRIvlaRLLLSERDMNKKA----SELSGGERMKLSFAMLFV 423
Cdd:cd03258 81 RRRIGMIfqhfNLlsSRTVFENVAlpleiaGVP-KAEIEERV---LELLELVGLEDKAdaypAQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1124469102 424 SDVNLLILDEPTNYLDIPSVEALEKMLV----EYEGTLIFTSHDKVFVDRIATDRLYIGDGKI 482
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILALLRdinrELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
292-482 |
2.13e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 56.11 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 292 RNPIV-IRGehISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREKvyvVPGAKIGYARQNMSQIDLSQ 370
Cdd:PRK09452 11 LSPLVeLRG--ISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFET---PDSGRIMLDGQDITHVPAEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 371 ----------------TVLVNV----RRVSIQSESISRIVLA--RLLLSERDMNKKASELSGGERMKLSFAMLFVSDVNL 428
Cdd:PRK09452 86 rhvntvfqsyalfphmTVFENVafglRMQKTPAAEITPRVMEalRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1124469102 429 LILDEPTNYLDIpsveALEK-MLVEYEG-------TLIFTSHDK----VFVDRIATDRlyigDGKI 482
Cdd:PRK09452 166 LLLDESLSALDY----KLRKqMQNELKAlqrklgiTFVFVTHDQeealTMSDRIVVMR----DGRI 223
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
296-450 |
2.14e-08 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 54.78 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 296 VIRGEHISFAY---DDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINN------------------------REKV 348
Cdd:cd03248 11 IVKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENfyqpqggqvlldgkpisqyehkylHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 349 YVVPGAKIGYARQNMSQID--LSQTVLVNVRRVSIQSESISRIVLARLLLSErDMNKKASELSGGERMKLSFAMLFVSDV 426
Cdd:cd03248 91 SLVGQEPVLFARSLQDNIAygLQSCSFECVKEAAQKAHAHSFISELASGYDT-EVGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180
....*....|....*....|....
gi 1124469102 427 NLLILDEPTNYLDIPSVEALEKML 450
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQAL 193
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
292-462 |
2.33e-08 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 53.90 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 292 RNPIVIRGEHisfayddhVIFDDADFMIKNGSKVALLGGNGAGKTTLLELI-------------NNRE--KVYVVPGAKI 356
Cdd:TIGR01189 4 RNLACSRGER--------MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILagllrpdsgevrwNGTPlaEQRDEPHENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 357 GYA-RQNMSQIDLsqTVLVNVRRVSIQSESISRIV---LARLLLSERDmNKKASELSGGERMKLSFAMLFVSDVNLLILD 432
Cdd:TIGR01189 76 LYLgHLPGLKPEL--SALENLHFWAAIHGGAQRTIedaLAAVGLTGFE-DLPAAQLSAGQQRRLALARLWLSRRPLWILD 152
|
170 180 190
....*....|....*....|....*....|...
gi 1124469102 433 EPTNYLDIPSVEALEKMLVEY---EGTLIFTSH 462
Cdd:TIGR01189 153 EPTTALDKAGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
297-448 |
2.42e-08 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 54.85 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYD---DHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELInnrEKVYVVPGAKIGYARQNMSQIDL----- 368
Cdd:cd03249 1 IEFKNVSFRYPsrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL---ERFYDPTSGEILLDGVDIRDLNLrwlrs 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 369 -----SQ-------TVLVNV---RRVSIQSESISRIVLARLL-LSERDMNK-------KASELSGGERMKLSFAMLFVSD 425
Cdd:cd03249 78 qiglvSQepvlfdgTIAENIrygKPDATDEEVEEAAKKANIHdFIMSLPDGydtlvgeRGSQLSGGQKQRIAIARALLRN 157
|
170 180
....*....|....*....|....*..
gi 1124469102 426 VNLLILDEPTNYLDIPS----VEALEK 448
Cdd:cd03249 158 PKILLLDEATSALDAESeklvQEALDR 184
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
297-462 |
2.59e-08 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 56.29 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYD-DHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNrekVYVVPGAKIGYARQNMSQID-------- 367
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVG---FFQARSGEILLNGFSLKDIDrhtlrqfi 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 368 ---------LSQTVLVNV----RRVSIQSESISRIVLARL--------LLSERDMNKKASELSGGERMKLSFAMLFVSDV 426
Cdd:TIGR01193 551 nylpqepyiFSGSILENLllgaKENVSQDEIWAACEIAEIkddienmpLGYQTELSEEGSSISGGQKQRIALARALLTDS 630
|
170 180 190
....*....|....*....|....*....|....*..
gi 1124469102 427 NLLILDEPTNYLD-IPSVEALEKMLVEYEGTLIFTSH 462
Cdd:TIGR01193 631 KVLILDESTSNLDtITEKKIVNNLLNLQDKTIIFVAH 667
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
296-463 |
2.61e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 55.24 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 296 VIRGEHISFAYDDHV-IFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREKvyvvPGAkiGYARQNMSQIDLSQTVLV 374
Cdd:PRK13636 5 ILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILK----PSS--GRILFDGKPIDYSRKGLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 375 NVRR---VSIQS-----------ESISRIVLaRLLLSERDM-----------------NKKASELSGGERMKLSFAMLFV 423
Cdd:PRK13636 79 KLREsvgMVFQDpdnqlfsasvyQDVSFGAV-NLKLPEDEVrkrvdnalkrtgiehlkDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1124469102 424 SDVNLLILDEPTNYLDIPSVEALEKMLVEYEG----TLIFTSHD 463
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelglTIIIATHD 201
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-63 |
2.67e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.19 E-value: 2.67e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1124469102 6 LIKAENIVHSYGEQTVLD---FDrfyLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTV 63
Cdd:COG3845 5 ALELRGITKRFGGVVANDdvsLT---VRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEI 62
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
292-462 |
2.99e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.80 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 292 RNPIVIRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTL------LE-------LINNREkvyVVPG----- 353
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLmkilygLYqpdsgeiLIDGKP---VRIRsprda 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 354 --AKIGYARQNMSQIDlSQTVLVNV-------RRVSIQSESISRIVLArllLSER-----DMNKKASELSGGERMKLSFA 419
Cdd:COG3845 78 iaLGIGMVHQHFMLVP-NLTVAENIvlgleptKGGRLDRKAARARIRE---LSERygldvDPDAKVEDLSVGEQQRVEIL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1124469102 420 MLFVSDVNLLILDEPTNYLDIPSVEALEKMLVEY--EG-TLIFTSH 462
Cdd:COG3845 154 KALYRGARILILDEPTAVLTPQEADELFEILRRLaaEGkSIIFITH 199
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
307-482 |
2.99e-08 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 54.57 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 307 DDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREKVYVVPGaKIGYARQNMSQI-------------------- 366
Cdd:TIGR01978 11 EDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYEVTSG-TILFKGQDLLELepderaraglflafqypeei 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 367 ------DLSQTVLvNVRRVSIQSESISRIVLARLL------------LSERDMNKKaseLSGGERMKLSFAMLFVSDVNL 428
Cdd:TIGR01978 90 pgvsnlEFLRSAL-NARRSARGEEPLDLLDFEKLLkeklalldmdeeFLNRSVNEG---FSGGEKKRNEILQMALLEPKL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1124469102 429 LILDEPTNYLDIPSV----EALEKMLVEYEGTLIFTSHDKVFvDRIATDRLYI-GDGKI 482
Cdd:TIGR01978 166 AILDEIDSGLDIDALkivaEGINRLREPDRSFLIITHYQRLL-NYIKPDYVHVlLDGRI 223
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
290-467 |
3.47e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 55.88 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 290 PPRNPIVIRGEHISFAY---DDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNrekVYVVPGAKIGYARQNMSQI 366
Cdd:TIGR00958 472 PLNLEGLIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQN---LYQPTGGQVLLDGVPLVQY 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 367 DL----SQTVLVNVRRVsIQSESISRIVLARLLLSERDM-------------------------NKKASELSGGERMKLS 417
Cdd:TIGR00958 549 DHhylhRQVALVGQEPV-LFSGSVRENIAYGLTDTPDEEimaaakaanahdfimefpngydtevGEKGSQLSGGQKQRIA 627
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1124469102 418 FAMLFVSDVNLLILDEPTNYLDIPSVEALEKMLVEYEGTLIFTSH--------DKVFV 467
Cdd:TIGR00958 628 IARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHrlstveraDQILV 685
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
297-462 |
3.57e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.56 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLEL-------------INNREKVYVVP--GAK--IGYA 359
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVlsgiheptkgtitINNINYNKLDHklAAQlgIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 360 RQNMSQIDlSQTVLVN----------VRRVSIQSESISRIVLARLLLS---ERDMNKKASELSGGERMKLSFAMLFVSDV 426
Cdd:PRK09700 86 YQELSVID-ELTVLENlyigrhltkkVCGVNIIDWREMRVRAAMMLLRvglKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 1124469102 427 NLLILDEPTNYLDIPSVEALEKML--VEYEGT-LIFTSH 462
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMnqLRKEGTaIVYISH 203
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
297-467 |
3.71e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 55.09 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREKvyvVPGAKIGYARQNMSQIDLSQ------ 370
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEH---QTSGHIRFHGTDVSRLHARDrkvgfv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 371 ----------TVLVNV--------RRVSIQSESISRIVlARLLlserDM-------NKKASELSGGERMKLSFAMLFVSD 425
Cdd:PRK10851 80 fqhyalfrhmTVFDNIafgltvlpRRERPNAAAIKAKV-TQLL----EMvqlahlaDRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1124469102 426 VNLLILDEPTNYLDIPSVEALEKMLVEYEGTLIFTShdkVFV 467
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTS---VFV 193
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
297-482 |
3.85e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 54.25 E-value: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTL--------------LELINNREKVYVVPGAKIGYA-RQ 361
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLlrvlnllemprsgtLNIAGNHFDFSKTPSDKAIRElRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 362 NM----SQIDL--SQTVLVN-------VRRVSiQSESISRI--VLARLLLSErdmnkKAS----ELSGGERMKLSFAMLF 422
Cdd:PRK11124 83 NVgmvfQQYNLwpHLTVQQNlieapcrVLGLS-KDQALARAekLLERLRLKP-----YADrfplHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1124469102 423 VSDVNLLILDEPTNYLDiPSVEA-LEKMLVEYEGTLI---FTSHDKVFVDRIATDRLYIGDGKI 482
Cdd:PRK11124 157 MMEPQVLLFDEPTAALD-PEITAqIVSIIRELAETGItqvIVTHEVEVARKTASRVVYMENGHI 219
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
6-174 |
4.69e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.42 E-value: 4.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELE--PTKGTVSSNCIPFFFEQFGSDSEYFE 83
Cdd:COG2401 30 VLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGREASLIDAIGRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 84 TDYAEA----GKMGVAD-HIWQ---ENVSGGEDTRIRLAQLFSSPHAVAFLDEPTSNLDYNGVEMLKKRLNEI-----ET 150
Cdd:COG2401 110 GDFKDAvellNAVGLSDaVLWLrrfKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLarragIT 189
|
170 180
....*....|....*....|....*
gi 1124469102 151 LVVISHDRSVLNEIC-DRIVEISFG 174
Cdd:COG2401 190 LVVATHHYDVIDDLQpDLLIFVGYG 214
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
27-168 |
4.93e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.30 E-value: 4.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 27 FYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPfffEQFGSdseyfETDYAEAG------------KMGV 94
Cdd:PRK11288 25 FDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE---MRFAS-----TTAALAAGvaiiyqelhlvpEMTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 95 ADHIW--QENVSGG--------EDTRIRLAQLFS--SPHA-------------------------VAFlDEPTSNLDYNG 137
Cdd:PRK11288 97 AENLYlgQLPHKGGivnrrllnYEAREQLEHLGVdiDPDTplkylsigqrqmveiakalarnarvIAF-DEPTSSLSARE 175
|
170 180 190
....*....|....*....|....*....|....*
gi 1124469102 138 VEMLKKRLNEI--ETLVVI--SHDRSVLNEICDRI 168
Cdd:PRK11288 176 IEQLFRVIRELraEGRVILyvSHRMEEIFALCDAI 210
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
7-176 |
4.98e-08 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 53.27 E-value: 4.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQTvLDFDrFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPFFFEQ---------FGS 77
Cdd:cd03298 1 VRLDKIRFSYGEQP-MHFD-LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPpadrpvsmlFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 78 DSEYFETDYAE-----------------------AGKMGVADHIWQ--ENVSGGEDTRIRLAQLFSSPHAVAFLDEPTSN 132
Cdd:cd03298 79 NNLFAHLTVEQnvglglspglkltaedrqaievaLARVGLAGLEKRlpGELSGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1124469102 133 LDYNGVEMLKKRLNEIE-----TLVVISHDRSVLNEICDRIVEISFGKL 176
Cdd:cd03298 159 LDPALRAEMLDLVLDLHaetkmTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
7-179 |
5.37e-08 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 53.27 E-value: 5.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSY--GEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTV----------------SSNCI 68
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSIlidgvdiskiglhdlrSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 69 ----PFFFEqfGS-------DSEYFETDYAEA-GKMGVADHIwqENVSGGEDTRI-----------RlaQLFS------S 119
Cdd:cd03244 83 ipqdPVLFS--GTirsnldpFGEYSDEELWQAlERVGLKEFV--ESLPGGLDTVVeeggenlsvgqR--QLLClarallR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1124469102 120 PHAVAFLDEPTSNLDYNGVEMLKKRLNEI---ETLVVISHdRsvLNEI--CDRIVEISFGKLQNY 179
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIREAfkdCTVLTIAH-R--LDTIidSDRILVLDKGRVVEF 218
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
309-482 |
5.54e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 53.92 E-value: 5.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 309 HVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREKvyvvP-GAKIGYARQNMSQIDLS---------QTVL----- 373
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLES----PsQGNVSWRGEPLAKLNRAqrkafrrdiQMVFqdsis 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 374 -VNVRRvsiqseSISRIV---------------LARLL-------LSERDMNKKASELSGGERMKLSFAMLFVSDVNLLI 430
Cdd:PRK10419 101 aVNPRK------TVREIIreplrhllsldkaerLARASemlravdLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1124469102 431 LDEPTNYLDI---PSVEALEKMLVEYEGT-LIFTSHDKVFVDRIATDRLYIGDGKI 482
Cdd:PRK10419 175 LDEAVSNLDLvlqAGVIRLLKKLQQQFGTaCLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
6-180 |
5.65e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 55.75 E-value: 5.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSY--GEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVS-SNC--------------- 67
Cdd:PLN03232 1234 SIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMiDDCdvakfgltdlrrvls 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 68 ----IPFFFE---QFGSD--SEYFETDYAEA------------GKMGVADHIWQ--ENVSGGEDTRIRLAQLFSSPHAVA 124
Cdd:PLN03232 1314 iipqSPVLFSgtvRFNIDpfSEHNDADLWEAlerahikdvidrNPFGLDAEVSEggENFSVGQRQLLSLARALLRRSKIL 1393
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1124469102 125 FLDEPTSNLDYNGVEMLKKRLNE---IETLVVISHDrsvLNEI--CDRIVEISFGKLQNYS 180
Cdd:PLN03232 1394 VLDEATASVDVRTDSLIQRTIREefkSCTMLVIAHR---LNTIidCDKILVLSSGQVLEYD 1451
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
286-447 |
5.75e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 53.04 E-value: 5.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 286 RLTNPPRNPIVIRGEHISFAYddhvIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREKVYVVPGAKI---GYARQN 362
Cdd:cd03233 1 ASTLSWRNISFTTGKGRSKIP----ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIhynGIPYKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 363 MSQIDLSQTVLVNVRRVSIQSESISRIVLARLLLSERDMNKKaseLSGGERMKLSFAMLFVSDVNLLILDEPTNYLDipS 442
Cdd:cd03233 77 FAEKYPGEIIYVSEEDVHFPTLTVRETLDFALRCKGNEFVRG---ISGGERKRVSIAEALVSRASVLCWDNSTRGLD--S 151
|
....*
gi 1124469102 443 VEALE 447
Cdd:cd03233 152 STALE 156
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
104-181 |
6.03e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 52.33 E-value: 6.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 104 SGGEDTRIRLA-QLFSSPHAVAF-LDEPTSNLDYNGVEMLKKRLNEI----ETLVVISHDRSVLNEiCDRIVEisFGKLQ 177
Cdd:cd03238 89 SGGELQRVKLAsELFSEPPGTLFiLDEPSTGLHQQDINQLLEVIKGLidlgNTVILIEHNLDVLSS-ADWIID--FGPGS 165
|
....
