|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-526 |
0e+00 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 676.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 3 RFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMRKGLTIGYLAQDQGLDSQNTIWEEMSSVF 82
Cdd:COG0488 7 SFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLDTVLDGD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 83 AELHAIEKRMHALENQLSDPaimnddqayQQTLKTYDQVQTEFQQKNGYGYQAEIRGVLHGFQFDADVYDKSVTELSGGQ 162
Cdd:COG0488 87 AELRALEAELEELEAKLAEP---------DEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSGGW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 163 KTqlalaklllekR-----------DLLILDEPTNHLDVETLTWLESYLQSYAGALLIVSHDRYFLDRVVNEVYDLSHHE 231
Cdd:COG0488 158 RR-----------RvalarallsepDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 232 MVHYTGNYDQFVQEKAARIQAQWKHYEKQQAEISKLEDFVNRNIVRASTTKRAQARRKQLAKMDRIDRPDSDeKTAHFGF 311
Cdd:COG0488 227 LTLYPGNYSAYLEQRAERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAKQAQSRIKALEKLEREEPPRRD-KTVEIRF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 312 HAAKQSGNIVLTVKDAAVGYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGYYDQ 391
Cdd:COG0488 306 PPPERLGKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 392 EQRNLNDKKTVLSELWDEHPTTPEKDIRTILESFLFTGADVDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDI 471
Cdd:COG0488 386 HQEELDPDKTVLDELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDI 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2269171783 472 DSREVLEVALNDFDGTLLFVSHDRYFINQVATSVVEVSPEGTELFLGDYDYYIDK 526
Cdd:COG0488 466 ETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLEK 520
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-650 |
2.78e-101 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 322.29 E-value: 2.78e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 4 FGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMRKGLTIGYLAQDQGLDSQNTIWEEMSSVFA 83
Cdd:PRK11147 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVEGTVYDFVAEGIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 84 ELHAIEKRMHALENQL-SDPAimnddqayQQTLKTYDQVQTEFQQKNGYGYQAEIRGVLHGFQFDADvydKSVTELSGGQ 162
Cdd:PRK11147 93 EQAEYLKRYHDISHLVeTDPS--------EKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDPD---AALSSLSGGW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 163 KTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYAGALLIVSHDRYFLDRVVNEVYDLSHHEMVHYTGNYDQF 242
Cdd:PRK11147 162 LRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 243 VQEK--AARIQA-QWKHYEKQQAEisklEDFVNRNIVRASTTkRAQARRKQLAKMdRIDRPDSDEK--TAHFGFHAAKQS 317
Cdd:PRK11147 242 LLEKeeALRVEElQNAEFDRKLAQ----EEVWIRQGIKARRT-RNEGRVRALKAL-RRERSERREVmgTAKMQVEEASRS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 318 GNIVLTVKDAAVGYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGYYDQEQRNLN 397
Cdd:PRK11147 316 GKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 398 DKKTVLSELWDEHPTTP----EKDIRTILESFLFTGADVDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDS 473
Cdd:PRK11147 396 PEKTVMDNLAEGKQEVMvngrPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 474 REVLEVALNDFDGTLLFVSHDRYFINQVATSVVEVSPEGT-ELFLGDYDyyiDKKqeqaeMAAAAASQAAESAASANAAE 552
Cdd:PRK11147 476 LELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGNGKiGRYVGGYH---DAR-----QQQAQYLALKQPAVKKKEEA 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 553 PSSAATAAPRSKGQQDYqaskQQQREkrkLErtvaALEEQMTTLDEQATKIQTEMAQPEVSADVGRLTdlQKELDEISAQ 632
Cdd:PRK11147 548 AAPKAETVKRSSKKLSY----KLQRE---LE----QLPQLLEDLEAEIEALQAQVADADFFSQPHEQT--QKVLADLADA 614
|
650
....*....|....*...
gi 2269171783 633 QEQVETEWtEQAEALEAF 650
Cdd:PRK11147 615 EQELEVAF-ERWEELEAL 631
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-527 |
1.90e-98 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 311.44 E-value: 1.90e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 4 FGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMRKGLTIGYLAQDQ-GLDSQNTI------WE 76
Cdd:PRK15064 11 FGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQfAFEEFTVLdtvimgHT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 77 EMSSVFAELHAIekrmhalenqLSDPAIMNDDqayqqTLKTYDqVQTEFQQKNGYgyQAEIRG--VLHGFQFDADVYDKS 154
Cdd:PRK15064 91 ELWEVKQERDRI----------YALPEMSEED-----GMKVAD-LEVKFAEMDGY--TAEARAgeLLLGVGIPEEQHYGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 155 VTELSGGQKTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYAGALLIVSHDRYFLDRVVNEVYDLSHHEMVH 234
Cdd:PRK15064 153 MSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 235 YTGNYDQFVQEKAARIQAQWKHYEKQQAEISKLEDFVNRNIVRASTTKRAQARRKQLAKMDRIDRPDSDEKTAHFGFHAA 314
Cdd:PRK15064 233 YPGNYDEYMTAATQARERLLADNAKKKAQIAELQSFVSRFSANASKAKQATSRAKQIDKIKLEEVKPSSRQNPFIRFEQD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 315 KQSGNIVLTVKDAAVGYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGYYDQEQR 394
Cdd:PRK15064 313 KKLHRNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 395 NLNDKKTVLSElWDEHPTTPEKD---IRTILESFLFTGADVDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDI 471
Cdd:PRK15064 393 YDFENDLTLFD-WMSQWRQEGDDeqaVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDM 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2269171783 472 DSREVLEVALNDFDGTLLFVSHDRYFINQVATSVVEVSPEGTELFLGDYDYYIDKK 527
Cdd:PRK15064 472 ESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRSQ 527
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
21-527 |
5.21e-96 |
|
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: 305.71 E-value: 5.21e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 21 ARVALVGRNGAGKSTLLKMIAGETVPDEGQISMRKGLTIGYLAQDQGLDSQNTIWEEMSSVFAELHAIEKRMHALENQLS 100
Cdd:TIGR03719 32 AKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLDPTKTVRENVEEGVAEIKDALDRFNEISAKYA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 101 DPaimndDQAYQQTLKTYDQVQTEFQQKNGYGYQAEIRGVLHGFQFDADvyDKSVTELSGGQKTQLALAKLLLEKRDLLI 180
Cdd:TIGR03719 112 EP-----DADFDKLAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPW--DADVTKLSGGERRRVALCRLLLSKPDMLL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 181 LDEPTNHLDVETLTWLESYLQSYAGALLIVSHDRYFLDRVVNEVYDLSHHEMVHYTGNYDQFVQEKAARIQAQWKHYEKQ 260
Cdd:TIGR03719 185 LDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKQKRLEQEEKEESAR 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 261 QAEISK-LEdfvnrnIVRASTTKRaQARRK-QLAKMDRIDRPDSDEK--TAHFGFHAAKQSGNIVLTVKDAAVGYDGHIL 336
Cdd:TIGR03719 265 QKTLKReLE------WVRQSPKGR-QAKSKaRLARYEELLSQEFQKRneTAEIYIPPGPRLGDKVIEAENLTKAFGDKLL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 337 SEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGYYDQEQRNLNDKKTVLSELWD--EHPTTP 414
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDPNKTVWEEISGglDIIKLG 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 415 EKDI--RTILESFLFTGADVDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLEVALNDFDGTLLFVS 492
Cdd:TIGR03719 418 KREIpsRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVIS 497
|
490 500 510
....*....|....*....|....*....|....*....
gi 2269171783 493 HDRYFINQVATSVveVSPEGT---ELFLGDY-DYYIDKK 527
Cdd:TIGR03719 498 HDRWFLDRIATHI--LAFEGDshvEWFEGNFsEYEEDKK 534
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-650 |
1.32e-94 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 304.79 E-value: 1.32e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 3 RFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMRKGLTIGYLAQDQGLDSQNTIWEEMSSvf 82
Cdd:PRK10636 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPALEYVIDG-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 83 aelhaiEKRMHALENQLSDPAIMNDDQAYQQTLKTYDQVQtefqqknGYGYQAEIRGVLHGFQFDADVYDKSVTELSGGQ 162
Cdd:PRK10636 88 ------DREYRQLEAQLHDANERNDGHAIATIHGKLDAID-------AWTIRSRAASLLHGLGFSNEQLERPVSDFSGGW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 163 KTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYAGALLIVSHDRYFLDRVVNEVYDLSHHEMVHYTGNYDQF 242
Cdd:PRK10636 155 RMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 243 VQEKAARIQAQWKHYEKQQAEISKLEDFVNRNIVRASTTKRAQARRKQLAKMDRIdRPDSDEKTAHFGFHAAKQSGNIVL 322
Cdd:PRK10636 235 EVQRATRLAQQQAMYESQQERVAHLQSYIDRFRAKATKAKQAQSRIKMLERMELI-APAHVDNPFHFSFRAPESLPNPLL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 323 TVKDAAVGYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGYYDQEQRN-LNDKKT 401
Cdd:PRK10636 314 KMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEfLRADES 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 402 VLSELWDEHPTTPEKDIRTILESFLFTGADVDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLEVAL 481
Cdd:PRK10636 394 PLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 482 NDFDGTLLFVSHDRYFINQVATSVVEVSPEGTELFLGDYDYYidkkqeqaemaaaaasqaaeSAASANAAEPSSAATAAP 561
Cdd:PRK10636 474 IDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDY--------------------QQWLSDVQKQENQTDEAP 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 562 RSKGQQDYQASKQQQREKRKLERTVAALEEQMTTLDEQATKIQTEMAQPEVSADVGRLTDLQK--ELDEISAQQ------ 633
Cdd:PRK10636 534 KENNANSAQARKDQKRREAELRTQTQPLRKEIARLEKEMEKLNAQLAQAEEKLGDSELYDQSRkaELTACLQQQasaksg 613
|
650
....*....|....*...
gi 2269171783 634 -EQVETEWTEQAEALEAF 650
Cdd:PRK10636 614 lEECEMAWLEAQEQLEQM 631
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
21-527 |
4.58e-84 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 274.69 E-value: 4.58e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 21 ARVALVGRNGAGKSTLLKMIAGETVPDEGQISMRKGLTIGYLAQDQGLDSQNTIWEEMSSVFAELHAIEKRMHALENQLS 100
Cdd:PRK11819 34 AKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQLDPEKTVRENVEEGVAEVKAALDRFNEIYAAYA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 101 DPaimndDQAYQQTLKTYDQVQTEFQQKNGY--GYQAEIRgvlhgfqfdADV-----YDKSVTELSGGQKtqlalaklll 173
Cdd:PRK11819 114 EP-----DADFDALAAEQGELQEIIDAADAWdlDSQLEIA---------MDAlrcppWDAKVTKLSGGER---------- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 174 ekR------------DLLILDEPTNHLDVETLTWLESYLQSYAGALLIVSHDRYFLDRVVNEVYDLSHHEMVHYTGNYDQ 241
Cdd:PRK11819 170 --RrvalcrlllekpDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 242 FVQEKAARIQAQWKHYEKQQAEISK-LEdfvnrnIVRASTTKRaQARRK-------QLAKMDRIDRPDsdekTAHFGFHA 313
Cdd:PRK11819 248 WLEQKAKRLAQEEKQEAARQKALKReLE------WVRQSPKAR-QAKSKarlaryeELLSEEYQKRNE----TNEIFIPP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 314 AKQSGNIVLTVKDAAVGYDGHILSepDNLNVK--KHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGYYDQ 391
Cdd:PRK11819 317 GPRLGDKVIEAENLSKSFGDRLLI--DDLSFSlpPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 392 EQRNLNDKKTVLSELWDEHpttpekDI----------RTILESFLFTGADVDKPVHALSGGERARLLLTKLAMQNDNFLI 461
Cdd:PRK11819 395 SRDALDPNKTVWEEISGGL------DIikvgnreipsRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLL 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 462 LDEPTNHLDIDSREVLEVALNDFDGTLLFVSHDRYFINQVATSVveVSPEGT---ELFLGDY-DYYIDKK 527
Cdd:PRK11819 469 LDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHI--LAFEGDsqvEWFEGNFqEYEEDKK 536
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
22-499 |
1.86e-60 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 215.11 E-value: 1.86e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 22 RVALVGRNGAGKSTLLK---MIAGETVPDEGQISMRKGLTIG--YLAQDQGLDS---QNTIWEEMSSVFAELHAIEKRMH 93
Cdd:PLN03073 205 HYGLVGRNGTGKTTFLRymaMHAIDGIPKNCQILHVEQEVVGddTTALQCVLNTdieRTQLLEEEAQLVAQQRELEFETE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 94 ALENQLSDPAIMNDDQAYQQTLKTYDQVqtefQQKNGYGYQAEIRGVLHGFQFDADVYDKSVTELSGGQKTQLALAKLLL 173
Cdd:PLN03073 285 TGKGKGANKDGVDKDAVSQRLEEIYKRL----ELIDAYTAEARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALF 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 174 EKRDLLILDEPTNHLDVETLTWLESYLQSYAGALLIVSHDRYFLDRVVNEVYDLSHHEMVHYTGNYDQFVQEKAARIQAQ 253
Cdd:PLN03073 361 IEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVTYKGDYDTFERTREEQLKNQ 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 254 WKHYEKQQAEISKLEDFVNR---NIVRASTTkraQARRKQLAKMDRIDR--PDSDEKtahFGFHAAK-QSGNIVLTVKDA 327
Cdd:PLN03073 441 QKAFESNERSRSHMQAFIDKfryNAKRASLV---QSRIKALDRLGHVDAvvNDPDYK---FEFPTPDdRPGPPIISFSDA 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 328 AVGY-DGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGYYDQEQRN-LNDKKTVLSE 405
Cdd:PLN03073 515 SFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDgLDLSSNPLLY 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 406 LWDEHPTTPEKDIRTILESFLFTGADVDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLEVALNDFD 485
Cdd:PLN03073 595 MMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQ 674
|
490
....*....|....
gi 2269171783 486 GTLLFVSHDRYFIN 499
Cdd:PLN03073 675 GGVLMVSHDEHLIS 688
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
322-512 |
8.01e-54 |
|
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: 180.72 E-value: 8.01e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 322 LTVKDAAVGYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGYYDQeqrnlndkkt 401
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 402 vlselwdehpttpekdirtilesflftgadvdkpvhaLSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLEVAL 481
Cdd:cd03221 71 -------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL 113
|
170 180 190
....*....|....*....|....*....|.
gi 2269171783 482 NDFDGTLLFVSHDRYFINQVATSVVEVSPEG 512
Cdd:cd03221 114 KEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
324-602 |
2.71e-48 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 177.18 E-value: 2.71e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 324 VKDAAVGYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGYYDQEQRnLNDKKTVL 403
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPP-LDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 404 -------SELWD---------EHPTTPEKD----------------------IRTILESFLFTGADVDKPVHALSGGERA 445
Cdd:COG0488 80 dtvldgdAELRAleaeleeleAKLAEPDEDlerlaelqeefealggweaearAEEILSGLGFPEEDLDRPVSELSGGWRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 446 RLLLTKLAMQNDNFLILDEPTNHLDIDSREVLEVALNDFDGTLLFVSHDRYFINQVATSVVEVSPEGTELFLGDYDYYID 525
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLE 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2269171783 526 KKQeqaemaaaaasqaaesaasanaaepssaataaprskgqqdyQASKQQQREKRKLERTVAALEEQMTTLDEQATK 602
Cdd:COG0488 240 QRA-----------------------------------------ERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARK 275
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-231 |
1.35e-42 |
|
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: 150.29 E-value: 1.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 3 RFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMRKGLTIGYLAQdqgldsqntiweemssvf 82
Cdd:cd03221 9 TYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ------------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 83 aelhaiekrmhalenqlsdpaimnddqayqqtlktydqvqtefqqkngygyqaeirgvlhgfqfdadvydksvteLSGGQ 162
Cdd:cd03221 71 ---------------------------------------------------------------------------LSGGE 75
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2269171783 163 KTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYAGALLIVSHDRYFLDRVVNEVYDLSHHE 231
Cdd:cd03221 76 KMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-248 |
3.32e-32 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 131.17 E-value: 3.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 4 FGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMRKGLTIGYLAQDQGLDSQN--TIWEEMSsv 81
Cdd:PRK15064 329 FDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYDFENdlTLFDWMS-- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 82 faelhaiekrmhalenQLSDPAimNDDQAyqqtlktydqvqtefqqkngygyqaeIRGVLHGFQFDADVYDKSVTELSGG 161
Cdd:PRK15064 407 ----------------QWRQEG--DDEQA--------------------------VRGTLGRLLFSQDDIKKSVKVLSGG 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 162 QKTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYAGALLIVSHDRYFLDRVVNEVYDLSHHEMVHYTGNYDQ 241
Cdd:PRK15064 443 EKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEE 522
|
....*..
gi 2269171783 242 FVQEKAA 248
Cdd:PRK15064 523 YLRSQGI 529
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-506 |
1.79e-31 |
|
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: 128.87 E-value: 1.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGEtVPDEGQISMR---------------KGLTIGYLAQDqGLDSQN--T 73
Cdd:COG1123 23 DGVSLTIAPGETVALVGESGSGKSTLALALMGL-LPHGGRISGEvlldgrdllelsealRGRRIGMVFQD-PMTQLNpvT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 74 IWEEMssvfAElhaiekrmhALENQLSDPAimnddQAYQQTLKTYDQVQTEfqqkngygyqaeirgvlhgfqfdaDVYDK 153
Cdd:COG1123 101 VGDQI----AE---------ALENLGLSRA-----EARARVLELLEAVGLE------------------------RRLDR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 154 SVTELSGGQKTQLALAKLLLEKRDLLILDEPTNHLDV----ETLTWLESYLQSYAGALLIVSHDryfldrvVNEVYDLSH 229
Cdd:COG1123 139 YPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVttqaEILDLLRELQRERGTTVLLITHD-------LGVVAEIAD 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 230 HEMVHYTGNydqfvqekaariqaqwkhyekqqaeiskledfvnrnIVRASTTKRAQARRKQLAKMDRIDRPDSDEktahf 309
Cdd:COG1123 212 RVVVMDDGR------------------------------------IVEDGPPEEILAAPQALAAVPRLGAARGRA----- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 310 gfHAAKQSGNIVLTVKDAAVGYDGHILSEPD-----NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGV 384
Cdd:COG1123 251 --APAAAAAEPLLEVRNLSKRYPVRGKGGVRavddvSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKD 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 385 VTGYYDQEQRN---------------LNDKKTVLSEL---WDEHPTTPEKDIR----TILESFLFTGADVDKPVHALSGG 442
Cdd:COG1123 329 LTKLSRRSLRElrrrvqmvfqdpyssLNPRMTVGDIIaepLRLHGLLSRAERRervaELLERVGLPPDLADRYPHELSGG 408
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 443 ERARLLL-TKLAMQNDnFLILDEPTNHLDIDSR-EVLEVaLND----FDGTLLFVSHDRYFINQVATSVV 506
Cdd:COG1123 409 QRQRVAIaRALALEPK-LLILDEPTSALDVSVQaQILNL-LRDlqreLGLTYLFISHDLAVVRYIADRVA 476
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-249 |
1.48e-30 |
|
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: 126.59 E-value: 1.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 4 FGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMRKGLTIGYLAQDQ-GLDSQNTIWEEMSSvf 82
Cdd:TIGR03719 332 FGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRdALDPNKTVWEEISG-- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 83 aelhaiekrmhalenqlsdpaimnddqayqqtlkTYDQVQTEfqqkngyGYQAEIRGVLHGFQFDADVYDKSVTELSGGQ 162
Cdd:TIGR03719 410 ----------------------------------GLDIIKLG-------KREIPSRAYVGRFNFKGSDQQKKVGQLSGGE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 163 KTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYAGALLIVSHDRYFLDRVVNEVYDL---SHheMVHYTGNY 239
Cdd:TIGR03719 449 RNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFegdSH--VEWFEGNF 526
|
250
....*....|
gi 2269171783 240 DQFVQEKAAR 249
Cdd:TIGR03719 527 SEYEEDKKRR 536
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
225-309 |
2.12e-30 |
|
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: 114.21 E-value: 2.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 225 YDLSHHEMVHYTGNYDQFVQEKAARIQAQWKHYEKQQAEISKLEDFVNRNIVRASTTKRAQARRKQLAKMDRIDRPDSDE 304
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKAKQAQSRIKALEKMERIEKPERDK 80
|
....*
gi 2269171783 305 KTAHF 309
Cdd:pfam12848 81 PKLRF 85
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
321-503 |
3.60e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 113.26 E-value: 3.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 321 VLTVKDAAVGYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQA-VFGTGVVT-----GYYDQeQR 394
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVrLFGKPPRRarrriGYVPQ-RA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 395 NLND------KKTVLSELWDEH-----PTTPEKD-IRTILESflfTGAD--VDKPVHALSGGERARLLLTKLAMQNDNFL 460
Cdd:COG1121 85 EVDWdfpitvRDVVLMGRYGRRglfrrPSRADREaVDEALER---VGLEdlADRPIGELSGGQQQRVLLARALAQDPDLL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2269171783 461 ILDEPTNHLDIDSREVL-EV--ALNDFDGTLLFVSHDryfINQVAT 503
Cdd:COG1121 162 LLDEPFAGVDAATEEALyELlrELRREGKTILVVTHD---LGAVRE 204
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
324-508 |
1.00e-27 |
|
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: 111.09 E-value: 1.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 324 VKDAAVGYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQA-VFGTGVVT-----GYYDQeQRNLN 397
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIrVFGKPLEKerkriGYVPQ-RRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 398 D------KKTVLSELWDE---HPTTPEKDIRTILESFLFTGAD--VDKPVHALSGGERARLLLTKLAMQNDNFLILDEPT 466
Cdd:cd03235 81 RdfpisvRDVVLMGLYGHkglFRRLSKADKAKVDEALERVGLSelADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2269171783 467 NHLDIDSRE-VLEV--ALNDFDGTLLFVSHDryfINQVATSVVEV 508
Cdd:cd03235 161 AGVDPKTQEdIYELlrELRREGMTILVVTHD---LGLVLEYFDRV 202
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-220 |
7.15e-26 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 112.13 E-value: 7.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 4 FGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMRKGLTIGYLaqDQ---GLDSQNTIWEEMSs 80
Cdd:PRK11819 334 FGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYV--DQsrdALDPNKTVWEEIS- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 81 vfaelhaiekrmhalenqlsdpaimnDDQayqqtlktyDQVQTEfqqkngyGYQAEIRGVLHGFQFDADVYDKSVTELSG 160
Cdd:PRK11819 411 --------------------------GGL---------DIIKVG-------NREIPSRAYVGRFNFKGGDQQKKVGVLSG 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 161 GQKTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYAGALLIVSHDRYFLDRV 220
Cdd:PRK11819 449 GERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRI 508
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
321-502 |
7.35e-26 |
|
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: 107.05 E-value: 7.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 321 VLTVKDAAVGYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGtgvvtgyyDQEQRNLNDKK 400
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLD--------GRDLASLSRRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 401 ------------------TVLsEL----------WDEHPTtpEKDIRTILESFLFTGAD--VDKPVHALSGGERARLLLT 450
Cdd:COG1120 73 larriayvpqeppapfglTVR-ELvalgryphlgLFGRPS--AEDREAVEEALERTGLEhlADRPVDELSGGERQRVLIA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2269171783 451 KLAMQNDNFLILDEPTNHLDIDSR-EVLEV--ALNDFDG-TLLFVSHDryfINQVA 502
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDLAHQlEVLELlrRLARERGrTVVMVLHD---LNLAA 202
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
323-502 |
1.23e-25 |
|
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: 104.05 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 323 TVKDAAVGYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQavfgtgvVTgyydqeqrnLNDKKtv 402
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGE-------IL---------LDGKD-- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 403 LSELwdehpttPEKDIRTILeSFLF-----TGAD--VDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSR- 474
Cdd:cd03214 63 LASL-------SPKELARKI-AYVPqalelLGLAhlADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQi 134
|
170 180 190
....*....|....*....|....*....|.
gi 2269171783 475 EVLEV--ALNDFDG-TLLFVSHDryfINQVA 502
Cdd:cd03214 135 ELLELlrRLARERGkTVVMVLHD---LNLAA 162
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-232 |
1.08e-24 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 102.20 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 2 RRFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISmrkgltigylaqdqgLDSQNtiweemssv 81
Cdd:COG4619 8 FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIY---------------LDGKP--------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 82 FAELHAIEKRMhalenQLS----DPAIMNDdqayqqTLktYDQVQTEFQQKNGYGYQAEIRGVLHGFQFDADVYDKSVTE 157
Cdd:COG4619 64 LSAMPPPEWRR-----QVAyvpqEPALWGG------TV--RDNLPFPFQLRERKFDRERALELLERLGLPPDILDKPVER 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 158 LSGGQK----------TQlalaklllekRDLLILDEPTNHLDVET----LTWLESYLQSYAGALLIVSHDRYFLDRVVNE 223
Cdd:COG4619 131 LSGGERqrlalirallLQ----------PDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADR 200
|
....*....
gi 2269171783 224 VYDLSHHEM 232
Cdd:COG4619 201 VLTLEAGRL 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-245 |
6.63e-23 |
|
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: 98.01 E-value: 6.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 3 RFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQIS-------------MRKgltIGYLAQDQGLD 69
Cdd:COG4555 10 KYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILidgedvrkepreaRRQ---IGVLPDERGLY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 70 SQNTIwEEMSSVFAELHAiekrmhalenqlsdpaiMNDDQAyqqtlktydqvqtefqqkngygyQAEIRGVLHGFQFDaD 149
Cdd:COG4555 87 DRLTV-RENIRYFAELYG-----------------LFDEEL-----------------------KKRIEELIELLGLE-E 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 150 VYDKSVTELSGGQKTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYAG---ALLIVSHDRYFLDRVVNEVYD 226
Cdd:COG4555 125 FLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKegkTVLFSSHIMQEVEALCDRVVI 204
|
250
....*....|....*....
gi 2269171783 227 LSHHEMVhYTGNYDQFVQE 245
Cdd:COG4555 205 LHKGKVV-AQGSLDELREE 222
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
321-494 |
5.08e-22 |
|
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: 94.47 E-value: 5.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 321 VLTVKDAAVGYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGYYDQEQRNL---- 396
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLaylg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 397 --NDKKTVLS-----ELWDE--HPTTPEKDIRTILESFLFTGADvDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTN 467
Cdd:COG4133 82 haDGLKPELTvrenlRFWAAlyGLRADREAIDEALEAVGLAGLA-DLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190
....*....|....*....|....*....|
gi 2269171783 468 HLDIDSREVLEVALNDF---DGTLLFVSHD 494
Cdd:COG4133 161 ALDAAGVALLAELIAAHlarGGAVLLTTHQ 190
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-231 |
6.52e-22 |
|
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: 94.08 E-value: 6.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 3 RFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMRKGLT----------IGYLAQDQGLDSQN 72
Cdd:COG4133 11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIrdaredyrrrLAYLGHADGLKPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 73 TIWEEMssvfaelhaiekRMHAlenqlsdpaimnddqayqqtlktydqvqtefQQKNGYGYQAEIRGVLHGFQFdADVYD 152
Cdd:COG4133 91 TVRENL------------RFWA-------------------------------ALYGLRADREAIDEALEAVGL-AGLAD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 153 KSVTELSGGQK----------TQlalaklllekRDLLILDEPTNHLDVETLTWLESYLQSYA---GALLIVSHDRYFLDR 219
Cdd:COG4133 127 LPVRQLSAGQKrrvalarlllSP----------APLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELAA 196
|
250
....*....|..
gi 2269171783 220 VvnEVYDLSHHE 231
Cdd:COG4133 197 A--RVLDLGDFK 206
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
323-506 |
1.04e-21 |
|
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: 91.92 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 323 TVKDAAVGYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAvfgtgvvtgyydqeqrnlndkktv 402
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 403 lseLWDEHPTTpEKDIRTILESFLFtgadvdkpVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLEVALN 482
Cdd:cd00267 57 ---LIDGKDIA-KLPLEELRRRIGY--------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLR 124
|
170 180
....*....|....*....|....*..
gi 2269171783 483 DF---DGTLLFVSHDRYFINQVATSVV 506
Cdd:cd00267 125 ELaeeGRTVIIVTHDPELAELAADRVI 151
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
341-509 |
1.06e-19 |
|
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: 87.91 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGtGVVTGYYDQEQR---------NLND---KKTVLSEL-- 406
Cdd:cd03225 21 SLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVD-GKDLTKLSLKELrrkvglvfqNPDDqffGPTVEEEVaf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 407 WDEHPTTPEKDIRTI---------LESFLftgadvDKPVHALSGGERARL-LLTKLAMQNDnFLILDEPTNHLDIDSR-E 475
Cdd:cd03225 100 GLENLGLPEEEIEERveealelvgLEGLR------DRSPFTLSGGQKQRVaIAGVLAMDPD-ILLLDEPTAGLDPAGRrE 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 2269171783 476 VLEV--ALNDFDGTLLFVSHDRYFINQVATSVVEVS 509
Cdd:cd03225 173 LLELlkKLKAEGKTIIIVTHDLDLLLELADRVIVLE 208
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
341-467 |
1.17e-19 |
|
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: 85.78 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVT-----------GYYDQEqRNLNDKKTVLSELWD- 408
Cdd:pfam00005 5 SLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTdderkslrkeiGYVFQD-PQLFPRLTVRENLRLg 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2269171783 409 ---EHPTTPEKDIR--TILESFLFTGAD---VDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTN 467
Cdd:pfam00005 84 lllKGLSKREKDARaeEALEKLGLGDLAdrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
341-521 |
1.42e-19 |
|
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: 88.38 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQA-VFGTGVVT---------GYYDQEqRNLNDKKTV------LS 404
Cdd:COG4555 21 SFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSIlIDGEDVRKeprearrqiGVLPDE-RGLYDRLTVreniryFA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 405 ELWDEHPTTPEKDIRTILESFLFTGaDVDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLE---VAL 481
Cdd:COG4555 100 ELYGLFDEELKKRIEELIELLGLEE-FLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLReilRAL 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2269171783 482 NDFDGTLLFVSHDRYFINQVATSVVEVSpEGTELFLGDYD 521
Cdd:COG4555 179 KKEGKTVLFSSHIMQEVEALCDRVVILH-KGKVVAQGSLD 217
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-230 |
1.52e-19 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 88.20 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 2 RRFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI-----SMRKGLT-----IGYLAQDQGLDSQ 71
Cdd:COG1131 8 KRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVrvlgeDVARDPAevrrrIGYVPQEPALYPD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 72 NTIWEEMsSVFAELHAIEKRmhalenqlsdpaimNDDQAYQQTLKtydqvqtefqqkngygyqaeirgvlhgfQFD-ADV 150
Cdd:COG1131 88 LTVRENL-RFFARLYGLPRK--------------EARERIDELLE----------------------------LFGlTDA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 151 YDKSVTELSGGQKTqlalaklllekR-----------DLLILDEPTNHLDVETLTWLESYLQSYAG---ALLIVSHdryf 216
Cdd:COG1131 125 ADRKVGTLSGGMKQ-----------RlglalallhdpELLILDEPTSGLDPEARRELWELLRELAAegkTVLLSTH---- 189
|
250
....*....|....
gi 2269171783 217 ldrVVNEVYDLSHH 230
Cdd:COG1131 190 ---YLEEAERLCDR 200
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
10-186 |
2.64e-19 |
|
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: 85.01 E-value: 2.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 10 FDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI-------------SMRKGltIGYLAQDQGLDSQNTIWE 76
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTIlldgqdltdderkSLRKE--IGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 77 EMssvfaelhAIEKRMHALENQLSdpaimnDDQAyqqtlktyDQVQTEFQQKNgygyqaeirgvlhgfqFDADVYDKSVT 156
Cdd:pfam00005 79 NL--------RLGLLLKGLSKREK------DARA--------EEALEKLGLGD----------------LADRPVGERPG 120
|
170 180 190
....*....|....*....|....*....|
gi 2269171783 157 ELSGGQKTQLALAKLLLEKRDLLILDEPTN 186
Cdd:pfam00005 121 TLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
341-494 |
3.02e-19 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 87.43 E-value: 3.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQA-VFGTGVVT---------GYYDQEQrNLNDKKTV------LS 404
Cdd:COG1131 20 SLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVrVLGEDVARdpaevrrriGYVPQEP-ALYPDLTVrenlrfFA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 405 ELWDEHPTTPEKDIRTILESFLFTGAdVDKPVHALSGGERARLLLTkLAMQND-NFLILDEPTNHLDIDSR-EVLEV--A 480
Cdd:COG1131 99 RLYGLPRKEARERIDELLELFGLTDA-ADRKVGTLSGGMKQRLGLA-LALLHDpELLILDEPTSGLDPEARrELWELlrE 176
|
170
....*....|....
gi 2269171783 481 LNDFDGTLLFVSHD 494
Cdd:COG1131 177 LAAEGKTVLLSTHY 190
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
341-506 |
3.65e-19 |
|
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: 85.14 E-value: 3.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQA-VFGTGVVtgyydqeqrnlndkktvlselwdEHPTTPEKDIR 419
Cdd:cd03230 20 SLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIkVLGKDIK-----------------------KEPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 420 TILESFLF----TGADVDKpvhaLSGGERARLLLTkLAMQND-NFLILDEPTNHLDIDSR-EVLEV--ALNDFDGTLLFV 491
Cdd:cd03230 77 YLPEEPSLyenlTVRENLK----LSGGMKQRLALA-QALLHDpELLILDEPTSGLDPESRrEFWELlrELKKEGKTILLS 151
|
170
....*....|....*
gi 2269171783 492 SHDRYFINQVATSVV 506
Cdd:cd03230 152 SHILEEAERLCDRVA 166
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
321-493 |
1.93e-18 |
|
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: 85.14 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 321 VLTVKDAAVGYDGH-ILsepDNLN--VKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQ--AVFG--TGVVT------- 386
Cdd:COG1119 3 LLELRNVTVRRGGKtIL---DDISwtVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvRLFGerRGGEDvwelrkr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 387 -GYYDQE-----QRNLNDKKTVLSELWD-----EHPTTPEKDI-RTILESFlftGAD--VDKPVHALSGGERARLLLTKL 452
Cdd:COG1119 80 iGLVSPAlqlrfPRDETVLDVVLSGFFDsiglyREPTDEQRERaRELLELL---GLAhlADRPFGTLSQGEQRRVLIARA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2269171783 453 AMQNDNFLILDEPTNHLDIDSREVLEVALNDF--DG--TLLFVSH 493
Cdd:COG1119 157 LVKDPELLILDEPTAGLDLGARELLLALLDKLaaEGapTLVLVTH 201
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
322-506 |
2.31e-18 |
|
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: 84.69 E-value: 2.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 322 LTVKDAAVGYDG--HILSEPdNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGtGVVTgyydqeqrnlndK 399
Cdd:COG1122 1 IELENLSFSYPGgtPALDDV-SLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVD-GKDI------------T 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 400 KTVLSELWDE-------------HPT-------------TPEKDIRTILESFLftgADV------DKPVHALSGGERARL 447
Cdd:COG1122 67 KKNLRELRRKvglvfqnpddqlfAPTveedvafgpenlgLPREEIRERVEEAL---ELVglehlaDRPPHELSGGQKQRV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2269171783 448 -LLTKLAMQNDnFLILDEPTNHLDIDSR-EVLEV--ALNDFDGTLLFVSHDRYFINQVATSVV 506
Cdd:COG1122 144 aIAGVLAMEPE-VLVLDEPTAGLDPRGRrELLELlkRLNKEGKTVIIVTHDLDLVAELADRVI 205
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
321-494 |
4.86e-18 |
|
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: 83.71 E-value: 4.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 321 VLTVKDAAVGYDGHILSEP--DNLN--VKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGYYDQEQRN- 395
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKalDDVSfsIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 396 --------------LNDKKTV---LSE-LWDEHPTTPEKDIRTI----LESFLFTGADVDKPVHALSGGERARLLLTK-L 452
Cdd:cd03257 81 rkeiqmvfqdpmssLNPRMTIgeqIAEpLRIHGKLSKKEARKEAvlllLVGVGLPEEVLNRYPHELSGGQRQRVAIARaL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2269171783 453 AMQNDnFLILDEPTNHLDIDSR-EVLEVaLND----FDGTLLFVSHD 494
Cdd:cd03257 161 ALNPK-LLIADEPTSALDVSVQaQILDL-LKKlqeeLGLTLLFITHD 205
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-221 |
7.80e-18 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 83.21 E-value: 7.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 3 RFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISM------RKGLTIGYLAQDQGLDSQN--TI 74
Cdd:COG1121 15 SYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfgkpprRARRRIGYVPQRAEVDWDFpiTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 75 WE--EM-----SSVFAELHAIEKR--MHALEnqlsdpaimnddqayqqtlktydQVQTEfqqkngygyqaeirgvlhgfq 145
Cdd:COG1121 95 RDvvLMgrygrRGLFRRPSRADREavDEALE-----------------------RVGLE--------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 146 fdaDVYDKSVTELSGGQKtQlalaklllekR-----------DLLILDEPTNHLDVETLTWLESYLQSYAG---ALLIVS 211
Cdd:COG1121 131 ---DLADRPIGELSGGQQ-Q----------RvllaralaqdpDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVT 196
|
250
....*....|....*
gi 2269171783 212 HD-----RYFlDRVV 221
Cdd:COG1121 197 HDlgavrEYF-DRVL 210
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
322-506 |
4.71e-17 |
|
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: 79.15 E-value: 4.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 322 LTVKDAAVGYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGYYDQeqrnlndkkt 401
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDE---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 402 vlselwdehPTTPEKDIRTILESF-LFTGADV-DKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSR-EVLE 478
Cdd:cd03229 71 ---------LPPLRRRIGMVFQDFaLFPHLTVlENIALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRrEVRA 141
|
170 180 190
....*....|....*....|....*....|.
gi 2269171783 479 V--ALNDFDG-TLLFVSHDRYFINQVATSVV 506
Cdd:cd03229 142 LlkSLQAQLGiTVVLVTHDLDEAARLADRVV 172
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-231 |
7.15e-17 |
|
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: 79.82 E-value: 7.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 5 GADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI-----------SMRKGLTIGYLAQDQglDSQ-- 71
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVlvdgkdltklsLKELRRKVGLVFQNP--DDQff 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 72 -NTIWEEMSsvFAelhaiekrmhaLENQLSDPAIMndDQAYQQTLKTYDqvqtefqqkngygyqaeirgvLHGFQfdadv 150
Cdd:cd03225 90 gPTVEEEVA--FG-----------LENLGLPEEEI--EERVEEALELVG---------------------LEGLR----- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 151 yDKSVTELSGGQKtqlalakllleKR-----------DLLILDEPTNHLDVETLTWLESYLQSYAGA---LLIVSHDRYF 216
Cdd:cd03225 129 -DRSPFTLSGGQK-----------QRvaiagvlamdpDILLLDEPTAGLDPAGRRELLELLKKLKAEgktIIIVTHDLDL 196
|
250
....*....|....*
gi 2269171783 217 LDRVVNEVYDLSHHE 231
Cdd:cd03225 197 LLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-233 |
1.07e-16 |
|
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: 79.68 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 5 GADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI-------------SMRKglTIGYLAQDQglDSQ 71
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVlvdgkditkknlrELRR--KVGLVFQNP--DDQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 72 ---NTIWEEMSsvFaelhaiekrmhALENQLSDPAIMndDQAYQQTLKTYDqvqtefqqkngygyqaeirgvLHGFQfda 148
Cdd:COG1122 88 lfaPTVEEDVA--F-----------GPENLGLPREEI--RERVEEALELVG---------------------LEHLA--- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 149 dvyDKSVTELSGGQKtqlalakllleKR-----------DLLILDEPTNHLDVETLTWLESYLQSYAGA---LLIVSHDR 214
Cdd:COG1122 129 ---DRPPHELSGGQK-----------QRvaiagvlamepEVLVLDEPTAGLDPRGRRELLELLKRLNKEgktVIIVTHDL 194
|
250
....*....|....*....
gi 2269171783 215 YFLDRVVNEVYDLSHHEMV 233
Cdd:COG1122 195 DLVAELADRVIVLDDGRIV 213
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
341-506 |
1.34e-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: 78.80 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQA-VFGTGVvtgyydqeQRNLNDKKTVLSEL----WDEHPTT-- 413
Cdd:cd03268 20 SLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEItFDGKSY--------QKNIEALRRIGALIeapgFYPNLTAre 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 414 -----------PEKDIRTILESFLFTGADvDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDS----REVLe 478
Cdd:cd03268 92 nlrllarllgiRKKRIDEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGikelRELI- 169
|
170 180
....*....|....*....|....*...
gi 2269171783 479 VALNDFDGTLLFVSHDRYFINQVATSVV 506
Cdd:cd03268 170 LSLRDQGITVLISSHLLSEIQKVADRIG 197
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-221 |
1.40e-16 |
|
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: 79.70 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 3 RFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISM---------RKGL--TIGYLAQDQGLDSQ 71
Cdd:COG1120 10 GYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdgrdlaslsRRELarRIAYVPQEPPAPFG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 72 NTIWE--EMSsvfaelhaiekRM--HALENQLSDpaimNDDQAYQQTLKtydqvQTefqqkngygyqaeirGVLHgFQfd 147
Cdd:COG1120 90 LTVRElvALG-----------RYphLGLFGRPSA----EDREAVEEALE-----RT---------------GLEH-LA-- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 148 advyDKSVTELSGGQKtQlalaklllekR-----------DLLILDEPTNHLD----VETLTWLESYLQSYAGALLIVSH 212
Cdd:COG1120 132 ----DRPVDELSGGER-Q----------RvliaralaqepPLLLLDEPTSHLDlahqLEVLELLRRLARERGRTVVMVLH 196
|
250
....*....|....
gi 2269171783 213 D-----RYFlDRVV 221
Cdd:COG1120 197 DlnlaaRYA-DRLV 209
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
301-494 |
1.79e-16 |
|
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: 82.88 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 301 DSDEKTAHFGFHAAKQSGNIVLTVKDAAVGY-DGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAV 379
Cdd:COG4988 316 DAPEPAAPAGTAPLPAAGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIL 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 380 FGtgvvtgyyDQEQRNLNdkktvlSELWDEH-----------------------PTTPEKDIRTILESflfTGAD----- 431
Cdd:COG4988 396 IN--------GVDLSDLD------PASWRRQiawvpqnpylfagtirenlrlgrPDASDEELEAALEA---AGLDefvaa 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2269171783 432 ----VDKPV----HALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLEVALNDF--DGTLLFVSHD 494
Cdd:COG4988 459 lpdgLDTPLgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLakGRTVILITHR 531
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-232 |
3.49e-16 |
|
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: 76.67 E-value: 3.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 3 RFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI-----SMRKGLT-----IGYLAQDQGLDSQN 72
Cdd:cd03230 9 RYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIkvlgkDIKKEPEevkrrIGYLPEEPSLYENL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 73 TIWEEMssvfaelhaiekrmhalenqlsdpaimnddqayqqtlktydqvqtefqqkngygyqaeirgvlhgfqfdadvyd 152
Cdd:cd03230 89 TVRENL-------------------------------------------------------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 153 ksvtELSGGQKTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYA---GALLIVSHDRYFLDRVVNEVYDLSH 229
Cdd:cd03230 95 ----KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKkegKTILLSSHILEEAERLCDRVAILNN 170
|
...
gi 2269171783 230 HEM 232
Cdd:cd03230 171 GRI 173
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
9-224 |
3.49e-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: 77.68 E-value: 3.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 9 LFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISM--------RKGLTIGYLAQDqgLDSQNTiweeMSS 80
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLngkpikakERRKSIGYVMQD--VDYQLF----TDS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 81 VFAELhaiekrmhalenQLSDPAIMNDDQAYQQTLKTYDqvqtefqqkngygyqaeirgvLHGFQfdadvyDKSVTELSG 160
Cdd:cd03226 89 VREEL------------LLGLKELDAGNEQAETVLKDLD---------------------LYALK------ERHPLSLSG 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2269171783 161 GQKTQLALAKLLLEKRDLLILDEPTNHLD---VETLTWLESYLQSYAGALLIVSHDRYFLDRVVNEV 224
Cdd:cd03226 130 GQKQRLAIAAALLSGKDLLIFDEPTSGLDyknMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRV 196
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
313-494 |
4.26e-16 |
|
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: 81.64 E-value: 4.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 313 AAKQSGNIVLTVKDAAVGYDGHILSEPD-NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQaVFGTGVVTGYYDQ 391
Cdd:TIGR02868 326 GAVGLGKPTLELRDLSAGYPGAPPVLDGvSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGE-VTLDGVPVSSLDQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 392 -----------EQRNLNDKkTVLSELWDEHPTTPEKDIRTILESF--------LFTGADVDKPVHA--LSGGERARLLLT 450
Cdd:TIGR02868 405 devrrrvsvcaQDAHLFDT-TVRENLRLARPDATDEELWAALERVgladwlraLPDGLDTVLGEGGarLSGGERQRLALA 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2269171783 451 KLAMQNDNFLILDEPTNHLDID-SREVLEVALNDFDG-TLLFVSHD 494
Cdd:TIGR02868 484 RALLADAPILLLDEPTEHLDAEtADELLEDLLAALSGrTVVLITHH 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
11-224 |
8.28e-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: 76.86 E-value: 8.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQIS-------------MRKGltIGYLAQDQGLdsqntiwee 77
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLldgtdirqldpadLRRN--IGYVPQDVTL--------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 78 mssVFAELHaiekrmhalEN-QLSDPAImnDDQAYQQTLKTydQVQTEFQQKNGYGYQAEIRGvlHGFQfdadvydksvt 156
Cdd:cd03245 90 ---FYGTLR---------DNiTLGAPLA--DDERILRAAEL--AGVTDFVNKHPNGLDLQIGE--RGRG----------- 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 157 eLSGGQKTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYAG--ALLIVSHdRYFLDRVVNEV 224
Cdd:cd03245 141 -LSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITH-RPSLLDLVDRI 208
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
9-247 |
1.48e-15 |
|
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: 80.26 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 9 LFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI-------------SMRKglTIGYLAQDQGLDSQnTIw 75
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIlidgidlrqidpaSLRR--QIGVVLQDVFLFSG-TI- 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 76 eemssvfaelhaiekrmhaLEN-QLSDPAImnDDQAYQQTLKtydQVQ-TEFQQKNGYGYQAEI--RGvlhgfqfdadvy 151
Cdd:COG2274 566 -------------------RENiTLGDPDA--TDEEIIEAAR---LAGlHDFIEALPMGYDTVVgeGG------------ 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 152 dksvTELSGGQKtQlalaklllekR-----------DLLILDEPTNHLDVETLTWLESYLQSYAG--ALLIVSH------ 212
Cdd:COG2274 610 ----SNLSGGQR-Q----------RlaiarallrnpRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHrlstir 674
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2269171783 213 --DR-YFLD--RVVNevyDLSHHEMVHYTGNYDQFVQEKA 247
Cdd:COG2274 675 laDRiIVLDkgRIVE---DGTHEELLARKGLYAELVQQQL 711
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-221 |
2.02e-15 |
|
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: 74.78 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 3 RFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISmrkgltigylaqdqgLDSQNTiwEEMSSvf 82
Cdd:cd03214 8 GYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL---------------LDGKDL--ASLSP-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 83 aelHAIEKRMhalenqlsdpAIMNddQAYQQTlktydqvqtefqqkngygyqaeirGVLHgfqfdadVYDKSVTELSGGQ 162
Cdd:cd03214 69 ---KELARKI----------AYVP--QALELL------------------------GLAH-------LADRPFNELSGGE 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2269171783 163 K---------TQLAlaklllekrDLLILDEPTNHLD----VETLTWLESYLQSYAGALLIVSHD-----RYFlDRVV 221
Cdd:cd03214 103 RqrvllaralAQEP---------PILLLDEPTSHLDiahqIELLELLRRLARERGKTVVMVLHDlnlaaRYA-DRVI 169
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
284-506 |
2.30e-15 |
|
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: 79.42 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 284 AQARRKQLAKMDRIDRPDSDEKTAHFGFHAAKQSGNIVLTVKDAAVGYDG--HILSEPDNLNVKKHEAIAIVGPNGIGKS 361
Cdd:COG4987 296 AQHLGRVRAAARRLNELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKS 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 362 TFLKSILGQIPFIKGQAVFGtGVVTGYYDQEQrnLNDKKTVLSElwDEH--------------PTTPEKDIRTILE---- 423
Cdd:COG4987 376 TLLALLLRFLDPQSGSITLG-GVDLRDLDEDD--LRRRIAVVPQ--RPHlfdttlrenlrlarPDATDEELWAALErvgl 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 424 -SFLFTGAD-VDKPVH----ALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDS-REVLEVALNDFDG-TLLFVSHDR 495
Cdd:COG4987 451 gDWLAALPDgLDTWLGeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATeQALLADLLEALAGrTVLLITHRL 530
|
250
....*....|.
gi 2269171783 496 YFINQVATSVV 506
Cdd:COG4987 531 AGLERMDRILV 541
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
323-506 |
3.98e-15 |
|
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: 74.60 E-value: 3.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 323 TVKDAAVGY-DGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGtGVVTGYYDQEQR------N 395
Cdd:cd03226 1 RIENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLN-GKPIKAKERRKSigyvmqD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 396 LNDK---KTVLSELWDEHPTTPEK--DIRTILESFLFTGADVDKPvHALSGGERARLLLTKLAMQNDNFLILDEPTNHLD 470
Cdd:cd03226 80 VDYQlftDSVREELLLGLKELDAGneQAETVLKDLDLYALKERHP-LSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 2269171783 471 IDSREVLEVALNDF---DGTLLFVSHDRYFINQVATSVV 506
Cdd:cd03226 159 YKNMERVGELIRELaaqGKAVIVITHDYEFLAKVCDRVL 197
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
330-494 |
4.69e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 73.81 E-value: 4.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 330 GYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGYYDQEqrnlndkktvlSELWDE 409
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQR-----------SEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 410 HPTT------------------PEKDIRTILESFL--FTGADVDK-PVHALSGGERARLLLTKLAMQNDNFLILDEPTNH 468
Cdd:NF040873 70 LPLTvrdlvamgrwarrglwrrLTRDDRAAVDDALerVGLADLAGrQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180
....*....|....*....|....*....
gi 2269171783 469 LDIDSREVLEVALNDF--DG-TLLFVSHD 494
Cdd:NF040873 150 LDAESRERIIALLAEEhaRGaTVVVVTHD 178
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
341-493 |
5.07e-15 |
|
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: 73.19 E-value: 5.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGqipfikgqavfgtgvvtgYYDQEQRNLndkktvlseLWDEHPTT--PEKDI 418
Cdd:cd03228 22 SLTIKPGEKVAIVGPSGSGKSTLLKLLLR------------------LYDPTSGEI---------LIDGVDLRdlDLESL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 419 RTIL-----ESFLFTGadvdkPVHA--LSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLEVALNDFDG--TLL 489
Cdd:cd03228 75 RKNIayvpqDPFLFSG-----TIREniLSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKgkTVI 149
|
....
gi 2269171783 490 FVSH 493
Cdd:cd03228 150 VIAH 153
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
321-506 |
6.92e-15 |
|
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: 77.64 E-value: 6.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 321 VLTVKDAAVGYDGHILSEPDNLN--VKKHEAIAIVGPNGIGKSTFLKSILGQIPF---IKGQAVF-GTGVVT-------- 386
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSltIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLdGRDLLElsealrgr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 387 --GYYDQEQRNLNDKKTVLSELWD--EHPTTPEKDIRT-ILESFLFTGAD--VDKPVHALSGGERARLLL-TKLAMQNDn 458
Cdd:COG1123 84 riGMVFQDPMTQLNPVTVGDQIAEalENLGLSRAEARArVLELLEAVGLErrLDRYPHQLSGGQRQRVAIaMALALDPD- 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2269171783 459 FLILDEPTNHLDIDS-REVLEV--ALNDFDG-TLLFVSHDRYFINQVATSVV 506
Cdd:COG1123 163 LLIADEPTTALDVTTqAEILDLlrELQRERGtTVLLITHDLGVVAEIADRVV 214
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
322-495 |
7.15e-15 |
|
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: 74.09 E-value: 7.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 322 LTVKDAAVGYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGyYDQEQRN------ 395
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG-VPPERRNigmvfq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 396 -------LNDKKTVLSELwdEHPTTPEKDIRT-ILESFLFTGAD--VDKPVHALSGGERARLLLTK-LAMQNDnFLILDE 464
Cdd:cd03259 80 dyalfphLTVAENIAFGL--KLRGVPKAEIRArVRELLELVGLEglLNRYPHELSGGQQQRVALARaLAREPS-LLLLDE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 2269171783 465 PTNHLDIDSREVL--EVA--LNDFDGTLLFVSHDR 495
Cdd:cd03259 157 PLSALDAKLREELreELKelQRELGITTIYVTHDQ 191
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-191 |
7.83e-15 |
|
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: 73.77 E-value: 7.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 3 RFGADVLFDNVQMDIQEhARVALVGRNGAGKSTLLKMIAGETVPDEGQI--------SMRKGL--TIGYLAQDQGLDSQN 72
Cdd:cd03264 9 RYGKKRALDGVSLTLGP-GMYGLLGPNGAGKTTLMRILATLTPPSSGTIridgqdvlKQPQKLrrRIGYLPQEFGVYPNF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 73 TIWEemssvFAELHAIEKRmhalenqlsdpaiMNDDQAYQQTLKTYDQVQTefqqkngygyqaeirgvlhgfqfdADVYD 152
Cdd:cd03264 88 TVRE-----FLDYIAWLKG-------------IPSKEVKARVDEVLELVNL------------------------GDRAK 125
|
170 180 190
....*....|....*....|....*....|....*....
gi 2269171783 153 KSVTELSGGQKTQLALAKLLLEKRDLLILDEPTNHLDVE 191
Cdd:cd03264 126 KKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPE 164
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-227 |
9.05e-15 |
|
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: 72.28 E-value: 9.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 3 RFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQIsmrkgltigylaqdqgldsqntiweemssvf 82
Cdd:cd00267 8 RYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI------------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 83 aelhaiekrmhalenQLSDPAIMNDDQAyqqtlktydqvqtefQQKNGYGYqaeirgvlhgfqfdadvydksVTELSGGQ 162
Cdd:cd00267 57 ---------------LIDGKDIAKLPLE---------------ELRRRIGY---------------------VPQLSGGQ 85
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2269171783 163 KTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYAG---ALLIVSHDRYFLDRVVNEVYDL 227
Cdd:cd00267 86 RQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAELAADRVIVL 153
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
294-494 |
1.40e-14 |
|
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: 77.18 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 294 MDRI----DRPDSDEKTAHFGfHAAKQSGNIvlTVKDAAVGYDGH---ILSEPdNLNVKKHEAIAIVGPNGIGKSTFLKS 366
Cdd:COG2274 445 LERLddilDLPPEREEGRSKL-SLPRLKGDI--ELENVSFRYPGDsppVLDNI-SLTIKPGERVAIVGRSGSGKSTLLKL 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 367 ILGQIPFIKGQAVFGtGV------------VTGYYDQEQRNLNDkkTVLSELWDEHPTTPEKDIRTILEsflFTGAD--- 431
Cdd:COG2274 521 LLGLYEPTSGRILID-GIdlrqidpaslrrQIGVVLQDVFLFSG--TIRENITLGDPDATDEEIIEAAR---LAGLHdfi 594
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2269171783 432 ------VDKPV----HALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLEVALNDFDG--TLLFVSHD 494
Cdd:COG2274 595 ealpmgYDTVVgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHR 669
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
5-242 |
1.71e-14 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 76.82 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 5 GADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMRKGLTIGYLAQDQ--GLDSQNTIWEEMSSVF 82
Cdd:PLN03073 520 GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHvdGLDLSSNPLLYMMRCF 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 83 aelhaiekrmhalenqlsdPAIMnddqayqqtlktydqvqtefQQKngygyqaeIRGVLHGFQFDADVYDKSVTELSGGQ 162
Cdd:PLN03073 600 -------------------PGVP--------------------EQK--------LRAHLGSFGVTGNLALQPMYTLSGGQ 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 163 KTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYAGALLIVSHDRYFLDRVVNEVYDLSHHEMVHYTGNYDQF 242
Cdd:PLN03073 633 KSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDY 712
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
343-506 |
2.92e-14 |
|
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: 72.83 E-value: 2.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 343 NVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAvfGTGVVTGYYDQEQRNLNDKKTV---LSELWDEHPTTPEKDIR 419
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI--EIELDTVSYKPQYIKADYEGTVrdlLSSITKDFYTHPYFKTE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 420 TI----LESFLftgadvDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLEVALNDF----DGTLLFV 491
Cdd:cd03237 99 IAkplqIEQIL------DREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFaennEKTAFVV 172
|
170
....*....|....*
gi 2269171783 492 SHDRYFINQVATSVV 506
Cdd:cd03237 173 EHDIIMIDYLADRLI 187
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
322-466 |
4.91e-14 |
|
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: 71.70 E-value: 4.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 322 LTVKDAAVGYDG-HILSEPDnLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGY-----------Y 389
Cdd:cd03224 1 LEVENLNAGYGKsQILFGVS-LTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLppheraragigY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 390 DQEQRNLNDKKTVLSEL----WDEHPTTPEKDIRTILESFLFTGADVDKPVHALSGGER-----ARLLltklaMQNDNFL 460
Cdd:cd03224 80 VPEGRRIFPELTVEENLllgaYARRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQqmlaiARAL-----MSRPKLL 154
|
....*.
gi 2269171783 461 ILDEPT 466
Cdd:cd03224 155 LLDEPS 160
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
11-220 |
6.23e-14 |
|
type I secretion system ATPase, LssB 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. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 75.29 E-value: 6.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQIS-------------MRKGltIGYLAQDQGLdsqntiwee 77
Cdd:TIGR03375 482 DNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLldgvdirqidpadLRRN--IGYVPQDPRL--------- 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 78 mssVFAELHaiekrmhalEN-QLSDPAImnDDQAYQQTlktydqvqtefqqkngygyqAEIRGVLHGFQFDADVYDKSVT 156
Cdd:TIGR03375 551 ---FYGTLR---------DNiALGAPYA--DDEEILRA--------------------AELAGVTEFVRRHPDGLDMQIG 596
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 157 E----LSGGQKTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYAG--ALLIVSHDRYFLDRV 220
Cdd:TIGR03375 597 ErgrsLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAgkTLVLVTHRTSLLDLV 666
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
23-506 |
8.79e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 74.46 E-value: 8.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 23 VALVGRNGAGKSTLLKMIAGETVPDEGQismrkgltigylaqdqgLDSQNTiWE---------EMSSVFAELHAIEKRMh 93
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELIPNLGD-----------------YEEEPS-WDevlkrfrgtELQNYFKKLYNGEIKV- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 94 ALENQLSDPAIMNDDQAYQQTLKTYDQvqtefqqkngygyqaeiRGVLHGF--QFDAD-VYDKSVTELSGGQKTQLALAK 170
Cdd:PRK13409 163 VHKPQYVDLIPKVFKGKVRELLKKVDE-----------------RGKLDEVveRLGLEnILDRDISELSGGELQRVAIAA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 171 LLLEKRDLLILDEPTNHLDVETLTWLESYLQSYAG--ALLIVSHDRYFLDRVVnevyDLSHhemVHY--TGNYDQFVQEK 246
Cdd:PRK13409 226 ALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEgkYVLVVEHDLAVLDYLA----DNVH---IAYgePGAYGVVSKPK 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 247 AAR--IQAQWKHYEKqqaeiskledfvNRNIvrasttkraqarrkqlakmdRIdRPDSDEktahFGFHA--AKQSGNIVL 322
Cdd:PRK13409 299 GVRvgINEYLKGYLP------------EENM--------------------RI-RPEPIE----FEERPprDESERETLV 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 323 TVKDAAVGYDGHILsEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGtgvVTGYY-------DQE--- 392
Cdd:PRK13409 342 EYPDLTKKLGDFSL-EVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE---LKISYkpqyikpDYDgtv 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 393 QRNLNDKKTVLSELWDEHPTTPEKDIRTILesflftgadvDKPVHALSGGERARLLLTK-LAMQNDNFLiLDEPTNHLDI 471
Cdd:PRK13409 418 EDLLRSITDDLGSSYYKSEIIKPLQLERLL----------DKNVKDLSGGELQRVAIAAcLSRDADLYL-LDEPSAHLDV 486
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2269171783 472 DSRevLEVA------LNDFDGTLLFVSHDRYFINQVATSVV 506
Cdd:PRK13409 487 EQR--LAVAkairriAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
322-478 |
9.69e-14 |
|
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: 70.47 E-value: 9.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 322 LTVKDAAVGYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGYYDQEQRNL----- 396
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENIlylgh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 397 -NDKKTVLSEL-----WDEHPTTPEKDIRTILESFLFTGADvDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLD 470
Cdd:TIGR01189 81 lPGLKPELSALenlhfWAAIHGGAQRTIEDALAAVGLTGFE-DLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
....*...
gi 2269171783 471 IDSREVLE 478
Cdd:TIGR01189 160 KAGVALLA 167
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-235 |
1.26e-13 |
|
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: 70.39 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 2 RRFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI-------SMRKGLTIGYLAQDQGLDSQNTI 74
Cdd:cd03269 8 KRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVlfdgkplDIAARNRIGYLPEERGLYPKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 75 WEEMsSVFAELHAIEKRmhalenqlsdpaimnddQAyqqtlktydqvqtefqqkngygyQAEIRGVLHGFQFdADVYDKS 154
Cdd:cd03269 88 IDQL-VYLAQLKGLKKE-----------------EA-----------------------RRRIDEWLERLEL-SEYANKR 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 155 VTELSGGQKTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYAGA---LLIVSHDRYFLDRVVNEVYDLSHHE 231
Cdd:cd03269 126 VEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgktVILSTHQMELVEELCDRVLLLNKGR 205
|
....
gi 2269171783 232 MVHY 235
Cdd:cd03269 206 AVLY 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
11-221 |
1.32e-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: 70.61 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQIsMRKGLTIGYLAQDQgldsQNTIWEEMSSVFAELhaiek 90
Cdd:cd03257 22 DDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSI-IFDGKDLLKLSRRL----RKIRRKEIQMVFQDP----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 91 rMHALenqlsDPaimnddqayqqTLKTYDQVQTEFQ-QKNGYGYQAEIRGV---LHGFQFDADVYDKSVTELSGGQKtQl 166
Cdd:cd03257 92 -MSSL-----NP-----------RMTIGEQIAEPLRiHGKLSKKEARKEAVlllLVGVGLPEEVLNRYPHELSGGQR-Q- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2269171783 167 alaklllekR-----------DLLILDEPTNHLDV----ETLTWLESYLQSYAGALLIVSHD----RYFLDRVV 221
Cdd:cd03257 153 ---------RvaiaralalnpKLLIADEPTSALDVsvqaQILDLLKKLQEELGLTLLFITHDlgvvAKIADRVA 217
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
341-493 |
1.34e-13 |
|
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: 69.17 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGtGVvtgyydqeqrnlnDKKTVLSELWDEHPTTPEKDIRt 420
Cdd:cd03246 22 SFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLD-GA-------------DISQWDPNELGDHVGYLPQDDE- 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2269171783 421 ilesfLFTGADVDkpvHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLEVALNDFD---GTLLFVSH 493
Cdd:cd03246 87 -----LFSGSIAE---NILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKaagATRIVIAH 154
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
9-244 |
1.44e-13 |
|
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: 73.65 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 9 LFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQIsmrkglTIGylaqdqGLD----SQNTIWEEMSSVFAE 84
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSI------TLG------GVDlrdlDEDDLRRRIAVVPQR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 85 LHAiekrMHA--LEN-QLSDPAImnDDQAYQQTLKtydQVQ-TEFQQKNGYGYQAEIRGvlHGFQfdadvydksvteLSG 160
Cdd:COG4987 418 PHL----FDTtlRENlRLARPDA--TDEELWAALE---RVGlGDWLAALPDGLDTWLGE--GGRR------------LSG 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 161 GQKTqlalaklllekR-----------DLLILDEPTNHLDVET-LTWLESYLQSYAG-ALLIVSHDRYFLDRvVNEVYDL 227
Cdd:COG4987 475 GERR-----------RlalarallrdaPILLLDEPTEGLDAATeQALLADLLEALAGrTVLLITHRLAGLER-MDRILVL 542
|
250 260
....*....|....*....|....*.
gi 2269171783 228 ---------SHHEMVHYTGNYDQFVQ 244
Cdd:COG4987 543 edgriveqgTHEELLAQNGRYRQLYQ 568
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
322-493 |
1.74e-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: 68.88 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 322 LTVKDAAVGYDGHILSEPDNLN--VKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGYydqeQRNLNDK 399
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSleLKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL----EKALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 400 KTVLSElwdehpttpekdirtilESFLFTGADVDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLD-IDSREVLE 478
Cdd:cd03247 77 ISVLNQ-----------------RPYLFDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDpITERQLLS 139
|
170
....*....|....*.