gi 1124469102 178 NYSG 181
Cdd:cd03238 166 GKSG 169
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
32-185 |
6.37e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 53.69 E-value: 6.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 32 GEKVGLVGMNGAGKSTLLKILAGeLEPTKGTVSSN---------------------------CIPFF-----FEQFGSDS 79
Cdd:COG4138 22 GELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNgrplsdwsaaelarhraylsqqqsppfAMPVFqylalHQPAGASS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 80 EYFETDYAE-AGKMGVAD----HIWQenVSGGEDTRIRLA----QLFSS--PHA-VAFLDEPTSNLDYNGVEMLKKRLNE 147
Cdd:COG4138 101 EAVEQLLAQlAEALGLEDklsrPLTQ--LSGGEWQRVRLAavllQVWPTinPEGqLLLLDEPMNSLDVAQQAALDRLLRE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1124469102 148 IE----TLVVISHDrsvLNEIC---DRIVEISFGKLQNySGNYDE 185
Cdd:COG4138 179 LCqqgiTVVMSSHD---LNHTLrhaDRVWLLKQGKLVA-SGETAE 219
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
10-176 |
6.39e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 53.53 E-value: 6.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 10 ENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPF---------FFEQ------ 74
Cdd:PRK11247 16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLaearedtrlMFQDarllpw 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 75 --------FGSDSEYFETDYAEAGKMGVADHI--WQENVSGGEDTRIRLAQ-LFSSPhAVAFLDEPTSNLD-YNGVEM-- 140
Cdd:PRK11247 96 kkvidnvgLGLKGQWRDAALQALAAVGLADRAneWPAALSGGQKQRVALARaLIHRP-GLLLLDEPLGALDaLTRIEMqd 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 1124469102 141 LKKRLNEIE--TLVVISHDRSVLNEICDRIVEISFGKL 176
Cdd:PRK11247 175 LIESLWQQHgfTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
300-450 |
6.47e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 53.55 E-value: 6.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 300 EHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELIN----------NREKVYVV-PGAKIGYARQNMSQIDL 368
Cdd:PRK11248 5 SHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAgfvpyqhgsiTLDGKPVEgPGAERGVVFQNEGLLPW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 369 sQTVLVNV------RRVS-IQSESISRIVLARLLLSERDmNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIP 441
Cdd:PRK11248 85 -RNVQDNVafglqlAGVEkMQRLEIAHQMLKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAF 162
|
....*....
gi 1124469102 442 SVEALEKML 450
Cdd:PRK11248 163 TREQMQTLL 171
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
7-63 |
6.62e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 53.49 E-value: 6.62e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1124469102 7 IKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTV 63
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRI 60
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
296-439 |
7.64e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 53.97 E-value: 7.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 296 VIRGEHISFAYDDHVIFD-----DADFMIKNGSKVALLGGNGAGKTTLLELIN--------------------NREKVYV 350
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFAsralfDIDLEVKKGSYTALIGHTGSGKSTLLQHLNgllqptegkvtvgdivvsstSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 351 VPGAKIGYARQNMSQIDLSQTVLVNV----RRVSIQSESISRIVLARLL---LSERDMNKKASELSGGERMKLSFAMLFV 423
Cdd:PRK13643 81 PVRKKVGVVFQFPESQLFEETVLKDVafgpQNFGIPKEKAEKIAAEKLEmvgLADEFWEKSPFELSGGQMRRVAIAGILA 160
|
170
....*....|....*.
gi 1124469102 424 SDVNLLILDEPTNYLD 439
Cdd:PRK13643 161 MEPEVLVLDEPTAGLD 176
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
296-482 |
7.94e-08 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 53.05 E-value: 7.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 296 VIRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLE-------------LINNRE----KVYVVPGAKIGY 358
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYmivglvrpdagkiLIDGQDithlPMHERARLGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 359 ARQNMSqIDLSQTVLVNVRRVSIQSESISRIVLARL---LLSE----RDMNKKASELSGGERMKLSFAMLFVSDVNLLIL 431
Cdd:TIGR04406 81 LPQEAS-IFRKLTVEENIMAVLEIRKDLDRAEREERleaLLEEfqisHLRDNKAMSLSGGERRRVEIARALATNPKFILL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1124469102 432 DEPTNYLDIPSVEALEKmLVEYE-----GTLIfTSHDKVFVDRIAtDRLYI-GDGKI 482
Cdd:TIGR04406 160 DEPFAGVDPIAVGDIKK-IIKHLkergiGVLI-TDHNVRETLDIC-DRAYIiSDGKV 213
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
271-462 |
8.99e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 54.43 E-value: 8.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 271 IKEKPKEELTVRpDFRLTNPprnpivirgehisfayDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINN-----R 345
Cdd:COG4178 355 IETSEDGALALE-DLTLRTP----------------DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGlwpygS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 346 EKVYVVPGAKIGYarqnmsqidLSQTV---LVNVRRVSI---QSESISRIVLARLL-------LSERdMNKKAS---ELS 409
Cdd:COG4178 418 GRIARPAGARVLF---------LPQRPylpLGTLREALLypaTAEAFSDAELREALeavglghLAER-LDEEADwdqVLS 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1124469102 410 GGERMKLSFAMLFVSDVNLLILDEPTNYLDIPSVEALEKMLVE--YEGTLIFTSH 462
Cdd:COG4178 488 LGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGH 542
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
326-476 |
9.41e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 55.02 E-value: 9.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 326 ALLGGNGAGKTTLLELINN----REKVYVVPGAKI----GYARQNMS----------QIDLSQTVLVNVRrVSIQSESIS 387
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGllppTSGTVLVGGKDIetnlDAVRQSLGmcpqhnilfhHLTVAEHILFYAQ-LKGRSWEEA 1038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 388 RIVLARLLLS---ERDMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIPSVEALEKMLVEYEG--TLIFTSH 462
Cdd:TIGR01257 1039 QLEMEAMLEDtglHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSgrTIIMSTH 1118
|
170 180
....*....|....*....|.
gi 1124469102 463 D----KVFVDRIA---TDRLY 476
Cdd:TIGR01257 1119 HmdeaDLLGDRIAiisQGRLY 1139
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
293-477 |
1.12e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 53.23 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 293 NPIVIRGehISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNR------------EKVYVVPGAKIGYAR 360
Cdd:PRK11831 6 NLVDMRG--VSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQiapdhgeilfdgENIPAMSRSRLYTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 361 QNMSQI--------DLsqTVLVNV----RRVSIQSESISR-IVLARL-LLSERDMNK-KASELSGGERMKLSFAMLFVSD 425
Cdd:PRK11831 84 KRMSMLfqsgalftDM--NVFDNVayplREHTQLPAPLLHsTVMMKLeAVGLRGAAKlMPSELSGGMARRAALARAIALE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1124469102 426 VNLLILDEPTNYLDIPSVEALEKMLVEYEGTL----IFTSHDKVFVDRIAtDRLYI 477
Cdd:PRK11831 162 PDLIMFDEPFVGQDPITMGVLVKLISELNSALgvtcVVVSHDVPEVLSIA-DHAYI 216
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
307-462 |
1.14e-07 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 52.11 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 307 DDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINN----REKVYVVPGAKIGYARQNMSQ----------IDLSQTV 372
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGlsppLAGRVLLNGGPLDFQRDSIARgllylghapgIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 373 LVNVRRV-SIQSESISRIVLARLLLSERDmNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIPSVEALEKML- 450
Cdd:cd03231 91 LENLRFWhADHSDEQVEEALARVGLNGFE-DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMa 169
|
170
....*....|....
gi 1124469102 451 --VEYEGTLIFTSH 462
Cdd:cd03231 170 ghCARGGMVVLTTH 183
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
314-470 |
1.20e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 52.51 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 314 DADFMIKNGSKVALLGGNGAGKTTLLELINNREKvyvvP-GAKIGYARQNMSQIDLSQ---------------------- 370
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDT----PtSGDVIFNGQPMSKLSSAAkaelrnqklgfiyqfhhllpdf 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 371 TVLVNV-------RRVSIQSESISRIVLARLLLSERDmNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIPSV 443
Cdd:PRK11629 103 TALENVamplligKKKPAEINSRALEMLAAVGLEHRA-NHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
|
170 180 190
....*....|....*....|....*....|.
gi 1124469102 444 EALEKMLVEY---EGT-LIFTSHDKVFVDRI 470
Cdd:PRK11629 182 DSIFQLLGELnrlQGTaFLVVTHDLQLAKRM 212
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
32-181 |
1.28e-07 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 52.27 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 32 GEKVGLVGMNGAGKSTLLKILAGELEP---TKGTVSSNCIPF----------FFEQFGSDSEYF---ETDY--------- 86
Cdd:cd03234 33 GQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRkpdqfqkcvaYVRQDDILLPGLtvrETLTytailrlpr 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 87 ---AEAGKMGVAD------------HIWQENVSGGEDTRIRLA-QLFSSPhAVAFLDEPTSNLD----YNGVEMLKK--R 144
Cdd:cd03234 113 kssDAIRKKRVEDvllrdlaltrigGNLVKGISGGERRRVSIAvQLLWDP-KVLILDEPTSGLDsftaLNLVSTLSQlaR 191
|
170 180 190
....*....|....*....|....*....|....*..