gi 2269171783 479 VALNDF-DGTLLFVSH 493
Cdd:cd03247 140 LIFEVLkDKTLIWITH 155
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-221 |
1.85e-13 |
|
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: 73.09 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 5 GADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISM---------RKGL--TIGYLAQDQGLDSQnT 73
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVngvpladadADSWrdQIAWVPQHPFLFAG-T 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 74 IWEEMSsvFAELHAIEkrmHALENQLSDPAIMnddqayqqtlktydqvqtEFQQKNGYGYQAEIrgvlhgfqfdadvyDK 153
Cdd:TIGR02857 412 IAENIR--LARPDASD---AEIREALERAGLD------------------EFVAALPQGLDTPI--------------GE 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2269171783 154 SVTELSGGQKTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYAG--ALLIVSHDR---YFLDRVV 221
Cdd:TIGR02857 455 GGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRLalaALADRIV 527
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
341-495 |
3.03e-13 |
|
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: 69.44 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGYYDQEQRNLNDKK--------------TVL--- 403
Cdd:cd03255 24 SLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFRRRHigfvfqsfnllpdlTALenv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 404 ---SELWDEHPTTPEKDIRTILESF-LftGADVDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDID-SREVLE 478
Cdd:cd03255 104 elpLLLAGVPKKERRERAEELLERVgL--GDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSEtGKEVME 181
|
170 180
....*....|....*....|
gi 2269171783 479 V--ALNDFDG-TLLFVSHDR 495
Cdd:cd03255 182 LlrELNKEAGtTIVVVTHDP 201
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
322-513 |
3.15e-13 |
|
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: 68.71 E-value: 3.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 322 LTVKD--AAVGyDGHILsEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGqIP---FIKGQAVFgtgvvtgyydqEQRNL 396
Cdd:cd03217 1 LEIKDlhVSVG-GKEIL-KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPkyeVTEGEILF-----------KGEDI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 397 NDKKTvlSE--------LWDEHPTTPEkdIRtiLESFLftgADVDKpvhALSGGERARLLLTKLAMQNDNFLILDEPTNH 468
Cdd:cd03217 67 TDLPP--EErarlgiflAFQYPPEIPG--VK--NADFL---RYVNE---GFSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2269171783 469 LDIDSREVLEVALNDF---DGTLLFVSHDRYFINQVATSVVEVSPEGT 513
Cdd:cd03217 135 LDIDALRLVAEVINKLreeGKSVLIITHYQRLLDYIKPDRVHVLYDGR 182
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-52 |
3.25e-13 |
|
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: 67.84 E-value: 3.25e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2269171783 3 RFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQIS 52
Cdd:cd03216 9 RFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL 58
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-212 |
5.81e-13 |
|
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: 68.40 E-value: 5.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 2 RRFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQIsmrkgltigylaQDQGLDSQNTI--WEEMS 79
Cdd:cd03268 8 KTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEI------------TFDGKSYQKNIeaLRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 80 SVFaELHAIEKRMHALEN-QLSDPAIMNDDQAYQQTLktydqvqtefqqkngygyqaEIRGVlhgfqfdADVYDKSVTEL 158
Cdd:cd03268 76 ALI-EAPGFYPNLTARENlRLLARLLGIRKKRIDEVL--------------------DVVGL-------KDSAKKKVKGF 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2269171783 159 SGGQKTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYA---GALLIVSH 212
Cdd:cd03268 128 SLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRdqgITVLISSH 184
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
324-494 |
6.08e-13 |
|
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: 68.68 E-value: 6.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 324 VKDAAVGYDG-HILSEPDnLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGYYDQEQRNLNDKKTV 402
Cdd:cd03261 3 LRGLTKSFGGrTVLKGVD-LDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 403 L---SELWD-------------EHPTTPEKDIRTILESFL-FTG--ADVDKPVHALSGGERARLLLTKLAMQNDNFLILD 463
Cdd:cd03261 82 LfqsGALFDsltvfenvafplrEHTRLSEEEIREIVLEKLeAVGlrGAEDLYPAELSGGMKKRVALARALALDPELLLYD 161
|
170 180 190
....*....|....*....|....*....|....*
gi 2269171783 464 EPTNHLD-IDSREVLEV--ALND-FDGTLLFVSHD 494
Cdd:cd03261 162 EPTAGLDpIASGVIDDLirSLKKeLGLTSIMVTHD 196
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
10-58 |
6.70e-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: 68.33 E-value: 6.70e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2269171783 10 FDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMRKGLT 58
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS 86
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-501 |
8.52e-13 |
|
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: 70.99 E-value: 8.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 2 RRFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAG--ETVPDEGQISMRKGL--TIGYLAQDQGLDSQ-----N 72
Cdd:TIGR03269 8 KKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHVALceKCGYVERPSKVGEPcpvcgG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 73 TIWEEMSSVF----AELHAIEKRMhalenqlsdpAIMnddqaYQQTLKTYDQ---VQTEFQQKNGYGYQAEirgvlHGFQ 145
Cdd:TIGR03269 88 TLEPEEVDFWnlsdKLRRRIRKRI----------AIM-----LQRTFALYGDdtvLDNVLEALEEIGYEGK-----EAVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 146 FDADVYDKS---------VTELSGGQKTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYL----QSYAGALLIVSH 212
Cdd:TIGR03269 148 RAVDLIEMVqlshrithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALeeavKASGISMVLTSH 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 213 DRYFLDRVVNEVYDLSHHEMVHyTGNYDQFVqekaARIQAQWKHYEK-----QQAEISKLEDF------VNRNIVRAstt 281
Cdd:TIGR03269 228 WPEVIEDLSDKAIWLENGEIKE-EGTPDEVV----AVFMEGVSEVEKeceveVGEPIIKVRNVskryisVDRGVVKA--- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 282 kraqarrkqlakMDRIDrpdsdektahfgfhaakqsgnivltvkdaavgydghilsepdnLNVKKHEAIAIVGPNGIGKS 361
Cdd:TIGR03269 300 ------------VDNVS-------------------------------------------LEVKEGEIFGIVGTSGAGKT 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 362 TFLKSILGQIPFIKGQ---------------AVFGTGVVTGYYD--QEQRNLNDKKTVLSELWD----EHPTtpEKDIRT 420
Cdd:TIGR03269 325 TLSKIIAGVLEPTSGEvnvrvgdewvdmtkpGPDGRGRAKRYIGilHQEYDLYPHRTVLDNLTEaiglELPD--ELARMK 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 421 ILESFLFTGADVDKPV-------HALSGGERARLLLTKLAMQNDNFLILDEPTNHLD-IDSREVLEVALN---DFDGTLL 489
Cdd:TIGR03269 403 AVITLKMVGFDEEKAEeildkypDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpITKVDVTHSILKareEMEQTFI 482
|
570
....*....|..
gi 2269171783 490 FVSHDRYFINQV 501
Cdd:TIGR03269 483 IVSHDMDFVLDV 494
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
322-494 |
1.18e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 70.26 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 322 LTVKDAAVGY-DGHILSEPDnLNVKKHEAIAIVGPNGIGKSTFLKSILGQI-PfikgqavfGTGVVT-GYYDQEQRNLND 398
Cdd:PRK09536 4 IDVSDLSVEFgDTTVLDGVD-LSVREGSLVGLVGPNGAGKTTLLRAINGTLtP--------TAGTVLvAGDDVEALSARA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 399 ---------KKTVLSELWD-----EHPTTP---------EKDIRTILESFLFTGAD--VDKPVHALSGGERARLLLTKLA 453
Cdd:PRK09536 75 asrrvasvpQDTSLSFEFDvrqvvEMGRTPhrsrfdtwtETDRAAVERAMERTGVAqfADRPVTSLSGGERQRVLLARAL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2269171783 454 MQNDNFLILDEPTNHLDIDSR-EVLEVA--LNDFDGTLLFVSHD 494
Cdd:PRK09536 155 AQATPVLLLDEPTASLDINHQvRTLELVrrLVDDGKTAVAAIHD 198
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
322-494 |
1.46e-12 |
|
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: 67.50 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 322 LTVKDAAVGYDG-----HILsEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIP------FIKGQAVFGTGVVTGYYD 390
Cdd:cd03293 1 LEVRNVSKTYGGgggavTAL-EDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERptsgevLVDGEPVTGPGPDRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 391 QEQRnLNDKKTVLS--ELWDEHPTTPEKDIRTILESFL----FTGADVDKPvHALSGGERARLLLTK-LAMQNDnFLILD 463
Cdd:cd03293 80 QQDA-LLPWLTVLDnvALGLELQGVPKAEARERAEELLelvgLSGFENAYP-HQLSGGMRQRVALARaLAVDPD-VLLLD 156
|
170 180 190
....*....|....*....|....*....|....*
gi 2269171783 464 EPTNHLDIDSREVLEVAL----NDFDGTLLFVSHD 494
Cdd:cd03293 157 EPFSALDALTREQLQEELldiwRETGKTVLLVTHD 191
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
351-514 |
1.50e-12 |
|
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: 66.86 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 351 AIVGPNGIGKSTFLKSIL-----GQIPFIKGQA----VFGTGVVTGYYDQEQRNLNDKKTVLS---ELWDEHPTTPEKDI 418
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKyaltgELPPNSKGGAhdpkLIREGEVRAQVKLAFENANGKKYTITrslAILENVIFCHQGES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 419 RTILEsflftgadvdKPVHALSGGERA------RLLLTKLAMQNDNFLILDEPTNHLDIDSR-----EVLEVALNDFDGT 487
Cdd:cd03240 106 NWPLL----------DMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIeeslaEIIEERKSQKNFQ 175
|
170 180
....*....|....*....|....*..
gi 2269171783 488 LLFVSHDRYFInQVATSVVEVSPEGTE 514
Cdd:cd03240 176 LIVITHDEELV-DAADHIYRVEKDGRQ 201
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-221 |
1.58e-12 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 69.41 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 2 RRFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAG-ETvPDEGQISM-------------RKgltIGYLAQDQG 67
Cdd:COG1118 10 KRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGlET-PDSGRIVLngrdlftnlppreRR---VGFVFQHYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 68 LdsqntiWEEMsSVFaelhaiekrmhalEN--------QLSDPAImnddqayqqtlktydqvqtefqqkngygyQAEIRG 139
Cdd:COG1118 86 L------FPHM-TVA-------------ENiafglrvrPPSKAEI-----------------------------RARVEE 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 140 VLHGFQFD--ADVYdksVTELSGGQKtQlalaklllekR-----------DLLILDEPTNHLDV----ETLTWLESYLQS 202
Cdd:COG1118 117 LLELVQLEglADRY---PSQLSGGQR-Q----------RvalaralavepEVLLLDEPFGALDAkvrkELRRWLRRLHDE 182
|
250 260
....*....|....*....|...
gi 2269171783 203 YAGALLIVSHDR---YFL-DRVV 221
Cdd:COG1118 183 LGGTTVFVTHDQeeaLELaDRVV 205
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
332-513 |
1.65e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 70.22 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 332 DGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFikgqavfGTGVVTGYYDQE-----QR------NLndkK 400
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPY-------GSGRIARPAGARvlflpQRpylplgTL---R 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 401 TVLSelwdeHPTTPEK----DIRTILESF--------LFTGADVDkpvHALSGGER-----ARLLLTKLAmqndnFLILD 463
Cdd:COG4178 444 EALL-----YPATAEAfsdaELREALEAVglghlaerLDEEADWD---QVLSLGEQqrlafARLLLHKPD-----WLFLD 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2269171783 464 EPTNHLDIDSREVLEVALND--FDGTLLFVSHdRYFINQVATSVVEVSPEGT 513
Cdd:COG4178 511 EATSALDEENEAALYQLLREelPGTTVISVGH-RSTLAAFHDRVLELTGDGS 561
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-246 |
1.90e-12 |
|
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: 70.17 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 5 GADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQIsmrkglTIGylaqdqGLDsqntiweemssvfae 84
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSI------LIN------GVD--------------- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 85 LHAIekRMHALENQLS----DPAIMN--------------DDQAYQQTLKtydqvqtefqqkngygyQAEIRGVLHGFQf 146
Cdd:COG4988 401 LSDL--DPASWRRQIAwvpqNPYLFAgtirenlrlgrpdaSDEELEAALE-----------------AAGLDEFVAALP- 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 147 daDVYDKSVTE----LSGGQKtQlalaklllekR-----------DLLILDEPTNHLDVETLTWLESYLQSYAG--ALLI 209
Cdd:COG4988 461 --DGLDTPLGEggrgLSGGQA-Q----------RlalarallrdaPLLLLDEPTAHLDAETEAEILQALRRLAKgrTVIL 527
|
250 260 270
....*....|....*....|....*....|....*..
gi 2269171783 210 VSHDRYFLDRvVNEVYDLSHHEMVHyTGNYDQFVQEK 246
Cdd:COG4988 528 ITHRLALLAQ-ADRILVLDDGRIVE-QGTHEELLAKN 562
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
10-54 |
2.10e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 67.41 E-value: 2.10e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2269171783 10 FDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMR 54
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVN 86
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
341-495 |
2.30e-12 |
|
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: 69.62 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGtgvvtgyyDQEQRNLNDKKTVLSELW-DEHPTTPEKdir 419
Cdd:TIGR02857 342 SFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVN--------GVPLADADADSWRDQIAWvPQHPFLFAG--- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 420 TILESFLF-----TGADVDKPVHA------------------------LSGGERARLLLTKLAMQNDNFLILDEPTNHLD 470
Cdd:TIGR02857 411 TIAENIRLarpdaSDAEIREALERagldefvaalpqgldtpigeggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLD 490
|
170 180
....*....|....*....|....*..
gi 2269171783 471 IDSREVLEVALNDFDG--TLLFVSHDR 495
Cdd:TIGR02857 491 AETEAEVLEALRALAQgrTVLLVTHRL 517
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
351-494 |
2.54e-12 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 67.53 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 351 AIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGY-----------YDQEQR---NLNDKKTVL------SELW--- 407
Cdd:TIGR03873 31 GLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLsrrararrvalVEQDSDtavPLTVRDVVAlgriphRSLWagd 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 408 --DEHPTTPEKDIRTILESFlftgadVDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLEVALNDFD 485
Cdd:TIGR03873 111 spHDAAVVDRALARTELSHL------ADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAQLETLALVRELA 184
|
170
....*....|..
gi 2269171783 486 G---TLLFVSHD 494
Cdd:TIGR03873 185 AtgvTVVAALHD 196
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
322-481 |
3.07e-12 |
|
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: 65.98 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 322 LTVKDAAVGYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGYYDQEQRNL----- 396
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLlylgh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 397 -NDKKTVLSELWDEHPTTPEKDIRTILESFlftgADV------DKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHL 469
Cdd:cd03231 81 aPGIKTTLSVLENLRFWHADHSDEQVEEAL----ARVglngfeDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170
....*....|..
gi 2269171783 470 DIDSREVLEVAL 481
Cdd:cd03231 157 DKAGVARFAEAM 168
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
341-493 |
3.17e-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: 65.14 E-value: 3.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGYYDQEQRNLNdkktvlselwdehpttpekdIRT 420
Cdd:cd03216 20 SLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAG--------------------IAM 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2269171783 421 ilesflftgadvdkpVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLEVALNDF--DG-TLLFVSH 493
Cdd:cd03216 80 ---------------VYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLraQGvAVIFISH 140
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
341-518 |
3.42e-12 |
|
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: 66.59 E-value: 3.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLK-------------SILGQIPFI-KGQAVFGTGVVTGYYDQEQRNLN--DKKTVLS 404
Cdd:cd03267 41 SFTIEKGEIVGFIGPNGAGKTTTLKilsgllqptsgevRVAGLVPWKrRKKFLRRIGVVFGQKTQLWWDLPviDSFYLLA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 405 ELWDEHPTTPEKDIRTILEsFLFTGADVDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDS----REVLEVA 480
Cdd:cd03267 121 AIYDLPPARFKKRLDELSE-LLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAqeniRNFLKEY 199
|
170 180 190
....*....|....*....|....*....|....*...
gi 2269171783 481 LNDFDGTLLFVSHDRYFINQVATSVVEVSpEGTELFLG 518
Cdd:cd03267 200 NRERGTTVLLTSHYMKDIEALARRVLVID-KGRLLYDG 236
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
5-212 |
4.04e-12 |
|
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: 65.59 E-value: 4.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 5 GADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMrkgltigylaQDQGLDSQNTIWEEMSSVFAE 84
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLL----------NGGPLDFQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 85 LHAIEKRMHALENqLSDPAIMNDDQAYQQTLKTYDqvqtefqqkngygyqaeirgvLHGFQfdadvyDKSVTELSGGQKT 164
Cdd:cd03231 81 APGIKTTLSVLEN-LRFWHADHSDEQVEEALARVG---------------------LNGFE------DRPVAQLSAGQQR 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2269171783 165 QLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYA---GALLIVSH 212
Cdd:cd03231 133 RVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCargGMVVLTTH 183
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
23-237 |
4.79e-12 |
|
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: 65.63 E-value: 4.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 23 VALVGRNGAGKSTLLKMIAGETVPDEGQISM------RKGLTIGYLAQDQGLDSQN--TIWEEMSSvfaelhAIEKRMHA 94
Cdd:cd03235 28 LAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfgkpleKERKRIGYVPQRRSIDRDFpiSVRDVVLM------GLYGHKGL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 95 LENQLSDpaimnDDQAYQQTLKTydqVQTEfqqkngygyqaeirgvlhgfqfdaDVYDKSVTELSGGQKTQLALAKLLLE 174
Cdd:cd03235 102 FRRLSKA-----DKAKVDEALER---VGLS------------------------ELADRQIGELSGGQQQRVLLARALVQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2269171783 175 KRDLLILDEPTNHLDVET---LTWLESYLQSYAGALLIVSHDRYFLDRVVNEVYDLSHHemVHYTG 237
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTqedIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT--VVASG 213
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
11-213 |
4.91e-12 |
|
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: 65.99 E-value: 4.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI-----SMRKGLT-----IGYLAQDqgldsqNTIWEEMSs 80
Cdd:cd03263 19 DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyingySIRTDRKaarqsLGYCPQF------DALFDELT- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 81 vfaelhaiekrmhALENqlsdpaimnddqayqqtLKTYdqvqTEFQQKNGYGYQAEIRGVLHGFQFdADVYDKSVTELSG 160
Cdd:cd03263 92 -------------VREH-----------------LRFY----ARLKGLPKSEIKEEVELLLRVLGL-TDKANKRARTLSG 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2269171783 161 GQKtqlalaklllekR------------DLLILDEPTNHLDVETLTWLESYLQSYAG--ALLIVSHD 213
Cdd:cd03263 137 GMK------------RklslaialiggpSVLLLDEPTSGLDPASRRAIWDLILEVRKgrSIILTTHS 191
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
11-221 |
6.73e-12 |
|
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: 65.98 E-value: 6.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI-------------SMRKglTIGYLAQDqgldsqntiwee 77
Cdd:COG1124 22 KDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVtfdgrpvtrrrrkAFRR--RVQMVFQD------------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 78 mssVFAELHAiekrMHALENQLSDP-AIMNDDQAyqqtlktydqvqtefqqkngygyQAEIRGVLHGFQFDADVYDKSVT 156
Cdd:COG1124 88 ---PYASLHP----RHTVDRILAEPlRIHGLPDR-----------------------EERIAELLEQVGLPPSFLDRYPH 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 157 ELSGGQKtQlalaklllekR-----------DLLILDEPTNHLDV----ETLTWLESYLQSYAGALLIVSHD----RYFL 217
Cdd:COG1124 138 QLSGGQR-Q----------RvaiaralilepELLLLDEPTSALDVsvqaEILNLLKDLREERGLTYLFVSHDlavvAHLC 206
|
....
gi 2269171783 218 DRVV 221
Cdd:COG1124 207 DRVA 210
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
16-224 |
9.23e-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: 65.51 E-value: 9.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 16 DIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMrKGLTIGYLAQDQGLDSQNTiweemssVFAELHAIEKRMHal 95
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQYIKADYEGT-------VRDLLSSITKDFY-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 96 enqlsdpaimnddqayqqtlkTYDQVQTEfqqkngygyqaeirgVLHGFQFDaDVYDKSVTELSGGQKTQLALAKLLLEK 175
Cdd:cd03237 91 ---------------------THPYFKTE---------------IAKPLQIE-QILDREVPELSGGELQRVAIAACLSKD 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2269171783 176 RDLLILDEPTNHLDVETLTWLESYLQSYA----GALLIVSHDRYFLDRVVNEV 224
Cdd:cd03237 134 ADIYLLDEPSAYLDVEQRLMASKVIRRFAenneKTAFVVEHDIIMIDYLADRL 186
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-221 |
1.28e-11 |
|
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: 63.75 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 2 RRFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMRkgltigylaqDQGLDSQNtiweemssv 81
Cdd:cd03229 8 KRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILID----------GEDLTDLE--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 82 faelhaiekrmhalenqlsdpaimnddqayQQTLKTYDQVQTEFQQKNGYgyqaeirgvlhgfqFDADVYDKSVTELSGG 161
Cdd:cd03229 69 ------------------------------DELPPLRRRIGMVFQDFALF--------------PHLTVLENIALGLSGG 104
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2269171783 162 QKTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYAG----ALLIVSHD----RYFLDRVV 221
Cdd:cd03229 105 QQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAqlgiTVVLVTHDldeaARLADRVV 172
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
341-494 |
1.58e-11 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 64.29 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLkSIL--------GQIpFIKGQAVFGtgvvtgyYDQEQR---------------NLN 397
Cdd:COG1136 28 SLSIEAGEFVAIVGPSGSGKSTLL-NILggldrptsGEV-LIDGQDISS-------LSERELarlrrrhigfvfqffNLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 398 DKKTVL------SELWDEHPTTPEKDIRTILESF-LftGADVDKPVHALSGGER-----ARllltklAMQNDNFLIL-DE 464
Cdd:COG1136 99 PELTALenvalpLLLAGVSRKERRERARELLERVgL--GDRLDHRPSQLSGGQQqrvaiAR------ALVNRPKLILaDE 170
|
170 180 190
....*....|....*....|....*....|....
gi 2269171783 465 PTNHLDID-SREVLEV--ALNDFDG-TLLFVSHD 494
Cdd:COG1136 171 PTGNLDSKtGEEVLELlrELNRELGtTIVMVTHD 204
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
5-212 |
1.80e-11 |
|
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: 63.53 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 5 GADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMrkgltigylaQDQGLDSQNTIWEEMSSVFAE 84
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRW----------NGTPLAEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 85 LHAIEKRMHALEN-----QLSDPAIMNDDQAyqqtLKTYDqvqtefqqkngygyqaeirgvLHGFQfdadvyDKSVTELS 159
Cdd:TIGR01189 81 LPGLKPELSALENlhfwaAIHGGAQRTIEDA----LAAVG---------------------LTGFE------DLPAAQLS 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2269171783 160 GGQKTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYA---GALLIVSH 212
Cdd:TIGR01189 130 AGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLargGIVLLTTH 185
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
321-478 |
1.84e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 63.74 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 321 VLTVKDAAVGYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGYYDQEQ------R 394
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAchylghR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 395 N-LNDKKTVLS--ELWDEHPTTPEKDIRTILESF-LftgADV-DKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHL 469
Cdd:PRK13539 82 NaMKPALTVAEnlEFWAAFLGGEELDIAAALEAVgL---APLaHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
....*....
gi 2269171783 470 DIDSREVLE 478
Cdd:PRK13539 159 DAAAVALFA 167
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-218 |
2.94e-11 |
|
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: 66.35 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 23 VALVGRNGAGKSTLLKMIAGETVPDEGqiSMRKGLTIGYLAQDQGLDSQNTIWEEMSSVFAelhaiekrmhalenqlsdp 102
Cdd:COG1245 369 LGIVGPNGIGKTTFAKILAGVLKPDEG--EVDEDLKISYKPQYISPDYDGTVEEFLRSANT------------------- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 103 aimnddqayqqtlktyDQVQTEFqqkngygYQAEIrgvLHGFQFDaDVYDKSVTELSGGQKTQLALAKLLLEKRDLLILD 182
Cdd:COG1245 428 ----------------DDFGSSY-------YKTEI---IKPLGLE-KLLDKNVKDLSGGELQRVAIAACLSRDADLYLLD 480
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2269171783 183 EPTNHLDVETLTWLESYLQSYA----GALLIVSHDRYFLD 218
Cdd:COG1245 481 EPSAHLDVEQRLAVAKAIRRFAenrgKTAMVVDHDIYLID 520
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
342-493 |
3.14e-11 |
|
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: 63.07 E-value: 3.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 342 LNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVF-GTGVVTGYYDQ-----EQRNLNDKKTV------LSELWDE 409
Cdd:cd03269 21 FSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFdGKPLDIAARNRigylpEERGLYPKMKVidqlvyLAQLKGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 410 HPTTPEKDIRTILESFLFTGADvDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLEVALNDFDG--- 486
Cdd:cd03269 101 KKEEARRRIDEWLERLELSEYA-NKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARagk 179
|
....*..
gi 2269171783 487 TLLFVSH 493
Cdd:cd03269 180 TVILSTH 186
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
322-500 |
3.14e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 64.26 E-value: 3.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 322 LTVKDAAVGY-DGHILSEPdNLNVKKHEAIAIVGPNGIGKSTFLKSILGQ-IPFikgqavfgTGVVTgYYDQEQRNLNDK 399
Cdd:PRK11231 3 LRTENLTVGYgTKRILNDL-SLSLPTGKITALIGPNGCGKSTLLKCFARLlTPQ--------SGTVF-LGDKPISMLSSR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 400 KtvLSE---LWDEHPTTPE------------------------KDIRTILESFLFTGAD--VDKPVHALSGGERARLLLT 450
Cdd:PRK11231 73 Q--LARrlaLLPQHHLTPEgitvrelvaygrspwlslwgrlsaEDNARVNQAMEQTRINhlADRRLTDLSGGQRQRAFLA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2269171783 451 KLAMQNDNFLILDEPTNHLDIdSREV----LEVALNDFDGTLLFVSHDryfINQ 500
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDI-NHQVelmrLMRELNTQGKTVVTVLHD---LNQ 200
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
11-222 |
3.16e-11 |
|
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: 63.28 E-value: 3.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMrKGLTIGYLAqDQGLDS-QNtiwEEMSSVFAELHAIE 89
Cdd:cd03255 21 KGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRV-DGTDISKLS-EKELAAfRR---RHIGFVFQSFNLLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 90 kRMHALENqLSDPAImnddqayqqtlktydqvqteFQQKNGYGYQAEIRGVLHGFQFdADVYDKSVTELSGGQKtQlala 169
Cdd:cd03255 96 -DLTALEN-VELPLL--------------------LAGVPKKERRERAEELLERVGL-GDRLNHYPSELSGGQQ-Q---- 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2269171783 170 klllekR-----------DLLILDEPTNHLDVET----LTWLESYLQSYAGALLIVSHDRYFL---DRVVN 222
Cdd:cd03255 148 ------RvaiaralandpKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDPELAeyaDRIIE 212
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
322-502 |
3.66e-11 |
|
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: 63.35 E-value: 3.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 322 LTVKDAAVGYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVfgTGVVtgyyDQEQRNLNDKKT 401
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPD--EGEV----LLDGKDIYDLDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 402 VLSELWDE------HPT-------------------TPEKDIRTILESFLFTGA---DVDKPVHA--LSGGERARLLLTK 451
Cdd:cd03260 75 DVLELRRRvgmvfqKPNpfpgsiydnvayglrlhgiKLKEELDERVEEALRKAAlwdEVKDRLHAlgLSGGQQQRLCLAR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2269171783 452 -LAMQNDnFLILDEPTNHLDIDSREVLE---VALNDfDGTLLFVSHDryfINQVA 502
Cdd:cd03260 155 aLANEPE-VLLLDEPTSALDPISTAKIEeliAELKK-EYTIVIVTHN---MQQAA 204
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-214 |
4.41e-11 |
|
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: 62.92 E-value: 4.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 2 RRFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISM----------RKGlTIGYLAQDQGLDSQ 71
Cdd:cd03259 8 KTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdgrdvtgvppERR-NIGMVFQDYALFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 72 NTIWEEMSSvfaelhaiekrmhALENQLsdpaiMNDDQAYQQTLKTYDQVqtefqqkngygyqaEIRGVLHgfqfdadvy 151
Cdd:cd03259 87 LTVAENIAF-------------GLKLRG-----VPKAEIRARVRELLELV--------------GLEGLLN--------- 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2269171783 152 dKSVTELSGGQKTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYAGAL----LIVSHDR 214
Cdd:cd03259 126 -RYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELgittIYVTHDQ 191
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
3-213 |
5.39e-11 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 62.25 E-value: 5.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 3 RFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMRKGLTIGYLAQDQGLDSQ--NTIWEEMS- 79
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSlpLTVRDLVAm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 80 SVFAELHAIeKRMHALENQLSDPAIMnddqayqqtlktydqvqtefqqkngygyqaeiRGVLHGFQfdadvyDKSVTELS 159
Cdd:NF040873 81 GRWARRGLW-RRLTRDDRAAVDDALE--------------------------------RVGLADLA------GRQLGELS 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2269171783 160 GGQKTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYAG---ALLIVSHD 213
Cdd:NF040873 122 GGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHD 178
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
341-506 |
5.72e-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: 62.84 E-value: 5.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGYYDQE----------QR-NLNDKKTVL------ 403
Cdd:cd03219 20 SFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEiarlgigrtfQIpRLFPELTVLenvmva 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 404 ------SELWDEHPTTPEKDIR----TILEsFLFTGADVDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDS 473
Cdd:cd03219 100 aqartgSGLLLARARREEREAReraeELLE-RVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEE 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 2269171783 474 REVLE---VALNDFDGTLLFVSHDRYFINQVATSVV 506
Cdd:cd03219 179 TEELAeliRELRERGITVLLVEHDMDVVMSLADRVT 214
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-506 |
6.99e-11 |
|
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: 65.19 E-value: 6.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 23 VALVGRNGAGKSTLLKMIAGETVPDEGQISMRkgltigyLAQDQGLDS-QNTiweEMSSVFAELHAIEKRMhALENQLSD 101
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGDYDEE-------PSWDEVLKRfRGT---ELQDYFKKLANGEIKV-AHKPQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 102 PAIMNDDQAYQQTLKTYDQvqtefqqkngygyqaeiRGVLHGF--QFDAD-VYDKSVTELSGGQKTQLALAKLLLEKRDL 178
Cdd:COG1245 171 LIPKVFKGTVRELLEKVDE-----------------RGKLDELaeKLGLEnILDRDISELSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 179 LILDEPTNHLDV-ETLTwLESYLQSYAG---ALLIVSHDRYFLDrvvnevYdLShhEMVHYT----GNYDQFVQEKAAR- 249
Cdd:COG1245 234 YFFDEPSSYLDIyQRLN-VARLIRELAEegkYVLVVEHDLAILD------Y-LA--DYVHILygepGVYGVVSKPKSVRv 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 250 -IQaqwkHYekqqaeiskLEDFV-NRNIvrasttkraqarrkqlakmdRIdRPDSDEktahFGFHAAK--QSGNIVLTVK 325
Cdd:COG1245 304 gIN----QY---------LDGYLpEENV--------------------RI-RDEPIE----FEVHAPRreKEEETLVEYP 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 326 DAAVGYDGHILS-EPDnlNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGqaVFGTGVVTGYYDQEQRNLNDkKTVLS 404
Cdd:COG1245 346 DLTKSYGGFSLEvEGG--EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEG--EVDEDLKISYKPQYISPDYD-GTVEE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 405 ELwdehpttpEKDIRTILESFLFTgADV----------DKPVHALSGGERARLLLTK-LAMQNDNFLiLDEPTNHLDIDS 473
Cdd:COG1245 421 FL--------RSANTDDFGSSYYK-TEIikplglekllDKNVKDLSGGELQRVAIAAcLSRDADLYL-LDEPSAHLDVEQ 490
|
490 500 510
....*....|....*....|....*....|....*....
gi 2269171783 474 RevLEVA------LNDFDGTLLFVSHDRYFINQVATSVV 506
Cdd:COG1245 491 R--LAVAkairrfAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
413-523 |
7.11e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 65.27 E-value: 7.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 413 TPEKDIRTILESFLFTGADVDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLEVALNDFDGTLLFVS 492
Cdd:PLN03073 319 TAEARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVS 398
|
90 100 110
....*....|....*....|....*....|.
gi 2269171783 493 HDRYFINQVATSVVEVSPEGTELFLGDYDYY 523
Cdd:PLN03073 399 HAREFLNTVVTDILHLHGQKLVTYKGDYDTF 429
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
341-494 |
7.95e-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: 62.80 E-value: 7.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIP------FIKGQAVFGTGVVTGYYDQEQRNLnDKKTVLS--ELWDEHPT 412
Cdd:COG1116 31 SLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKptsgevLVDGKPVTGPGPDRGVVFQEPALL-PWLTVLDnvALGLELRG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 413 TPEKDIRTILESFLftgADV------DKPVHALSGGER-----ARLlltkLAMQNDnFLILDEPTNHLDIDSREVLEVAL 481
Cdd:COG1116 110 VPKAERRERARELL---ELVglagfeDAYPHQLSGGMRqrvaiARA----LANDPE-VLLMDEPFGALDALTRERLQDEL 181
|
170
....*....|....*..
gi 2269171783 482 ----NDFDGTLLFVSHD 494
Cdd:COG1116 182 lrlwQETGKTVLFVTHD 198
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
301-493 |
1.02e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 64.48 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 301 DSDEKTAHFGFHAAKQSGNIVLTVKDAAV-GYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGqipFIKGQav 379
Cdd:PRK11174 329 ETPLAHPQQGEKELASNDPVTIEAEDLEIlSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG---FLPYQ-- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 380 fGTGVVTGyydQEQRNLNDKK-----------------TVLSELWDEHPTTPEKDIRTILE-----SFLFTGAD-VDKPV 436
Cdd:PRK11174 404 -GSLKING---IELRELDPESwrkhlswvgqnpqlphgTLRDNVLLGNPDASDEQLQQALEnawvsEFLPLLPQgLDTPI 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2269171783 437 H----ALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLEVALND--FDGTLLFVSH 493
Cdd:PRK11174 480 GdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAasRRQTTLMVTH 542
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-193 |
1.08e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 63.20 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 2 RRFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISM-------RKGLTIGYLAQDQGLDSQNTI 74
Cdd:COG4152 9 KRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWdgepldpEDRRRIGYLPEERGLYPKMKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 75 WEEMsSVFAELH-----AIEKRMHALenqlsdpaimnddqayqqtLKtydqvqtefqqkngygyqaeirgvlhgfQFD-A 148
Cdd:COG4152 89 GEQL-VYLARLKglskaEAKRRADEW-------------------LE----------------------------RLGlG 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2269171783 149 DVYDKSVTELSGG--QKTQlalaklllekrDLLILDEPTNHLD---VETL 193
Cdd:COG4152 121 DRANKKVEELSKGnqQKVQliaal--lhdpELLILDEPFSGLDpvnVELL 168
|
|
| ABC_tran_CTD |
pfam16326 |
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. ... |
573-645 |
1.23e-10 |
|
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. It has a coiled coil structure with an atypical 3(10)-helix in the alpha-hairpin region. It is involved in DNA_binding.