gi 1124469102 145 LNEIeTLVVISHDRSVLNEICDRIVEISFGKLQnYSG 181
Cdd:cd03234 192 RNRI-VILTIHQPRSDLFRLFDRILLLSSGEIV-YSG 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
297-482 |
1.28e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 53.13 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDDHVIF-----DDADFMIKNGSKVALLGGNGAGKTTLLELIN-----NREKVYVvPGAKIGYARQNMSQI 366
Cdd:PRK13637 3 IKIENLTHIYMEGTPFekkalDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNgllkpTSGKIII-DGVDITDKKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 367 DLSQTVLVNVRRVSIQSESISRIV---LARLLLSERDMNKKAS-------------------ELSGGERMKLSFAMLFVS 424
Cdd:PRK13637 82 RKKVGLVFQYPEYQLFEETIEKDIafgPINLGLSEEEIENRVKramnivgldyedykdkspfELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1124469102 425 DVNLLILDEPTNYLDiPS-----VEALEKMLVEYEGTLIFTSHDKVFVDRIATDRLYIGDGKI 482
Cdd:PRK13637 162 EPKILILDEPTAGLD-PKgrdeiLNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKC 223
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
296-482 |
1.62e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 52.71 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 296 VIRGEHISFAYDD--HVIFDDADFMIKNGSKVALLGGNGAGKTTLLELIN-----------------NREKVYVVPgAKI 356
Cdd:PRK13635 5 IIRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNglllpeagtitvggmvlSEETVWDVR-RQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 357 GYARQNMSQIDLSQTV-------LVN--VRRvsiqSESISRIVLA-RLLLSERDMNKKASELSGGERMKLSFAMLFVSDV 426
Cdd:PRK13635 84 GMVFQNPDNQFVGATVqddvafgLENigVPR----EEMVERVDQAlRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1124469102 427 NLLILDEPTNYLD-IPSVEALE--KMLVEYEG-TLIFTSHD---KVFVDRIatdrLYIGDGKI 482
Cdd:PRK13635 160 DIIILDEATSMLDpRGRREVLEtvRQLKEQKGiTVLSITHDldeAAQADRV----IVMNKGEI 218
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
7-176 |
1.66e-07 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 52.23 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYG-EQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSN--------------CI--- 68
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDgqdirevtldslrrAIgvv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 69 ----PFFFE------QFGSDSEYFETDYAEAGKMGVADHIWQEN-------------VSGGEDTRIRLAQLFSSPHAVAF 125
Cdd:cd03253 81 pqdtVLFNDtigyniRYGRPDATDEEVIEAAKAAQIHDKIMRFPdgydtivgerglkLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1124469102 126 LDEPTSNLDYNGVEMLKKRLNEI---ETLVVISHD-RSVLNeiCDRIVEISFGKL 176
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVskgRTTIVIAHRlSTIVN--ADKIIVLKDGRI 213
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
300-472 |
2.19e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 52.04 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 300 EHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELI-------------NNRE----KVYVVpgAKIGYAR-- 360
Cdd:COG4674 14 EDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVItgktrpdsgsvlfGGTDltglDEHEI--ARLGIGRkf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 361 QNMSqIDLSQTVLVNV----------------RRVSIQSESISRIvLARLLLSERdMNKKASELSGGERMKLSFAMLFVS 424
Cdd:COG4674 92 QKPT-VFEELTVFENLelalkgdrgvfaslfaRLTAEERDRIEEV-LETIGLTDK-ADRLAGLLSHGQKQWLEIGMLLAQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1124469102 425 DVNLLILDEPTNYLDIPSVEALEKMLVEYEG--TLIFTSHDKVFVDRIAT 472
Cdd:COG4674 169 DPKLLLLDEPVAGMTDAETERTAELLKSLAGkhSVVVVEHDMEFVRQIAR 218
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
313-482 |
2.42e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 52.14 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 313 DDADFMIKNGSKVALLGGNGAGKTTLLELINNREK----VYVVPGAKIGYARQNMSQIDL----------------SQTV 372
Cdd:PRK13641 24 DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKpssgTITIAGYHITPETGNKNLKKLrkkvslvfqfpeaqlfENTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 373 LVNVR------RVSIQSESISRIV-LARLLLSERDMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIPSVEA 445
Cdd:PRK13641 104 LKDVEfgpknfGFSEDEAKEKALKwLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKE 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1124469102 446 LEKMLVEYEG---TLIFTSHDKVFVDRIATDRLYIGDGKI 482
Cdd:PRK13641 184 MMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
7-176 |
2.87e-07 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 51.57 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEqTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSN-----CIPFFFEQFGsdseY 81
Cdd:cd03299 1 LKVENLSKDWKE-FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgkditNLPPEKRDIS----Y 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 82 FETDYA-------------------------------EAGKMGVaDHIWQ---ENVSGGEDTRIRLAQLFSSPHAVAFLD 127
Cdd:cd03299 76 VPQNYAlfphmtvykniayglkkrkvdkkeierkvleIAEMLGI-DHLLNrkpETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1124469102 128 EPTSNLDYNG----VEMLKKRLNEIETLVV-ISHDRSVLNEICDRIVEISFGKL 176
Cdd:cd03299 155 EPFSALDVRTkeklREELKKIRKEFGVTVLhVTHDFEEAWALADKVAIMLNGKL 208
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-176 |
2.94e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 51.93 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 22 LDFDRFYLyegekVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPFFFEQFG--------------SDSEYFETD-- 85
Cdd:PRK13638 22 LDFSLSPV-----TGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGllalrqqvatvfqdPEQQIFYTDid 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 86 --------------------YAEAGKMGVADHIWQENV---SGGEDTRIRLAQLFSSPHAVAFLDEPTSNLDYNG----V 138
Cdd:PRK13638 97 sdiafslrnlgvpeaeitrrVDEALTLVDAQHFRHQPIqclSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGrtqmI 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 1124469102 139 EMLKKRLNEIETLVVISHDRSVLNEICDRIVEISFGKL 176
Cdd:PRK13638 177 AIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQI 214
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
297-439 |
2.97e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 52.05 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDDHVIFD-----DADFMIKNGSKVALLGGNGAGKTTLLELINN----REKVYVVPGAKIGYARQNM---- 363
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEgralfDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGlhvpTQGSVRVDDTLITSTSKNKdikq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 364 -------------SQIdLSQTVLVNVR------RVS-IQSESISRIVLARLLLSERDMNKKASELSGGERMKLSFAMLFV 423
Cdd:PRK13649 83 irkkvglvfqfpeSQL-FEETVLKDVAfgpqnfGVSqEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILA 161
|
170
....*....|....*.
gi 1124469102 424 SDVNLLILDEPTNYLD 439
Cdd:PRK13649 162 MEPKILVLDEPTAGLD 177
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
307-463 |
3.57e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.40 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 307 DDHVIFDDADFMIKNGSKVALLGGNGAGKTT----LLELINN----------------------REKVYVV---PGAKIG 357
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSqgeiwfdgqplhnlnrrqllpvRHRIQVVfqdPNSSLN 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 358 yARQNMSQIdLSQTVLVNVRRVSI-QSESISRIVLARLLLSERDMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTN 436
Cdd:PRK15134 377 -PRLNVLQI-IEEGLRVHQPTLSAaQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190
....*....|....*....|....*....|..
gi 1124469102 437 YLDiPSVEA-----LEKMLVEYEGTLIFTSHD 463
Cdd:PRK15134 455 SLD-KTVQAqilalLKSLQQKHQLAYLFISHD 485
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
288-482 |
3.64e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 51.22 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 288 TNPPR----NPIVIRGehISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREKV---YVVPG-AKIGYA 359
Cdd:PRK11247 2 MNTARlnqgTPLLLNA--VSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPsagELLAGtAPLAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 360 RQN---MSQiDLS----QTVLVNV--------RRVSIQSesisrivLARLLLSERdMNKKASELSGGERMKLSFAMLFVS 424
Cdd:PRK11247 80 REDtrlMFQ-DARllpwKKVIDNVglglkgqwRDAALQA-------LAAVGLADR-ANEWPAALSGGQKQRVALARALIH 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1124469102 425 DVNLLILDEPTNYLD----IPSVEALEKMLVEYEGTLIFTSHDKVFVDRIAtDR-LYIGDGKI 482
Cdd:PRK11247 151 RPGLLLLDEPLGALDaltrIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMA-DRvLLIEEGKI 212
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
6-185 |
3.83e-07 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 51.12 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSYGEQTvLDFDrFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSN-----CIP--------FFF 72
Cdd:PRK10771 1 MLKLTDITWLYHHLP-MRFD-LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNgqdhtTTPpsrrpvsmLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 73 EQ--FGS-----------------DSEYFETDYAEAGKMGVADHIWQ--ENVSGGEDTRIRLAQLFSSPHAVAFLDEPTS 131
Cdd:PRK10771 79 ENnlFSHltvaqniglglnpglklNAAQREKLHAIARQMGIEDLLARlpGQLSGGQRQRVALARCLVREQPILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1124469102 132 NLD---YNgvEMLkKRLNEI-----ETLVVISHDRSVLNEICDRIVEISFGKLQnYSGNYDE 185
Cdd:PRK10771 159 ALDpalRQ--EML-TLVSQVcqerqLTLLMVSHSLEDAARIAPRSLVVADGRIA-WDGPTDE 216
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
300-482 |
4.11e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 51.55 E-value: 4.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 300 EHISFAYDDHVIF-----DDADFMIKNGSKVALLGGNGAGKTTLLELIN-------------------NREKVYVVP--- 352
Cdd:PRK13645 10 DNVSYTYAKKTPFefkalNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNgliisetgqtivgdyaipaNLKKIKEVKrlr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 353 ---GAKIGYARQNMSQIDLSQTVLVNVRRVSIQSESISRIV--LARLLLSERDMNKKAS-ELSGGERMKLSFAMLFVSDV 426
Cdd:PRK13645 90 keiGLVFQFPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVpeLLKLVQLPEDYVKRSPfELSGGQKRRVALAGIIAMDG 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 427 NLLILDEPTNYLDIPSVE----ALEKMLVEYEGTLIFTSHDKVFVDRIATDRLYIGDGKI 482
Cdd:PRK13645 170 NTLVLDEPTGGLDPKGEEdfinLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-265 |
4.39e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.67 E-value: 4.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 32 GEKVGLVGMNGAGKSTLLKILAGELEPT-------KGTVS-SNCIPFFFEQ-------FGSDSE---YFET--------- 84
Cdd:PLN03232 643 GSLVAIVGGTGEGKTSLISAMLGELSHAetssvviRGSVAyVPQVSWIFNAtvrenilFGSDFEserYWRAidvtalqhd 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 85 -------DYAEAGKMGVadhiwqeNVSGGEDTRIRLAQLFSSPHAVAFLDEPTSNLDYNGVEM-----LKKRLNEiETLV 152
Cdd:PLN03232 723 ldllpgrDLTEIGERGV-------NISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQvfdscMKDELKG-KTRV 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 153 VISHDRSVLNEIcDRIVEISFGKLQNySGNYDEYVVQKEEQRKTQQAEYENYQAEKKRLQSVYVEKKAKAKTVDKKPKNM 232
Cdd:PLN03232 795 LVTNQLHFLPLM-DRIILVSEGMIKE-EGTFAELSKSGSLFKKLMENAGKMDATQEVNTNDENILKLGPTVTIDVSERNL 872
|
250 260 270
....*....|....*....|....*....|...
gi 1124469102 233 SASEAKVRAFIGNRKPEDKARGIerSATNVLKR 265
Cdd:PLN03232 873 GSTKQGKRGRSVLVKQEERETGI--ISWNVLMR 903
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
307-439 |
4.73e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 51.24 E-value: 4.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 307 DDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELIN-----------------NREKVYVVpgAK-IGYARQN------ 362
Cdd:COG1101 17 NEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAgslppdsgsilidgkdvTKLPEYKR--AKyIGRVFQDpmmgta 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 363 --MsqidlsqTVLVN-------------VRRVSIQSESISRIVLARLLLS-ERDMNKKASELSGGERMKLSFAMLFVSDV 426
Cdd:COG1101 95 psM-------TIEENlalayrrgkrrglRRGLTKKRRELFRELLATLGLGlENRLDTKVGLLSGGQRQALSLLMATLTKP 167
|
170
....*....|...
gi 1124469102 427 NLLILDEPTNYLD 439
Cdd:COG1101 168 KLLLLDEHTAALD 180
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-175 |
4.74e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 51.76 E-value: 4.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVS------SNCIPF--------- 70
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMldgvdlSHVPPYqrpinmmfq 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 71 ---FF-----EQ---FGSDSEYFETD--YAEAGKMGVADHIWQ------ENVSGGEDTRIRLAQLFSSPHAVAFLDEPTS 131
Cdd:PRK11607 99 syaLFphmtvEQniaFGLKQDKLPKAeiASRVNEMLGLVHMQEfakrkpHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1124469102 132 NLDYNGVEMLKKRLNEI-----ETLVVISHDRSVLNEICDRIVEISFGK 175
Cdd:PRK11607 179 ALDKKLRDRMQLEVVDIlervgVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
32-176 |
5.58e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 50.70 E-value: 5.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 32 GEKVGLVGMNGAGKSTLLKILAGeLEPTKGTVSSN---------------------------CIPFFfeQF--------- 75
Cdd:PRK03695 22 GEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAgqpleawsaaelarhraylsqqqtppfAMPVF--QYltlhqpdkt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 76 -GSDSEYFETDYAEAGKMG--VADHIWQenVSGGEDTRIRLAQLF------SSPHA-VAFLDEPTSNLDYNGVEMLKKRL 145
Cdd:PRK03695 99 rTEAVASALNEVAEALGLDdkLGRSVNQ--LSGGEWQRVRLAAVVlqvwpdINPAGqLLLLDEPMNSLDVAQQAALDRLL 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 1124469102 146 NEIE----TLVVISHDrsvLNEI---CDRIVEISFGKL 176
Cdd:PRK03695 177 SELCqqgiAVVMSSHD---LNHTlrhADRVWLLKQGKL 211
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
300-462 |
5.81e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 52.03 E-value: 5.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 300 EHISFAY-DDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNrekVYVV----------PGAKIGYA--RQN--MS 364
Cdd:PRK10790 344 DNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMG---YYPLtegeirldgrPLSSLSHSvlRQGvaMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 365 QID---LSQTVLVNV---RRVSIQS--ESISRIVLARLLLSERD-----MNKKASELSGGERMKLSFAMLFVSDVNLLIL 431
Cdd:PRK10790 421 QQDpvvLADTFLANVtlgRDISEEQvwQALETVQLAELARSLPDglytpLGEQGNNLSVGQKQLLALARVLVQTPQILIL 500
|
170 180 190
....*....|....*....|....*....|...
gi 1124469102 432 DEPTNYLDIPSVEALEKML--VEYEGTLIFTSH 462
Cdd:PRK10790 501 DEATANIDSGTEQAIQQALaaVREHTTLVVIAH 533
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
259-439 |
7.02e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 52.26 E-value: 7.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 259 ATNVLKRLE----HMEIKEKPKEELTVRPDfrltnpPRNPIVIRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAG 334
Cdd:TIGR00957 603 ASVSLKRLRiflsHEELEPDSIERRTIKPG------EGNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCG 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 335 KTTLLE-LINNREKV--YVVPGAKIGYARQN--MSQIDLSQTVLVNVrrvSIQSESISRIVLARLLLSERDM-------- 401
Cdd:TIGR00957 677 KSSLLSaLLAEMDKVegHVHMKGSVAYVPQQawIQNDSLRENILFGK---ALNEKYYQQVLEACALLPDLEIlpsgdrte 753
|
170 180 190
....*....|....*....|....*....|....*....
gi 1124469102 402 -NKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLD 439
Cdd:TIGR00957 754 iGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
287-462 |
7.48e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.85 E-value: 7.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 287 LTNPPRN-PIVIRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELI----------------------N 343
Cdd:PRK13543 1 MIEPLHTaPPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLagllhvesgqiqidgktatrgdR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 344 NREKVYV--VPGAKigyarQNMSQID-LSQTVLVNVRRVsiQSESISRIVLARLLLSERDMNKkasELSGGERMKLSFAM 420
Cdd:PRK13543 81 SRFMAYLghLPGLK-----ADLSTLEnLHFLCGLHGRRA--KQMPGSALAIVGLAGYEDTLVR---QLSAGQKKRLALAR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1124469102 421 LFVSDVNLLILDEPTNYLDIPSVEALEKMLVEY---EGTLIFTSH 462
Cdd:PRK13543 151 LWLSPAPLWLLDEPYANLDLEGITLVNRMISAHlrgGGAALVTTH 195
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
37-172 |
7.55e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 49.53 E-value: 7.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 37 LVGMNGAGKSTLLK----ILAGELEP-TKGTVSSNCIPFFFEQFGSDSEYFET----DYAEAGKMGVADH---IWQE--- 101
Cdd:cd03240 27 IVGQNGAGKTTIIEalkyALTGELPPnSKGGAHDPKLIREGEVRAQVKLAFENangkKYTITRSLAILENvifCHQGesn 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 102 --------NVSGGEDT------RIRLAQLFSSPHAVAFLDEPTSNLDYNGVE------MLKKRLNEIETLVVISHDRSVL 161
Cdd:cd03240 107 wplldmrgRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEeslaeiIEERKSQKNFQLIVITHDEELV 186
|
170
....*....|.
gi 1124469102 162 NEIcDRIVEIS 172
Cdd:cd03240 187 DAA-DHIYRVE 196
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
297-452 |
8.21e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 51.56 E-value: 8.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYD--DHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINnreKVYVVPGAKIgyarqNMSQIDLSQTVLV 374
Cdd:PRK11176 342 IEFRNVTFTYPgkEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLT---RFYDIDEGEI-----LLDGHDLRDYTLA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 375 NVRR-VSIQSESI--------SRIVLARLLLSERDMNKKASE-------------------------LSGGERMKLSFAM 420
Cdd:PRK11176 414 SLRNqVALVSQNVhlfndtiaNNIAYARTEQYSREQIEEAARmayamdfinkmdngldtvigengvlLSGGQRQRIAIAR 493
|
170 180 190
....*....|....*....|....*....|..
gi 1124469102 421 LFVSDVNLLILDEPTNYLDIPSVEALEKMLVE 452
Cdd:PRK11176 494 ALLRDSPILILDEATSALDTESERAIQAALDE 525
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
29-63 |
8.86e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 50.08 E-value: 8.86e-07
10 20 30
....*....|....*....|....*....|....*
gi 1124469102 29 LYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTV 63
Cdd:COG1101 29 IEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSI 63
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-177 |
9.94e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 50.85 E-value: 9.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNC------------IPFFFEQ 74
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdvsrlhardrkVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 75 fgsdseyfetdYAEAGKMGVADHI-------------------------------------WQENVSGGEDTRIRLAQLF 117
Cdd:PRK10851 83 -----------YALFRHMTVFDNIafgltvlprrerpnaaaikakvtqllemvqlahladrYPAQLSGGQKQRVALARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1124469102 118 SSPHAVAFLDEPTSNLDYNGVEMLKKRLNEIE-----TLVVISHDRSVLNEICDRIVEISFGKLQ 177
Cdd:PRK10851 152 AVEPQILLLDEPFGALDAQVRKELRRWLRQLHeelkfTSVFVTHDQEEAMEVADRVVVMSQGNIE 216
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
300-439 |
1.01e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 51.12 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 300 EHISFAYDDHV-IFDDADFMIKNGSKVALLGGNGAGKTTLLELInnrEKVYVVPGAKIgyarqnmsQIDlsqtvLVNVRR 378
Cdd:PRK13657 338 DDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLL---QRVFDPQSGRI--------LID-----GTDIRT 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 379 VSIQS----------------ESIS-RIVLARLLLSERDMNKKA------------------------SELSGGERMKLS 417
Cdd:PRK13657 402 VTRASlrrniavvfqdaglfnRSIEdNIRVGRPDATDEEMRAAAeraqahdfierkpdgydtvvgergRQLSGGERQRLA 481
|
170 180
....*....|....*....|..
gi 1124469102 418 FAMLFVSDVNLLILDEPTNYLD 439
Cdd:PRK13657 482 IARALLKDPPILILDEATSALD 503
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
309-463 |
1.05e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 50.27 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 309 HVIFDDADFMIKNGSKVALLGGNGAGKTTLLE-------LINNREKVYVVPGAK------IGYARQNmSQIDLSQTVLVN 375
Cdd:PRK15056 20 HTALRDASFTVPGGSIAALVGVNGSGKSTLFKalmgfvrLASGKISILGQPTRQalqknlVAYVPQS-EEVDWSFPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 376 -------------VRRVSIQSESISRIVLARLLLSERdMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIPS 442
Cdd:PRK15056 99 dvvmmgryghmgwLRRAKKRDRQIVTAALARVDMVEF-RHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180
....*....|....*....|....
gi 1124469102 443 VEALEKMLVEY--EG-TLIFTSHD 463
Cdd:PRK15056 178 EARIISLLRELrdEGkTMLVSTHN 201
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
6-176 |
1.22e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 49.99 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSYGEQT-VLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTV---------------SSNCIP 69
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsgidtgdfsklqgIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 70 FFFEQ---------------FGSDS---------EYFETDYAEAGkMGVADHIWQENVSGGEDTRIRLAQLFS-SPHAVA 124
Cdd:PRK13644 81 IVFQNpetqfvgrtveedlaFGPENlclppieirKRVDRALAEIG-LEKYRHRSPKTLSGGQGQCVALAGILTmEPECLI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1124469102 125 FlDEPTSNLD-YNGVEMLK--KRLNEI-ETLVVISHDRSVLnEICDRIVEISFGKL 176
Cdd:PRK13644 160 F-DEVTSMLDpDSGIAVLEriKKLHEKgKTIVYITHNLEEL-HDADRIIVMDRGKI 213
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
306-482 |
1.40e-06 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 49.36 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 306 YDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNRE-------KV--YVVPGAK---------------IGYARQ 361
Cdd:PRK11264 13 FHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEqpeagtiRVgdITIDTARslsqqkglirqlrqhVGFVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 362 NMSQIDlSQTVLVNVRRVSIQSESISR---IVLARLLLSERDMNKKAS----ELSGGERMKLSFAMLFVSDVNLLILDEP 434
Cdd:PRK11264 93 NFNLFP-HRTVLENIIEGPVIVKGEPKeeaTARARELLAKVGLAGKETsyprRLSGGQQQRVAIARALAMRPEVILFDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1124469102 435 TNYLD---IPSVEALEKMLVEYEGTLIFTSHDKVFVDRIATDRLYIGDGKI 482
Cdd:PRK11264 172 TSALDpelVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
27-176 |
1.71e-06 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 48.20 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 27 FYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNcipfffeqfgsDSEYFETDYAEAGKMGVA----DH----- 97
Cdd:cd03215 21 FEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLD-----------GKPVTRRSPRDAIRAGIAyvpeDRkregl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 98 -----IWqENV------SGGEDTRIRLAQLFSSPHAVAFLDEPTSNLDYNGVEMLKKRLNEIE----TLVVISHDRSVLN 162
Cdd:cd03215 90 vldlsVA-ENIalssllSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAdagkAVLLISSELDELL 168
|
170
....*....|....
gi 1124469102 163 EICDRIVEISFGKL 176
Cdd:cd03215 169 GLCDRILVMYEGRI 182
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
27-168 |
1.74e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 49.70 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 27 FYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVS-----------------SNCIPFFFEqfgsD----------- 78
Cdd:PRK15079 42 LRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwlgkdllgmkddewravRSDIQMIFQ----Dplaslnprmti 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 79 ----SEYFETDYAEAGKMGVADHIWQ--------ENV--------SGGEDTRIRLAQ-LFSSPHAVaFLDEPTSNLDYN- 136
Cdd:PRK15079 118 geiiAEPLRTYHPKLSRQEVKDRVKAmmlkvgllPNLinryphefSGGQCQRIGIARaLILEPKLI-ICDEPVSALDVSi 196
|
170 180 190
....*....|....*....|....*....|....*.
gi 1124469102 137 ---GVEMLKKRLNEIE-TLVVISHDRSVLNEICDRI 168
Cdd:PRK15079 197 qaqVVNLLQQLQREMGlSLIFIAHDLAVVKHISDRV 232
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
311-482 |
1.90e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 50.49 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 311 IFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREK----VYVVPGakigyarQNMSQID---LSQ------------- 370
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKptsgTYRVAG-------QDVATLDadaLAQlrrehfgfifqry 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 371 ------TVLVNVRRVSI-------QSESISRIVLARLLLSERdMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNY 437
Cdd:PRK10535 96 hllshlTAAQNVEVPAVyaglerkQRLLRAQELLQRLGLEDR-VEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1124469102 438 LDIPS---VEALEKMLVEYEGTLIFTSHDKVF---VDRIatdrLYIGDGKI 482
Cdd:PRK10535 175 LDSHSgeeVMAILHQLRDRGHTVIIVTHDPQVaaqAERV----IEIRDGEI 221
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
296-482 |
1.90e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 49.34 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 296 VIRGEHISFAYD---DHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELIN-----------------NREKVYVVPgAK 355
Cdd:PRK13650 4 IIEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDglleaesgqiiidgdllTEENVWDIR-HK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 356 IGYARQNMSQIDLSQTVLVNV------RRVSIQsESISRIVLARLLLSERDM-NKKASELSGGERMKLSFAMLFVSDVNL 428
Cdd:PRK13650 83 IGMVFQNPDNQFVGATVEDDVafglenKGIPHE-EMKERVNEALELVGMQDFkEREPARLSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1124469102 429 LILDEPTNYLD-------IPSVEALEKmlvEYEGTLIFTSHDkvfVDRIA-TDR-LYIGDGKI 482
Cdd:PRK13650 162 IILDEATSMLDpegrlelIKTIKGIRD---DYQMTVISITHD---LDEVAlSDRvLVMKNGQV 218
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
11-163 |
2.18e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.41 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 11 NIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTvssncIPFFFEQFGSDSEYFETDYAEAG 90
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGE-----ILFERQSIKKDLCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 91 -KMGVADHI-WQEN---------------------------------VSGGEDTRIRLAQLFSSPHAVAFLDEPTSNLDY 135
Cdd:PRK13540 81 hRSGINPYLtLRENclydihfspgavgitelcrlfslehlidypcglLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
170 180 190
....*....|....*....|....*....|..
gi 1124469102 136 NGVEMLKKRLNEIE----TLVVISHDRSVLNE 163
Cdd:PRK13540 161 LSLLTIITKIQEHRakggAVLLTSHQDLPLNK 192
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
261-439 |
2.37e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.36 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 261 NVLKRLEHMEIKEKPKEELTVRPDFRLT-NPPRNPIV--IRGEHISFAYDDHV---IFDDADFMIKNGSKVALLGGNGAG 334
Cdd:PLN03232 576 NLLSQVVNANVSLQRIEELLLSEERILAqNPPLQPGApaISIKNGYFSWDSKTskpTLSDINLEIPVGSLVAIVGGTGEG 655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 335 KTTLLEL----INNREKVYVVPGAKIGYARQnMSQIdLSQTVLVNVRRVS-IQSESISRIVLARLLLSERDM-------- 401
Cdd:PLN03232 656 KTSLISAmlgeLSHAETSSVVIRGSVAYVPQ-VSWI-FNATVRENILFGSdFESERYWRAIDVTALQHDLDLlpgrdlte 733
|
170 180 190
....*....|....*....|....*....|....*....
gi 1124469102 402 -NKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLD 439
Cdd:PLN03232 734 iGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
297-471 |
2.38e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 48.88 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINN-------------------------------R 345
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRmnelesevrvegrveffnqniyerrvnlnrlR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 346 EKVYVVpgakigYARQNMSQIDLSQTVLVNVRRVSIQSE-SISRIVLARLLLSE------RDMNKKASELSGGERMKLSF 418
Cdd:PRK14258 88 RQVSMV------HPKPNLFPMSVYDNVAYGVKIVGWRPKlEIDDIVESALKDADlwdeikHKIHKSALDLSGGQQQRLCI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1124469102 419 AMLFVSDVNLLILDEPTNYLDIPSVEALEKML----VEYEGTLIFTSHDKVFVDRIA 471
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIqslrLRSELTMVIVSHNLHQVSRLS 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
300-471 |
2.47e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.09 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 300 EHISFAY----DDHVIFDDADFMIKNGSKVALLGGNGAGKT----TLLELINNREKVYvvPGAKIGYARQnmSQIDLSQT 371
Cdd:PRK15134 9 ENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVY--PSGDIRFHGE--SLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 372 VLVNVR--RVSI--QSESIS-------RIVLARLLLSERDMNKKAS-------------------------ELSGGERMK 415
Cdd:PRK15134 85 TLRGVRgnKIAMifQEPMVSlnplhtlEKQLYEVLSLHRGMRREAArgeilncldrvgirqaakrltdyphQLSGGERQR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1124469102 416 LSFAMLFVSDVNLLILDEPTNYLDIpSVEA-----LEKMLVEYEGTLIFTSHDKVFVDRIA 471
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALDV-SVQAqilqlLRELQQELNMGLLFITHNLSIVRKLA 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
7-187 |
2.54e-06 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 48.64 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYG--EQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKG----------TVSSNcipFFFEQ 74
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGrvlvdghdlaLADPA---WLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 75 FG---SDSEYFE---------TDYA-------EAGKMGVA-----------DHIWQEN---VSGGEDTRIRLAQ-LFSSP 120
Cdd:cd03252 78 VGvvlQENVLFNrsirdnialADPGmsmerviEAAKLAGAhdfiselpegyDTIVGEQgagLSGGQRQRIAIARaLIHNP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 121 HAVAFlDEPTSNLDYNGVEMLKKRLNEI---ETLVVISHDRSVLNEiCDRIVEISFGKLQNySGNYDEYV 187
Cdd:cd03252 158 RILIF-DEATSALDYESEHAIMRNMHDIcagRTVIIIAHRLSTVKN-ADRIIVMEKGRIVE-QGSHDELL 224
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
4-177 |
2.64e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 48.66 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 4 HLLIKAENIVHSYGE---QT-VLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPF--------- 70
Cdd:PRK11629 3 KILLQCDNLCKRYQEgsvQTdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklssaaka 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 71 --------FFEQF------------------------GSDSEYFETDYAEAGKMGVADHIWQEnVSGGEDTRIRLAQ-LF 117
Cdd:PRK11629 83 elrnqklgFIYQFhhllpdftalenvamplligkkkpAEINSRALEMLAAVGLEHRANHRPSE-LSGGERQRVAIARaLV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1124469102 118 SSPHAVaFLDEPTSNLDYNGVEMLKKRLNEIE-----TLVVISHDRSVLNEIcDRIVEISFGKLQ 177
Cdd:PRK11629 162 NNPRLV-LADEPTGNLDARNADSIFQLLGELNrlqgtAFLVVTHDLQLAKRM-SRQLEMRDGRLT 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
7-176 |
3.34e-06 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 48.21 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIP----------------- 69
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITidtarslsqqkglirql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 70 -----FFFEQFG---------------------SDSEYFETDYAEAGKMGVA--DHIWQENVSGGEDTRIRLAQLFSSPH 121
Cdd:PRK11264 84 rqhvgFVFQNFNlfphrtvleniiegpvivkgePKEEATARARELLAKVGLAgkETSYPRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1124469102 122 AVAFLDEPTSNLDyngVEMLKKRLNEI-------ETLVVISHDRSVLNEICDRIVEISFGKL 176
Cdd:PRK11264 164 EVILFDEPTSALD---PELVGEVLNTIrqlaqekRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
289-463 |
3.37e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 48.63 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 289 NPPRNPIVIRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLE-------------LINNR------EKVY 349
Cdd:PRK10575 4 YTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKmlgrhqppsegeiLLDAQpleswsSKAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 350 vvpGAKIGYARQNMSQIDlSQTV--LVNVRRVSIQ--------------SESISRIVLARLllserdMNKKASELSGGER 413
Cdd:PRK10575 84 ---ARKVAYLPQQLPAAE-GMTVreLVAIGRYPWHgalgrfgaadrekvEEAISLVGLKPL------AHRLVDSLSGGER 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1124469102 414 MKLSFAMLFVSDVNLLILDEPTNYLDIP---SVEALEKMLVEYEG-TLIFTSHD 463
Cdd:PRK10575 154 QRAWIAMLVAQDSRCLLLDEPTSALDIAhqvDVLALVHRLSQERGlTVIAVLHD 207
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-190 |
3.44e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 49.44 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 4 HLLIKAENIVHSY--GEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPFffeqfgsdsey 81
Cdd:PRK11160 336 QVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPI----------- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 82 feTDYAEAG----------------------------------------KMGVADHIWQEN------------VSGGEDT 109
Cdd:PRK11160 405 --ADYSEAAlrqaisvvsqrvhlfsatlrdnlllaapnasdealievlqQVGLEKLLEDDKglnawlgeggrqLSGGEQR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 110 RIRLAQLFSSPHAVAFLDEPTSNLDyngvemlKKRLNEI----------ETLVVISHdRSVLNEICDRIVEISFGKLQNy 179
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLD-------AETERQIlellaehaqnKTVLMITH-RLTGLEQFDRICVMDNGQIIE- 553
|
250
....*....|.