Pssm-ID: 465095 [Multi-domain] Cd Length: 69 Bit Score: 57.48 E-value: 1.23e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2269171783 573 KQQQREKRKLErtvaALEEQMTTLDEQATKIQTEMAQPEVSADVGRLTDLQKELDEISAQQEQVETEWTEQAE 645
Cdd:pfam16326 1 KLSYKEQRELE----ELEAEIEKLEEEIAELEAQLADPELYSDYEKLQELSAELEELEAELEELYERWEELEE 69
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
5-65 |
1.26e-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: 62.41 E-value: 1.26e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2269171783 5 GADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISM------RKGLTIGYLAQD 65
Cdd:COG1116 22 GGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdgkpvtGPGPDRGVVFQE 88
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
341-506 |
1.34e-10 |
|
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: 61.39 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSI-------LGQIpFIKGQAVFGTGVVTGYYDQE------QRNLNDKKTVLSELw 407
Cdd:cd03262 20 DLTVKKGEVVVIIGPSGSGKSTLLRCInlleepdSGTI-IIDGLKLTDDKKNINELRQKvgmvfqQFNLFPHLTVLENI- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 408 DEHPTT----PEKDIRTILESFLftgADV------DKPVHALSGGERARLLLTK-LAMQNDnFLILDEPTNHLDID-SRE 475
Cdd:cd03262 98 TLAPIKvkgmSKAEAEERALELL---EKVgladkaDAYPAQLSGGQQQRVAIARaLAMNPK-VMLFDEPTSALDPElVGE 173
|
170 180 190
....*....|....*....|....*....|....
gi 2269171783 476 VLEVaLNDF--DG-TLLFVSHDRYFINQVATSVV 506
Cdd:cd03262 174 VLDV-MKDLaeEGmTMVVVTHEMGFAREVADRVI 206
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-221 |
1.63e-10 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 62.10 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 3 RFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMrkgltigylaQDQGLDSqntiW--EEMSS 80
Cdd:PRK13548 11 RLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRL----------NGRPLAD----WspAELAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 81 VFAEL--HA-------IEK--RM----HALENQLSDPAImndDQAYQQTlktydqvqtefqqkngygyqaeirGVLHgfq 145
Cdd:PRK13548 77 RRAVLpqHSslsfpftVEEvvAMgrapHGLSRAEDDALV---AAALAQV------------------------DLAH--- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 146 fdadVYDKSVTELSGGQK---------TQlalAKLLLEKRDLLILDEPTNHLDV----ETLTWLESYLQSYAGALLIVSH 212
Cdd:PRK13548 127 ----LAGRDYPQLSGGEQqrvqlarvlAQ---LWEPDGPPRWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLH 199
|
250
....*....|....
gi 2269171783 213 D-----RYfLDRVV 221
Cdd:PRK13548 200 DlnlaaRY-ADRIV 212
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
341-499 |
1.75e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.13 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFgtgvvtgyyDQEQRNLNDKKTVLSELWDEHPTTPEKDIRT 420
Cdd:COG2401 50 NLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV---------DVPDNQFGREASLIDAIGRKGDFKDAVELLN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 421 IL---ESFLFTgadvdKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLD-----IDSREVLEVAlNDFDGTLLFVS 492
Cdd:COG2401 121 AVglsDAVLWL-----RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtakRVARNLQKLA-RRAGITLVVAT 194
|
....*..
gi 2269171783 493 HDRYFIN 499
Cdd:COG2401 195 HHYDVID 201
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
11-222 |
1.80e-10 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 61.21 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISM---------RKGLT------IGYLAQDQGLDSQNTIW 75
Cdd:COG1136 25 RGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIdgqdisslsERELArlrrrhIGFVFQFFNLLPELTAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 76 E--EMSSVFAELHAIEKRMHALEnqlsdpAImnddqayqqtlktyDQVqtefqqkngygyqaeirGVlhgfqfdADVYDK 153
Cdd:COG1136 105 EnvALPLLLAGVSRKERRERARE------LL--------------ERV-----------------GL-------GDRLDH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 154 SVTELSGGQKtQlalaklllekR-----------DLLILDEPTNHLDVET----LTWLESYLQSYAGALLIVSHDR---Y 215
Cdd:COG1136 141 RPSQLSGGQQ-Q----------RvaiaralvnrpKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDPelaA 209
|
....*..
gi 2269171783 216 FLDRVVN 222
Cdd:COG1136 210 RADRVIR 216
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
332-512 |
2.15e-10 |
|
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: 59.86 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 332 DGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGYYDQeqrnlndkktvlselwdeHP 411
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQ------------------RP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 412 TTPEKDIRTILesfLFTGADVdkpvhaLSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLEVALNDFDGTLLFV 491
Cdd:cd03223 74 YLPLGTLREQL---IYPWDDV------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISV 144
|
170 180
....*....|....*....|.
gi 2269171783 492 SHdRYFINQVATSVVEVSPEG 512
Cdd:cd03223 145 GH-RPSLWKFHDRVLDLDGEG 164
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
341-494 |
2.34e-10 |
|
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: 60.77 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVK---KHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGtGVVtgYYDQEQR-NLNDKKTVLSELWDEHPTTPEK 416
Cdd:cd03297 14 TLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLN-GTV--LFDSRKKiNLPPQQRKIGLVFQQYALFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 417 DIRTILESFLFTGAD-------------------VDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVL 477
Cdd:cd03297 91 NVRENLAFGLKRKRNredrisvdelldllgldhlLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180
....*....|....*....|.
gi 2269171783 478 EVALN----DFDGTLLFVSHD 494
Cdd:cd03297 171 LPELKqikkNLNIPVIFVTHD 191
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
341-494 |
2.36e-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: 61.43 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGYYDQEQRNLNDK-----------------KTVL 403
Cdd:cd03256 21 SLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQigmifqqfnlierlsvlENVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 404 SELWDEHPTtpekdIRTILEsfLFTGADVDKPVHAL----------------SGGERARLLLTKLAMQNDNFLILDEPTN 467
Cdd:cd03256 101 SGRLGRRST-----WRSLFG--LFPKEEKQRALAALervglldkayqradqlSGGQQQRVAIARALMQQPKLILADEPVA 173
|
170 180 190
....*....|....*....|....*....|.
gi 2269171783 468 HLD-IDSREVLEV--ALNDFDG-TLLFVSHD 494
Cdd:cd03256 174 SLDpASSRQVMDLlkRINREEGiTVIVSLHQ 204
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
341-527 |
2.38e-10 |
|
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: 61.12 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSIL---------GQIPFiKGQAVF--------GTGVVTGYYDQEQ----RNLNDK 399
Cdd:TIGR01978 20 NLTVKKGEIHAIMGPNGSGKSTLSKTIAghpsyevtsGTILF-KGQDLLelepderaRAGLFLAFQYPEEipgvSNLEFL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 400 KTVLSELWDEHPTTP------EKDIRTILESFLFTGADVDKPVH-ALSGGERARLLLTKLAMQNDNFLILDEPTNHLDID 472
Cdd:TIGR01978 99 RSALNARRSARGEEPldlldfEKLLKEKLALLDMDEEFLNRSVNeGFSGGEKKRNEILQMALLEPKLAILDEIDSGLDID 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2269171783 473 S-REVLEVaLNDF---DGTLLFVSHDRYFINQVATSVVEVSPEGTELFLGDYDYY--IDKK 527
Cdd:TIGR01978 179 AlKIVAEG-INRLrepDRSFLIITHYQRLLNYIKPDYVHVLLDGRIVKSGDVELAkeLEAK 238
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
342-494 |
2.54e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 61.28 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 342 LNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGYYDQEqrnLNDKKTV---LSELWDEHPTTPEKDI 418
Cdd:PRK09544 25 LELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQK---LYLDTTLpltVNRFLRLRPGTKKEDI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 419 RTILESfLFTGADVDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSrevlEVALND--------FDGTLLF 490
Cdd:PRK09544 102 LPALKR-VQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG----QVALYDlidqlrreLDCAVLM 176
|
....
gi 2269171783 491 VSHD 494
Cdd:PRK09544 177 VSHD 180
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
11-221 |
2.72e-10 |
|
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: 61.36 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMRkGLTIGYLAQDQGLDSQNTIweemSSVFAELHAiek 90
Cdd:TIGR02769 28 TNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFR-GQDLYQLDRKQRRAFRRDV----QLVFQDSPS--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 91 rmhALENQLSDPAIMNDDQAYQQTLKTYDQvqtefqqkngygyQAEIRGVLHGFQFDADVYDKSVTELSGGQKTQLALAK 170
Cdd:TIGR02769 100 ---AVNPRMTVRQIIGEPLRHLTSLDESEQ-------------KARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2269171783 171 LLLEKRDLLILDEPTNHLDV----ETLTWLESYLQSYAGALLIVSHD----RYFLDRVV 221
Cdd:TIGR02769 164 ALAVKPKLIVLDEAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHDlrlvQSFCQRVA 222
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
2-221 |
3.16e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 61.24 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 2 RRFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMRkGLTIGYLAQDQGLDSQNTIweEMssV 81
Cdd:PRK10419 20 GKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWR-GEPLAKLNRAQRKAFRRDI--QM--V 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 82 FAE-LHAIEKRmHALENQLSDPA--IMNDDQAYQQtlktydqvqtefqqkngygyqAEIRGVLHGFQFDADVYDKSVTEL 158
Cdd:PRK10419 95 FQDsISAVNPR-KTVREIIREPLrhLLSLDKAERL---------------------ARASEMLRAVDLDDSVLDKRPPQL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2269171783 159 SGGQKTQLALAKLLLEKRDLLILDEPTNHLDV----ETLTWLESYLQSYAGALLIVSHD----RYFLDRVV 221
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDlrlvERFCQRVM 223
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-213 |
3.30e-10 |
|
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: 62.76 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 2 RRFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMrKGLTIGYLAQDqglDSQNTIweemsSV 81
Cdd:TIGR02868 343 GYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTL-DGVPVSSLDQD---EVRRRV-----SV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 82 FAElhaiekRMHALENQLSDP-AIMNDDQAYQQTLKTYDQVQTEfqqkngygyqAEIRGVLHGfqfdadvYDKSVTE--- 157
Cdd:TIGR02868 414 CAQ------DAHLFDTTVRENlRLARPDATDEELWAALERVGLA----------DWLRALPDG-------LDTVLGEgga 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2269171783 158 -LSGGQKTQLALAKLLLEKRDLLILDEPTNHLDVET-LTWLESYLQSYAG-ALLIVSHD 213
Cdd:TIGR02868 471 rLSGGERQRLALARALLADAPILLLDEPTEHLDAETaDELLEDLLAALSGrTVVLITHH 529
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
340-494 |
3.36e-10 |
|
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: 60.81 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 340 DNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGYYDQEQR------------NLNDKKTVLSELw 407
Cdd:cd03299 18 VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDisyvpqnyalfpHMTVYKNIAYGL- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 408 dEHPTTPEKDI-RTILESFLFTGAD--VDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLEVALND- 483
Cdd:cd03299 97 -KKRKVDKKEIeRKVLEIAEMLGIDhlLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKi 175
|
170
....*....|....
gi 2269171783 484 ---FDGTLLFVSHD 494
Cdd:cd03299 176 rkeFGVTVLHVTHD 189
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
341-465 |
3.65e-10 |
|
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: 60.63 E-value: 3.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVT------------GYYDQEQ---RNLNDKKTVLSE 405
Cdd:cd03218 20 SLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITklpmhkrarlgiGYLPQEAsifRKLTVEENILAV 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2269171783 406 LwdEHPTTPEKDIRTILESFL--FTGADV-DKPVHALSGGERARLLLTKLAMQNDNFLILDEP 465
Cdd:cd03218 100 L--EIRGLSKKEREEKLEELLeeFHITHLrKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-230 |
3.93e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.90 E-value: 3.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 4 FGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMRKGLTIGYLAQDQGLDsqntiweemssvfA 83
Cdd:PRK09544 14 FGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLD-------------T 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 84 ELHAIEKRMHALEnqlsdPAIMNDDqayqqTLKTYDQVQTefqqkngygyqaeirgvlhgfqfdADVYDKSVTELSGGQK 163
Cdd:PRK09544 81 TLPLTVNRFLRLR-----PGTKKED-----ILPALKRVQA------------------------GHLIDAPMQKLSGGET 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2269171783 164 TQLALAKLLLEKRDLLILDEPTNHLDVE---TLTWLESYLQSYAG-ALLIVSHDRYFLDRVVNEVYDLSHH 230
Cdd:PRK09544 127 QRVLLARALLNRPQLLVLDEPTQGVDVNgqvALYDLIDQLRRELDcAVLMVSHDLHLVMAKTDEVLCLNHH 197
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-212 |
4.18e-10 |
|
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: 60.48 E-value: 4.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 3 RFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQismrkglTIGYLAQDQGLDSqntIWE---EMS 79
Cdd:COG1119 12 RRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGN-------DVRLFGERRGGED---VWElrkRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 80 SVFAELHA-IEKRMHALENQLSdpaimnddqAYQQTLKTYDQVQTEFQQKngygyqaeIRGVLHGFQFdADVYDKSVTEL 158
Cdd:COG1119 82 LVSPALQLrFPRDETVLDVVLS---------GFFDSIGLYREPTDEQRER--------ARELLELLGL-AHLADRPFGTL 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 159 SGGQKtqlalaklllekR------------DLLILDEPTNHLDVET----LTWLESYLQSYAGALLIVSH 212
Cdd:COG1119 144 SQGEQ------------RrvliaralvkdpELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVTH 201
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-53 |
4.19e-10 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 60.90 E-value: 4.19e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2269171783 3 RFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISM 53
Cdd:COG4559 10 RLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRL 60
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
9-65 |
4.79e-10 |
|
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: 58.93 E-value: 4.79e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 9 LFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI-------------SMRKglTIGYLAQD 65
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEIlidgvdlrdldleSLRK--NIAYVPQD 84
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-54 |
6.74e-10 |
|
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: 60.05 E-value: 6.74e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2269171783 2 RRFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMR 54
Cdd:COG0411 12 KRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFD 64
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
3-233 |
9.47e-10 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 59.83 E-value: 9.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 3 RFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMRKGltigylaqdqgldsqntiweemssvf 82
Cdd:TIGR03873 10 SAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGV-------------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 83 aELHAIEKRMHALENQLSDPAimNDDQAyqqTLKTYDQV---QTEFQQKNGYGYQAEIRGVLH--GFQFDADVYDKSVTE 157
Cdd:TIGR03873 64 -DLHGLSRRARARRVALVEQD--SDTAV---PLTVRDVValgRIPHRSLWAGDSPHDAAVVDRalARTELSHLADRDMST 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2269171783 158 LSGGQKTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYAG---ALLIVSHDRYFLDRVVNEVYDLSHHEMV 233
Cdd:TIGR03873 138 LSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAQLETLALVRELAAtgvTVVAALHDLNLAASYCDHVVVLDGGRVV 216
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
353-545 |
1.08e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.45 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 353 VGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGYYDQEQRNLNDKK---TVL---SELWD---------EHPTTPEKD 417
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFTvldTVImghTELWEvkqerdriyALPEMSEED 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 418 -IRTI-LES-F--------------LFTGADVDKPVH-----ALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSRE 475
Cdd:PRK15064 113 gMKVAdLEVkFaemdgytaearageLLLGVGIPEEQHyglmsEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIR 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 476 VLEVALNDFDGTLLFVSHDRYFINQVATSVVEVSPEGTELFLGDYDYYIdkkqeqaemaaAAASQAAESA 545
Cdd:PRK15064 193 WLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYM-----------TAATQARERL 251
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
341-508 |
1.14e-09 |
|
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: 58.57 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSIL-------GQIpFIKGQAVFG-TGVVTGYYDQE------------QRNLNDKK 400
Cdd:cd03292 21 NISISAGEFVFLVGPSGAGKSTLLKLIYkeelptsGTI-RVNGQDVSDlRGRAIPYLRRKigvvfqdfrllpDRNVYENV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 401 TVLSELWDEHPTTPEKDIRTILESFLFTGADVDKPVHaLSGGERARLLLTKLAMQNDNFLILDEPTNHLDID-SREVLEV 479
Cdd:cd03292 100 AFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAE-LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDtTWEIMNL 178
|
170 180 190
....*....|....*....|....*....|.
gi 2269171783 480 --ALNDFDGTLLFVSHDRYFINQVATSVVEV 508
Cdd:cd03292 179 lkKINKAGTTVVVATHAKELVDTTRHRVIAL 209
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-68 |
1.28e-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: 58.60 E-value: 1.28e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2269171783 5 GADVLFDnVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISM--------------RKGltIGYLAQDQGL 68
Cdd:cd03224 12 KSQILFG-VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdgrditglppheraRAG--IGYVPEGRRI 86
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
13-265 |
1.34e-09 |
|
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: 60.13 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 13 VQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISM--------RKGL-------TIGYLAQDQGLDSQntiwee 77
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLngrtlfdsRKGIflppekrRIGYVFQEARLFPH------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 78 mSSVFAELHAIEKRMHALENQLSDPAIMnddqayqqtlktydqvqtefqqkngygyqaEIRGVLHgfqfdadVYDKSVTE 157
Cdd:TIGR02142 90 -LSVRGNLRYGMKRARPSERRISFERVI------------------------------ELLGIGH-------LLGRLPGR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 158 LSGGQKTQLALAKLLLEKRDLLILDEPTNHLDV----ETLTWLESYLQSYAGALLIVSHDryfldrvVNEVYDLSHHEMV 233
Cdd:TIGR02142 132 LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDprkyEILPYLERLHAEFGIPILYVSHS-------LQEVLRLADRVVV 204
|
250 260 270
....*....|....*....|....*....|....
gi 2269171783 234 HYTGNYDQF--VQEKAARIQAQWKHYEKQQAEIS 265
Cdd:TIGR02142 205 LEDGRVAAAgpIAEVWASPDLPWLAREDQGSLIE 238
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
346-498 |
1.51e-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: 57.00 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 346 KHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGvvtgyydqeqrnlndkktvlselwdehpttpekDIRTILESF 425
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG---------------------------------EDILEEVLD 47
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2269171783 426 LFTGADVDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLEVALNDFDGTLLFVSHDRYFI 498
Cdd:smart00382 48 QLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVI 120
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
2-53 |
1.70e-09 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 60.09 E-value: 1.70e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2269171783 2 RRFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAG-ETvPDEGQISM 53
Cdd:COG3839 11 KSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGlED-PTSGEILI 62
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
177-493 |
1.89e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.41 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 177 DLLILDEPTNHLDVETLTWLESYLQSyagalliVSHDRYFLDRVVNEVYDLShhemvhytgnydQFVQEKAARIQAQWKH 256
Cdd:PRK10938 155 DLLILDEPFDGLDVASRQQLAELLAS-------LHQSGITLVLVLNRFDEIP------------DFVQFAGVLADCTLAE 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 257 yekqQAEISKLEdfvnrnivrasttkrAQARRKQLA---KMDRIDRPDSDEKTAHFgfHAAKQSGNIVLtvKDAAVGY-D 332
Cdd:PRK10938 216 ----TGEREEIL---------------QQALVAQLAhseQLEGVQLPEPDEPSARH--ALPANEPRIVL--NNGVVSYnD 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 333 GHILsepDNLN--VKKHEAIAIVGPNGIGKSTFLKSILGQIP--FIKGQAVFG---------------TGVVTGYYDQEQ 393
Cdd:PRK10938 273 RPIL---HNLSwqVNPGEHWQIVGPNGAGKSTLLSLITGDHPqgYSNDLTLFGrrrgsgetiwdikkhIGYVSSSLHLDY 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 394 R-NLNDKKTVLSELWDE---HPTTPEKDiRTILESFL----FTGADVDKPVHALSGGERaRLLLTKLAM-QNDNFLILDE 464
Cdd:PRK10938 350 RvSTSVRNVILSGFFDSigiYQAVSDRQ-QKLAQQWLdilgIDKRTADAPFHSLSWGQQ-RLALIVRALvKHPTLLILDE 427
|
330 340 350
....*....|....*....|....*....|...
gi 2269171783 465 PTNHLDIDSREV----LEVALNDFDGTLLFVSH 493
Cdd:PRK10938 428 PLQGLDPLNRQLvrrfVDVLISEGETQLLFVSH 460
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
341-518 |
1.96e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 59.09 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGtGVVTGYYDQEQRNLN----------DKKTVLSELWDE- 409
Cdd:PRK13636 26 NINIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFD-GKPIDYSRKGLMKLResvgmvfqdpDNQLFSASVYQDv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 410 -----HPTTPEKDIRTILESFLF-TGAD--VDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLD-IDSREVLEVA 480
Cdd:PRK13636 105 sfgavNLKLPEDEVRKRVDNALKrTGIEhlKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDpMGVSEIMKLL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2269171783 481 LN---DFDGTLLFVSHDryfINQVA--TSVVEVSPEGTELFLG 518
Cdd:PRK13636 185 VEmqkELGLTIIIATHD---IDIVPlyCDNVFVMKEGRVILQG 224
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
322-471 |
2.28e-09 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 58.31 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 322 LTVKDAAVGydgHILSePDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFiKGQAVFGtgvvtgyydqeQRNLND--- 398
Cdd:COG4138 1 LQLNDVAVA---GRLG-PISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLN-----------GRPLSDwsa 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 399 -----KKTVLSE---------------LWDEHPTTPEKDIRTILE--SFLFTGADVDKPVHALSGGERARLLLTKLAMQ- 455
Cdd:COG4138 65 aelarHRAYLSQqqsppfampvfqylaLHQPAGASSEAVEQLLAQlaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQv 144
|
170 180
....*....|....*....|..
gi 2269171783 456 --NDN----FLILDEPTNHLDI 471
Cdd:COG4138 145 wpTINpegqLLLLDEPMNSLDV 166
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-233 |
2.83e-09 |
|
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: 57.83 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 2 RRFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMRkGLTIGYLAQDQ------GLDSQNTiw 75
Cdd:cd03219 8 KRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFD-GEDITGLPPHEiarlgiGRTFQIP-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 76 eemsSVFAELHAIEKRMHALENQLSDPAIMNDDQAYQQTLktydqvqtefqqkngygyQAEIRGVLHgfQFD-ADVYDKS 154
Cdd:cd03219 85 ----RLFPELTVLENVMVAAQARTGSGLLLARARREEREA------------------RERAEELLE--RVGlADLADRP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 155 VTELSGGQKtqlalaklllekR------------DLLILDEPT---NHLDVETLTWLESYLQSYAGALLIVSHDryfLDR 219
Cdd:cd03219 141 AGELSYGQQ------------RrleiaralatdpKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHD---MDV 205
|
250
....*....|....
gi 2269171783 220 vvneVYDLSHHEMV 233
Cdd:cd03219 206 ----VMSLADRVTV 215
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
11-221 |
3.22e-09 |
|
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: 57.96 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMrkgltIGYLAQDQGLDSQNTIWEEMSSVFAELHAIEk 90
Cdd:cd03256 18 KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLI-----DGTDINKLKGKALRQLRRQIGMIFQQFNLIE- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 91 RMHALENQLSDPAimnddqAYQQTLKTYDQVQTEfqqkngygyqAEIRGVLH-----GFqfdADVYDKSVTELSGGQKTQ 165
Cdd:cd03256 92 RLSVLENVLSGRL------GRRSTWRSLFGLFPK----------EEKQRALAalervGL---LDKAYQRADQLSGGQQQR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2269171783 166 LALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYA---GALLIVS-HD----RYFLDRVV 221
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINreeGITVIVSlHQvdlaREYADRIV 216
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-201 |
3.24e-09 |
|
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: 57.38 E-value: 3.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 2 RRFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQ------------ISMRKglTIGYLAQDQGLD 69
Cdd:cd03265 8 KKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdvvrepREVRR--RIGIVFQDLSVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 70 SQNTIWEEMssvfaELHAiekRMHALENQlsdpaimnddqayqqtlktydqvqtEFQQKngygyqaeIRGVLHGFQFdAD 149
Cdd:cd03265 86 DELTGWENL-----YIHA---RLYGVPGA-------------------------ERRER--------IDELLDFVGL-LE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2269171783 150 VYDKSVTELSGGQKTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQ 201
Cdd:cd03265 124 AADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIE 175
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
301-527 |
3.39e-09 |
|
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: 60.14 E-value: 3.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 301 DSDEKTAHFGFHAAKQSGNIVLTVKDAAVGYDGHILSEPdNLNVKKHEAIAIVGPNGIGKSTFLKSILGqipFIkgQAVF 380
Cdd:TIGR01193 455 DSEFINKKKRTELNNLNGDIVINDVSYSYGYGSNILSDI-SLTIKMNSKTTIVGMSGSGKSTLAKLLVG---FF--QARS 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 381 GTGVVTGYydqeqrNLND-KKTVLSELWDEHPTTPEKDIRTILESFLF----------------------------TGAD 431
Cdd:TIGR01193 529 GEILLNGF------SLKDiDRHTLRQFINYLPQEPYIFSGSILENLLLgakenvsqdeiwaaceiaeikddienmpLGYQ 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 432 VDKPVHA--LSGGERARLLLTKLAMQNDNFLILDEPTNHLD-IDSREVLEVALNDFDGTLLFVSHdRYFINQVATSVVEV 508
Cdd:TIGR01193 603 TELSEEGssISGGQKQRIALARALLTDSKVLILDESTSNLDtITEKKIVNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVL 681
|
250
....*....|....*....
gi 2269171783 509 SpEGTELFLGDYDYYIDKK 527
Cdd:TIGR01193 682 D-HGKIIEQGSHDELLDRN 699
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
341-493 |
3.46e-09 |
|
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: 57.60 E-value: 3.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGtGV------------VTGYYDQEQR----NLNDKKTVLS 404
Cdd:cd03245 24 SLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLD-GTdirqldpadlrrNIGYVPQDVTlfygTLRDNITLGA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 405 elwdehpttPEKDIRTILESFLFTGADVDKPVHA-------------LSGGERARLLLTKLAMQNDNFLILDEPTNHLDI 471
Cdd:cd03245 103 ---------PLADDERILRAAELAGVTDFVNKHPngldlqigergrgLSGGQRQAVALARALLNDPPILLLDEPTSAMDM 173
|
170 180
....*....|....*....|....
gi 2269171783 472 DSREVLEVALNDF--DGTLLFVSH 493
Cdd:cd03245 174 NSEERLKERLRQLlgDKTLIIITH 197
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
322-465 |
3.76e-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: 57.09 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 322 LTVKDAAVGYDGHILSEP-----DNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVvtGYYDQEQRNL 396
Cdd:cd03250 1 ISVEDASFTWDSGEQETSftlkdINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSI--AYVSQEPWIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 397 NDkktvlselwdehpttpekdirTILESFLFtGADVDKP-----VHA------------------------LSGGERARL 447
Cdd:cd03250 79 NG---------------------TIRENILF-GKPFDEEryekvIKAcalepdleilpdgdlteigekginLSGGQKQRI 136
|
170
....*....|....*...
gi 2269171783 448 LLTKLAMQNDNFLILDEP 465
Cdd:cd03250 137 SLARAVYSDADIYLLDDP 154
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
341-508 |
5.10e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 57.38 E-value: 5.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSIL---------GQIpFIKGQAVFGTGVvtgyydqEQR----------------- 394
Cdd:COG0396 20 NLTIKPGEVHAIMGPNGSGKSTLAKVLMghpkyevtsGSI-LLDGEDILELSP-------DERaragiflafqypveipg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 395 --NLNDKKTVLSELWDEHPTTPE--KDIRTIL------ESFLftgadvDKPVHA-LSGGERARLLLTKLAMQNDNFLILD 463
Cdd:COG0396 92 vsVSNFLRTALNARRGEELSAREflKLLKEKMkelgldEDFL------DRYVNEgFSGGEKKRNEILQMLLLEPKLAILD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2269171783 464 EPTNHLDIDS-REVLEV--ALNDFDGTLLFVSHDRYFINQVATSVVEV 508
Cdd:COG0396 166 ETDSGLDIDAlRIVAEGvnKLRSPDRGILIITHYQRILDYIKPDFVHV 213
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-51 |
6.96e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.49 E-value: 6.96e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2269171783 3 RFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI 51
Cdd:COG1129 13 SFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEI 61
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
329-512 |
7.07e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 57.30 E-value: 7.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 329 VGYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGYYDQE---------QRNLNDK 399
Cdd:PRK10253 15 LGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvarrigllaQNATTPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 400 KTVLSEL--WDEHPTTP------EKDIRTILESFLFTGAD--VDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHL 469
Cdd:PRK10253 95 DITVQELvaRGRYPHQPlftrwrKEDEEAVTKAMQATGIThlADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2269171783 470 DIDSR-EVLEV--ALNDFDG-TLLFVSHD-----RYFINQVATSVVEVSPEG 512
Cdd:PRK10253 175 DISHQiDLLELlsELNREKGyTLAAVLHDlnqacRYASHLIALREGKIVAQG 226
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-233 |
7.21e-09 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 56.60 E-value: 7.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 5 GADVLfDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISM---------RKGL-----TIGYLAQDQGLDS 70
Cdd:COG2884 14 GREAL-SDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVngqdlsrlkRREIpylrrRIGVVFQDFRLLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 71 QNTIWEEMSsvFAeLHAIEKRMHALENQLsdPAIMnddqayqqtlktyDQVqtefqqkngygyqaeirGVLHgfqfdadV 150
Cdd:COG2884 93 DRTVYENVA--LP-LRVTGKSRKEIRRRV--REVL-------------DLV-----------------GLSD-------K 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 151 YDKSVTELSGGQKtQlalaklllekR-----------DLLILDEPTNHLDVETLTWLESYLQSY--AG-ALLIVSHDRYF 216
Cdd:COG2884 131 AKALPHELSGGEQ-Q----------RvaiaralvnrpELLLADEPTGNLDPETSWEIMELLEEInrRGtTVLIATHDLEL 199
|
250
....*....|....*..