gi 1124469102 180 SGNYDEYVVQK 190
Cdd:PRK11160 554 QGTHQELLAQQ 564
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
250-442 |
4.89e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 49.07 E-value: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 250 DKARGIerSATNVLKRLEHMEIKEKPKEELTVRPDfrltnpprNPIVIRGEHIS-FAYDDHVIFDDADFMIKNGSKVALL 328
Cdd:PRK11174 313 AKAQAV--GAAESLVTFLETPLAHPQQGEKELASN--------DPVTIEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 329 GGNGAGKTTLLE------------LINNREKVYVVPGA---KIGYARQNmSQIdLSQTVLVNVR--RVSIQSESISRiVL 391
Cdd:PRK11174 383 GPSGAGKTSLLNallgflpyqgslKINGIELRELDPESwrkHLSWVGQN-PQL-PHGTLRDNVLlgNPDASDEQLQQ-AL 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1124469102 392 ARLLLSE----------RDMNKKASELSGG--ERMKLSFAMLfvSDVNLLILDEPTNYLDIPS 442
Cdd:PRK11174 460 ENAWVSEflpllpqgldTPIGDQAAGLSVGqaQRLALARALL--QPCQLLLLDEPTASLDAHS 520
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-54 |
5.18e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.77 E-value: 5.18e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1124469102 1 MERHLLiKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAG 54
Cdd:PRK13549 1 MMEYLL-EMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG 53
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
12-176 |
5.32e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 49.24 E-value: 5.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 12 IVHSYGEQTVldfDRFYL--YEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNcipfffeqfGSDSEYFETDYAEA 89
Cdd:TIGR01257 937 IFEPSGRPAV---DRLNItfYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVG---------GKDIETNLDAVRQS 1004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 90 GKM-----------GVADHI----------WQE-----------------------NVSGGEDTRIRLAQLFSSPHAVAF 125
Cdd:TIGR01257 1005 LGMcpqhnilfhhlTVAEHIlfyaqlkgrsWEEaqlemeamledtglhhkrneeaqDLSGGMQRKLSVAIAFVGDAKVVV 1084
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1124469102 126 LDEPTSNLD-YNGVE----MLKKRLNeiETLVVISHDRSVLNEICDRIVEISFGKL 176
Cdd:TIGR01257 1085 LDEPTSGVDpYSRRSiwdlLLKYRSG--RTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
313-479 |
6.22e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 47.88 E-value: 6.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 313 DDADFMIKNGSKVALLGGNGAGKTTLLELINNREK----VYVVPGAKI------------GYARQNMSQIDLSQTVLVNV 376
Cdd:PRK13652 21 NNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKptsgSVLIRGEPItkenirevrkfvGLVFQNPDDQIFSPTVEQDI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 377 R----RVSIQSESISRIV--LARLLLSERDMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIPSVEAL---- 446
Cdd:PRK13652 101 AfgpiNLGLDEETVAHRVssALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELidfl 180
|
170 180 190
....*....|....*....|....*....|...
gi 1124469102 447 EKMLVEYEGTLIFTSHDKVFVDRIAtDRLYIGD 479
Cdd:PRK13652 181 NDLPETYGMTVIFSTHQLDLVPEMA-DYIYVMD 212
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
7-189 |
8.38e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 48.30 E-value: 8.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAEN-IVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELePTKGTVSSNCI----------------- 68
Cdd:PRK11174 350 IEAEDlEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIelreldpeswrkhlswv 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 69 ---PFFFEQ-------FG----SDSEY-------FETDYAEAGKMGVaDHIWQEN---VSGGEDTRIRLAQLFSSPHAVA 124
Cdd:PRK11174 429 gqnPQLPHGtlrdnvlLGnpdaSDEQLqqalenaWVSEFLPLLPQGL-DTPIGDQaagLSVGQAQRLALARALLQPCQLL 507
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1124469102 125 FLDEPTSNLDYNGVEMLKKRLNEI---ETLVVISHDRSVLNEiCDRIVEISFGKL-QnySGNYDEYVVQ 189
Cdd:PRK11174 508 LLDEPTASLDAHSEQLVMQALNAAsrrQTTLMVTHQLEDLAQ-WDQIWVMQDGQIvQ--QGDYAELSQA 573
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
11-169 |
8.70e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 47.72 E-value: 8.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 11 NIVHSYGEQTV---LDFDrfyLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTV------------SSNCIPFFFEQF 75
Cdd:PRK11000 8 NVTKAYGDVVIskdINLD---IHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLfigekrmndvppAERGVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 76 G-------SDSEYFETDYAEAGKMGVADHIWQ---------------ENVSGGEDTRIRLAQLFSSPHAVAFLDEPTSNL 133
Cdd:PRK11000 85 AlyphlsvAENMSFGLKLAGAKKEEINQRVNQvaevlqlahlldrkpKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1124469102 134 DYN-GVEM------LKKRLNeiETLVVISHDRSVLNEICDRIV 169
Cdd:PRK11000 165 DAAlRVQMrieisrLHKRLG--RTMIYVTHDQVEAMTLADKIV 205
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
32-134 |
1.08e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.13 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 32 GEKVGLVGMNGAGKSTLLKILAGELEPT--------KGTVSSN-------------CIPFFFEQFGSDSEYFETD----- 85
Cdd:PRK13547 27 GRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNgeplaaidaprlaRLRAVLPQAAQPAFAFSAReivll 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 86 --YAEAGKMGVADH-----IWQ---------------ENVSGGEDTRIR----LAQLFSSPHAVA-----FLDEPTSNLD 134
Cdd:PRK13547 107 grYPHARRAGALTHrdgeiAWQalalagatalvgrdvTTLSGGELARVQfarvLAQLWPPHDAAQpprylLLDEPTAALD 186
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
296-450 |
1.09e-05 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 46.81 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 296 VIRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELInnrekVYVVP--GAKIGYARQNMSQIDLSQTVL 373
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMV-----VGIVPrdAGNIIIDDEDISLLPLHARAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 374 VNV----------RRVSIqSESISRIVLARLLLSERDMNKKASE-----------------LSGGERMKLSFAMLFVSDV 426
Cdd:PRK10895 78 RGIgylpqeasifRRLSV-YDNLMAVLQIRDDLSAEQREDRANElmeefhiehlrdsmgqsLSGGERRRVEIARALAANP 156
|
170 180
....*....|....*....|....
gi 1124469102 427 NLLILDEPTNYLDIPSVEALEKML 450
Cdd:PRK10895 157 KFILLDEPFAGVDPISVIDIKRII 180
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
37-134 |
1.17e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.24 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 37 LVGMNGAGKSTLLKILAGELEPTKG--------------------TVSSNcIPFFFEQFGSDSE------YFETDYA--- 87
Cdd:PTZ00243 691 VLGATGSGKSTLLQSLLSQFEISEGrvwaersiayvpqqawimnaTVRGN-ILFFDEEDAARLAdavrvsQLEADLAqlg 769
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1124469102 88 -----EAGKMGVadhiwqeNVSGGEDTRIRLAQLFSSPHAVAFLDEPTSNLD 134
Cdd:PTZ00243 770 ggletEIGEKGV-------NLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
7-176 |
1.24e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 47.13 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQTV-----LDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTV----------SSN----- 66
Cdd:PRK13641 3 IKFENVDYIYSPGTPmekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTItiagyhitpeTGNknlkk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 67 -----CIPFFFEQ-------------FGSDSEYFETDYAEAG------KMGVADHIWQEN---VSGGEDTRIRLAQLFSS 119
Cdd:PRK13641 83 lrkkvSLVFQFPEaqlfentvlkdveFGPKNFGFSEDEAKEKalkwlkKVGLSEDLISKSpfeLSGGQMRRVAIAGVMAY 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1124469102 120 PHAVAFLDEPTSNLDYNG-VEMLKKRLN---EIETLVVISHDRSVLNEICDRIVEISFGKL 176
Cdd:PRK13641 163 EPEILCLDEPAAGLDPEGrKEMMQLFKDyqkAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
321-476 |
1.29e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 45.43 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 321 NGSKVALLGGNGAGKTTLLElinnrekvyvvpgaKIGYArqnmsqidLSQTVLVNVRRVSIQSESISRIVLARLLLSerd 400
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILD--------------AIGLA--------LGGAQSATRRRSGVKAGCIVAAVSAELIFT--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 401 mnkkASELSGGERMKLSFAMLF----VSDVNLLILDEPTNYLDIPSVEALEKMLVEY---EGTLIFTSHDKVFVDRIatD 473
Cdd:cd03227 75 ----RLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHlvkGAQVIVITHLPELAELA--D 148
|
...
gi 1124469102 474 RLY 476
Cdd:cd03227 149 KLI 151
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
5-194 |
1.59e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 46.65 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 5 LLIKAENIVHSYGEQT-VLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTV--------SSNC-------- 67
Cdd:PRK13647 3 NIIEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkvmgrevnAENEkwvrskvg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 68 ------------------IPFFFEQFGSDSEYFETDYAEAGK---MGVADHIWQENVSGGEDTRIRLAQLFSSPHAVAFL 126
Cdd:PRK13647 83 lvfqdpddqvfsstvwddVAFGPVNMGLDKDEVERRVEEALKavrMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1124469102 127 DEPTSNLDYNGVEMLKKRLNEI----ETLVVISHDRSVLNEICDRIVEISFGKLQNYSGN---YDEYVVQKEEQR 194
Cdd:PRK13647 163 DEPMAYLDPRGQETLMEILDRLhnqgKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKsllTDEDIVEQAGLR 237
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
301-347 |
1.60e-05 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 47.02 E-value: 1.60e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1124469102 301 HISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREK 347
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEK 57
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-177 |
1.66e-05 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 46.86 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 1 MERHLLIKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKG------------------- 61
Cdd:PRK09452 9 SSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGrimldgqdithvpaenrhv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 62 -TVSSNCIPF----FFEQ--FG-----SDSEYFETDYAEAGKMGVADHIWQENV---SGGEDTRIRLAQLFSSPHAVAFL 126
Cdd:PRK09452 89 nTVFQSYALFphmtVFENvaFGlrmqkTPAAEITPRVMEALRMVQLEEFAQRKPhqlSGGQQQRVAIARAVVNKPKVLLL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1124469102 127 DEPTSNLDY-------NGVEMLKKRLNeIeTLVVISHDRSVLNEICDRIVEISFGKLQ 177
Cdd:PRK09452 169 DESLSALDYklrkqmqNELKALQRKLG-I-TFVFVTHDQEEALTMSDRIVVMRDGRIE 224
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
7-64 |
1.71e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 46.55 E-value: 1.71e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1124469102 7 IKAENIVHSYGEQTvlDFDRFYLY-------EGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVS 64
Cdd:PRK13634 3 ITFQKVEHRYQYKT--PFERRALYdvnvsipSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVT 65
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-54 |
1.98e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 47.13 E-value: 1.98e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1124469102 6 LIKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAG 54
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG 49
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
30-66 |
2.06e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.96 E-value: 2.06e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1124469102 30 YEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSN 66
Cdd:PRK13546 48 YEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRN 84
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
307-439 |
2.12e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.41 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 307 DDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREKVYVVPGA---------------KIGYARQNmsQIDLSQT 371
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVITGGdrlvngrpldssfqrSIGYVQQQ--DLHLPTS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 372 VLVNVRRVSI---QSESIS-----RIV--LARLLlserDMNKKASELSG--GE------RMKLSFAMLFVSDVNLLI-LD 432
Cdd:TIGR00956 852 TVRESLRFSAylrQPKSVSksekmEYVeeVIKLL----EMESYADAVVGvpGEglnveqRKRLTIGVELVAKPKLLLfLD 927
|
....*..
gi 1124469102 433 EPTNYLD 439
Cdd:TIGR00956 928 EPTSGLD 934
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
7-157 |
2.18e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 46.23 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQT-----VLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVS-------SNCIPFFFEQ 74
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdekNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 75 FGSD---------------------------SEY--FE---------------TDYAEAGK--------MGVADHIWQE- 101
Cdd:PRK13651 83 VLEKlviqktrfkkikkikeirrrvgvvfqfAEYqlFEqtiekdiifgpvsmgVSKEEAKKraakyielVGLDESYLQRs 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1124469102 102 --NVSGGEDTRIRLAQLFSSPHAVAFLDEPTSNLDYNGV-EMLK--KRLNEI-ETLVVISHD 157
Cdd:PRK13651 163 pfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVkEILEifDNLNKQgKTIILVTHD 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
297-471 |
2.36e-05 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 46.20 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDDHVIF--DDADFMIKNGSKVALLGGNGAGKTTLLELINNREKVYVVPGAKIGYARQNMSqiDLSQTVLV 374
Cdd:COG0444 4 VRNLKVYFPTRRGVVKavDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGITSGEILFDGEDLL--KLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 375 NVRRVSIQ----------------SESISRIVLARLLLSERDMNKKA--------------------SELSGGERMKLSF 418
Cdd:COG0444 82 KIRGREIQmifqdpmtslnpvmtvGDQIAEPLRIHGGLSKAEARERAiellervglpdperrldrypHELSGGMRQRVMI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1124469102 419 AMLFVSDVNLLILDEPTNYLDIpSVEA-----LEKMLVEYEGTLIFTSHD----KVFVDRIA 471
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDV-TIQAqilnlLKDLQRELGLAILFITHDlgvvAEIADRVA 222
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
318-461 |
2.38e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 46.80 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 318 MIKNGSKVALLGGNGAGKTTLLE---------------LINNREKVYVVPgAKIGYARQN---MSQIDLSQT-VLVNVRR 378
Cdd:PLN03211 90 MASPGEILAVLGPSGSGKSTLLNalagriqgnnftgtiLANNRKPTKQIL-KRTGFVTQDdilYPHLTVRETlVFCSLLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 379 VSIQSESISRIVLARLLLSERDMNKKASE---------LSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIPSVEALEKM 449
Cdd:PLN03211 169 LPKSLTKQEKILVAESVISELGLTKCENTiignsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLT 248
|
170
....*....|....