gi 2269171783 217 LDRVVNEVYDLSHHEMV 233
Cdd:COG2884 200 VDRMPKRVLELEDGRLV 216
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
11-221 |
7.32e-09 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 57.46 E-value: 7.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMrKGLTIgylAQDQGLDSQNtIWEEMSSVFaelhaiek 90
Cdd:TIGR04521 22 DDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTI-DGRDI---TAKKKKKLKD-LRKKVGLVF-------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 91 rmHALENQLSDPAIMNDdqayqqtlktydqvqTEFQQKNgYGY-QAEI----RGVLHGFQFDADVYDKSVTELSGGQKtq 165
Cdd:TIGR04521 89 --QFPEHQLFEETVYKD---------------IAFGPKN-LGLsEEEAeervKEALELVGLDEEYLERSPFELSGGQM-- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2269171783 166 lalaklllekR------------DLLILDEPTNHLD----VETLTWLESYLQSYAGALLIVSHD-----RYfLDRVV 221
Cdd:TIGR04521 149 ----------RrvaiagvlamepEVLILDEPTAGLDpkgrKEILDLFKRLHKEKGLTVILVTHSmedvaEY-ADRVI 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-51 |
7.63e-09 |
|
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: 56.53 E-value: 7.63e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2269171783 3 RFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI 51
Cdd:COG1127 14 SFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEI 62
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-51 |
7.92e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 58.50 E-value: 7.92e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2269171783 3 RFGADVLFDNVQMDIQE---HArvaLVGRNGAGKSTLLKMIAGETVPDEGQI 51
Cdd:COG3845 14 RFGGVVANDDVSLTVRPgeiHA---LLGENGAGKSTLMKILYGLYQPDSGEI 62
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
10-68 |
8.17e-09 |
|
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: 56.33 E-value: 8.17e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2269171783 10 FDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISM------RKGLTIGYLAQDQGL 68
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepvtGPGPDRGYVFQQDAL 84
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
321-380 |
8.63e-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: 56.53 E-value: 8.63e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2269171783 321 VLTVKDAAVGYDG-HILSEPDnLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVF 380
Cdd:COG0410 3 MLEVENLHAGYGGiHVLHGVS-LEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRF 62
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
304-477 |
8.75e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 57.53 E-value: 8.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 304 EKTAHFGFHA-AKQSGNIVLTVKDAA---VGYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQ-- 377
Cdd:PRK13536 20 ERKHQGISEAkASIPGSMSTVAIDLAgvsKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKit 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 378 ------------AVFGTGVVTGY--YDQE---QRNLndkkTVLSELWDEHPTTPEKDIRTILEsFLFTGADVDKPVHALS 440
Cdd:PRK13536 100 vlgvpvpararlARARIGVVPQFdnLDLEftvRENL----LVFGRYFGMSTREIEAVIPSLLE-FARLESKADARVSDLS 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 2269171783 441 GGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVL 477
Cdd:PRK13536 175 GGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLI 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-232 |
9.51e-09 |
|
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: 55.88 E-value: 9.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 2 RRFGADVL-FDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI-------SMRKGLTIGYLAQDQGLDSQNt 73
Cdd:cd03292 8 KTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIrvngqdvSDLRGRAIPYLRRKIGVVFQD- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 74 iweemSSVFAELHAIEKRMHALENQLSDPAIMNddqayQQTLKTYDQVqtefqqkngyGYQAEIRGVlhgfqfdadvydk 153
Cdd:cd03292 87 -----FRLLPDRNVYENVAFALEVTGVPPREIR-----KRVPAALELV----------GLSHKHRAL------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 154 sVTELSGGQKTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSY--AGALLIVS-HDRYFLDRVVNEVYDLSHH 230
Cdd:cd03292 134 -PAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKInkAGTTVVVAtHAKELVDTTRHRVIALERG 212
|
..
gi 2269171783 231 EM 232
Cdd:cd03292 213 KL 214
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-51 |
1.04e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 56.63 E-value: 1.04e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2269171783 8 VLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI 51
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSI 63
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
341-506 |
1.04e-08 |
|
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: 56.00 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQ--------AVFGTGV-----VTGYydqeqRNLNDKKTVLSelw 407
Cdd:cd03220 42 SFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTvtvrgrvsSLLGLGGgfnpeLTGR-----ENIYLNGRLLG--- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 408 dehptTPEKDIRTILESFL-FT--GADVDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLEVALNDF 484
Cdd:cd03220 114 -----LSRKEIDEKIDEIIeFSelGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLREL 188
|
170 180
....*....|....*....|....*
gi 2269171783 485 ---DGTLLFVSHDRYFINQVATSVV 506
Cdd:cd03220 189 lkqGKTVILVSHDPSSIKRLCDRAL 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-221 |
1.05e-08 |
|
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: 56.00 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 3 RFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMrKGLTIgylaqDQGLDSQNTIWEEMSSVF 82
Cdd:cd03262 9 SFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIII-DGLKL-----TDDKKNINELRQKVGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 83 AELHAIEkRMHALENQLSDPAI---MNDDQAYQQTLKTYDQVqtefqqkngygyqaeirGVLHgfqfDADVYDKsvtELS 159
Cdd:cd03262 83 QQFNLFP-HLTVLENITLAPIKvkgMSKAEAEERALELLEKV-----------------GLAD----KADAYPA---QLS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2269171783 160 GGQKTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYAG---ALLIVSHDRYFL----DRVV 221
Cdd:cd03262 138 GGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEegmTMVVVTHEMGFArevaDRVI 206
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
320-471 |
1.12e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 56.32 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 320 IVLTVKDAAVGYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQ-AVFGtgvvtgyydqeqRNLND 398
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEvRLNG------------RPLAD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 399 KKT--------VLSE--------LWDE--------HPTTPEKDIRTILESFLFTGAD--VDKPVHALSGGERARL----L 448
Cdd:PRK13548 69 WSPaelarrraVLPQhsslsfpfTVEEvvamgrapHGLSRAEDDALVAAALAQVDLAhlAGRDYPQLSGGEQQRVqlarV 148
|
170 180
....*....|....*....|....*
gi 2269171783 449 LTKLAMQNDN--FLILDEPTNHLDI 471
Cdd:PRK13548 149 LAQLWEPDGPprWLLLDEPTSALDL 173
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
12-213 |
1.32e-08 |
|
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: 55.76 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 12 NVQMDIQEHaRVALVGRNGAGKSTLLKMIAGETVPDEGQISM--------RKGLT-------IGYLAQDQGLDSQNTIWE 76
Cdd:cd03297 16 KIDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLngtvlfdsRKKINlppqqrkIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 77 EMSSVFAELHAIEKRMhaLENQLSDpaIMNDDQayqqtlktydqvqtefqqkngygyqaeirgvlhgfqfdadVYDKSVT 156
Cdd:cd03297 95 NLAFGLKRKRNREDRI--SVDELLD--LLGLDH----------------------------------------LLNRYPA 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2269171783 157 ELSGGQKTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYL----QSYAGALLIVSHD 213
Cdd:cd03297 131 QLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELkqikKNLNIPVIFVTHD 191
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-51 |
1.45e-08 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 57.03 E-value: 1.45e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2269171783 2 RRFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI 51
Cdd:COG3842 13 KRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRI 62
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-51 |
1.75e-08 |
|
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: 55.34 E-value: 1.75e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2269171783 2 RRFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI 51
Cdd:cd03301 8 KRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRI 57
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
5-54 |
1.83e-08 |
|
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: 55.37 E-value: 1.83e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2269171783 5 GADVLFDnVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMR 54
Cdd:COG0410 15 GIHVLHG-VSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFD 63
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
321-494 |
2.03e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 55.67 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 321 VLTVKDAAVGYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVT------------GY 388
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplhararrgiGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 389 YDQEQ---RNLNDKKTVLSELWDEHPTTPEKD---IRTILESFLFTGADvDKPVHALSGGERARLLLTKLAMQNDNFLIL 462
Cdd:PRK10895 83 LPQEAsifRRLSVYDNLMAVLQIRDDLSAEQRedrANELMEEFHIEHLR-DSMGQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 2269171783 463 DEPTNHLD----IDSREVLEvALNDFDGTLLFVSHD 494
Cdd:PRK10895 162 DEPFAGVDpisvIDIKRIIE-HLRDSGLGVLITDHN 196
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
5-212 |
2.08e-08 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 57.10 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 5 GADVLfDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQIsmrkglTIGylaqdqGLD----SQNTIWEEMSS 80
Cdd:COG1132 352 DRPVL-KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRI------LID------GVDirdlTLESLRRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 81 VFAELHaiekRMHA--LEN-QLSDPAImnDDQAYQQTLKtydQVQ-TEFQQKNGYGYQAEI--RGVlhgfqfdadvydks 154
Cdd:COG1132 419 VPQDTF----LFSGtiRENiRYGRPDA--TDEEVEEAAK---AAQaHEFIEALPDGYDTVVgeRGV-------------- 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2269171783 155 vtELSGGQKtQlalaklllekR-----------DLLILDEPTNHLDVETltwlESYLQSYAGAL------LIVSH 212
Cdd:COG1132 476 --NLSGGQR-Q----------RiaiarallkdpPILILDEATSALDTET----EALIQEALERLmkgrttIVIAH 533
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-225 |
2.18e-08 |
|
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: 55.20 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 3 RFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISmrkgltigylaqdqgLDSQNtiWEEMSSvf 82
Cdd:cd03261 9 SFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVL---------------IDGED--ISGLSE-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 83 AELHAIEKRMHALenqLSDPAIMNDdqayqqtLKTYDQVQ------TEFQQKngygyqaEIRGV---------LHGFQfd 147
Cdd:cd03261 70 AELYRLRRRMGML---FQSGALFDS-------LTVFENVAfplrehTRLSEE-------EIREIvlekleavgLRGAE-- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 148 advyDKSVTELSGGQKTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYAGAL----LIVSHDRYFLDRVVNE 223
Cdd:cd03261 131 ----DLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELgltsIMVTHDLDTAFAIADR 206
|
..
gi 2269171783 224 VY 225
Cdd:cd03261 207 IA 208
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
322-494 |
2.32e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 55.32 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 322 LTVKDAAVGydgHILSePDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFiKGQAVF-GTGVVT----------GYYD 390
Cdd:PRK03695 1 MQLNDVAVS---TRLG-PLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFaGQPLEAwsaaelarhrAYLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 391 QEQRNLndkktVLSELWD-----EHPTTPEKDIRTILE---SFLFTGADVDKPVHALSGGERARLLLTKLAMQ------- 455
Cdd:PRK03695 76 QQQTPP-----FAMPVFQyltlhQPDKTRTEAVASALNevaEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinp 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2269171783 456 NDNFLILDEPTNHLDIDSREVLEVALNDF---DGTLLFVSHD 494
Cdd:PRK03695 151 AGQLLLLDEPMNSLDVAQQAALDRLLSELcqqGIAVVMSSHD 192
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
11-226 |
2.35e-08 |
|
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: 57.12 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMRKG-----LT-------------IGYLAQDQGLDSQN 72
Cdd:TIGR03269 301 DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGdewvdMTkpgpdgrgrakryIGILHQEYDLYPHR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 73 TIWEEMS-SVFAELHAIEKRMHALenqlsdpaimnddqayqQTLKTydqvqTEFQQKngygyQAEirgvlhgfqfdaDVY 151
Cdd:TIGR03269 381 TVLDNLTeAIGLELPDELARMKAV-----------------ITLKM-----VGFDEE-----KAE------------EIL 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2269171783 152 DKSVTELSGGQKTQLALAKLLLEKRDLLILDEPTNHLD-VETLTWLESYLQS---YAGALLIVSHDRYFldrvVNEVYD 226
Cdd:TIGR03269 422 DKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpITKVDVTHSILKAreeMEQTFIIVSHDMDF----VLDVCD 496
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-184 |
2.35e-08 |
|
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: 55.24 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 2 RRFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISM------------RKGLTIGYLAQDqgld 69
Cdd:cd03218 8 KRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLdgqditklpmhkRARLGIGYLPQE---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 70 sqntiweemSSVFAELHAIEKRMHALEnqlsdpaIMNDDQAYQQTlktydqvqtefqqkngygyqaEIRGVLHGFQFDAd 149
Cdd:cd03218 84 ---------ASIFRKLTVEENILAVLE-------IRGLSKKEREE---------------------KLEELLEEFHITH- 125
|
170 180 190
....*....|....*....|....*....|....*
gi 2269171783 150 VYDKSVTELSGGQKTQLALAKLLLEKRDLLILDEP 184
Cdd:cd03218 126 LRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
341-510 |
2.54e-08 |
|
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: 56.21 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIP---FIKGQAVFGtGV-VTGYYDQEQRN----------------LNDKK 400
Cdd:COG0444 25 SFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFD-GEdLLKLSEKELRKirgreiqmifqdpmtsLNPVM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 401 TV---LSELWDEHPTTPEKDIRTILESFLftgADV--DKPV-------HALSGGERARLLL-TKLAMQNDnFLILDEPTN 467
Cdd:COG0444 104 TVgdqIAEPLRIHGGLSKAEARERAIELL---ERVglPDPErrldrypHELSGGMRQRVMIaRALALEPK-LLIADEPTT 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2269171783 468 HLDIDSR-EVLEVaLND----FDGTLLFVSHD----RYFINQVAT----SVVEVSP 510
Cdd:COG0444 180 ALDVTIQaQILNL-LKDlqreLGLAILFITHDlgvvAEIADRVAVmyagRIVEEGP 234
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
11-52 |
2.86e-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: 2.86e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQIS 52
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
10-230 |
3.14e-08 |
|
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: 54.75 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 10 FDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI--------------------SMRKGlTIGYLAQdqgld 69
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrhdggwvdlaqaspreilALRRR-TIGYVSQ----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 70 sqntiweemssvFaeLHAIeKRMHALEnQLSDPAI---MNDDQAyqqtlktydqvqtefqqkngygyQAEIRGVLHGFQF 146
Cdd:COG4778 101 ------------F--LRVI-PRVSALD-VVAEPLLergVDREEA-----------------------RARARELLARLNL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 147 DADVYDKSVTELSGGQKTQLALAKLLLEKRDLLILDEPTNHLDVET----LTWLESYLQsyAGALLI-VSHDRYFLDRVV 221
Cdd:COG4778 142 PERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANravvVELIEEAKA--RGTAIIgIFHDEEVREAVA 219
|
....*....
gi 2269171783 222 NEVYDLSHH 230
Cdd:COG4778 220 DRVVDVTPF 228
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
341-494 |
3.18e-08 |
|
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: 54.57 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGYYDQEqRN---------LNDKKTVLSELwdEHP 411
Cdd:cd03301 20 NLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-RDiamvfqnyaLYPHMTVYDNI--AFG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 412 ----TTPEKDIRTILES---FLFTGADVDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLEVALNDF 484
Cdd:cd03301 97 lklrKVPKDEIDERVREvaeLLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRL 176
|
170
....*....|....
gi 2269171783 485 ----DGTLLFVSHD 494
Cdd:cd03301 177 qqrlGTTTIYVTHD 190
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
341-506 |
3.28e-08 |
|
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: 55.89 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVF--------GTGVVT-------GYYDQEQR---NLNDKKTV 402
Cdd:TIGR02142 17 DFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLngrtlfdsRKGIFLppekrriGYVFQEARlfpHLSVRGNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 403 LSELWDEHPTTPEKDIRTILEsFLFTGADVDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSR-EV---LE 478
Cdd:TIGR02142 97 RYGMKRARPSERRISFERVIE-LLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKyEIlpyLE 175
|
170 180
....*....|....*....|....*...
gi 2269171783 479 VALNDFDGTLLFVSHDRYFINQVATSVV 506
Cdd:TIGR02142 176 RLHAEFGIPILYVSHSLQEVLRLADRVV 203
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
351-494 |
3.77e-08 |
|
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: 53.13 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 351 AIVGPNGIGKSTFLKSIlgqipfikGQAVFGTGVVTGYYDQEQRNLNdkkTVLSELwdehpttpekdirtileSFLFTga 430
Cdd:cd03227 25 IITGPNGSGKSTILDAI--------GLALGGAQSATRRRSGVKAGCI---VAAVSA-----------------ELIFT-- 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2269171783 431 dvdkpVHALSGGERAR----LLLTKLAMQNDNFLILDEPTNHLDIDSREVLEVALNDF---DGTLLFVSHD 494
Cdd:cd03227 75 -----RLQLSGGEKELsalaLILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHlvkGAQVIVITHL 140
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
331-477 |
4.16e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 55.20 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 331 YDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILG--------------QIPFIKGQAVFGTGVVTGYydqeqRNL 396
Cdd:PRK13537 17 YGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGlthpdagsislcgePVPSRARHARQRVGVVPQF-----DNL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 397 NDKKTVLSEL------WDEHPTTPEKDIRTILEsFLFTGADVDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLD 470
Cdd:PRK13537 92 DPDFTVRENLlvfgryFGLSAAAARALVPPLLE-FAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
....*..
gi 2269171783 471 IDSREVL 477
Cdd:PRK13537 171 PQARHLM 177
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
5-56 |
4.23e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 54.11 E-value: 4.23e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2269171783 5 GADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMRKG 56
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG 64
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-189 |
4.39e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 55.61 E-value: 4.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 2 RRFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISM------------RKGltIGYLAQDQGLD 69
Cdd:PRK13536 49 KSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlgvpvpararlaRAR--IGVVPQFDNLD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 70 SQNTIWEEMsSVFAELHaiekRMHALENQLSDPAIMnddqayqqtlktydqvqtEFQQkngygyqaeirgvlhgFQFDAD 149
Cdd:PRK13536 127 LEFTVRENL-LVFGRYF----GMSTREIEAVIPSLL------------------EFAR----------------LESKAD 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2269171783 150 VydkSVTELSGGQKTQLALAKLLLEKRDLLILDEPTNHLD 189
Cdd:PRK13536 168 A---RVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-51 |
4.54e-08 |
|
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: 54.27 E-value: 4.54e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2269171783 2 RRFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI 51
Cdd:cd03296 10 KRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTI 59
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-212 |
5.80e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 54.81 E-value: 5.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 2 RRFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISM----------RKGLTIGYLAQDQGLDSQ 71
Cdd:PRK13537 15 KRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcgepvpsrarHARQRVGVVPQFDNLDPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 72 NTIWEEMSsVFAEL-----HAIEKRMHALenqlsdpaimnddqayqqtlktydqvqTEFQQkngygyqAEIRGvlhgfqf 146
Cdd:PRK13537 95 FTVRENLL-VFGRYfglsaAAARALVPPL---------------------------LEFAK-------LENKA------- 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 147 dadvyDKSVTELSGGQKTQLALAKLLLEKRDLLILDEPTNHLDVET--LTW--LESYLQSyAGALLIVSH 212
Cdd:PRK13537 133 -----DAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQArhLMWerLRSLLAR-GKTILLTTH 196
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
352-494 |
6.69e-08 |
|
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: 54.29 E-value: 6.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 352 IVGPNGIGKSTFLKSILGQIpfIKGQAVFG-----TGVVTGYYDQEQRN-----LND--KKTVLSELWDEHPTTPEKDIR 419
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKL--KPNLGKFDdppdwDEILDEFRGSELQNyftklLEGdvKVIVKPQYVDLIPKAVKGKVG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 420 TILESFLFTGAD------------VDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSRevLEVA-----LN 482
Cdd:cd03236 109 ELLKKKDERGKLdelvdqlelrhvLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQR--LNAArlireLA 186
|
170
....*....|..
gi 2269171783 483 DFDGTLLFVSHD 494
Cdd:cd03236 187 EDDNYVLVVEHD 198
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
11-192 |
6.70e-08 |
|
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: 53.77 E-value: 6.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI-------------SMRKglTIGYLAQDQGLDSqNTIWEE 77
Cdd:cd03251 19 RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRIlidghdvrdytlaSLRR--QIGLVSQDVFLFN-DTVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 78 MSsvFAELHAIEKR-MHALENQLSDPAIMNDDQayqqtlktydqvqtefqqkngyGYQAEI--RGVlhgfqfdadvydks 154
Cdd:cd03251 96 IA--YGRPGATREEvEEAARAANAHEFIMELPE----------------------GYDTVIgeRGV-------------- 137
|
170 180 190
....*....|....*....|....*....|....*...
gi 2269171783 155 vtELSGGQKTQLALAKLLLEKRDLLILDEPTNHLDVET 192
Cdd:cd03251 138 --KLSGGQRQRIAIARALLKDPPILILDEATSALDTES 173
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
3-52 |
7.54e-08 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 53.93 E-value: 7.54e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2269171783 3 RFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQIS 52
Cdd:COG4604 10 RYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVL 59
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
11-213 |
7.80e-08 |
|
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: 53.49 E-value: 7.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMR-KGLT--------IGYLAQDQGLDSQNTIWEEMssv 81
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgKDITnlppekrdISYVPQNYALFPHMTVYKNI--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 82 faelhaiekrmhalenqlsdpaimnddqAYQQTLKTYDQVQTEFQQKNgygyQAEIRGVLHgfqfdadVYDKSVTELSGG 161
Cdd:cd03299 93 ----------------------------AYGLKKRKVDKKEIERKVLE----IAEMLGIDH-------LLNRKPETLSGG 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2269171783 162 QKTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYL----QSYAGALLIVSHD 213
Cdd:cd03299 134 EQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELkkirKEFGVTVLHVTHD 189
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
344-494 |
8.59e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.20 E-value: 8.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 344 VKKHEAIAIVGPNGIGKSTFLKsIL-GQ-IPFIkgqavfgtgvvtGYYDQEQrnlnDKKTVL-----SELWDEHPTTPEK 416
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVK-ILsGElIPNL------------GDYEEEP----SWDEVLkrfrgTELQNYFKKLYNG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 417 DIRTIL---------ESF------LFTGAD-----------------VDKPVHALSGGERARLLLTKLAMQNDNFLILDE 464
Cdd:PRK13409 159 EIKVVHkpqyvdlipKVFkgkvreLLKKVDergkldevverlgleniLDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190
....*....|....*....|....*....|....
gi 2269171783 465 PTNHLDIdsREVLEVA--LNDF--DGTLLFVSHD 494
Cdd:PRK13409 239 PTSYLDI--RQRLNVArlIRELaeGKYVLVVEHD 270
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
341-465 |
9.16e-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: 53.43 E-value: 9.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVT------------GYYDQEQ---RNL---NDKKTV 402
Cdd:TIGR04406 21 SLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDIThlpmherarlgiGYLPQEAsifRKLtveENIMAV 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2269171783 403 LSELWDEHPTTPEKDIRTILESFLFTGADvDKPVHALSGGERARLLLTKLAMQNDNFLILDEP 465
Cdd:TIGR04406 101 LEIRKDLDRAEREERLEALLEEFQISHLR-DNKAMSLSGGERRRVEIARALATNPKFILLDEP 162
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
345-494 |
1.06e-07 |
|
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: 55.18 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 345 KKHEAIAIVGPNGIGKSTFLKsIL-GQ-IPFIkgqavfgtgvvtGYYDQEqrnlNDKKTVL-----SELWDEHPTTPEKD 417
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALK-ILsGElKPNL------------GDYDEE----PSWDEVLkrfrgTELQDYFKKLANGE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 418 IRTIL---------ESF------LFTGAD-----------------VDKPVHALSGGERARLLLTKLAMQNDNFLILDEP 465
Cdd:COG1245 160 IKVAHkpqyvdlipKVFkgtvreLLEKVDergkldelaeklgleniLDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|....
gi 2269171783 466 TNHLDIdsREVLEVA-----LNDFDGTLLFVSHD 494
Cdd:COG1245 240 SSYLDI--YQRLNVArlireLAEEGKYVLVVEHD 271
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
294-495 |
1.33e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 54.07 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 294 MDRIDRPDSdektahfgfhAAKQSGNIVLTVKDAAVGYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPF 373
Cdd:PRK11607 2 NDAIPRPQA----------KTRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 374 IKGQAVFgTGVVTGYYDQEQRNLNdkktVLSELWDEHP-TTPEKDIRTILESFLFTGADVDKPV---------------- 436
Cdd:PRK11607 72 TAGQIML-DGVDLSHVPPYQRPIN----MMFQSYALFPhMTVEQNIAFGLKQDKLPKAEIASRVnemlglvhmqefakrk 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2269171783 437 -HALSGGERARLLLTKLAMQNDNFLILDEPTNHLD--IDSREVLEVA--LNDFDGTLLFVSHDR 495
Cdd:PRK11607 147 pHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDkkLRDRMQLEVVdiLERVGVTCVMVTHDQ 210
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-221 |
1.36e-07 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 53.07 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 5 GADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQIsmrkgLTIGYLAQDQGLDSQNTIWEEMSSVFAE 84
Cdd:TIGR02315 13 NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSI-----LLEGTDITKLRGKKLRKLRRRIGMIFQH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 85 LHAIEkRMHALENQLSdPAImnddqAYQQTLKTYDQVQTEFQQKNGYgYQAEIRGVlhgfqfdADVYDKSVTELSGGQKT 164
Cdd:TIGR02315 88 YNLIE-RLTVLENVLH-GRL-----GYKPTWRSLLGRFSEEDKERAL-SALERVGL-------ADKAYQRADQLSGGQQQ 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2269171783 165 QLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYA---GALLIVS-HD----RYFLDRVV 221
Cdd:TIGR02315 153 RVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINkedGITVIINlHQvdlaKKYADRIV 217
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
341-506 |
1.41e-07 |
|
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: 53.12 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIP------FIKGQAVfgTG-----------------------------VV 385
Cdd:COG0411 24 SLEVERGEIVGLIGPNGAGKTTLFNLITGFYRptsgriLFDGRDI--TGlpphriarlgiartfqnprlfpeltvlenVL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 386 TGYYDQEQRNLNDKKTVLSELWDEHPTTPEKdIRTILEsflFTG-ADV-DKPVHALSGGER-----ARLLLT--KLamqn 456
Cdd:COG0411 102 VAAHARLGRGLLAALLRLPRARREEREARER-AEELLE---RVGlADRaDEPAGNLSYGQQrrleiARALATepKL---- 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2269171783 457 dnfLILDEPT---NHLDIDsrEVLEV--ALNDFDG-TLLFVSHDRYFINQVATSVV 506
Cdd:COG0411 174 ---LLLDEPAaglNPEETE--ELAELirRLRDERGiTILLIEHDMDLVMGLADRIV 224
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
352-515 |
1.59e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 52.41 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 352 IVGPNGIGKSTFLKSILGQIPFIKGQAVF-GTGVVT----------GYYDQEQRNLNDkkTVLSEL---WDEHPTTPE-K 416
Cdd:PRK10247 38 ITGPSGCGKSTLLKIVASLISPTSGTLLFeGEDISTlkpeiyrqqvSYCAQTPTLFGD--TVYDNLifpWQIRNQQPDpA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 417 DIRTILESFLFTGADVDKPVHALSGGERARLLLtklaMQNDNF----LILDEPTNHLDIDSR----EVLEVALNDFDGTL 488
Cdd:PRK10247 116 IFLDDLERFALPDTILTKNIAELSGGEKQRISL----IRNLQFmpkvLLLDEITSALDESNKhnvnEIIHRYVREQNIAV 191
|
170 180
....*....|....*....|....*..
gi 2269171783 489 LFVSHDRYFINQvATSVVEVSPEGTEL 515
Cdd:PRK10247 192 LWVTHDKDEINH-ADKVITLQPHAGEM 217
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
322-471 |
1.61e-07 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 52.81 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 322 LTVKDAAVGYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFgtgvvtgyydqEQRNLNDKKT 401
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRL-----------NGRPLAAWSP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 402 --------VL---SEL----------------WDEHPTTPEKDIRTILESflfTGAD--VDKPVHALSGGERARL----L 448
Cdd:COG4559 71 welarrraVLpqhSSLafpftveevvalgrapHGSSAAQDRQIVREALAL---VGLAhlAGRSYQTLSGGEQQRVqlarV 147
|
170 180
....*....|....*....|....*.
gi 2269171783 449 LTKLAMQND---NFLILDEPTNHLDI 471
Cdd:COG4559 148 LAQLWEPVDggpRWLFLDEPTSALDL 173
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
11-237 |
2.14e-07 |
|
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: 51.98 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMrKGL-----------TIGYLAQDQGLDSQNTIWEeMS 79
Cdd:cd03266 22 DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV-DGFdvvkepaearrRLGFVSDSTGLYDRLTARE-NL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 80 SVFAELHAiekrmhalenqlsdpaiMNDDQAYQQTLKTYDQVQTEfqqkngygyqaeirgvlhgfqfdaDVYDKSVTELS 159
Cdd:cd03266 100 EYFAGLYG-----------------LKGDELTARLEELADRLGME------------------------ELLDRRVGGFS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 160 GGQKTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSY--AG-ALLIVSHDRYFLDRVVNEVYDLsHHEMVHYT 236
Cdd:cd03266 139 TGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLraLGkCILFSTHIMQEVERLCDRVVVL-HRGRVVYE 217
|
.
gi 2269171783 237 G 237
Cdd:cd03266 218 G 218
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
9-65 |
2.32e-07 |
|
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: 51.06 E-value: 2.32e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2269171783 9 LFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI-----------SMRKGLTIGYLAQD 65
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVrldgadisqwdPNELGDHVGYLPQD 84
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
8-212 |
2.34e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 51.73 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 8 VLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMRkGLTIGylAQDqglDS--QNTIWeemssvFAEL 85
Cdd:PRK13538 15 ILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQ-GEPIR--RQR---DEyhQDLLY------LGHQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 86 HAIEKRMHALEN-----QLSDPAimnDDQAYQQTLktyDQVqtefqqknGygyqaeirgvLHGFQfdadvyDKSVTELSG 160
Cdd:PRK13538 83 PGIKTELTALENlrfyqRLHGPG---DDEALWEAL---AQV--------G----------LAGFE------DVPVRQLSA 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2269171783 161 GQKTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYA---GALLIVSH 212
Cdd:PRK13538 133 GQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAeqgGMVILTTH 187
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-474 |
2.46e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.52 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 24 ALVGRNGAGKSTLLKMIAGETVPDEGQISM----RKGLTIG-------YLA-QDQGLDSQNTIWEEMSSVFAELHAIEKR 91
Cdd:PRK15439 41 ALLGGNGAGKSTLMKIIAGIVPPDSGTLEIggnpCARLTPAkahqlgiYLVpQEPLLFPNLSVKENILFGLPKRQASMQK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 92 MHALENQLS---DPaimnDDQAyqQTLKTYDQVQTEfqqkngygyqaeirgVLHGFQFDADVydksvtelsggqktqlal 168
Cdd:PRK15439 121 MKQLLAALGcqlDL----DSSA--GSLEVADRQIVE---------------ILRGLMRDSRI------------------ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 169 aklllekrdlLILDEPTNHL---DVETL-TWLESYLQSYAGALLIvSHDryfldrvVNEVYDLSHHEMVHYTGNYdqfvq 244
Cdd:PRK15439 162 ----------LILDEPTASLtpaETERLfSRIRELLAQGVGIVFI-SHK-------LPEIRQLADRISVMRDGTI----- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 245 ekaariqaqwkhyekqqAEISKLEDFVNRNIVRASTTKraqARRKQLAKMDR--IDRPdsdektahfGFHAAKQSGNIVL 322
Cdd:PRK15439 219 -----------------ALSGKTADLSTDDIIQAITPA---AREKSLSASQKlwLELP---------GNRRQQAAGAPVL 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 323 TVKD-AAVGYDgHIlsepdNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFgtgvvtgyydqEQRNLNDKKT 401
Cdd:PRK15439 270 TVEDlTGEGFR-NI-----SLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIML-----------NGKEINALST 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 402 V---------LSE------LWDEHPTT----------------PEKDiRTILESFL------FTGAdvDKPVHALSGGER 444
Cdd:PRK15439 333 AqrlarglvyLPEdrqssgLYLDAPLAwnvcalthnrrgfwikPARE-NAVLERYRralnikFNHA--EQAARTLSGGNQ 409
|
490 500 510
....*....|....*....|....*....|
gi 2269171783 445 ARLLLTKLAMQNDNFLILDEPTNHLDIDSR 474
Cdd:PRK15439 410 QKVLIAKCLEASPQLLIVDEPTRGVDVSAR 439
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
341-474 |
2.49e-07 |
|
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: 51.74 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQA-VFGTGVVTGYYDQEQR--------NLNDKKTVLselwdEH- 410
Cdd:cd03263 22 SLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyINGYSIRTDRKAARQSlgycpqfdALFDELTVR-----EHl 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2269171783 411 ---------PTTPEKDIRTILESFLFTGADVDKPVHALSGGERARLlltKLAMQ---NDNFLILDEPTNHLDIDSR 474
Cdd:cd03263 97 rfyarlkglPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKL---SLAIAligGPSVLLLDEPTSGLDPASR 169
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2-213 |
2.62e-07 |
|
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: 51.95 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 2 RRFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISM-------RKgltIGYLAQDQGLDSQ-NT 73
Cdd:cd03267 29 RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVaglvpwkRR---KKFLRRIGVVFGQkTQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 74 IWEEMSSvfAELHAIEKRMHALenqlsdpaimnDDQAYQQTL-KTYDQVQTEfqqkngygyqaeirgvlhgfqfdaDVYD 152
Cdd:cd03267 106 LWWDLPV--IDSFYLLAAIYDL-----------PPARFKKRLdELSELLDLE------------------------ELLD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2269171783 153 KSVTELSGGQKTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSY----AGALLIVSHD 213
Cdd:cd03267 149 TPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHY 213
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
8-51 |
3.11e-07 |
|
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: 50.77 E-value: 3.11e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2269171783 8 VLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI 51
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI 59
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
320-484 |
3.52e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.95 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 320 IVLTVKDAAVGYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPF--IKGQAVF-GTGVVtgYYDQEQR-- 394
Cdd:CHL00131 6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYkiLEGDILFkGESIL--DLEPEERah 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 395 --------------------------NLNDKKTVLSELwdeHPTTPEKDIRTILE------SFLftGADVDKpvhALSGG 442
Cdd:CHL00131 84 lgiflafqypieipgvsnadflrlayNSKRKFQGLPEL---DPLEFLEIINEKLKlvgmdpSFL--SRNVNE---GFSGG 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2269171783 443 ERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLEVALNDF 484
Cdd:CHL00131 156 EKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKL 197
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2-474 |
3.54e-07 |
|
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: 53.29 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 2 RRFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIA---------GETVPDEGQI-------SMRKGLTIgylaqd 65
Cdd:TIGR02633 9 KTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSgvyphgtwdGEIYWSGSPLkasnirdTERAGIVI------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 66 qgldsqntIWEEMSSVfAELHAIEKRMhaLENQLSDP-AIMNDDQAYQQTLKTYDQVQtefqqkngygyqaeirgvlhgf 144
Cdd:TIGR02633 83 --------IHQELTLV-PELSVAENIF--LGNEITLPgGRMAYNAMYLRAKNLLRELQ---------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 145 qFDADVYDKSVTELSGGQKTQLALAKLLLEKRDLLILDEPTNHL---DVETLTWLESYLQSYAGALLIVSHDryfldrvV 221
Cdd:TIGR02633 130 -LDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLtekETEILLDIIRDLKAHGVACVYISHK-------L 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 222 NEVYDLSHHEMVHYTGNY-----------DQFVQEKAAR-IQAQWKHYEKQQA-EISKLE-----DFVNRNIVRASTTKR 283
Cdd:TIGR02633 202 NEVKAVCDTICVIRDGQHvatkdmstmseDDIITMMVGReITSLYPHEPHEIGdVILEARnltcwDVINPHRKRVDDVSF 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 284 AQARRKQLAKMDRIDRPDSDEKTAHFGFHAAKQSGNIVLT-----VKDAAVGYDGHILSEPDNLnvKKHeaiAIVGPNGI 358
Cdd:TIGR02633 282 SLRRGEILGVAGLVGAGRTELVQALFGAYPGKFEGNVFINgkpvdIRNPAQAIRAGIAMVPEDR--KRH---GIVPILGV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 359 GKSTFLKSIlgqipfikgqavfgtgvvtgyydqeqrnlnDKKTVLSELWDEhptTPEKDIRTILESFLFTGADVDKPVHA 438
Cdd:TIGR02633 357 GKNITLSVL------------------------------KSFCFKMRIDAA---AELQIIGSAIQRLKVKTASPFLPIGR 403
|
490 500 510
....*....|....*....|....*....|....*.