gi 1124469102 450 LVE--YEGTLIFTS 461
Cdd:PLN03211 249 LGSlaQKGKTIVTS 262
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-165 |
2.57e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 45.75 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTV----------------------S 64
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiqhyaskevarrigllA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 65 SNCI-------------------PFFFEQFGSDSEyfetdyAEAGKM---GVADHIWQ--ENVSGGEDTRIRLAQLFSSP 120
Cdd:PRK10253 88 QNATtpgditvqelvargryphqPLFTRWRKEDEE------AVTKAMqatGITHLADQsvDTLSGGQRQRAWIAMVLAQE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1124469102 121 HAVAFLDEPTSNLDYNGVEMLKKRLNEIE-----TLVVISHDrsvLNEIC 165
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELNrekgyTLAAVLHD---LNQAC 208
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
290-463 |
3.92e-05 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 46.22 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 290 PPRNPIVIRGEHISFAY-----------DDHVIFDDADFMIKNGSKVALLGGNGAGKTTL----LELINnrekvyvvPGA 354
Cdd:COG4172 269 PPDAPPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIP--------SEG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 355 KIGYARQNMSQidLSQTVLVNVRRvSIQ--------SES----ISRIV-----------------------LARLLLSER 399
Cdd:COG4172 341 EIRFDGQDLDG--LSRRALRPLRR-RMQvvfqdpfgSLSprmtVGQIIaeglrvhgpglsaaerrarvaeaLEEVGLDPA 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1124469102 400 DMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIpSVEA-----LEKMLVEYEGTLIFTSHD 463
Cdd:COG4172 418 ARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDV-SVQAqildlLRDLQREHGLAYLFISHD 485
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
6-63 |
3.98e-05 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 44.87 E-value: 3.98e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1124469102 6 LIKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTV 63
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRI 62
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
296-442 |
5.11e-05 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 45.00 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 296 VIRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREKVYVVPGAKI------------------- 356
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIellgrtvqregrlardirk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 357 -----GYARQNMSQIDlSQTVLVNVRRVSIQSESISRIVL----------ARLLLSERDM----NKKASELSGGERMKLS 417
Cdd:PRK09984 84 srantGYIFQQFNLVN-RLSVLENVLIGALGSTPFWRTCFswftreqkqrALQALTRVGMvhfaHQRVSTLSGGQQQRVA 162
|
170 180
....*....|....*....|....*
gi 1124469102 418 FAMLFVSDVNLLILDEPTNYLDIPS 442
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPES 187
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
27-80 |
5.87e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 44.78 E-value: 5.87e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1124469102 27 FYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPFFFEQFGSDSE 80
Cdd:PRK15112 34 FTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQ 87
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
27-228 |
5.91e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 45.65 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 27 FYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTV----SSNCIPFFFEQFG--SDSEYFE----------------- 83
Cdd:PRK13545 45 FEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVdikgSAALIAISSGLNGqlTGIENIElkglmmgltkekikeii 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 84 ---TDYAEAGKMgvadhIWQ--ENVSGGEDTRIRLAQLFSSPHAVAFLDEPTSNLDYNGVEMLKKRLNEI----ETLVVI 154
Cdd:PRK13545 125 peiIEFADIGKF-----IYQpvKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFkeqgKTIFFI 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 155 SHDRSVLNEICDRIVEISFGKLQNYS------GNYDEYV-----VQKEEQRKTQQAEYENYQ------AEKKRLQSVYVE 217
Cdd:PRK13545 200 SHSLSQVKSFCTKALWLHYGQVKEYGdikevvDHYDEFLkkynqMSVEERKDFREEQISQFQhgllqeDQTGRERKRKKG 279
|
250
....*....|.
gi 1124469102 218 KKAKAKTVDKK 228
Cdd:PRK13545 280 KKTSRKFKKKR 290
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
297-482 |
6.04e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 44.77 E-value: 6.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYD-----DHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELIN----------NREKVYVVPGAKIGYARQ 361
Cdd:PRK13646 3 IRFDNVSYTYQkgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINallkpttgtvTVDDITITHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 362 NMSQIDL------SQTVLVNVRRVSI-----------QSESISRIVLARLLLSERDMNKKASELSGGERMKLSFAMLFVS 424
Cdd:PRK13646 83 VRKRIGMvfqfpeSQLFEDTVEREIIfgpknfkmnldEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAM 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1124469102 425 DVNLLILDEPTNYLDIPS----VEALEKMLVEYEGTLIFTSHDKVFVDRIATDRLYIGDGKI 482
Cdd:PRK13646 163 NPDIIVLDEPTAGLDPQSkrqvMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
27-177 |
6.35e-05 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 45.48 E-value: 6.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 27 FYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPffFEQF--------------------GSDSE---YFE 83
Cdd:TIGR00958 502 FTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVP--LVQYdhhylhrqvalvgqepvlfsGSVREniaYGL 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 84 TDYAEAGKMGVA------DHI------WQENV-------SGGEDTRIRLAQLFSSPHAVAFLDEPTSNLDYNgVEMLKKR 144
Cdd:TIGR00958 580 TDTPDEEIMAAAkaanahDFImefpngYDTEVgekgsqlSGGQKQRIAIARALVRKPRVLILDEATSALDAE-CEQLLQE 658
|
170 180 190
....*....|....*....|....*....|....*
gi 1124469102 145 LNEIE--TLVVISHDRSVLnEICDRIVEISFGKLQ 177
Cdd:TIGR00958 659 SRSRAsrTVLLIAHRLSTV-ERADQILVLKKGSVV 692
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-134 |
7.54e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 45.67 E-value: 7.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 21 VLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPFFFEQFG-------SDSEYFETDYAEAGKMG 93
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSwimpgtiKDNIIFGLSYDEYRYTS 520
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 94 VADHIWQE-------------------NVSGGEDTRIRLAQLFSSPHAVAFLDEPTSNLD 134
Cdd:TIGR01271 521 VIKACQLEedialfpekdktvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
30-168 |
8.06e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.99 E-value: 8.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 30 YEGEKVGLVGMNGAGKSTLLKIL-------AGELE----PT--KGTVSS------------NCIP--------F----FF 72
Cdd:PRK10762 28 YPGRVMALVGENGAGKSTMMKVLtgiytrdAGSILylgkEVtfNGPKSSqeagigiihqelNLIPqltiaeniFlgreFV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 73 EQFGSDSeyFETDYAEAGK----MGV--ADHIWQENVSGGEDTRIRLAQLFSSPHAVAFLDEPTSNLDYNGVEMLKKRLN 146
Cdd:PRK10762 108 NRFGRID--WKKMYAEADKllarLNLrfSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIR 185
|
170 180
....*....|....*....|....*.
gi 1124469102 147 EIET----LVVISHDRSVLNEICDRI 168
Cdd:PRK10762 186 ELKSqgrgIVYISHRLKEIFEICDDV 211
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
27-169 |
8.19e-05 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 44.66 E-value: 8.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 27 FYLYEGEKVGLVGMNGAGKSTLLKILAGELEP---TKGTVssncipfFFEqfGSD-SEYFETDYAE--AGKMG------- 93
Cdd:COG0444 26 FDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEI-------LFD--GEDlLKLSEKELRKirGREIQmifqdpm 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 94 ------------VADHIWQENVSGGEDTRIRLAQLFSS-------------PH--------------AVA----FL--DE 128
Cdd:COG0444 97 tslnpvmtvgdqIAEPLRIHGGLSKAEARERAIELLERvglpdperrldryPHelsggmrqrvmiarALAlepkLLiaDE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1124469102 129 PTSNLDyngV-------EMLKKRLNEIE-TLVVISHDRSVLNEICDRIV 169
Cdd:COG0444 177 PTTALD---VtiqaqilNLLKDLQRELGlAILFITHDLGVVAEIADRVA 222
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
304-477 |
8.45e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 44.23 E-value: 8.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 304 FAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLE----LINNREKVYVVPGAKIGYA-------RQNMSQI------ 366
Cdd:PRK13638 9 FRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMnlsgLLRPQKGAVLWQGKPLDYSkrgllalRQQVATVfqdpeq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 367 -----DLSQTVLVNVRRVSIQSESISRIVLARLLL--SERDMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLD 439
Cdd:PRK13638 89 qifytDIDSDIAFSLRNLGVPEAEITRRVDEALTLvdAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1124469102 440 iPS----VEALEKMLVEYEGTLIFTSHDKVFVDRIaTDRLYI 477
Cdd:PRK13638 169 -PAgrtqMIAIIRRIVAQGNHVIISSHDIDLIYEI-SDAVYV 208
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
319-481 |
1.28e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.56 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 319 IKNGSKVALLGGNGAGKTTLLELINNREKVyvvPGAKIGYARQnmsqidlsqtvlvnvrRVSIQSESISrivlarlllse 398
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIP---NGDNDEWDGI----------------TPVYKPQYID----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 399 rdmnkkaseLSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIP----SVEALEKMLVEYEGTLIFTSHDKVFVDRIAtDR 474
Cdd:cd03222 72 ---------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAARAIRRLSEEGKKTALVVEHDLAVLDYLS-DR 141
|
....*..
gi 1124469102 475 LYIGDGK 481
Cdd:cd03222 142 IHVFEGE 148
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
7-180 |
1.46e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.73 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQ--TVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVS-------------------- 64
Cdd:PLN03130 1238 IKFEDVVLRYRPElpPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILidgcdiskfglmdlrkvlgi 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 65 --------SNCIPFFFEQFG--SDSEYFET-------------------DYAEAGkmgvadhiwqENVSGGEDTRIRLAQ 115
Cdd:PLN03130 1318 ipqapvlfSGTVRFNLDPFNehNDADLWESlerahlkdvirrnslgldaEVSEAG----------ENFSVGQRQLLSLAR 1387
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1124469102 116 LFSSPHAVAFLDEPTSNLDYNGVEMLKKRLNEiE----TLVVISHDrsvLNEI--CDRIVEISFGKLQNYS 180
Cdd:PLN03130 1388 ALLRRSKILVLDEATAAVDVRTDALIQKTIRE-EfkscTMLIIAHR---LNTIidCDRILVLDAGRVVEFD 1454
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
301-482 |
1.51e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 43.55 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 301 HISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINN-REKV--YVVPG-------------------AKIG- 357
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRmNDKVsgYRYSGdvllggrsifnyrdvlefrRRVGm 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 358 -YARQNMSQIDLSQTVLVNVR------RVSIQSESISRIVLARLLLSERD-MNKKASELSGGERMKLSFAMLFVSDVNLL 429
Cdd:PRK14271 106 lFQRPNPFPMSIMDNVLAGVRahklvpRKEFRGVAQARLTEVGLWDAVKDrLSDSPFRLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1124469102 430 ILDEPTNYLDIPSVEALEKMLVEYEG--TLIFTSHDKVFVDRIATDRLYIGDGKI 482
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
16-177 |
1.56e-04 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 43.42 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 16 YGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNC---------------------------I 68
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgqlkvadknqlrllrtrL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 69 PFFFEQFG---------------------SDSEYFETDYAEAGKMGVADHIWQE---NVSGGEDTRIRLAQLFSSPHAVA 124
Cdd:PRK10619 95 TMVFQHFNlwshmtvlenvmeapiqvlglSKQEARERAVKYLAKVGIDERAQGKypvHLSGGQQQRVSIARALAMEPEVL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1124469102 125 FLDEPTSNLDYNGV----EMLKKRLNEIETLVVISHDRSVLNEICDRIVEISFGKLQ 177
Cdd:PRK10619 175 LFDEPTSALDPELVgevlRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
312-482 |
1.60e-04 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 42.42 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 312 FDDADFMIKNGSKVALLGGNGAGKTTLLELI-------------NNREKVYVVPG----AKIGYA---RQNMSQIdLSQT 371
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALfglrppasgeitlDGKPVTRRSPRdairAGIAYVpedRKREGLV-LDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 372 VLVNvrrvsiqsesisrIVLARLLlserdmnkkaselSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIPSVEALEKMLV 451
Cdd:cd03215 95 VAEN-------------IALSSLL-------------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIR 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 1124469102 452 EY--EGT---LIFTSHDKVF--VDRIATdrlyIGDGKI 482
Cdd:cd03215 149 ELadAGKavlLISSELDELLglCDRILV----MYEGRI 182
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
319-462 |
1.68e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 44.62 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 319 IKNGSKVALLGGNGAGKTTLLELINNREKVY----VVPG----AKIGYARQNMS---QIDLSQTVLVN-------VRRVS 380
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTsgdaTVAGksilTNISDVHQNMGycpQFDAIDDLLTGrehlylyARLRG 2041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 381 IQSESISRIV---LARLLLSERdMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIPSVEALEKMLVEY---E 454
Cdd:TIGR01257 2042 VPAEEIEKVAnwsIQSLGLSLY-ADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIireG 2120
|
....*...
gi 1124469102 455 GTLIFTSH 462
Cdd:TIGR01257 2121 RAVVLTSH 2128
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
18-176 |
1.68e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 43.25 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 18 EQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEP-----TKGTVS---------------------------- 64
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnpnSKITVDgitltaktvwdirekvgivfqnpdnqfv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 65 ----SNCIPFFFEQFGSDSEYFETDYAEA-GKMGVADHIWQE--NVSGGEDTRIRLAQLFSSPHAVAFLDEPTSNLDYNG 137
Cdd:PRK13640 99 gatvGDDVAFGLENRAVPRPEMIKIVRDVlADVGMLDYIDSEpaNLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1124469102 138 VEMLKKRLNEIE-----TLVVISHDrsvLNE--ICDRIVEISFGKL 176
Cdd:PRK13640 179 KEQILKLIRKLKkknnlTVISITHD---IDEanMADQVLVLDDGKL 221
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
103-471 |
1.91e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.08 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 103 VSGGEDTRIRLAQLFSSPHAVAFLDEPTSNLDyngVEMLKKRLNEIETL--------VVISHDRSVLNEICDRIVEIsfg 174
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALD---VTIQAQILQLIKVLqkemsmgvIFITHDMGVVAEIADRVLVM--- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 175 klqnysgnydeyvvqkeeqrktqqaeyenYQAEKkrLQSVYVEKKAKAKTvdkKPKNMSASEAKVRafIGNRKPEDKARG 254
Cdd:PRK10261 243 -----------------------------YQGEA--VETGSVEQIFHAPQ---HPYTRALLAAVPQ--LGAMKGLDYPRR 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 255 IErsatnvLKRLEHMEIKEKPKEELTV---RPDFRLTN-----PPRNPIVIRGEHISFAYDDhVIFDdadfmIKNGSKVA 326
Cdd:PRK10261 287 FP------LISLEHPAKQEPPIEQDTVvdgEPILQVRNlvtrfPLRSGLLNRVTREVHAVEK-VSFD-----LWPGETLS 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 327 LLGGNGAGKTT----LLELIN--------NREKVYVVPGAKIGYARQNM--------SQIDLSQTV---LVNVRRVS--I 381
Cdd:PRK10261 355 LVGESGSGKSTtgraLLRLVEsqggeiifNGQRIDTLSPGKLQALRRDIqfifqdpyASLDPRQTVgdsIMEPLRVHglL 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 382 QSESISRIV---LARLLLSERDMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIPSVEALEKMLVEYEGTL- 457
Cdd:PRK10261 435 PGKAAAARVawlLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFg 514
|
410
....*....|....*..
gi 1124469102 458 ---IFTSHDKVFVDRIA 471
Cdd:PRK10261 515 iayLFISHDMAVVERIS 531
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
296-464 |
1.99e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 43.97 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 296 VIRGEHISFAY-DDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNREKVY-----VVPGAKIGYARQN--MSQID 367
Cdd:TIGR00954 451 GIKFENIPLVTpNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYggrltKPAKGKLFYVPQRpyMTLGT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 368 LSQTVLVNVRRVSIQSESISRIVLARLL-------LSERDMNKKA-----SELSGGERMKLSFAMLFVSDVNLLILDEPT 435
Cdd:TIGR00954 531 LRDQIIYPDSSEDMKRRGLSDKDLEQILdnvqlthILEREGGWSAvqdwmDVLSGGEKQRIAMARLFYHKPQFAILDECT 610
|
170 180
....*....|....*....|....*....
gi 1124469102 436 NYLDIPSVEALEKMLVEYEGTLIFTSHDK 464
Cdd:TIGR00954 611 SAVSVDVEGYMYRLCREFGITLFSVSHRK 639
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
293-463 |
2.02e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 43.06 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 293 NPIVIRGEHISFAYDDHV--IFDDADFMIKNGSKVALLGGNGAGKTTLLELIN-----------------NREKVYVVPG 353
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTgllkpqsgeikidgitiSKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 354 aKIGYARQNMSQIDLSQTV-------LVNVRrvsIQSESISRIV--LARLLLSERDMNKKASELSGGERMKLSFAMLFVS 424
Cdd:PRK13632 84 -KIGIIFQNPDNQFIGATVeddiafgLENKK---VPPKKMKDIIddLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1124469102 425 DVNLLILDEPTNYLDIPSVEALEKMLVEYEG----TLIFTSHD 463
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrkkTLISITHD 202
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
7-63 |
2.05e-04 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 42.67 E-value: 2.05e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1124469102 7 IKAENIVHSYGEQT--VLDFDrFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTV 63
Cdd:cd03295 1 IEFENVTKRYGGGKkaVNNLN-LEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEI 58
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
19-171 |
2.06e-04 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 42.95 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 19 QTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPF--FFEQ----FGSDSEyfETDYA----- 87
Cdd:PRK15056 20 HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTrqALQKnlvaYVPQSE--EVDWSfpvlv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 88 -------EAGKMG---------------------VADHIWQE--NVSGGEDTRIRLAQLFSSPHAVAFLDEPTSNLDYNG 137
Cdd:PRK15056 98 edvvmmgRYGHMGwlrrakkrdrqivtaalarvdMVEFRHRQigELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 1124469102 138 ----VEMLKKRLNEIETLVVISHDRSVLNEICDRIVEI 171
Cdd:PRK15056 178 eariISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMV 215
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
294-462 |
2.82e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 43.50 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 294 PIVIRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNRE-------KVYVVPGAKIGYARQNMSQI 366
Cdd:PRK15439 9 PPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVppdsgtlEIGGNPCARLTPAKAHQLGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 367 DL---------SQTVLVNVR-RVSIQSESISRIV-LARLLLSERDMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPT 435
Cdd:PRK15439 89 YLvpqepllfpNLSVKENILfGLPKRQASMQKMKqLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPT 168
|
170 180 190
....*....|....*....|....*....|.
gi 1124469102 436 NYLDIPSVEAL----EKMLVEYEGtLIFTSH 462
Cdd:PRK15439 169 ASLTPAETERLfsriRELLAQGVG-IVFISH 198
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
296-434 |
2.91e-04 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 42.32 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 296 VIRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELI-----NNREKVYV-------VP-------GakI 356
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIvglvkPDSGRIFLdgedithLPmhkrarlG--I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 357 GYARQNMSqI--DLsqTVLVNVRRV-SIQSESISRIvLARL--LLSE------RDmnKKASELSGGERMKLSFAMLFVSD 425
Cdd:COG1137 81 GYLPQEAS-IfrKL--TVEDNILAVlELRKLSKKER-EERLeeLLEEfgithlRK--SKAYSLSGGERRRVEIARALATN 154
|
....*....
gi 1124469102 426 VNLLILDEP 434
Cdd:COG1137 155 PKFILLDEP 163
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
6-176 |
3.28e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 42.38 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSY------GEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTV---------------- 63
Cdd:PRK13633 4 MIKCKNVSYKYesneesTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVyvdgldtsdeenlwdi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 64 SSNC-------------------IPFFFEQFGSDSEYFETDYAEA-GKMGV------ADHIwqenVSGGEDTRIRLAQLF 117
Cdd:PRK13633 84 RNKAgmvfqnpdnqivativeedVAFGPENLGIPPEEIRERVDESlKKVGMyeyrrhAPHL----LSGGQKQRVAIAGIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1124469102 118 S-SPHAVAFlDEPTSNLDYNG-VEMLK--KRLNEIE--TLVVISHdrsVLNEI--CDRIVEISFGKL 176
Cdd:PRK13633 160 AmRPECIIF-DEPTAMLDPSGrREVVNtiKELNKKYgiTIILITH---YMEEAveADRIIVMDSGKV 222
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
401-471 |
4.17e-04 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 41.97 E-value: 4.17e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1124469102 401 MNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIP---SVEALEKMLVEYEGTLIFTSHDKVFVDRIA 471
Cdd:cd03236 133 LDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKqrlNAARLIRELAEDDNYVLVVEHDLAVLDYLS 206
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
306-472 |
4.81e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 41.49 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 306 YDDHVIfddaDFMIKNGSKVALLGG-NGAGKTTLLELINnrekvYVVPGAKIGYARQNMSQIDLS---QTVLVN------ 375
Cdd:cd03279 15 REEQVI----DFTGLDNNGLFLICGpTGAGKSTILDAIT-----YALYGKTPRYGRQENLRSVFApgeDTAEVSftfqlg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 376 ------VRRVSIQSESISRIVL------ARLLlsERDmnkkASELSGGERMKLSFAM-LFVSDV---------NLLILDE 433
Cdd:cd03279 86 gkkyrvERSRGLDYDQFTRIVLlpqgefDRFL--ARP----VSTLSGGETFLASLSLaLALSEVlqnrggarlEALFIDE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1124469102 434 PTNYLDIPSVEALEKML--VEYEGTLI-FTSHDKVFVDRIAT 472
Cdd:cd03279 160 GFGTLDPEALEAVATALelIRTENRMVgVISHVEELKERIPQ 201
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
401-482 |
4.82e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 41.75 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 401 MNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIPSVEALEKMLVEY--EGTLIFTSHDKVFVDRIATDRLYIG 478
Cdd:PRK14267 143 LNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELkkEYTIVLVTHSPAQAARVSDYVAFLY 222
|
....
gi 1124469102 479 DGKI 482
Cdd:PRK14267 223 LGKL 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
296-477 |
5.00e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 42.00 E-value: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 296 VIRGEHISFAYD---DHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINNR----EKVYVVPGA------------KI 356
Cdd:PRK13642 4 ILEVENLVFKYEkesDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLfeefEGKVKIDGElltaenvwnlrrKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 357 GYARQNMSQIDLSQTVLVNV-----RRVSIQSESISRIVLARLLLSERDM-NKKASELSGGERMKLSFAMLFVSDVNLLI 430
Cdd:PRK13642 84 GMVFQNPDNQFVGATVEDDVafgmeNQGIPREEMIKRVDEALLAVNMLDFkTREPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1124469102 431 LDEPTNYLDIPSVEALEKMLVE----YEGTLIFTSHDkvFVDRIATDRLYI 477
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIHEikekYQLTVLSITHD--LDEAASSDRILV 212
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-54 |
5.28e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.80 E-value: 5.28e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1124469102 7 IKAENIVHSYGEQTVLD---FDrfyLYEGEKVGLVGMNGAGKSTLLKILAG 54
Cdd:NF033858 2 ARLEGVSHRYGKTVALDdvsLD---IPAGCMVGLIGPDGVGKSSLLSLIAG 49
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
407-482 |
5.69e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 41.61 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 407 ELSGG--ERMKLSFAMLfvSDVNLLILDEPTNYLDIPS----VEALEKMLVEYE-GTLIFTsHDKVFVDRIATDRLYIGD 479
Cdd:PRK10418 140 EMSGGmlQRMMIALALL--CEAPFIIADEPTTDLDVVAqariLDLLESIVQKRAlGMLLVT-HDMGVVARLADDVAVMSH 216
|
...
gi 1124469102 480 GKI 482
Cdd:PRK10418 217 GRI 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
313-474 |
5.75e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 42.31 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 313 DDADFMIKNGSKVALLGGNGAGKTTLLelinnrekvyvvpgaKIgyarqnMS---QIDlSQTVLVNVRRVSIQS--ESIS 387
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLM---------------KI------LSgvyQPD-SGEILLDGEPVRFRSprDAQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 388 R--------------------IVLARL-----LLSERDMNKKA-----------------SELSGGERMKLSFAMLFVSD 425
Cdd:COG1129 79 AgiaiihqelnlvpnlsvaenIFLGREprrggLIDWRAMRRRArellarlgldidpdtpvGDLSVAQQQLVEIARALSRD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1124469102 426 VNLLILDEPTNYLDIPSVEALEKMLVEY--EG-TLIFTSH--DKVFvdRIAtDR 474
Cdd:COG1129 159 ARVLILDEPTASLTEREVERLFRIIRRLkaQGvAIIYISHrlDEVF--EIA-DR 209
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
297-482 |
5.92e-04 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 42.36 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYDDHV--IFDDADFMIKNGSKVALLGGNGAGKT----TLLELINNREkvyVVPGAKIGYARQNMsqIDLSQ 370
Cdd:COG4172 9 VEDLSVAFGQGGGTveAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPA---AHPSGSILFDGQDL--LGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 371 TVLVNVR--RVSI--QsE---------SISRIVLARLLLSeRDMNKKAS-------------------------ELSGGE 412
Cdd:COG4172 84 RELRRIRgnRIAMifQ-EpmtslnplhTIGKQIAEVLRLH-RGLSGAAAraralellervgipdperrldayphQLSGGQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1124469102 413 RMKLSFAMLFVSDVNLLILDEPTNYLDIpSVEA----LEKMLVEYEGT-LIFTSHDKVFVDRIAtDRLYI-GDGKI 482
Cdd:COG4172 162 RQRVMIAMALANEPDLLIADEPTTALDV-TVQAqildLLKDLQRELGMaLLLITHDLGVVRRFA-DRVAVmRQGEI 235
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
396-439 |
6.19e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.58 E-value: 6.19e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1124469102 396 LSERDMNKKASELSGGERMKLSFAM------LFVSDVNLLILDEPTNYLD 439
Cdd:PRK01156 790 VSRGGMVEGIDSLSGGEKTAVAFALrvavaqFLNNDKSLLIMDEPTAFLD 839
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
31-176 |
6.24e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 41.71 E-value: 6.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 31 EGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNC-----------------IPFFFEQFG--SDSEYFE-------- 83
Cdd:PRK11153 30 AGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGqdltalsekelrkarrqIGMIFQHFNllSSRTVFDnvalplel 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 84 --TDYAEAGK--------MGVADH--IWQENVSGGEDTRIRLAQ-LFSSPHaVAFLDEPTSNLD---YNGVEMLKKRLNE 147
Cdd:PRK11153 110 agTPKAEIKArvtellelVGLSDKadRYPAQLSGGQKQRVAIARaLASNPK-VLLCDEATSALDpatTRSILELLKDINR 188
|
170 180 190
....*....|....*....|....*....|..
gi 1124469102 148 iE---TLVVISHDRSVLNEICDRIVEISFGKL 176
Cdd:PRK11153 189 -ElglTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-63 |
6.72e-04 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 41.60 E-value: 6.72e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1124469102 7 IKAENIVHSY----GEQTVLD---FDrfyLYEGEKVGLVGMNGAGKSTLLKILAGeLE-PTKGTV 63
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDdvsLT---IEKGEIFGIIGYSGAGKSTLIRCINL-LErPTSGSV 62
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
104-171 |
6.79e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 41.09 E-value: 6.79e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1124469102 104 SGGEDTRIRLA-QLFSSPHAVAF-LDEPTSNL----DYNGVEMLKKRLNEIETLVVISHDRSVLnEICDRIVEI 171
Cdd:cd03270 139 SGGEAQRIRLAtQIGSGLTGVLYvLDEPSIGLhprdNDRLIETLKRLRDLGNTVLVVEHDEDTI-RAADHVIDI 211
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
290-460 |
7.19e-04 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 40.86 E-value: 7.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 290 PPRNPIVIRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTL-------LELINNREKVYVVPGAKIGYA--R 360
Cdd:cd03369 2 PEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLilalfrfLEAEEGKIEIDGIDISTIPLEdlR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 361 QNMSQID-----LSQTVLVNVRRVSIQSEsisRIVLARLLLSERDMNkkaseLSGGERMKLSFAMLFVSDVNLLILDEPT 435
Cdd:cd03369 82 SSLTIIPqdptlFSGTIRSNLDPFDEYSD---EEIYGALRVSEGGLN-----LSQGQRQLLCLARALLKRPRVLVLDEAT 153
|
170 180
....*....|....*....|....*.