gi 2269171783 439 LSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSR 474
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAK 439
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
322-502 |
5.10e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 51.58 E-value: 5.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 322 LTVKDAAVGYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSiLGQIPFIKGQA-VFGTGVVTGYYDQEQR-NLNDK 399
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVrVEGRVEFFNQNIYERRvNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 400 KTVLSELwdeHPTT---------------------PEKDIRTILESFLFTGA---DVDKPVHA----LSGGERARLLLTK 451
Cdd:PRK14258 87 RRQVSMV---HPKPnlfpmsvydnvaygvkivgwrPKLEIDDIVESALKDADlwdEIKHKIHKsaldLSGGQQQRLCIAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2269171783 452 LAMQNDNFLILDEPTNHLDIDSREVLEVALNDF----DGTLLFVSHDRYFINQVA 502
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlrsELTMVIVSHNLHQVSRLS 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-215 |
5.12e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.86 E-value: 5.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 2 RRFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMrkgLTIGYLAQDQGLDSQNTIweemSSV 81
Cdd:PRK09700 13 KSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI---NNINYNKLDHKLAAQLGI----GII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 82 FAELHAIEKrMHALEN----QLSDPAIMNddqayqqtlktYDQVQTEFQQKngygyQAEIRGVLHGFQFDADVYdksVTE 157
Cdd:PRK09700 86 YQELSVIDE-LTVLENlyigRHLTKKVCG-----------VNIIDWREMRV-----RAAMMLLRVGLKVDLDEK---VAN 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 158 LSGGQKTQLALAKLLLEKRDLLILDEPTNHL---DVETLTWLESYLQSYAGALLIVSH---------DRY 215
Cdd:PRK09700 146 LSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtnkEVDYLFLIMNQLRKEGTAIVYISHklaeirricDRY 215
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
341-506 |
5.38e-07 |
|
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: 51.19 E-value: 5.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGYYDQEqRN---------LNDKKTVLS------E 405
Cdd:cd03296 22 SLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-RNvgfvfqhyaLFRHMTVFDnvafglR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 406 LWDEHPTTPEKDIRTILESFL-FTGAD--VDKPVHALSGGERARLLLTK-LAMQnDNFLILDEPTNHLDIDSREVLEVAL 481
Cdd:cd03296 101 VKPRSERPPEAEIRAKVHELLkLVQLDwlADRYPAQLSGGQRQRVALARaLAVE-PKVLLLDEPFGALDAKVRKELRRWL 179
|
170 180
....*....|....*....|....*....
gi 2269171783 482 ----NDFDGTLLFVSHDRYFINQVATSVV 506
Cdd:cd03296 180 rrlhDELHVTTVFVTHDQEEALEVADRVV 208
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
332-511 |
5.50e-07 |
|
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: 50.26 E-value: 5.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 332 DGHILSEPDNlnVKKHEAIAIVGPNGIGKSTFLKSILGQ-IPfikgqavfgtgvvtgyydqeqrnlNDKKTvlselwdeh 410
Cdd:cd03222 12 VFFLLVELGV--VKEGEVIGIVGPNGTGKTTAVKILAGQlIP------------------------NGDND--------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 411 pttpEKDIRTIlesflftgadVDKPVH-ALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLEVALNDF----D 485
Cdd:cd03222 57 ----EWDGITP----------VYKPQYiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegK 122
|
170 180
....*....|....*....|....*.
gi 2269171783 486 GTLLFVSHDRYFINQVATSVVEVSPE 511
Cdd:cd03222 123 KTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
5-192 |
5.51e-07 |
|
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: 52.80 E-value: 5.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 5 GADVLfDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMRkgltiGYLAQDQGLDSQntiweemssvfae 84
Cdd:TIGR02203 344 DRPAL-DSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLD-----GHDLADYTLASL------------- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 85 lhaieKRMHALENQ---LSDPAIMNDdQAYQQTlKTYDQVQTEFQQKNGYGyQAEIRGVLHGFQFDadVYDKSVtELSGG 161
Cdd:TIGR02203 405 -----RRQVALVSQdvvLFNDTIANN-IAYGRT-EQADRAEIERALAAAYA-QDFVDKLPLGLDTP--IGENGV-LLSGG 473
|
170 180 190
....*....|....*....|....*....|.
gi 2269171783 162 QKTQLALAKLLLEKRDLLILDEPTNHLDVET 192
Cdd:TIGR02203 474 QRQRLAIARALLKDAPILILDEATSALDNES 504
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
4-190 |
5.55e-07 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 52.15 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 4 FGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMrKGLTIGYLaqdqgldSQNTIWEEMSSV-- 81
Cdd:PRK09536 13 FGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLV-AGDDVEAL-------SARAASRRVASVpq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 82 -------FAELHAIEKRMHALENQLsDPAIMNDDQAYQQTLktyDQVQTEfqqkngygyqaeirgvlhgfQFdadvYDKS 154
Cdd:PRK09536 85 dtslsfeFDVRQVVEMGRTPHRSRF-DTWTETDRAAVERAM---ERTGVA--------------------QF----ADRP 136
|
170 180 190
....*....|....*....|....*....|....*.
gi 2269171783 155 VTELSGGQKTQLALAKLLLEKRDLLILDEPTNHLDV 190
Cdd:PRK09536 137 VTSLSGGERQRVLLARALAQATPVLLLDEPTASLDI 172
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
342-506 |
5.61e-07 |
|
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: 50.57 E-value: 5.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 342 LNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGtGVVTGYYDQEQR---NLNDKKTVLSELWDEH-------P 411
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLIN-GVDVTAAPPADRpvsMLFQENNLFAHLTVEQnvglglsP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 412 T---TPE--KDIRTILESFLFTGADVDKPvHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLEVALNDF-- 484
Cdd:cd03298 98 GlklTAEdrQAIEVALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLha 176
|
170 180
....*....|....*....|....
gi 2269171783 485 --DGTLLFVSHDRYFINQVATSVV 506
Cdd:cd03298 177 etKMTVLMVTHQPEDAKRLAQRVV 200
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
341-506 |
6.21e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 50.85 E-value: 6.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAV----------FGTGVV---TGYydqeqRN--LN------DK 399
Cdd:COG1134 46 SFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEvngrvsalleLGAGFHpelTGR-----ENiyLNgrllglSR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 400 KTVlselwDEHpttpEKDIR--TILESFLftgadvDKPVHALSGGERARLLLTkLAMQND-NFLILDeptnhldidsrEV 476
Cdd:COG1134 121 KEI-----DEK----FDEIVefAELGDFI------DQPVKTYSSGMRARLAFA-VATAVDpDILLVD-----------EV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2269171783 477 LEV-----------ALNDF---DGTLLFVSHDRYFINQVATSVV 506
Cdd:COG1134 174 LAVgdaafqkkclaRIRELresGRTVIFVSHSMGAVRRLCDRAI 217
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-51 |
6.28e-07 |
|
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: 50.70 E-value: 6.28e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2269171783 2 RRFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI 51
Cdd:cd03300 8 KFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEI 57
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
341-494 |
7.41e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 51.26 E-value: 7.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSIL-------GQIpFIKGQAV-------FGtgvvtgyYDQEQRNLNDKKTV---- 402
Cdd:COG4152 21 SFTVPKGEIFGLLGPNGAGKTTTIRIILgilapdsGEV-LWDGEPLdpedrrrIG-------YLPEERGLYPKMKVgeql 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 403 --LSELWDEHPTTPEKDIRTILESFlftgaDV----DKPVHALSGGERARL-LLTKLAMQNDnFLILDEPTNHLDIDSRE 475
Cdd:COG4152 93 vyLARLKGLSKAEAKRRADEWLERL-----GLgdraNKKVEELSKGNQQKVqLIAALLHDPE-LLILDEPFSGLDPVNVE 166
|
170 180
....*....|....*....|..
gi 2269171783 476 VLEVALNDF--DG-TLLFVSHD 494
Cdd:COG4152 167 LLKDVIRELaaKGtTVIFSSHQ 188
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
348-470 |
7.51e-07 |
|
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: 49.86 E-value: 7.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 348 EAIAIVGPNGIGKSTFLKSILGQIPF--IKGQ-AVFGTGV-------VTGYYDQEQrnlndkkTVLSELwdehpttpekd 417
Cdd:cd03213 36 ELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEvLINGRPLdkrsfrkIIGYVPQDD-------ILHPTL----------- 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2269171783 418 irTILESFLFTGAdvdkpVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLD 470
Cdd:cd03213 98 --TVRETLMFAAK-----LRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
341-493 |
7.69e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 51.94 E-value: 7.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKsIL--------GQIpFIKGQAV-FGT-------GVVTGYydQEqRNLNDKKTVLS 404
Cdd:COG1129 24 SLELRPGEVHALLGENGAGKSTLMK-ILsgvyqpdsGEI-LLDGEPVrFRSprdaqaaGIAIIH--QE-LNLVPNLSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 405 ELW-DEHPTTP--------EKDIRTILESFlftGADVD--KPVHALSGGER-----ARllltklAMQND-NFLILDEPTN 467
Cdd:COG1129 99 NIFlGREPRRGglidwramRRRARELLARL---GLDIDpdTPVGDLSVAQQqlveiAR------ALSRDaRVLILDEPTA 169
|
170 180
....*....|....*....|....*....
gi 2269171783 468 HLDIDSREVLEVALNDF--DG-TLLFVSH 493
Cdd:COG1129 170 SLTEREVERLFRIIRRLkaQGvAIIYISH 198
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
350-507 |
7.72e-07 |
|
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: 50.27 E-value: 7.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 350 IAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVT----------GYYDQEQRnLNDKKTV------LSELWDEHPTT 413
Cdd:cd03264 28 YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLkqpqklrrriGYLPQEFG-VYPNFTVrefldyIAWLKGIPSKE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 414 PEKDIRTILEsfLFTGADV-DKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVlevalndFDGTLLFVS 492
Cdd:cd03264 107 VKARVDEVLE--LVNLGDRaKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIR-------FRNLLSELG 177
|
170
....*....|....*
gi 2269171783 493 HDRYFInqVATSVVE 507
Cdd:cd03264 178 EDRIVI--LSTHIVE 190
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
2-220 |
8.47e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 50.48 E-value: 8.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 2 RRFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQismrkgLTIGYLAQDQGLDSQNTIWEEMSSV 81
Cdd:PRK09493 9 KHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGD------LIVDGLKVNDPKVDERLIRQEAGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 82 FAELHAIeKRMHALENQLSDPAI---MNDDQAYQQTLKTYDQVqtefqqkngygyqaeirgvlhGFQFDADVYDksvTEL 158
Cdd:PRK09493 83 FQQFYLF-PHLTALENVMFGPLRvrgASKEEAEKQARELLAKV---------------------GLAERAHHYP---SEL 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2269171783 159 SGGQKTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYAG---ALLIVSHDRYFLDRV 220
Cdd:PRK09493 138 SGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEegmTMVIVTHEIGFAEKV 202
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
11-221 |
8.72e-07 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 50.54 E-value: 8.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMrKGLTIGYLAQDQGLDSQNTiweemsSVFAELHAIEK 90
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIL-EGKQITEPGPDRMVVFQNY------SLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 91 RMHALENQLSDPAIMNDDQAYQQTLKtydqvqtefqqkngygyqaeirgvLHGFQFDADvydKSVTELSGGQKTQLALAK 170
Cdd:TIGR01184 75 IALAVDRVLPDLSKSERRAIVEEHIA------------------------LVGLTEAAD---KRPGQLSGGMKQRVAIAR 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2269171783 171 LLLEKRDLLILDEPTNHLDVETLTWLESYL----QSYAGALLIVSHD---RYFL-DRVV 221
Cdd:TIGR01184 128 ALSIRPKVLLLDEPFGALDALTRGNLQEELmqiwEEHRVTVLMVTHDvdeALLLsDRVV 186
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
11-233 |
9.00e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 50.98 E-value: 9.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMrKGLTIGYLAQDQGLDSqntIWEEMSSVFaelhaiek 90
Cdd:PRK13641 24 DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITI-AGYHITPETGNKNLKK---LRKKVSLVF-------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 91 rmHALENQLSDPAIMNDdqayqqtlktydqvqTEFQQKNgYGY---QAEIRGV--LHGFQFDADVYDKSVTELSGGQKTQ 165
Cdd:PRK13641 92 --QFPEAQLFENTVLKD---------------VEFGPKN-FGFsedEAKEKALkwLKKVGLSEDLISKSPFELSGGQMRR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2269171783 166 LALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYAGA---LLIVSHDRYFLDRVVNEVYDLSHHEMV 233
Cdd:PRK13641 154 VAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAghtVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
340-502 |
9.02e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.94 E-value: 9.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 340 DNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAV--FGTGVVTGYYDQE-------QRNLNDkktVLSELWDEH 410
Cdd:PRK10938 22 PSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQsqFSHITRLSFEQLQklvsdewQRNNTD---MLSPGEDDT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 411 PTTPEKDIR---------TILESFLFTGADVDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLEVAL 481
Cdd:PRK10938 99 GRTTAEIIQdevkdparcEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELL 178
|
170 180
....*....|....*....|....*....
gi 2269171783 482 NDFDG---TLLFVShDRY-----FINQVA 502
Cdd:PRK10938 179 ASLHQsgiTLVLVL-NRFdeipdFVQFAG 206
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
341-503 |
9.99e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 50.48 E-value: 9.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSI--LGQIP----FIKGQAVFGTGVVTGYYDQE------QRNLNDKKTVLselwd 408
Cdd:PRK09493 21 DLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEITsgdlIVDGLKVNDPKVDERLIRQEagmvfqQFYLFPHLTAL----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 409 EH----PT----TPEKDIRTILESFLftgADVDKPVHA------LSGGERARLLLTK-LAMQnDNFLILDEPTNHLDIDS 473
Cdd:PRK09493 96 ENvmfgPLrvrgASKEEAEKQARELL---AKVGLAERAhhypseLSGGQQQRVAIARaLAVK-PKLMLFDEPTSALDPEL 171
|
170 180 190
....*....|....*....|....*....|...
gi 2269171783 474 R-EVLEV--ALNDFDGTLLFVSHDRYFINQVAT 503
Cdd:PRK09493 172 RhEVLKVmqDLAEEGMTMVIVTHEIGFAEKVAS 204
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-54 |
1.11e-06 |
|
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: 49.87 E-value: 1.11e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2269171783 4 FGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAG-----ETVPDEGQISMR 54
Cdd:cd03260 10 YGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLD 65
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
2-56 |
1.12e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 50.31 E-value: 1.12e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2269171783 2 RRFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQIS--MRKG 56
Cdd:PRK11701 14 KLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrMRDG 70
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
341-494 |
1.14e-06 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 50.16 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILG-QIP-----FIKGQAVFGTG----VVTGYYdqeqrNLNDKKTVLSELW--- 407
Cdd:TIGR01184 5 NLTIQQGEFISLIGHSGCGKSTLLNLISGlAQPtsggvILEGKQITEPGpdrmVVFQNY-----SLLPWLTVRENIAlav 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 408 DE-HPTTPEKDIRTILESFLFT---GADVDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLEVAL-- 481
Cdd:TIGR01184 80 DRvLPDLSKSERRAIVEEHIALvglTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELmq 159
|
170
....*....|....*
gi 2269171783 482 --NDFDGTLLFVSHD 494
Cdd:TIGR01184 160 iwEEHRVTVLMVTHD 174
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
309-493 |
1.14e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 51.75 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 309 FGFHAAKQSGNIVLTVKDAAVGYDGHILSEPDNLN--VKKHEAIAIVGPNGIGKSTFLkSIL--------GQIpFIKGQA 378
Cdd:PRK11160 326 FPTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSlqIKAGEKVALLGRTGCGKSTLL-QLLtrawdpqqGEI-LLNGQP 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 379 VfgtgvvTGYYDQEQRNLndkKTVLSE--------LWDE----HPTTPEKDIRTILESF-LFTGADVDKPVHA------- 438
Cdd:PRK11160 404 I------ADYSEAALRQA---ISVVSQrvhlfsatLRDNlllaAPNASDEALIEVLQQVgLEKLLEDDKGLNAwlgeggr 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2269171783 439 -LSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDS-REVLEVaLNDF--DGTLLFVSH 493
Cdd:PRK11160 475 qLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETeRQILEL-LAEHaqNKTVLMITH 532
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
342-516 |
1.28e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 50.40 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 342 LNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQ-AVFGTgvvtgyydqeqrnlndkktVLSE--LWD---------E 409
Cdd:PRK13635 28 FSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTiTVGGM-------------------VLSEetVWDvrrqvgmvfQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 410 HP------TTPEKDI-----------------------RTILESFLftgadvDKPVHALSGGERARLLLTKLAMQNDNFL 460
Cdd:PRK13635 89 NPdnqfvgATVQDDVafglenigvpreemvervdqalrQVGMEDFL------NREPHRLSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2269171783 461 ILDEPTNHLDIDSR-EVLEVA--LNDFDG-TLLFVSHDryfINQVATS---VV----EVSPEGT--ELF 516
Cdd:PRK13635 163 ILDEATSMLDPRGRrEVLETVrqLKEQKGiTVLSITHD---LDEAAQAdrvIVmnkgEILEEGTpeEIF 228
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
12-65 |
1.30e-06 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 50.87 E-value: 1.30e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2269171783 12 NVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISM--------RKGLT-------IGYLAQD 65
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLggevlqdsARGIFlpphrrrIGYVFQE 85
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
341-493 |
1.56e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.18 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTfLKSIL--------GQIpFIKGQAV----------FGTGVVtgyydqEQ-----RNLn 397
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKST-LMKILyglyqpdsGEI-LIDGKPVrirsprdaiaLGIGMV------HQhfmlvPNL- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 398 dkkTVLsE---LWDEHPTTP-------EKDIRTILESFlftGADVD--KPVHALSGGERARLLLTKLAMQNDNFLILDEP 465
Cdd:COG3845 96 ---TVA-EnivLGLEPTKGGrldrkaaRARIRELSERY---GLDVDpdAKVEDLSVGEQQRVEILKALYRGARILILDEP 168
|
170 180 190
....*....|....*....|....*....|.
gi 2269171783 466 TNHL-DIDSREVLEV--ALNDFDGTLLFVSH 493
Cdd:COG3845 169 TAVLtPQEADELFEIlrRLAAEGKSIIFITH 199
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
4-212 |
1.74e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 50.12 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 4 FGADVLFDnVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMrkgltigylaqdqgldsqNTIWEEMSSVFA 83
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV------------------GDIVVSSTSKQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 84 ELHAIEKRMHAL----ENQLSDPAIMND----DQAYQQTLKTYDQVQTEfqqkngygyQAEIRGVLHGFqfdadvYDKSV 155
Cdd:PRK13643 78 EIKPVRKKVGVVfqfpESQLFEETVLKDvafgPQNFGIPKEKAEKIAAE---------KLEMVGLADEF------WEKSP 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2269171783 156 TELSGGQKTQLALAKLLLEKRDLLILDEPTNHLD----VETLTWLESYLQSyAGALLIVSH 212
Cdd:PRK13643 143 FELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDpkarIEMMQLFESIHQS-GQTVVLVTH 202
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
341-494 |
1.75e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 50.47 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLK-------------SILGQIPFIKGQA-VFGTGVVTGyydqeQRnlndkktvlSEL 406
Cdd:COG4586 42 SFTIEPGEIVGFIGPNGAGKSTTIKmltgilvptsgevRVLGYVPFKRRKEfARRIGVVFG-----QR---------SQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 407 WDEHPTT------------PEKDIR-TI--------LESFLftgadvDKPVHALSGGERARLLLT-------KLamqndn 458
Cdd:COG4586 108 WWDLPAIdsfrllkaiyriPDAEYKkRLdelvelldLGELL------DTPVRQLSLGQRMRCELAaallhrpKI------ 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2269171783 459 fLILDEPTNHLDIDS----REVLEvALN-DFDGTLLFVSHD 494
Cdd:COG4586 176 -LFLDEPTIGLDVVSkeaiREFLK-EYNrERGTTILLTSHD 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
11-502 |
1.81e-06 |
|
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: 50.84 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKS----TLLKMIAGETVPDEGQIS-------------MRK--GLTIGYLAQdqgldsq 71
Cdd:COG4172 27 KGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILfdgqdllglsereLRRirGNRIAMIFQ------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 72 ntiwEEMSSvFAELHAIEKrmhalenQLSDPAI----MNDDQAYQQTLKTYDQVQTEfqqkngygyQAEIRgvLHGFQFd 147
Cdd:COG4172 100 ----EPMTS-LNPLHTIGK-------QIAEVLRlhrgLSGAAARARALELLERVGIP---------DPERR--LDAYPH- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 148 advydksvtELSGGQKtQlalaklllekR-----------DLLILDEPTNHLDV----ETLTWLESyLQSYAG-ALLIVS 211
Cdd:COG4172 156 ---------QLSGGQR-Q----------RvmiamalanepDLLIADEPTTALDVtvqaQILDLLKD-LQRELGmALLLIT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 212 HD----RYFLDRVVneVydLSHHEMVHytgnydqfvQEKAARIQAQWKH-YekqqaeiskledfvnrnivrasTtkraqa 286
Cdd:COG4172 215 HDlgvvRRFADRVA--V--MRQGEIVE---------QGPTAELFAAPQHpY----------------------T------ 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 287 rRKQLAKMDRIDRPDSDEktahfgfhaakqSGNIVLTVKDAAVGYDGH--ILSEPD---------NLNVKKHEAIAIVGP 355
Cdd:COG4172 254 -RKLLAAEPRGDPRPVPP------------DAPPLLEARDLKVWFPIKrgLFRRTVghvkavdgvSLTLRRGETLGLVGE 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 356 NGIGKSTFLKSILGQIPFiKGQAVFGTGVVTGYYDQEQR---------------NLNDKKTV---LSE---LWDEHPTTP 414
Cdd:COG4172 321 SGSGKSTLGLALLRLIPS-EGEIRFDGQDLDGLSRRALRplrrrmqvvfqdpfgSLSPRMTVgqiIAEglrVHGPGLSAA 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 415 EKD--IRTILESFLFTGADVDKPVHALSGGERARLLLTK-LAMQNDnFLILDEPTNHLDIDSR-EVLEVaLND----FDG 486
Cdd:COG4172 400 ERRarVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARaLILEPK-LLVLDEPTSALDVSVQaQILDL-LRDlqreHGL 477
|
570 580
....*....|....*....|
gi 2269171783 487 TLLFVSHD----RYFINQVA 502
Cdd:COG4172 478 AYLFISHDlavvRALAHRVM 497
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
4-189 |
1.88e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 50.13 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 4 FGADVLFDnVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMrkgltigylaQDQGLDSQntiweemsSVFA 83
Cdd:PRK13649 18 FEGRALFD-VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRV----------DDTLITST--------SKNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 84 ELHAIEKRMHAL----ENQLSDPAIMNDdqayqqtlktydqvqTEFQQKNgYGYQAE-----IRGVLHGFQFDADVYDKS 154
Cdd:PRK13649 79 DIKQIRKKVGLVfqfpESQLFEETVLKD---------------VAFGPQN-FGVSQEeaealAREKLALVGISESLFEKN 142
|
170 180 190
....*....|....*....|....*....|....*
gi 2269171783 155 VTELSGGQKTQLALAKLLLEKRDLLILDEPTNHLD 189
Cdd:PRK13649 143 PFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
321-470 |
1.93e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 50.08 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 321 VLTVKDAAVGY-DGHILSEPDNLNVKKHEAIAIVGPNGIGKSTF-------LKSILGQIpFIKGQAVfgtgvvtgYYDQE 392
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLflhfngiLKPTSGEV-LIKGEPI--------KYDKK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 393 QRnLNDKKTV--LSELWDEHPTTP--------------------EKDIRTILESFLFTGADvDKPVHALSGGERARLLLT 450
Cdd:PRK13639 72 SL-LEVRKTVgiVFQNPDDQLFAPtveedvafgplnlglskeevEKRVKEALKAVGMEGFE-NKPPHHLSGGQKKRVAIA 149
|
170 180
....*....|....*....|.
gi 2269171783 451 K-LAMQNDnFLILDEPTNHLD 470
Cdd:PRK13639 150 GiLAMKPE-IIVLDEPTSGLD 169
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-190 |
2.03e-06 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 49.63 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 4 FGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMR----KGLTIGYLAQDQGLDSQNTIWEEMS 79
Cdd:PRK11231 12 YGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGdkpiSMLSSRQLARRLALLPQHHLTPEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 80 SVfAELHAIEKRMH-ALENQLSDPAIMNDDQAYQQTlktydqvQTEfqqkngygyqaeirgvlhgfqfdaDVYDKSVTEL 158
Cdd:PRK11231 92 TV-RELVAYGRSPWlSLWGRLSAEDNARVNQAMEQT-------RIN------------------------HLADRRLTDL 139
|
170 180 190
....*....|....*....|....*....|..
gi 2269171783 159 SGGQKTQLALAKLLLEKRDLLILDEPTNHLDV 190
Cdd:PRK11231 140 SGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDI 171
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-235 |
2.19e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 49.62 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 3 RFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQIsmrkgltigyLAQDQGLDSQntiweemssvf 82
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAV----------LWQGKPLDYS----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 83 aelhaiEKRMHALENQLSdpAIMNDDQayQQTLKTYDQVQTEFQQKNGYGYQAEI-RGVLHGFQF-DADVY-DKSVTELS 159
Cdd:PRK13638 69 ------KRGLLALRQQVA--TVFQDPE--QQIFYTDIDSDIAFSLRNLGVPEAEItRRVDEALTLvDAQHFrHQPIQCLS 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2269171783 160 GGQKTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYAGA---LLIVSHDRYFLDRVVNEVYDLSHHEMVHY 235
Cdd:PRK13638 139 HGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQgnhVIISSHDIDLIYEISDAVYVLRQGQILTH 217
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-251 |
2.30e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 49.58 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 2 RRFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMrKGLTIgYLAQDQglDSQNTIWEE---- 77
Cdd:PRK10619 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVV-NGQTI-NLVRDK--DGQLKVADKnqlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 78 -----MSSVFAELHaIEKRMHALENQLSDPAI---MNDDQAYQQTLKTYDQVQTEFQQKNGYGyqaeirgvlhgfqfdad 149
Cdd:PRK10619 89 llrtrLTMVFQHFN-LWSHMTVLENVMEAPIQvlgLSKQEARERAVKYLAKVGIDERAQGKYP----------------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 150 vydksvTELSGGQKTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYA---GALLIVSHDRYFLDRVVNEVYD 226
Cdd:PRK10619 151 ------VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeegKTMVVVTHEMGFARHVSSHVIF 224
|
250 260
....*....|....*....|....*.
gi 2269171783 227 LsHHEMVHYTGNYDQ-FVQEKAARIQ 251
Cdd:PRK10619 225 L-HQGKIEEEGAPEQlFGNPQSPRLQ 249
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
342-493 |
3.02e-06 |
|
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: 48.52 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 342 LNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKG--------------QAVFGTGVV---TGYYDQ------------- 391
Cdd:cd03266 26 FTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGfatvdgfdvvkepaEARRRLGFVsdsTGLYDRltarenleyfagl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 392 ---EQRNLNDKKTVLSELWDehpttpekdirtiLESFLftgadvDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNH 468
Cdd:cd03266 106 yglKGDELTARLEELADRLG-------------MEELL------DRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTG 166
|
170 180
....*....|....*....|....*....
gi 2269171783 469 LDIDS----REVLEvALNDFDGTLLFVSH 493
Cdd:cd03266 167 LDVMAtralREFIR-QLRALGKCILFSTH 194
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-213 |
3.14e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 48.78 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 23 VALVGRNGAGKSTLLKMIAGeTVPDEGQISMrkgltigylaQDQGLDSQNTiweemssvfAELhaieKRMHA-LENQLSD 101
Cdd:PRK03695 25 LHLVGPNGAGKSTLLARMAG-LLPGSGSIQF----------AGQPLEAWSA---------AEL----ARHRAyLSQQQTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 102 PAIMNddqAYQQ-TLKTYDQVQTefqqkngYGYQAEIRGVLHGFQFDaDVYDKSVTELSGG--QKTQLALAK-----LLL 173
Cdd:PRK03695 81 PFAMP---VFQYlTLHQPDKTRT-------EAVASALNEVAEALGLD-DKLGRSVNQLSGGewQRVRLAAVVlqvwpDIN 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2269171783 174 EKRDLLILDEPTNHLDVETLTWLESYLQSYA---GALLIVSHD 213
Cdd:PRK03695 150 PAGQLLLLDEPMNSLDVAQQAALDRLLSELCqqgIAVVMSSHD 192
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-213 |
3.23e-06 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 49.07 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 22 RVALVGRNGAGKSTLLKMIAGETvPDEGQIsmrkgltigyLAQDQGLDSQNTiweemssvfAELhaieKRMHA-LENQLS 100
Cdd:COG4138 24 LIHLIGPNGAGKSTLLARMAGLL-PGQGEI----------LLNGRPLSDWSA---------AEL----ARHRAyLSQQQS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 101 DPAIMnddQAYQQ-TLKTYDQVQTEFQQkngygyqAEIRGVLHGFQFDaDVYDKSVTELSGGQ-------KTQLALAKLL 172
Cdd:COG4138 80 PPFAM---PVFQYlALHQPAGASSEAVE-------QLLAQLAEALGLE-DKLSRPLTQLSGGEwqrvrlaAVLLQVWPTI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2269171783 173 LEKRDLLILDEPTNHLDVE----TLTWLESYLQSyAGALLIVSHD 213
Cdd:COG4138 149 NPEGQLLLLDEPMNSLDVAqqaaLDRLLRELCQQ-GITVVMSSHD 192
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
341-493 |
3.31e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 49.28 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQaVFGTGVvtgyydqeqrNLNDKKTVLSEL---------WDEH- 410
Cdd:PRK13637 27 NIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGK-IIIDGV----------DITDKKVKLSDIrkkvglvfqYPEYq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 411 --PTTPEKDI---------------RTILESFLFTGADV----DKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHL 469
Cdd:PRK13637 96 lfEETIEKDIafgpinlglseeeieNRVKRAMNIVGLDYedykDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180
....*....|....*....|....*...
gi 2269171783 470 DIDSR-EVLEVALN---DFDGTLLFVSH 493
Cdd:PRK13637 176 DPKGRdEILNKIKElhkEYNMTIILVSH 203
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
21-53 |
3.36e-06 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 48.60 E-value: 3.36e-06
10 20 30
....*....|....*....|....*....|...
gi 2269171783 21 ARVALVGRNGAGKSTLLKMIAGETVPDEGQISM 53
Cdd:COG3840 26 ERVAILGPSGAGKSTLLNLIAGFLPPDSGRILW 58
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
341-527 |
3.60e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 48.99 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVF-GTGVVT----GYYDQEQR------------NLNDKKTVL 403
Cdd:PRK11831 27 SLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdGENIPAmsrsRLYTVRKRmsmlfqsgalftDMNVFDNVA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 404 SELwDEHPTTPEKDIRTI----LESFLFTGADVDKPVHaLSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLEV 479
Cdd:PRK11831 107 YPL-REHTQLPAPLLHSTvmmkLEAVGLRGAAKLMPSE-LSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVK 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2269171783 480 ALNDFDGTL----LFVSHDryfinqvatsVVEVspegteLFLGDYDYYI-DKK 527
Cdd:PRK11831 185 LISELNSALgvtcVVVSHD----------VPEV------LSIADHAYIVaDKK 221
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
11-54 |
3.80e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.91 E-value: 3.80e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMR 54
Cdd:PRK11288 21 DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILID 64
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
9-227 |
3.80e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.02 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 9 LFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMRKgltigylaqdQGLDSQNTIWEEMSSVFAELHAI 88
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFER----------QSIKKDLCTYQKQLCFVGHRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 89 EKRMHALENQLSDpaimnddQAYQQTLKTYDQVQTEFQQKNGYGYQAEIrgvlhgfqfdadvydksvteLSGGQKTQLAL 168
Cdd:PRK13540 86 NPYLTLRENCLYD-------IHFSPGAVGITELCRLFSLEHLIDYPCGL--------------------LSSGQKRQVAL 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2269171783 169 AKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSY---AGALLIVSHDRYFLDRVVNEVYDL 227
Cdd:PRK13540 139 LRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHrakGGAVLLTSHQDLPLNKADYEEYHL 200
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-51 |
4.18e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 49.33 E-value: 4.18e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2269171783 2 RRFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI 51
Cdd:PRK11432 14 KRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQI 63
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
3-244 |
4.20e-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: 4.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 3 RFGAD--VLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQIsmrkgLTIGYlaqDQGLDSQNTIWEEMSS 80
Cdd:cd03252 9 RYKPDgpVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRV-----LVDGH---DLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 81 VFAElHAIEKRMHALENQLSDPAIMNDDQAYQQTLKtydqvqtefqqkngyGYQAEIRGVLHGfqfdadvYDKSVTE--- 157
Cdd:cd03252 81 VLQE-NVLFNRSIRDNIALADPGMSMERVIEAAKLA---------------GAHDFISELPEG-------YDTIVGEqga 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 158 -LSGGQKTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSY-AGALLIVSHDRYFL----DRVV-----NEVYD 226
Cdd:cd03252 138 gLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDIcAGRTVIIIAHRLSTvknaDRIIvmekgRIVEQ 217
|
250
....*....|....*...
gi 2269171783 227 LSHHEMVHYTGNYDQFVQ 244
Cdd:cd03252 218 GSHDELLAENGLYAYLYQ 235
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
323-519 |
4.65e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 48.63 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 323 TVKDAAVGYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGY----------YDQE 392
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWsskafarkvaYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 393 QRNLNDKKTVlSEL-------WdeHPTTPE---KDIRTILESFLFTGAdvdKP-----VHALSGGERARLLLTKLAMQND 457
Cdd:PRK10575 93 QLPAAEGMTV-RELvaigrypW--HGALGRfgaADREKVEEAISLVGL---KPlahrlVDSLSGGERQRAWIAMLVAQDS 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2269171783 458 NFLILDEPTNHLDIDSR-EVLEVA--LNDFDG-TLLFVSHD-----RYFINQVATSVVEVSPEGT--ELFLGD 519
Cdd:PRK10575 167 RCLLLDEPTSALDIAHQvDVLALVhrLSQERGlTVIAVLHDinmaaRYCDYLVALRGGEMIAQGTpaELMRGE 239
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
2-228 |
4.77e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.54 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 2 RRFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGeTVPD---EGQI--------------SMRKGLTIgylaq 64
Cdd:PRK13549 13 KTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIifegeelqasnirdTERAGIAI----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 65 dqgldsqntIWEEMSSVfaelhaieKRMHALEN-----QLSDPAIMNDDQAYQQTLKTYDQVqtefqqkngygyqaeirg 139
Cdd:PRK13549 87 ---------IHQELALV--------KELSVLENiflgnEITPGGIMDYDAMYLRAQKLLAQL------------------ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 140 vlhgfQFDADVYDKsVTELSGGQKTQLALAKLLLEKRDLLILDEPTNHL---DVETLTWLESYLQSYAGALLIVSHDryf 216
Cdd:PRK13549 132 -----KLDINPATP-VGNLGLGQQQLVEIAKALNKQARLLILDEPTASLtesETAVLLDIIRDLKAHGIACIYISHK--- 202
|
250
....*....|..
gi 2269171783 217 ldrvVNEVYDLS 228
Cdd:PRK13549 203 ----LNEVKAIS 210
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
11-212 |
4.78e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 48.89 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMrkgltigylaqdQGLDsqntIWEEMssvfAELHAIEK 90
Cdd:PRK13637 24 DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIII------------DGVD----ITDKK----VKLSDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 91 RMHAL----ENQLSDPAIMNDdqayqqtlktydqvqTEFQQKNGYGYQAEI----RGVLHGFQFDADVY-DKSVTELSGG 161
Cdd:PRK13637 84 KVGLVfqypEYQLFEETIEKD---------------IAFGPINLGLSEEEIenrvKRAMNIVGLDYEDYkDKSPFELSGG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2269171783 162 QKTQLALAKLLLEKRDLLILDEPTNHLDV----ETLTWLESYLQSYAGALLIVSH 212
Cdd:PRK13637 149 QKRRVAIAGVVAMEPKILILDEPTAGLDPkgrdEILNKIKELHKEYNMTIILVSH 203
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-51 |
4.86e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 48.52 E-value: 4.86e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2269171783 2 RRFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI 51
Cdd:PRK11247 20 KRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL 69
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
11-81 |
5.18e-06 |
|
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: 48.07 E-value: 5.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI-------------SMRKglTIGYLAQDQGLDSQNTIWEE 77
Cdd:cd03295 18 NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIfidgedireqdpvELRR--KIGYVIQQIGLFPHMTVEEN 95
|
....
gi 2269171783 78 MSSV 81
Cdd:cd03295 96 IALV 99
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
313-470 |
5.38e-06 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 48.49 E-value: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 313 AAKQSGNIVLTVKDAAVGYDG-HILSepD-NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVfgTGVVtgYYD 390
Cdd:COG1117 3 APASTLEPKIEVRNLNVYYGDkQALK--DiNLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGARV--EGEI--LLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 391 QEqrNLNDKKTVLSEL------------------WD-------EHPTTPEKDIRTILESFLfTGA----DV----DKPVH 437
Cdd:COG1117 77 GE--DIYDPDVDVVELrrrvgmvfqkpnpfpksiYDnvayglrLHGIKSKSELDEIVEESL-RKAalwdEVkdrlKKSAL 153
|
170 180 190
....*....|....*....|....*....|....
gi 2269171783 438 ALSGGERARLLLTK-LAMQNDnFLILDEPTNHLD 470
Cdd:COG1117 154 GLSGGQQQRLCIARaLAVEPE-VLLMDEPTSALD 186
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
341-481 |
5.40e-06 |
|
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: 47.99 E-value: 5.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSIL-------GQIpFIKGQAVFGTGVVT-----GYYDQEQRNLNDkkTVLSELWD 408
Cdd:cd03254 23 NFSIKPGETVAIVGPTGAGKTTLINLLMrfydpqkGQI-LIDGIDIRDISRKSlrsmiGVVLQDTFLFSG--TIMENIRL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 409 EHPTTPEKDIRTILE--------SFLFTGAD--VDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLE 478
Cdd:cd03254 100 GRPNATDEEVIEAAKeagahdfiMKLPNGYDtvLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQ 179
|
...
gi 2269171783 479 VAL 481
Cdd:cd03254 180 EAL 182
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
342-527 |
5.97e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 48.19 E-value: 5.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 342 LNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQA-VFGTgVVTGYYDQEQRNL-------NDKKTVLSELWDEHPTT 413
Cdd:PRK13647 26 LSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkVMGR-EVNAENEKWVRSKvglvfqdPDDQVFSSTVWDDVAFG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 414 P------EKDIRTILESFLftgADV------DKPVHALSGGERARLLLTK-LAMQNDnFLILDEPTNHLDIDSREVLEVA 480
Cdd:PRK13647 105 PvnmgldKDEVERRVEEAL---KAVrmwdfrDKPPYHLSYGQKKRVAIAGvLAMDPD-VIVLDEPMAYLDPRGQETLMEI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2269171783 481 LNDFDG---TLLFVSHDRYFINQVATSVVeVSPEGTELFLGDYDYYIDKK 527
Cdd:PRK13647 181 LDRLHNqgkTVIVATHDVDLAAEWADQVI-VLKEGRVLAEGDKSLLTDED 229
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
9-64 |
6.82e-06 |
|
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: 47.46 E-value: 6.82e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2269171783 9 LFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMRKglTIGYLAQ 64
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAYVSQ 73
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
321-478 |
9.10e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 47.11 E-value: 9.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 321 VLTVKDAAVGYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKsIL--------GQIpFIKGQAVFGTGvvtgyyDQE 392
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLR-ILaglarpdaGEV-LWQGEPIRRQR------DEY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 393 QRNL------NDKKTVLSELwdE--------HPTTPEKDIRTILESFLFTG-ADVdkPVHALSGGERARLLLTKLAMQND 457
Cdd:PRK13538 73 HQDLlylghqPGIKTELTAL--EnlrfyqrlHGPGDDEALWEALAQVGLAGfEDV--PVRQLSAGQQRRVALARLWLTRA 148
|
170 180
....*....|....*....|.
gi 2269171783 458 NFLILDEPTNHLDIDSREVLE 478
Cdd:PRK13538 149 PLWILDEPFTAIDKQGVARLE 169
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
23-212 |
1.02e-05 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 48.57 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 23 VALVGRNGAGKSTLLKMIAGETVPDEGQISmrkgltigylaqdqgLDSQNTiwEEMSSVFaeLHaiekRMHALENQlsDP 102
Cdd:TIGR00958 510 VALVGPSGSGKSTVAALLQNLYQPTGGQVL---------------LDGVPL--VQYDHHY--LH----RQVALVGQ--EP 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 103 AIMN----DDQAYQQTLKTYDQVQTEFQQKNGYGYqaeIRGVLHGFqfDADVYDKSvTELSGGQKTQLALAKLLLEKRDL 178
Cdd:TIGR00958 565 VLFSgsvrENIAYGLTDTPDEEIMAAAKAANAHDF---IMEFPNGY--DTEVGEKG-SQLSGGQKQRIAIARALVRKPRV 638
|
170 180 190
....*....|....*....|....*....|....
gi 2269171783 179 LILDEPTNHLDVETLTWLESYLQSYAGALLIVSH 212
Cdd:TIGR00958 639 LILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
341-494 |
1.10e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 47.77 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTF---LKSIL----GQIPFIkgqavfgtgvvtgYYDQEqrnlNDKKTVLSELWDE---- 409
Cdd:PRK13651 27 SVEINQGEFIAIIGQTGSGKTTFiehLNALLlpdtGTIEWI-------------FKDEK----NKKKTKEKEKVLEklvi 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 410 HPTTPEK-----DIR-----------------TILESFLF----------------------TGADVD---KPVHALSGG 442
Cdd:PRK13651 90 QKTRFKKikkikEIRrrvgvvfqfaeyqlfeqTIEKDIIFgpvsmgvskeeakkraakyielVGLDESylqRSPFELSGG 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2269171783 443 ERARLLLTK-LAMQNDnFLILDEPTNHLD-IDSREVLEV--ALNDFDGTLLFVSHD 494
Cdd:PRK13651 170 QKRRVALAGiLAMEPD-FLVFDEPTAGLDpQGVKEILEIfdNLNKQGKTIILVTHD 224
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
348-493 |
1.22e-05 |
|
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: 47.08 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 348 EAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGYydqEQRNLNDKKTVLSElwdeHPTTPEKDIR-------- 419
Cdd:cd03248 41 EVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQY---EHKYLHSKVSLVGQ----EPVLFARSLQdniayglq 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 420 -----TILESFLFTGA-------------DVDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLEVAL 481
Cdd:cd03248 114 scsfeCVKEAAQKAHAhsfiselasgydtEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQAL 193
|
170
....*....|....
gi 2269171783 482 NDF--DGTLLFVSH 493
Cdd:cd03248 194 YDWpeRRTVLVIAH 207
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
10-275 |
1.29e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 47.31 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 10 FDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI---------SMRKGLTIGYLAQDQGLDSQNTIWEemss 80
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTivgdyaipaNLKKIKEVKRLRKEIGLVFQFPEYQ---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 81 VFAElhAIEKRMHALENQLSDpaimNDDQAYQQTLKTYDQVQtefqqkngygyqaeirgvlhgfqFDADVYDKSVTELSG 160
Cdd:PRK13645 103 LFQE--TIEKDIAFGPVNLGE----NKQEAYKKVPELLKLVQ-----------------------LPEDYVKRSPFELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 161 GQKTQLALAKLLLEKRDLLILDEPTNHLDV----ETLTWLESYLQSYAGALLIVSHDRYFLDRVVNEVYDLSHHEMVHYT 236
Cdd:PRK13645 154 GQKRRVALAGIIAMDGNTLVLDEPTGGLDPkgeeDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2269171783 237 GNYDQFV-QEKAARIQAQ-WKHYEKQQAEISKLEDFVNRNI 275
Cdd:PRK13645 234 SPFEIFSnQELLTKIEIDpPKLYQLMYKLKNKGIDLLNKNI 274
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
341-470 |
1.53e-05 |
|
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: 46.50 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPfikgqavfGTGVVTG--YYDQEQRNlndKKTVL--------SELWDEH 410
Cdd:cd03234 27 SLHVESGQVMAILGSSGSGKTTLLDAISGRVE--------GGGTTSGqiLFNGQPRK---PDQFQkcvayvrqDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 411 PTTPE---------------KDIRTILESFLFTGADVDKPV-----HALSGGERARLLLTKLAMQNDNFLILDEPTNHLD 470
Cdd:cd03234 96 LTVREtltytailrlprkssDAIRKKRVEDVLLRDLALTRIggnlvKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
11-189 |
1.70e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 47.05 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQIsmrkgltigyLAQDQGLDSQN--TIWEEMSSVFAELhai 88
Cdd:PRK13648 26 KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI----------FYNNQAITDDNfeKLRKHIGIVFQNP--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 89 ekrmhalENQLSDpAIMNDDQAY--QQTLKTYDQVQTEFQQkngygyqaeirgVLHgfqfDADVYDKSVTE---LSGGQK 163
Cdd:PRK13648 93 -------DNQFVG-SIVKYDVAFglENHAVPYDEMHRRVSE------------ALK----QVDMLERADYEpnaLSGGQK 148
|
170 180
....*....|....*....|....*.
gi 2269171783 164 TQLALAKLLLEKRDLLILDEPTNHLD 189
Cdd:PRK13648 149 QRVAIAGVLALNPSVIILDEATSMLD 174
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
11-51 |
1.82e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.80 E-value: 1.82e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI 51
Cdd:PRK10982 15 DNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSI 55
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
9-212 |
1.87e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 46.50 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 9 LFDNVQM----DIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISM-----------RKGLTIgyLAQDQGLDSQNT 73
Cdd:PRK10771 10 LYHHLPMrfdlTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLngqdhtttppsRRPVSM--LFQENNLFSHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 74 IWEEMSsvfAELHAIEKRMHALENQLSDPAimnddqayqqtlktyDQVQTEfqqkngygyqaeirgvlhgfqfdaDVYDK 153
Cdd:PRK10771 88 VAQNIG---LGLNPGLKLNAAQREKLHAIA---------------RQMGIE------------------------DLLAR 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2269171783 154 SVTELSGGQKTQLALAKLLLEKRDLLILDEPTNHLD----VETLTWLESYLQSYAGALLIVSH 212
Cdd:PRK10771 126 LPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQERQLTLLMVSH 188
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
11-51 |
1.98e-05 |
|
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: 46.27 E-value: 1.98e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI 51
Cdd:COG4181 29 KGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTV 69
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
322-510 |
2.05e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 46.62 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 322 LTVKDAAVGYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPF------IKGQAVFGTGVVTGYYDQEQ-- 393
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYqhgsitLDGKPVEGPGAERGVVFQNEgl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 394 ---RNLNDKKTVLSELWDEHPTTPEKDIRTILESFLFTGADvDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLD 470
Cdd:PRK11248 82 lpwRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2269171783 471 IDSREVLEVAL----NDFDGTLLFVSHDryfINQ---VATSVVEVSP 510
Cdd:PRK11248 161 AFTREQMQTLLlklwQETGKQVLLITHD---IEEavfMATELVLLSP 204
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-99 |
2.06e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 46.52 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 1 MRRFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMRkGLTIgylaqdQGLDSQNTIWEEMSS 80
Cdd:PRK11300 12 MMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLR-GQHI------EGLPGHQIARMGVVR 84
|
90
....*....|....*....
gi 2269171783 81 VFAELHAIeKRMHALENQL 99
Cdd:PRK11300 85 TFQHVRLF-REMTVIENLL 102
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
322-506 |
2.46e-05 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 46.28 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 322 LTVKDAAVGYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSI-LGQIPfIKGQAVFGTGVVTG--YYDQEQR---- 394
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInLLEQP-EAGTIRVGDITIDTarSLSQQKGlirq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 395 ------------NLNDKKTVLSELWdEHPTTPEKDI--------RTILESFLFTGADVDKPvHALSGGERARLLLTK-LA 453
Cdd:PRK11264 83 lrqhvgfvfqnfNLFPHRTVLENII-EGPVIVKGEPkeeataraRELLAKVGLAGKETSYP-RRLSGGQQQRVAIARaLA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2269171783 454 MQNDNFLiLDEPTNHLDID-SREVLEV--ALNDFDGTLLFVSHDRYFINQVATSVV 506
Cdd:PRK11264 161 MRPEVIL-FDEPTSALDPElVGEVLNTirQLAQEKRTMVIVTHEMSFARDVADRAI 215
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
11-214 |
2.50e-05 |
|
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: 46.06 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI-------------SMRKGltIGYLAQDQGLDSqNTIwee 77
Cdd:cd03254 20 KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlidgidirdisrkSLRSM--IGVVLQDTFLFS-GTI--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 78 mssvfaelhaiekrmhaLEN-QLSDPaiMNDDQAYQQTLKtydQVQ-TEFQQK--NGYGYQAEIRGvlhgfqfdadvydk 153
Cdd:cd03254 94 -----------------MENiRLGRP--NATDEEVIEAAK---EAGaHDFIMKlpNGYDTVLGENG-------------- 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2269171783 154 svTELSGGQKTQLALAKLLLEKRDLLILDEPTNHLDVETltwlESYLQSyagALLIVSHDR 214
Cdd:cd03254 138 --GNLSQGERQLLAIARAMLRDPKILILDEATSNIDTET----EKLIQE---ALEKLMKGR 189
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
9-231 |
2.56e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.72 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 9 LFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMRKGLT------------IGYLAQDQGLDSqNTIWE 76
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNlkdinlkwwrskIGVVSQDPLLFS-NSIKN 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 77 EMSSVFAELhaieKRMHALENQLSDPAIMNDDQA-------------YQQTLKTYD-----QVQTEFQQ-KNGYGYQAEI 137
Cdd:PTZ00265 479 NIKYSLYSL----KDLEALSNYYNEDGNDSQENKnkrnscrakcagdLNDMSNTTDsneliEMRKNYQTiKDSEVVDVSK 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 138 RGVLHGFQFD-ADVYDKSV----TELSGGQKTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYAG----ALL 208
Cdd:PTZ00265 555 KVLIHDFVSAlPDKYETLVgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGnenrITI 634
|
250 260
....*....|....*....|...
gi 2269171783 209 IVSHdRYFLDRVVNEVYDLSHHE 231
Cdd:PTZ00265 635 IIAH-RLSTIRYANTIFVLSNRE 656
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
341-498 |
2.91e-05 |
|
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: 45.81 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKsILGQIpfikGQAVFGTGVVTGyydQEQRNLNDKKtvLSELWDE--------HPT 412
Cdd:TIGR02211 25 SLSIGKGEIVAIVGSSGSGKSTLLH-LLGGL----DNPTSGEVLFNG---QSLSKLSSNE--RAKLRNKklgfiyqfHHL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 413 TPEkdiRTILES----FLFTGADVD----------KPVH----------ALSGGERARLLLTKLAMQNDNFLILDEPTNH 468
Cdd:TIGR02211 95 LPD---FTALENvampLLIGKKSVKeakerayemlEKVGlehrinhrpsELSGGERQRVAIARALVNQPSLVLADEPTGN 171
|
170 180 190
....*....|....*....|....*....|....
gi 2269171783 469 LDID-SREVLEV--ALNDFDGT-LLFVSHDRYFI 498
Cdd:TIGR02211 172 LDNNnAKIIFDLmlELNRELNTsFLVVTHDLELA 205
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-218 |
2.92e-05 |
|
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: 46.21 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 23 VALVGRNGAGKSTLLKMIAGETVPDegqismrkgltigyLAQDQGLDSqntiWEEMSSVFA--ELHAIEKRMhaLENQLs 100
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLKPN--------------LGKFDDPPD----WDEILDEFRgsELQNYFTKL--LEGDV- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 101 DPAI--MNDDQAYQQT-------LKTYDqvqtEFQQKNGYGYQAEIRGVLhgfqfdadvyDKSVTELSGGQKTQLALAKL 171
Cdd:cd03236 88 KVIVkpQYVDLIPKAVkgkvgelLKKKD----ERGKLDELVDQLELRHVL----------DRNIDQLSGGELQRVAIAAA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2269171783 172 LLEKRDLLILDEPTNHLDVE---TLTWLESYLQSYAGALLIVSHDRYFLD 218
Cdd:cd03236 154 LARDADFYFFDEPSSYLDIKqrlNAARLIRELAEDDNYVLVVEHDLAVLD 203
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
341-493 |
2.95e-05 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 47.08 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSIL-------GQIpFIKGQAVfgtgvvtgyydqeqRNLNdkktvLSELWDEhptt 413
Cdd:COG1132 360 SLTIPPGETVALVGPSGSGKSTLVNLLLrfydptsGRI-LIDGVDI--------------RDLT-----LESLRRQ---- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 414 pekdIRTIL-ESFLFTG------------ADVDKPVHA---------------------------LSGGER-----ARLL 448
Cdd:COG1132 416 ----IGVVPqDTFLFSGtirenirygrpdATDEEVEEAakaaqahefiealpdgydtvvgergvnLSGGQRqriaiARAL 491
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2269171783 449 LtklamQNDNFLILDEPTNHLDIDS-REVLEvALNDF--DGTLLFVSH 493
Cdd:COG1132 492 L-----KDPPILILDEATSALDTETeALIQE-ALERLmkGRTTIVIAH 533
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-221 |
3.01e-05 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 46.62 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 4 FGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMrKGLTIGYL-AQDQgldsqntiweEMSSVF 82
Cdd:PRK10851 12 FGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRF-HGTDVSRLhARDR----------KVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 83 AElHAIEKRMHALENqlsdpaimnddQAYQQTlktydqVQTEFQQKNGYGYQAEIRGVLHGFQFD--ADVYDksvTELSG 160
Cdd:PRK10851 81 QH-YALFRHMTVFDN-----------IAFGLT------VLPRRERPNAAAIKAKVTQLLEMVQLAhlADRYP---AQLSG 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2269171783 161 GQKTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYAGAL----LIVSHDRY----FLDRVV 221
Cdd:PRK10851 140 GQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELkftsVFVTHDQEeameVADRVV 208
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-220 |
3.18e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 46.18 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 9 LFDNVQMDIQEHARVALVGRNGAGKSTLLKMiagetvpdegqismrkgltigyLAQDQGLDSQNTIweEMSSVFAELHAI 88
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC----------------------LNRMNELESEVRV--EGRVEFFNQNIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 89 EKRMHAleNQLSDPAIMNDDQAYQQTLKTYDQVQTEFQQKnGYGYQAEIRGVLHGFQFDADVYD-------KSVTELSGG 161
Cdd:PRK14258 78 ERRVNL--NRLRRQVSMVHPKPNLFPMSVYDNVAYGVKIV-GWRPKLEIDDIVESALKDADLWDeikhkihKSALDLSGG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2269171783 162 QKTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYA----GALLIVSHDRYFLDRV 220
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrseLTMVIVSHNLHQVSRL 217
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
341-478 |
3.31e-05 |
|
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: 46.00 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQ-------------IPF-----------IKGQAVFGTGvvtgyYDQEQRnl 396
Cdd:cd03291 57 NLKIEKGEMLAITGSTGSGKTSLLMLILGElepsegkikhsgrISFssqfswimpgtIKENIIFGVS-----YDEYRY-- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 397 ndkKTVLS--ELWDEHPTTPEKDIRTILESFLftgadvdkpvhALSGGERARLLLTKLAMQNDNFLILDEPTNHLDI-DS 473
Cdd:cd03291 130 ---KSVVKacQLEEDITKFPEKDNTVLGEGGI-----------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVfTE 195
|
....*
gi 2269171783 474 REVLE 478
Cdd:cd03291 196 KEIFE 200
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
341-493 |
3.33e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 45.73 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQaVFGTGvvtgyydQEQRNLNDKKTVLSELWDE----------- 409
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGS-LTLNG-------QDHTTTPPSRRPVSMLFQEnnlfshltvaq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 410 ------HP----TTPEKD-IRTI-----LESFLftgadvDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDS 473
Cdd:PRK10771 91 niglglNPglklNAAQREkLHAIarqmgIEDLL------ARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPAL 164
|
170 180
....*....|....*....|....
gi 2269171783 474 R----EVLEVALNDFDGTLLFVSH 493
Cdd:PRK10771 165 RqemlTLVSQVCQERQLTLLMVSH 188
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
321-493 |
3.69e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 45.92 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 321 VLTVKDAAVGYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSI--LGQ-IPFIkgqavfgtgVVTGYYDQEQRNLN 397
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDlNPEV---------TITGSIVYNGHNIY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 398 DKKTVLSELWDE----------HPTT------------PEKDIRTI---LESFLFTGA---DVDKPVH----ALSGGERA 445
Cdd:PRK14239 76 SPRTDTVDLRKEigmvfqqpnpFPMSiyenvvyglrlkGIKDKQVLdeaVEKSLKGASiwdEVKDRLHdsalGLSGGQQQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2269171783 446 RLLLTKLAMQNDNFLILDEPTNHLD-IDSREVLEVALN-DFDGTLLFVSH 493
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDpISAGKIEETLLGlKDDYTMLLVTR 205
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
11-242 |
3.92e-05 |
|
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: 45.65 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISM---------RKGLT-----IGYLAQDQGLDSQNTIWE 76
Cdd:cd03258 22 KDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVdgtdltllsGKELRkarrrIGMIFQHFNLLSSRTVFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 77 EMssvfaelhaiekrMHALEnqlsdpaIMNDDQAYQqtlktydqvqtefqqkngygyQAEIRGVLH--GFQFDADVYDks 154
Cdd:cd03258 102 NV-------------ALPLE-------IAGVPKAEI---------------------EERVLELLElvGLEDKADAYP-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 155 vTELSGGQKTQLALAKLLLEKRDLLILDEPTNHLDVET----LTWLESYLQSYAGALLIVSHDRYFLDRVVNEVYDLSHH 230
Cdd:cd03258 139 -AQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETtqsiLALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKG 217
|
250
....*....|..
gi 2269171783 231 EMVHYTGNYDQF 242
Cdd:cd03258 218 EVVEEGTVEEVF 229
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
274-470 |
3.94e-05 |
|
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: 47.25 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 274 NIVRASTTKRaqaRRKQLAKMDRIDrPDSDEKtahfgfHAAKQSGNIVLTVKDAAVGYdghILSEPDNLN-----VKKHE 348
Cdd:TIGR00957 599 SIVQASVSLK---RLRIFLSHEELE-PDSIER------RTIKPGEGNSITVHNATFTW---ARDLPPTLNgitfsIPEGA 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 349 AIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVvtGYYDQEQRNLNDkkTVLSELWDEHPTTPeKDIRTILESF--- 425
Cdd:TIGR00957 666 LVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSV--AYVPQQAWIQND--SLRENILFGKALNE-KYYQQVLEACall 740
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2269171783 426 ----LFTGADV----DKPVHaLSGGERARLLLTKLAMQNDNFLILDEPTNHLD 470
Cdd:TIGR00957 741 pdleILPSGDRteigEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
22-53 |
4.31e-05 |
|
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: 45.18 E-value: 4.31e-05
10 20 30
....*....|....*....|....*....|..
gi 2269171783 22 RVALVGRNGAGKSTLLKMIAGETVPDEGQISM 53
Cdd:cd03298 26 ITAIVGPSGSGKSTLLNLIAGFETPQSGRVLI 57
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
341-494 |
5.69e-05 |
|
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: 45.18 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQaVFGTGVVTGYYDQEQRN----------------LNDKKTV-- 402
Cdd:TIGR02769 31 SLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGT-VSFRGQDLYQLDRKQRRafrrdvqlvfqdspsaVNPRMTVrq 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 403 -----LSELWDEHPTTPEKDIRTILESFLFTGADVDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSR--- 474
Cdd:TIGR02769 110 iigepLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQavi 189
|
170 180
....*....|....*....|.
gi 2269171783 475 -EVLEVALNDFDGTLLFVSHD 494
Cdd:TIGR02769 190 lELLRKLQQAFGTAYLFITHD 210
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-246 |
6.12e-05 |
|
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: 46.27 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 4 FGADVLfDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISM---------RKGL--TIGYLAQDQGLDSqN 72
Cdd:TIGR01193 485 YGSNIL-SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLngfslkdidRHTLrqFINYLPQEPYIFS-G 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 73 TIweemssvfaelhaiekrmhaLENQLsdpaIMNDDQAYQQTLKTYDQVqtefqqkngygyqAEIRGVLHGFQ--FDADV 150
Cdd:TIGR01193 563 SI--------------------LENLL----LGAKENVSQDEIWAACEI-------------AEIKDDIENMPlgYQTEL 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 151 YDKSvTELSGGQKTQLALAKLLLEKRDLLILDEPTNHLDVET-LTWLESYLQSYAGALLIVSHdRYFLDRVVNEVYDLSH 229
Cdd:TIGR01193 606 SEEG-SSISGGQKQRIALARALLTDSKVLILDESTSNLDTITeKKIVNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLDH 683
|
250
....*....|....*..
gi 2269171783 230 HEMVHyTGNYDQFVQEK 246
Cdd:TIGR01193 684 GKIIE-QGSHDELLDRN 699
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
341-526 |
6.55e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 45.18 E-value: 6.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGYYDQEQRNL------NDKKTVLSelwdehpTTP 414
Cdd:PRK13652 24 NFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFvglvfqNPDDQIFS-------PTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 415 EKDI---------------RTILESFLFTGAD--VDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVL 477
Cdd:PRK13652 97 EQDIafgpinlgldeetvaHRVSSALHMLGLEelRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2269171783 478 EVALNDFDG----TLLFVSHDryfinqvatsvVEVSPEgtelfLGDYDYYIDK 526
Cdd:PRK13652 177 IDFLNDLPEtygmTVIFSTHQ-----------LDLVPE-----MADYIYVMDK 213
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
12-192 |
6.76e-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: 46.44 E-value: 6.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 12 NVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQIsmRKGLTIGYLAQdqgldsqnTIWEEmssvfaelhaiekr 91
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI--KHSGRISFSPQ--------TSWIM-------------- 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 92 mhalenqlsdPAIMNDDQAYQQtlkTYDQvqtefqqkngYGYqaeiRGVLHGFQFDADVY-----DKSV-----TELSGG 161
Cdd:TIGR01271 500 ----------PGTIKDNIIFGL---SYDE----------YRY----TSVIKACQLEEDIAlfpekDKTVlgeggITLSGG 552
|
170 180 190
....*....|....*....|....*....|.