gi 1124469102 436 NYLDIPSVEALEKML-VEYEGTLIFT 460
Cdd:cd03369 154 ASIDYATDALIQKTIrEEFTNSTILT 179
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
401-463 |
7.72e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 41.63 E-value: 7.72e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1124469102 401 MNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIpSVEA-----LEKMLVEYEGTLIFTSHD 463
Cdd:PRK09473 155 MKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDV-TVQAqimtlLNELKREFNTAIIMITHD 221
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
10-190 |
9.00e-04 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 40.68 E-value: 9.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 10 ENIVHSYG--EQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCI------------------- 68
Cdd:cd03251 4 KNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdytlaslrrqiglvsq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 69 -PFFFE-------QFGSDSEYFEtDYAEAGKMGVADHIWQE--------------NVSGGEDTRIRLAQLFSSPHAVAFL 126
Cdd:cd03251 84 dVFLFNdtvaeniAYGRPGATRE-EVEEAARAANAHEFIMElpegydtvigergvKLSGGQRQRIAIARALLKDPPILIL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1124469102 127 DEPTSNLDyNGVEMLKK----RLNEIETLVVISHDRSVLNEIcDRIVEISFGKLQNySGNYDEYVVQK 190
Cdd:cd03251 163 DEATSALD-TESERLVQaaleRLMKNRTTFVIAHRLSTIENA-DRIVVLEDGKIVE-RGTHEELLAQG 227
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
27-176 |
9.11e-04 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 41.09 E-value: 9.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 27 FYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVS------------------SNCIPFFFEQF------------- 75
Cdd:cd03294 45 LDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLidgqdiaamsrkelrelrRKKISMVFQSFallphrtvlenva 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 76 ------GSDSEYFETDYAEA----GKMGVADHIWQEnVSGGEDTRIRLAQLFSSPHAVAFLDEPTSNLD-----YNGVEM 140
Cdd:cd03294 125 fglevqGVPRAEREERAAEAlelvGLEGWEHKYPDE-LSGGMQQRVGLARALAVDPDILLMDEAFSALDplirrEMQDEL 203
|
170 180 190
....*....|....*....|....*....|....*....
gi 1124469102 141 LKKRLNEIETLVVISHDrsvLNE---ICDRIVEISFGKL 176
Cdd:cd03294 204 LRLQAELQKTIVFITHD---LDEalrLGDRIAIMKDGRL 239
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-134 |
9.39e-04 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 40.84 E-value: 9.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIP---------------- 69
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPvegpgaergvvfqneg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 70 ------------FFFEQFGSDSEYFET---------DYAEAGKMgvadHIWQenVSGGEDTRIRLAQLFSSPHAVAFLDE 128
Cdd:PRK11248 81 llpwrnvqdnvaFGLQLAGVEKMQRLEiahqmlkkvGLEGAEKR----YIWQ--LSGGQRQRVGIARALAANPQLLLLDE 154
|
....*.
gi 1124469102 129 PTSNLD 134
Cdd:PRK11248 155 PFGALD 160
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
297-361 |
9.92e-04 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 40.53 E-value: 9.92e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1124469102 297 IRGEHISFAYDD-----HVIFDDADFMIKNGSKVALLGGNGAGKTTLL-----ELINNREKVYVVPGakIGYARQ 361
Cdd:cd03250 1 ISVEDASFTWDSgeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLsallgELEKLSGSVSVPGS--IAYVSQ 73
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
102-176 |
1.23e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 40.60 E-value: 1.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1124469102 102 NVSGGEDTRIRLAQLFSSPHAVAFLDEPTSNLDYNGVEMLKKRLNEIE---TLVVISHDRSVLNEICDRIVEISFGKL 176
Cdd:PRK14267 149 NLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKkeyTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
6-176 |
1.23e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 40.85 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSYGEQT---VLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVS------------------ 64
Cdd:PRK13642 4 ILEVENLVFKYEKESdvnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKidgelltaenvwnlrrki 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 65 ----------------SNCIPFFFEQFGSDSEYFETDYAEA-GKMGVADHIWQE--NVSGGEDTRIRLAQLFSSPHAVAF 125
Cdd:PRK13642 84 gmvfqnpdnqfvgatvEDDVAFGMENQGIPREEMIKRVDEAlLAVNMLDFKTREpaRLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1124469102 126 LDEPTSNLDYNGVEMLKKRLNEIE-----TLVVISHDrsvLNEIC--DRIVEISFGKL 176
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIHEIKekyqlTVLSITHD---LDEAAssDRILVMKAGEI 218
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
293-470 |
1.32e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 40.46 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 293 NPIVIRGEHISFAYDD------HVIFDDADFMIKNGSKVALLGGNGAGKTTLLELIN-----NREKVYVVP--------- 352
Cdd:PRK13633 1 MNEMIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNallipSEGKVYVDGldtsdeenl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 353 ---GAKIGYARQNM-SQI---DLSQTVLVNVRRVSIQSESISRIV---LARLLLSErdMNKKASE-LSGGERMKLSFAML 421
Cdd:PRK13633 81 wdiRNKAGMVFQNPdNQIvatIVEEDVAFGPENLGIPPEEIRERVdesLKKVGMYE--YRRHAPHlLSGGQKQRVAIAGI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1124469102 422 FVSDVNLLILDEPTNYLDiPS-----VEALEKMLVEYEGTLIFTSH---DKVFVDRI 470
Cdd:PRK13633 159 LAMRPECIIFDEPTAMLD-PSgrrevVNTIKELNKKYGITIILITHymeEAVEADRI 214
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
10-63 |
1.37e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 41.11 E-value: 1.37e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1124469102 10 ENIVHSYGEQTvldFD----RFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTV 63
Cdd:PRK10522 326 RNVTFAYQDNG---FSvgpiNLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI 380
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
6-55 |
1.75e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.77 E-value: 1.75e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGE 55
Cdd:PRK10938 260 RIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGD 309
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
104-171 |
1.87e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 39.91 E-value: 1.87e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1124469102 104 SGGEDTRIRLAQLFSSP---HAVAFLDEPTSNLDYNGVEMLKKRLNEI----ETLVVISHDRSVLnEICDRIVEI 171
Cdd:cd03271 171 SGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLvdkgNTVVVIEHNLDVI-KCADWIIDL 244
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
263-342 |
1.91e-03 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 40.55 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 263 LKRLEHMEikEKPKEELTVRPDFRLTNPPRNPIVIRGEHISFAYDDHvifDDA--------DFMIKNGSKVALLGGNGAG 334
Cdd:COG4615 296 LRKIEELE--LALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGE---DGDegftlgpiDLTIRRGELVFIVGGNGSG 370
|
....*...
gi 1124469102 335 KTTLLELI 342
Cdd:COG4615 371 KSTLAKLL 378
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
27-66 |
2.06e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 40.37 E-value: 2.06e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1124469102 27 FYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSN 66
Cdd:PRK10762 273 FTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLD 312
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
27-134 |
2.41e-03 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 39.84 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 27 FYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSNCIPFFFEQFG---------------SDSEYF--------- 82
Cdd:cd03291 58 LKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSwimpgtikeniifgvSYDEYRyksvvkacq 137
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1124469102 83 ---------ETDYAEAGKMGVadhiwqeNVSGGEDTRIRLAQLFSSPHAVAFLDEPTSNLD 134
Cdd:cd03291 138 leeditkfpEKDNTVLGEGGI-------TLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-176 |
2.55e-03 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 39.49 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 6 LIKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTVSSN-----CIPF---------F 71
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDdedisLLPLhararrgigY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 72 FEQ----FGSDSEY--------FETDYAEAGKMGVADHIWQE------------NVSGGEDTRIRLAQLFSSPHAVAFLD 127
Cdd:PRK10895 83 LPQeasiFRRLSVYdnlmavlqIRDDLSAEQREDRANELMEEfhiehlrdsmgqSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1124469102 128 EPTSNLDYNGVEMLKKRLNEIET----LVVISHDRSVLNEICDRIVEISFGKL 176
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHLRDsglgVLITDHNVRETLAVCERAYIVSQGHL 215
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
7-176 |
2.58e-03 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 39.61 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 7 IKAENIVHSYGEQTVLdFD-RFYLYEGEKVGLVGMNGAGKSTLLKIL-------AGELE-------------PTKG---- 61
Cdd:PRK11124 3 IQLNGINCFYGAHQAL-FDiTLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNiagnhfdfsktpsDKAIrelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 62 ----------------TVSSNCIPFFFEQFG-SDSEYFE-----------TDYAEAgkmgvadhiWQENVSGGEDTRIRL 113
Cdd:PRK11124 82 rnvgmvfqqynlwphlTVQQNLIEAPCRVLGlSKDQALAraekllerlrlKPYADR---------FPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1124469102 114 AQ-LFSSPHAVAFlDEPTSNLD---YNGVEMLKKRLNEIE-TLVVISHDRSVLNEICDRIVEISFGKL 176
Cdd:PRK11124 153 ARaLMMEPQVLLF-DEPTAALDpeiTAQIVSIIRELAETGiTQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
288-343 |
2.64e-03 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 39.63 E-value: 2.64e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1124469102 288 TNPPRNPIVIRGEHISFAYDDHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELIN 343
Cdd:COG1117 3 APASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLN 58
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
91-245 |
2.88e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 39.83 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 91 KMGVADHIWQEN---VSGGEDTRIRLAQLFSSPHAVAFLDEPTSNLDYNG----VEMLKKRLNEIETLVVISHDRSVLNE 163
Cdd:PRK13631 162 KMGLDDSYLERSpfgLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGehemMQLILDAKANNKTVFVITHTMEHVLE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 164 ICDRIVEISFGKLQNYSGNYDEYvvqkeeqrkTQQAEYENYQAEKKRLQSV---YVEKKAK-AKTVDKKPKNMSASEAKV 239
Cdd:PRK13631 242 VADEVIVMDKGKILKTGTPYEIF---------TDQHIINSTSIQVPRVIQVindLIKKDPKyKKLYQKQPRTIEQLADAI 312
|
....*.
gi 1124469102 240 RAFIGN 245
Cdd:PRK13631 313 NEFIKG 318
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-192 |
3.16e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 39.26 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 19 QTVLDFDRFYLYEGEKV---------------GLVGMNGAGKSTLLKILAG--ELEPTKGTVSSNCIPFFFEQFGSDSEY 81
Cdd:PRK14246 8 EDVFNISRLYLYINDKAilkditikipnnsifGIMGPSGSGKSTLLKVLNRliEIYDSKIKVDGKVLYFGKDIFQIDAIK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 82 FETDYAEAGK-------MGVADHI----------------------------WQE----------NVSGGEDTRIRLAQL 116
Cdd:PRK14246 88 LRKEVGMVFQqpnpfphLSIYDNIayplkshgikekreikkiveeclrkvglWKEvydrlnspasQLSGGQQQRLTIARA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1124469102 117 FSSPHAVAFLDEPTSNLDYNGVEMLKKRLNEIE---TLVVISHDRSVLNEICDRIVEISFGKLQNYSGNYDEYVVQKEE 192
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDIVNSQAIEKLITELKneiAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNE 246
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
31-54 |
3.81e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.77 E-value: 3.81e-03
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
27-63 |
4.11e-03 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 38.82 E-value: 4.11e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1124469102 27 FYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTV 63
Cdd:PRK11300 26 LEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTI 62
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
27-63 |
4.38e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 39.62 E-value: 4.38e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1124469102 27 FYLYEGEKVGLVGMNGAGKSTLLKILAGELEPTKGTV 63
Cdd:COG1129 273 FSVRAGEILGIAGLVGAGRTELARALFGADPADSGEI 309
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
297-455 |
4.39e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.01 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 297 IRGEHISFAYD---DHVIFDDADFMIKNGSKVALLGGNGAGKTTLLELINN-------------------------REKV 348
Cdd:PTZ00265 383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERlydptegdiiindshnlkdinlkwwRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 349 YVVPGAKIGYARQNMSQIDLSQTVLVNVRRVSIQSE-------------------------------------------- 384
Cdd:PTZ00265 463 GVVSQDPLLFSNSIKNNIKYSLYSLKDLEALSNYYNedgndsqenknkrnscrakcagdlndmsnttdsneliemrknyq 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 385 --------SISRIVLARLLLS------ERDMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDIPSVEALEKML 450
Cdd:PTZ00265 543 tikdsevvDVSKKVLIHDFVSalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
|
....*
gi 1124469102 451 VEYEG 455
Cdd:PTZ00265 623 NNLKG 627
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
282-338 |
4.66e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 39.57 E-value: 4.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 282 RPDFRLTNPPRNPIVIRGEHISFAYDD---HVifDDADFMIKNGSKVALLGGNGAGKTTL 338
Cdd:PRK10522 308 KAEFPRPQAFPDWQTLELRNVTFAYQDngfSV--GPINLTIKRGELLFLIGGNGSGKSTL 365
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-54 |
6.95e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 38.08 E-value: 6.95e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1124469102 1 MERHLLIKAENIVHSYGEQTVLDFDRFYLYEGEKVGLVGMNGAGKSTLLKILAG 54
Cdd:CHL00131 2 NKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
313-439 |
7.25e-03 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 38.63 E-value: 7.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124469102 313 DDADFMIKNGSKVALLGGNGAGKTTLLELINNREK-----VYV-------VPGAKIGYARQNMSQI----DL--SQTVLV 374
Cdd:PRK11153 22 NNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERptsgrVLVdgqdltaLSEKELRKARRQIGMIfqhfNLlsSRTVFD 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1124469102 375 NV----RRVSIQSESISRIV---LARLLLSERdMNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLD 439
Cdd:PRK11153 102 NValplELAGTPKAEIKARVtelLELVGLSDK-ADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
401-463 |
7.32e-03 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 38.35 E-value: 7.32e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1124469102 401 MNKKASELSGGERMKLSFAMLFVSDVNLLILDEPTNYLDiPSVEA-----LEKMLVEYEGTLIFTSHD 463
Cdd:COG4170 152 MNSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAME-STTQAqifrlLARLNQLQGTSILLISHD 218
|
|
| |