gi 2269171783 162 QKTQLALAKLLLEKRDLLILDEPTNHLDVET 192
Cdd:TIGR01271 553 QRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
322-493 |
7.50e-05 |
|
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: 44.53 E-value: 7.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 322 LTVKDAAVGYDGH--ILSEPdNLNVKKHEAIAIVGPNGIGKSTFLKSIL-------GQIpFIKGQAVFGtgvVT------ 386
Cdd:cd03253 1 IEFENVTFAYDPGrpVLKDV-SFTIPAGKKVAIVGPSGSGKSTILRLLFrfydvssGSI-LIDGQDIRE---VTldslrr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 387 --GYYDQEQRNLNDkkTVLSELWDEHPTTPEKDIRTILESflftgADVDKPVHA---------------LSGGERARLLL 449
Cdd:cd03253 76 aiGVVPQDTVLFND--TIGYNIRYGRPDATDEEVIEAAKA-----AQIHDKIMRfpdgydtivgerglkLSGGEKQRVAI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2269171783 450 TKLAMQNDNFLILDEPTNHLDIDS-REVLEvALND-FDG-TLLFVSH 493
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTeREIQA-ALRDvSKGrTTIVIAH 194
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
11-221 |
7.65e-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: 45.04 E-value: 7.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAG---ETVPDEGQISMrKGLTIGYLAQDQgldsQNTI-WEEMSSVFAElh 86
Cdd:COG0444 22 DGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILF-DGEDLLKLSEKE----LRKIrGREIQMIFQD-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 87 aiekRMHAL------ENQLSDPAI----MNDDQAYQQTLKTYDQVqtefqqkngygyqaeirgvlhGFQFDADVYDKSVT 156
Cdd:COG0444 95 ----PMTSLnpvmtvGDQIAEPLRihggLSKAEARERAIELLERV---------------------GLPDPERRLDRYPH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 157 ELSGGQKtQlalaklllekR-----------DLLILDEPTNHLDV----ETLTWLESyLQSYAG-ALLIVSHD----RYF 216
Cdd:COG0444 150 ELSGGMR-Q----------RvmiaralalepKLLIADEPTTALDVtiqaQILNLLKD-LQRELGlAILFITHDlgvvAEI 217
|
....*
gi 2269171783 217 LDRVV 221
Cdd:COG0444 218 ADRVA 222
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
6-43 |
8.36e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 44.82 E-value: 8.36e-05
10 20 30
....*....|....*....|....*....|....*...
gi 2269171783 6 ADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGE 43
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGD 50
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
341-511 |
9.20e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 44.59 E-value: 9.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQaVFGTGVVTGYYD--QEQRNL------NDK-----KTVLSEL- 406
Cdd:PRK13644 22 NLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGK-VLVSGIDTGDFSklQGIRKLvgivfqNPEtqfvgRTVEEDLa 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 407 -WDEHPTTPEKDIRTILESFLfTGADVDKPVH----ALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSRE-VLE-- 478
Cdd:PRK13644 101 fGPENLCLPPIEIRKRVDRAL-AEIGLEKYRHrspkTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIaVLEri 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2269171783 479 VALNDFDGTLLFVSH--------DRYFINQVATSVVEVSPE 511
Cdd:PRK13644 180 KKLHEKGKTIVYITHnleelhdaDRIIVMDRGKIVLEGEPE 220
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
23-213 |
9.22e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 44.38 E-value: 9.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 23 VALVGRNGAGKSTLLKMIAGETVPDEGQISMRkGLTIGYLAQDQ--GLDSQNtiweeMSSVFAELHAIEKrMHALEN-QL 99
Cdd:PRK10584 39 IALIGESGSGKSTLLAILAGLDDGSSGEVSLV-GQPLHQMDEEAraKLRAKH-----VGFVFQSFMLIPT-LNALENvEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 100 sdPAIM---NDDQAYQQTLKTYDQVqtefqqknGYGYQaeirgvlhgfqfdadvYDKSVTELSGGQKTQLALAKLLLEKR 176
Cdd:PRK10584 112 --PALLrgeSSRQSRNGAKALLEQL--------GLGKR----------------LDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2269171783 177 DLLILDEPTNHLDVET----LTWLESYLQSYAGALLIVSHD 213
Cdd:PRK10584 166 DVLFADEPTGNLDRQTgdkiADLLFSLNREHGTTLILVTHD 206
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
350-507 |
9.74e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 44.96 E-value: 9.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 350 IAIVGPNGIGKSTfLKSILGQI--P-----FIKGQAVFGtgvvtgyYDQEQRNLNDKKTvlsELWDEHP---TTPEKDIR 419
Cdd:PRK11308 44 LAVVGESGCGKST-LARLLTMIetPtggelYYQGQDLLK-------ADPEAQKLLRQKI---QIVFQNPygsLNPRKKVG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 420 TILESFLFTGADVD-----------------KPVHA------LSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSR-E 475
Cdd:PRK11308 113 QILEEPLLINTSLSaaerrekalammakvglRPEHYdryphmFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQaQ 192
|
170 180 190
....*....|....*....|....*....|....*
gi 2269171783 476 VLEVALN---DFDGTLLFVSHDryfinqvaTSVVE 507
Cdd:PRK11308 193 VLNLMMDlqqELGLSYVFISHD--------LSVVE 219
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
11-51 |
1.01e-04 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 45.21 E-value: 1.01e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI 51
Cdd:PRK11607 36 DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQI 76
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
4-42 |
1.03e-04 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 45.02 E-value: 1.03e-04
10 20 30
....*....|....*....|....*....|....*....
gi 2269171783 4 FGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAG 42
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAG 51
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
7-220 |
1.10e-04 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 44.04 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 7 DVLfDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQIsMRKGLTIGYLAQDQGLDSQNtiwEEMSSVFaELH 86
Cdd:PRK11629 23 DVL-HNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDV-IFNGQPMSKLSSAAKAELRN---QKLGFIY-QFH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 87 AIEKRMHALENqLSDPAI---MNDDQAYQQTLKTYDQVqtefqqknGYGYQAEIRGvlhgfqfdadvydksvTELSGGQK 163
Cdd:PRK11629 97 HLLPDFTALEN-VAMPLLigkKKPAEINSRALEMLAAV--------GLEHRANHRP----------------SELSGGER 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2269171783 164 TQLALAKLLLEKRDLLILDEPTNHLDVET----LTWLESYLQSYAGALLIVSHDRYFLDRV 220
Cdd:PRK11629 152 QRVAIARALVNNPRLVLADEPTGNLDARNadsiFQLLGELNRLQGTAFLVVTHDLQLAKRM 212
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-189 |
1.29e-04 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 44.24 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMrKGLTIgylaqdqgldSQNTIWEemssvfaelhaIEK 90
Cdd:PRK13635 24 KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITV-GGMVL----------SEETVWD-----------VRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 91 RMHAL----ENQLSDpAIMNDDQAYqqTLKTYDQVQTEFQQKngygYQAEIRGVlhGFQfdaDVYDKSVTELSGGQKTQL 166
Cdd:PRK13635 82 QVGMVfqnpDNQFVG-ATVQDDVAF--GLENIGVPREEMVER----VDQALRQV--GME---DFLNREPHRLSGGQKQRV 149
|
170 180
....*....|....*....|...
gi 2269171783 167 ALAKLLLEKRDLLILDEPTNHLD 189
Cdd:PRK13635 150 AIAGVLALQPDIIILDEATSMLD 172
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
5-51 |
1.32e-04 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 44.37 E-value: 1.32e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2269171783 5 GADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI 51
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI 64
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
11-224 |
1.34e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 44.39 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMrKGLTIGYLAQDQGLdsqNTIWEEMSSVFaelhaiek 90
Cdd:PRK13646 24 HDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV-DDITITHKTKDKYI---RPVRKRIGMVF-------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 91 rmHALENQLSDpaimndDQAYQQTLKTYDQVQTEFQQKNGYGYQaeirgVLHGFQFDADVYDKSVTELSGGQKTQLALAK 170
Cdd:PRK13646 92 --QFPESQLFE------DTVEREIIFGPKNFKMNLDEVKNYAHR-----LLMDLGFSRDVMSQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2269171783 171 LLLEKRDLLILDEPTNHLD----VETLTWLESYLQSYAGALLIVSHDRYFLDRVVNEV 224
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDpqskRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEV 216
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
341-481 |
1.37e-04 |
|
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: 45.29 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILG-------------------QIPFI-----KGQAVFGTGvvtgyYDQEQRNL 396
Cdd:TIGR01271 446 SFKLEKGQLLAVAGSTGSGKSSLLMMIMGelepsegkikhsgrisfspQTSWImpgtiKDNIIFGLS-----YDEYRYTS 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 397 NDKKTVLSElwdEHPTTPEKDIRTILESFLftgadvdkpvhALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDS-RE 475
Cdd:TIGR01271 521 VIKACQLEE---DIALFPEKDKTVLGEGGI-----------TLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTeKE 586
|
....*.
gi 2269171783 476 VLEVAL 481
Cdd:TIGR01271 587 IFESCL 592
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
11-189 |
1.37e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 44.21 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMrKGLTIGYLAQDQGLDSQNTIWEEMSSVFAELHAIEK 90
Cdd:PRK13632 26 KNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI-DGITISKENLKEIRKKIGIIFQNPDNQFIGATVEDD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 91 RMHALENQLSDPAIMNDdqayqQTLKTYDQVQTEfqqkngygyqaeirgvlhgfqfdaDVYDKSVTELSGGQKTQLALAK 170
Cdd:PRK13632 105 IAFGLENKKVPPKKMKD-----IIDDLAKKVGME------------------------DYLDKEPQNLSGGQKQRVAIAS 155
|
170
....*....|....*....
gi 2269171783 171 LLLEKRDLLILDEPTNHLD 189
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLD 174
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
11-73 |
1.48e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.88 E-value: 1.48e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMRKGLTIgyLAQDQGLDSQNT 73
Cdd:PRK13545 41 NNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAL--IAISSGLNGQLT 101
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-51 |
1.57e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.12 E-value: 1.57e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2269171783 3 RFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI 51
Cdd:NF033858 10 RYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRV 58
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-185 |
1.67e-04 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 43.67 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 5 GADVLFDnVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISM--------------RKGltIGYLAQDQGLDS 70
Cdd:TIGR03410 12 QSHILRG-VSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLdgeditklppheraRAG--IAYVPQGREIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 71 QNTIWEEMSSVFAELHAIEKRMhalenqlsdpaimnDDQAYQqtlktYDQVQTEFQQKNGygyqaeirgvlhgfqfdadv 150
Cdd:TIGR03410 89 RLTVEENLLTGLAALPRRSRKI--------------PDEIYE-----LFPVLKEMLGRRG-------------------- 129
|
170 180 190
....*....|....*....|....*....|....*
gi 2269171783 151 ydksvTELSGGQKTQLALAKLLLEKRDLLILDEPT 185
Cdd:TIGR03410 130 -----GDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
2-224 |
1.68e-04 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 43.59 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 2 RRFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQIsmRKG-LTIG---YLAQDQGLDSQntIWEE 77
Cdd:PRK11264 11 KKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTI--RVGdITIDtarSLSQQKGLIRQ--LRQH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 78 MSSVFAELHAIEKRMhALENQLSDPAIMND---DQAYQQTLKTYDQVqtefqqkngygyqaeirgvlhGFQFDADVYDKs 154
Cdd:PRK11264 87 VGFVFQNFNLFPHRT-VLENIIEGPVIVKGepkEEATARARELLAKV---------------------GLAGKETSYPR- 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2269171783 155 vtELSGGQKTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYAG---ALLIVSHDRYFLDRVVNEV 224
Cdd:PRK11264 144 --RLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQekrTMVIVTHEMSFARDVADRA 214
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
322-493 |
1.73e-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: 43.17 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 322 LTVKDAAVGYDGHILSEPDNLN--VKKHEAIAIVGPNGIGKSTFLKSIL-------GQIPfIKGQAVFGTGVVTgyydqe 392
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLKNVSfkVKAGEKIGIVGRTGAGKSTLILALFrfleaeeGKIE-IDGIDISTIPLED------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 393 qrnLNDKKTVLSElwdeHPTTPEKDIRTILESF-------LFTGADVDKPVHALSGGERARLLLTKLAMQNDNFLILDEP 465
Cdd:cd03369 80 ---LRSSLTIIPQ----DPTLFSGTIRSNLDPFdeysdeeIYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEA 152
|
170 180 190
....*....|....*....|....*....|
gi 2269171783 466 TNHLDIDS-REVLEVALNDF-DGTLLFVSH 493
Cdd:cd03369 153 TASIDYATdALIQKTIREEFtNSTILTIAH 182
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
354-500 |
1.77e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 43.01 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 354 GPNGIGKSTFLKSILGQIPFIKGQAVF-GTGV---VTGYYDQ-----EQRNLNDKKTVLSE-LWDEHPTTPEKDIRTILE 423
Cdd:PRK13540 34 GSNGAGKTTLLKLIAGLLNPEKGEILFeRQSIkkdLCTYQKQlcfvgHRSGINPYLTLRENcLYDIHFSPGAVGITELCR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 424 SFLFtGADVDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLEVALNDF---DGTLLFVSHDRYFINQ 500
Cdd:PRK13540 114 LFSL-EHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHrakGGAVLLTSHQDLPLNK 192
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
341-493 |
1.83e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 43.95 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGYYDQEQRNLNDKKTVL------SELWDE----- 409
Cdd:PRK13643 26 DLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVvfqfpeSQLFEEtvlkd 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 410 ----------HPTTPEKDIRTILESFLFTGADVDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSR-EVLE 478
Cdd:PRK13643 106 vafgpqnfgiPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARiEMMQ 185
|
170
....*....|....*..
gi 2269171783 479 V--ALNDFDGTLLFVSH 493
Cdd:PRK13643 186 LfeSIHQSGQTVVLVTH 202
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-233 |
1.92e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 44.31 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 2 RRFGADVLFDNVQMDIQEHARVALVGRNGAGKST----LLKMIAGEtvpdeGQISMrKGLTIGYLAQDQGLdsqnTIWEE 77
Cdd:PRK15134 294 RTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ-----GEIWF-DGQPLHNLNRRQLL----PVRHR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 78 MSSVFAELH-AIEKRMHALEnqlsdpAIMNDDQAYQQTLKTYDQvqtefqqkngygyQAEIRGVLHGFQFDADVYDKSVT 156
Cdd:PRK15134 364 IQVVFQDPNsSLNPRLNVLQ------IIEEGLRVHQPTLSAAQR-------------EQQVIAVMEEVGLDPETRHRYPA 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 157 ELSGGQKTQLALAKLLLEKRDLLILDEPTNHLD----VETLTWLESYLQSYAGALLIVSHDRYFLDRVVNEVYDLSHHEM 232
Cdd:PRK15134 425 EFSGGQRQRIAIARALILKPSLIILDEPTSSLDktvqAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEV 504
|
.
gi 2269171783 233 V 233
Cdd:PRK15134 505 V 505
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
340-512 |
2.08e-04 |
|
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: 42.70 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 340 DNLNVKKHEAIAIVGPNGIGKSTFLKSILgqipfikgqavfgtgvvtgyYDQEQRNLNDkktvLSELWDEHPTTPEKDIR 419
Cdd:cd03238 14 LDVSIPLNVLVVVTGVSGSGKSTLVNEGL--------------------YASGKARLIS----FLPKFSRNKLIFIDQLQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 420 TILESFLfTGADVDKPVHALSGGERARLLLTKLAMQN--DNFLILDEPTNHLD-IDSREVLEV--ALNDFDGTLLFVSHD 494
Cdd:cd03238 70 FLIDVGL-GYLTLGQKLSTLSGGELQRVKLASELFSEppGTLFILDEPSTGLHqQDINQLLEVikGLIDLGNTVILIEHN 148
|
170
....*....|....*...
gi 2269171783 495 RYFINQvATSVVEVSPEG 512
Cdd:cd03238 149 LDVLSS-ADWIIDFGPGS 165
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
11-51 |
2.34e-04 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 43.91 E-value: 2.34e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI 51
Cdd:COG1135 22 DDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSV 62
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
322-493 |
2.64e-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: 42.99 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 322 LTVKDAAVGYDGHILSEPDNLN--VKKHEAIAIVGPNGIGKSTFLKSIL-------GQIpFIKGQAVFG---------TG 383
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISldIPAGETVALVGPSGSGKSTLVNLIPrfydvdsGRI-LIDGHDVRDytlaslrrqIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 384 VVTgyydQEQRNLNDkkTVLSELWDEHPTTPEKDIRtilesflftgaDVDKPVHA---------------------LSGG 442
Cdd:cd03251 80 LVS----QDVFLFND--TVAENIAYGRPGATREEVE-----------EAARAANAhefimelpegydtvigergvkLSGG 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2269171783 443 ERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLEVALNDF--DGTLLFVSH 493
Cdd:cd03251 143 QRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLmkNRTTFVIAH 195
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
3-214 |
2.69e-04 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 42.78 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 3 RFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGqismrkglTIGYLAQDQGLDSQNTIWEEMSSVF 82
Cdd:PRK10247 16 LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSG--------TLLFEGEDISTLKPEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 83 aelhaiekrmhalenqlSDPAIMNDdqayqqtlKTYDQVQTEFQQKNGYGYQAEIRGVLHGFQFDADVYDKSVTELSGGQ 162
Cdd:PRK10247 88 -----------------QTPTLFGD--------TVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGE 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2269171783 163 KTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYAG----ALLIVSHDR 214
Cdd:PRK10247 143 KQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVReqniAVLWVTHDK 198
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
322-506 |
2.98e-04 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 43.03 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 322 LTVKDAAVGYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGYYDQE-QRNLNDKK 400
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgQLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 401 ------TVLS------ELWdEHPTTPEKDIRTILESFLFTGAD--------VDK-----------PVHaLSGGERARLLL 449
Cdd:PRK10619 86 qlrllrTRLTmvfqhfNLW-SHMTVLENVMEAPIQVLGLSKQEareravkyLAKvgideraqgkyPVH-LSGGQQQRVSI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2269171783 450 TK-LAMQNDnFLILDEPTNHLDID-SREVLEV--ALNDFDGTLLFVSHDRYFINQVATSVV 506
Cdd:PRK10619 164 ARaLAMEPE-VLLFDEPTSALDPElVGEVLRImqQLAEEGKTMVVVTHEMGFARHVSSHVI 223
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
12-51 |
3.12e-04 |
|
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: 42.51 E-value: 3.12e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2269171783 12 NVQMDIQEHARVALVGRNGAGKSTLLKMIAG--ETVPDEGQI 51
Cdd:cd03217 18 GVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEI 59
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
12-116 |
3.26e-04 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 42.56 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 12 NVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMR-KGLTIGYLAQdqgldsqntIWEEMSSVFAELHAIEK 90
Cdd:PRK11614 23 EVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDgKDITDWQTAK---------IMREAVAIVPEGRRVFS 93
|
90 100
....*....|....*....|....*.
gi 2269171783 91 RMHALENqLSDPAIMNDDQAYQQTLK 116
Cdd:PRK11614 94 RMTVEEN-LAMGGFFAERDQFQERIK 118
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
9-53 |
3.41e-04 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 42.64 E-value: 3.41e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2269171783 9 LFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGE--TVPDEGQISM 53
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAlkGTPVAGCVDV 91
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
22-212 |
3.66e-04 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 42.16 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 22 RVALVGRNGAGKSTLLKMIAGETVPDEGQISMrkgltigylaQDQGLDSQNTIWEEMSSVFAElhaiekrmHALENQLSd 101
Cdd:TIGR01277 26 IVAIMGPSGAGKSTLLNLIAGFIEPASGSIKV----------NDQSHTGLAPYQRPVSMLFQE--------NNLFAHLT- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 102 pAIMNDDQAYQQTLKTYDQVQTEFQQKngygyqAEIRGVlhgfqfdADVYDKSVTELSGGQKTQLALAKLLLEKRDLLIL 181
Cdd:TIGR01277 87 -VRQNIGLGLHPGLKLNAEQQEKVVDA------AQQVGI-------ADYLDRLPEQLSGGQRQRVALARCLVRPNPILLL 152
|
170 180 190
....*....|....*....|....*....|....*
gi 2269171783 182 DEPTNHLD----VETLTWLESYLQSYAGALLIVSH 212
Cdd:TIGR01277 153 DEPFSALDpllrEEMLALVKQLCSERQRTLLMVTH 187
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
11-250 |
4.02e-04 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 42.57 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISM--------------RKGltIGYLAQDqgldsqntiwe 76
Cdd:PRK10895 20 EDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddedisllplharaRRG--IGYLPQE----------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 77 emSSVFAELHAIEKRMHALEnqlsdpaiMNDDQAYQQTLKTYDQVQTEFQqkngygyqaeirgVLHgfqfdadVYDKSVT 156
Cdd:PRK10895 87 --ASIFRRLSVYDNLMAVLQ--------IRDDLSAEQREDRANELMEEFH-------------IEH-------LRDSMGQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 157 ELSGGQKTQLALAKLLLEKRDLLILDEPTNHLD---VETLTWLESYLQSYAGALLIVSHD-RYFLDrVVNEVYDLSHHEM 232
Cdd:PRK10895 137 SLSGGERRRVEIARALAANPKFILLDEPFAGVDpisVIDIKRIIEHLRDSGLGVLITDHNvRETLA-VCERAYIVSQGHL 215
|
250
....*....|....*...
gi 2269171783 233 VHYTGNYDQFVQEKAARI 250
Cdd:PRK10895 216 IAHGTPTEILQDEHVKRV 233
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
437-506 |
4.54e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 43.16 E-value: 4.54e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2269171783 437 HALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLEVALNDFDG----TLLFVSHDRYFINQVATSVV 506
Cdd:PRK15134 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelnmGLLFITHNLSIVRKLADRVA 228
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
439-493 |
4.63e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 43.47 E-value: 4.63e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2269171783 439 LSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLEVALNDF--DGTLLFVSH 493
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELqkNRTSLVIAH 537
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
316-501 |
4.65e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.43 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 316 QSGNIVLTVKDAAVGYDGHiLSEPD----NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVtGYYDQ 391
Cdd:PLN03232 609 QPGAPAISIKNGYFSWDSK-TSKPTlsdiNLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSV-AYVPQ 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 392 EQRNLNdkKTVLSELWDEHPTTPEKDIRTILESF------LFTGADV----DKPVHaLSGGERARLLLTKLAMQNDNFLI 461
Cdd:PLN03232 687 VSWIFN--ATVRENILFGSDFESERYWRAIDVTAlqhdldLLPGRDLteigERGVN-ISGGQKQRVSMARAVYSNSDIYI 763
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2269171783 462 LDEPTNHLDID-SREVLEVALND-FDG-TLLFVSHDRYFINQV 501
Cdd:PLN03232 764 FDDPLSALDAHvAHQVFDSCMKDeLKGkTRVLVTNQLHFLPLM 806
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
23-51 |
4.67e-04 |
|
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: 41.20 E-value: 4.67e-04
10 20
....*....|....*....|....*....
gi 2269171783 23 VALVGRNGAGKSTLLKMIAGETVPDEGQI 51
Cdd:smart00382 5 ILIVGPPGSGKTTLARALARELGPPGGGV 33
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
24-65 |
4.82e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 42.94 E-value: 4.82e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 24 ALVGRNGAGKSTLLKMIAGETVPDEGQISM------------------RKgltIGYLAQD 65
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLngrvlfdaekgiclppekRR---IGYVFQD 84
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
13-213 |
5.36e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 42.53 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 13 VQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQIsMRKGLTIGYLAQdqGLdsqNTIWEEMSSVFAELhaiekrm 92
Cdd:PRK13636 25 ININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI-LFDGKPIDYSRK--GL---MKLRESVGMVFQDP------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 93 halENQLSDPAIMNDDQAYQQTLK-TYDQVQTEFQQKngygyqAEIRGVLHgfqfdadVYDKSVTELSGGQKTQLALAKL 171
Cdd:PRK13636 92 ---DNQLFSASVYQDVSFGAVNLKlPEDEVRKRVDNA------LKRTGIEH-------LKDKPTHCLSFGQKKRVAIAGV 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2269171783 172 LLEKRDLLILDEPTNHLD----VETLTWLESYLQSYAGALLIVSHD 213
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHD 201
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
341-481 |
5.61e-04 |
|
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: 43.17 E-value: 5.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 341 NLNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQAVFGTGVVTGYYDQEQRN-----------LNDkkTVLSEL-WD 408
Cdd:TIGR02203 352 SLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRqvalvsqdvvlFND--TIANNIaYG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 409 EHPTTPEKDIRTILE-SFLFTGAD-----VDKPVHA----LSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLE 478
Cdd:TIGR02203 430 RTEQADRAEIERALAaAYAQDFVDklplgLDTPIGEngvlLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQ 509
|
...
gi 2269171783 479 VAL 481
Cdd:TIGR02203 510 AAL 512
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
4-213 |
6.36e-04 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 41.90 E-value: 6.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 4 FGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMrKGLTIGYLAQDQgldsqntiweemssvfa 83
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWL-DGEHIQHYASKE----------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 84 elhaIEKRMHALENQLSDPAIMNDDQAYQQTLKTYDQVQTEFQQKNGYGYQAEIR--GVLHgfqfdadVYDKSVTELSGG 161
Cdd:PRK10253 79 ----VARRIGLLAQNATTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQatGITH-------LADQSVDTLSGG 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2269171783 162 QKTQLALAKLLLEKRDLLILDEPTNHLDVE---TLTWLESYLQSYAG-ALLIVSHD 213
Cdd:PRK10253 148 QRQRAWIAMVLAQETAIMLLDEPTTWLDIShqiDLLELLSELNREKGyTLAAVLHD 203
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
13-192 |
7.69e-04 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 41.92 E-value: 7.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 13 VQMDIQEHARVALVGRNGAGKSTLLK----MIAGETVPdEGQISMRkGLTI---GYLAQDQGLDSQNTiweemSSVFAEL 85
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSA-GSHIELL-GRTVqreGRLARDIRKSRANT-----GYIFQQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 86 HAIeKRMHALENQLSdpAIMNDDQAYQQTLKTYDQVQTEfqqkngYGYQAEIR-GVLHgfqfdadVYDKSVTELSGGQKT 164
Cdd:PRK09984 96 NLV-NRLSVLENVLI--GALGSTPFWRTCFSWFTREQKQ------RALQALTRvGMVH-------FAHQRVSTLSGGQQQ 159
|
170 180
....*....|....*....|....*...
gi 2269171783 165 QLALAKLLLEKRDLLILDEPTNHLDVET 192
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPES 187
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
12-51 |
7.90e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 41.70 E-value: 7.90e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2269171783 12 NVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI 51
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEL 70
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
10-52 |
8.37e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 42.50 E-value: 8.37e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2269171783 10 FDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQIS 52
Cdd:PRK11160 356 LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEIL 398
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
350-494 |
8.38e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.15 E-value: 8.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 350 IAIVGPNGIGKSTFLKSIL---------------------------------------------GQIPFIKG-----QAV 379
Cdd:COG0419 26 NLIVGPNGAGKSTILEAIRyalygkarsrsklrsdlinvgseeasvelefehggkryrierrqgEFAEFLEAkpserKEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 380 FGTGVVTGYYDQEQRNLNDKKTVLSELWDEhpttpeKDIRTILESFLFTGADVDKPVHALSGGERARLLLTKLAMqndnf 459
Cdd:COG0419 106 LKRLLGLEIYEELKERLKELEEALESALEE------LAELQKLKQEILAQLSGLDPIETLSGGERLRLALADLLS----- 174
|
170 180 190
....*....|....*....|....*....|....*
gi 2269171783 460 LILDepTNHLDIDSREVLEVALNDfdgtLLFVSHD 494
Cdd:COG0419 175 LILD--FGSLDEERLERLLDALEE----LAIITHV 203
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
177-225 |
8.47e-04 |
|
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: 41.05 E-value: 8.47e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2269171783 177 DLLILDEPTNHLDVETLTW-----LESYLQSYAGALLIVSHDRYFLDRvVNEVY 225
Cdd:cd03240 141 GILALDEPTTNLDEENIEEslaeiIEERKSQKNFQLIVITHDEELVDA-ADHIY 193
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
434-515 |
8.54e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 8.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 434 KPVHALSGGERARLLLTK---LAMQNDNFLILDEPTNHLDI-DSREVLEV--ALNDFDGTLLFVSHDRYFInQVATSVVE 507
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAYellAPSKKPTLYVLDEPTTGLHThDIKALIYVlqSLTHQGHTVVIIEHNMHVV-KVADYVLE 883
|
....*...
gi 2269171783 508 VSPEGTEL 515
Cdd:PRK00635 884 LGPEGGNL 891
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3-214 |
8.82e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 42.26 E-value: 8.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 3 RFGADVLFDNVQM----------DIQEHAR----VALVGRNGAGKSTLLKMIAGETVPDEGQISM---------RKGL-- 57
Cdd:PRK13657 330 RVKGAVEFDDVSFsydnsrqgveDVSFEAKpgqtVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdgtdirtvtRASLrr 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 58 TIGYLAQDQGLDSQnTIWEEMS-----SVFAELHAIEKRMHALEnqlsdpaimnddqayqqtlktydqvqteFQQKNGYG 132
Cdd:PRK13657 410 NIAVVFQDAGLFNR-SIEDNIRvgrpdATDEEMRAAAERAQAHD----------------------------FIERKPDG 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 133 YQAEI--RGvlhgfqfdadvydksvTELSGGQKTQLALAKLLLEKRDLLILDEPTNHLDVETltwlESYLQsyaGALLIV 210
Cdd:PRK13657 461 YDTVVgeRG----------------RQLSGGERQRLAIARALLKDPPILILDEATSALDVET----EAKVK---AALDEL 517
|
....
gi 2269171783 211 SHDR 214
Cdd:PRK13657 518 MKGR 521
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
11-213 |
9.95e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 41.64 E-value: 9.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMrkgltigyLAQDQGLDSQNTIWEEMSSVFaelhaiek 90
Cdd:PRK13647 22 KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKV--------MGREVNAENEKWVRSKVGLVF-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 91 rmhalenqlSDPaimnDDQAYQQTLktYDQVQteFQQKNGYGYQAEI----RGVLHGFQFDaDVYDKSVTELSGGQKTQL 166
Cdd:PRK13647 86 ---------QDP----DDQVFSSTV--WDDVA--FGPVNMGLDKDEVerrvEEALKAVRMW-DFRDKPPYHLSYGQKKRV 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2269171783 167 ALAKLLLEKRDLLILDEPTNHLD---VETLTWLESYLQSYAGALLIVSHD 213
Cdd:PRK13647 148 AIAGVLAMDPDVIVLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHD 197
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
336-469 |
1.15e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 41.14 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 336 LSEPDNLNVkkheaiaIVGPNGIGKSTFLKSI----------LGQIPF----IKGQAVFGTGVVTGYYDQEQRNLNDKKT 401
Cdd:COG3950 21 FDNPPRLTV-------LVGENGSGKTTLLEAIalalsgllsrLDDVKFrkllIRNGEFGDSAKLILYYGTSRLLLDGPLK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 402 VLSEL--------------------------W-DEHPTTPEKD-----------IRTILESFL--FTGADVDK------- 434
Cdd:COG3950 94 KLERLkeeyfsrldgydslldedsnlrefleWlREYLEDLENKlsdeldekleaVREALNKLLpdFKDIRIDRdpgrlvi 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2269171783 435 --------PVHALSGGERARL-LLTKLAMQ------------NDNFLIL-DEPTNHL 469
Cdd:COG3950 174 ldkngeelPLNQLSDGERSLLaLVGDLARRlaelnpalenplEGEGIVLiDEIDLHL 230
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-51 |
1.19e-03 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 42.01 E-value: 1.19e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2269171783 3 RFGADVLfDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI 51
Cdd:PRK10790 351 RDDNLVL-QNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEI 398
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
27-215 |
1.21e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 40.60 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 27 GRNGAGKSTLLKMIAGETVPDEGQISMrkgltigylaqdQGLDSQNTIWEEMSSVFAELHAIEKRMHALENQlsdpaimn 106
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQI------------DGKTATRGDRSRFMAYLGHLPGLKADLSTLENL-------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 107 ddqAYQQTLKTYDQVQTEfqqkngyGYQAEIRGVlhgfqfdADVYDKSVTELSGGQKTQLALAKLLLEKRDLLILDEPTN 186
Cdd:PRK13543 104 ---HFLCGLHGRRAKQMP-------GSALAIVGL-------AGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYA 166
|
170 180 190
....*....|....*....|....*....|..
gi 2269171783 187 HLDVETLTWLESYLQSY---AGALLIVSHDRY 215
Cdd:PRK13543 167 NLDLEGITLVNRMISAHlrgGGAALVTTHGAY 198
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
23-211 |
1.27e-03 |
|
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: 40.61 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 23 VALVGRNGAGKSTLLKMIAG--ETVPDEGQI----------SMRKglTIGYLAQDQGLDSQNTIWEEMSsvfaelhaiek 90
Cdd:cd03213 38 TAIMGPSGAGKSTLLNALAGrrTGLGVSGEVlingrpldkrSFRK--IIGYVPQDDILHPTLTVRETLM----------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 91 rmhalenqlsdpaimnddqayqqtlktydqvqtefqqkngygYQAEIRGvlhgfqfdadvydksvteLSGGQKTQLALAK 170
Cdd:cd03213 105 ------------------------------------------FAAKLRG------------------LSGGERKRVSIAL 124
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2269171783 171 LLLEKRDLLILDEPTNHLDVETLTWLESYLQSYA--GALLIVS 211
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAdtGRTIICS 167
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
13-52 |
1.30e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 41.37 E-value: 1.30e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2269171783 13 VQMDIQEHARVALVGRNGAGKSTLLKMIAG-ETVpDEGQIS 52
Cdd:PRK11650 23 IDLDVADGEFIVLVGPSGCGKSTLLRMVAGlERI-TSGEIW 62
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
13-183 |
1.32e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 41.88 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 13 VQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQIsmrkgltigyLAQDQGLDSQNtiWEE----MSSVFAELHAI 88
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI----------LLDGKPVTAEQ--PEDyrklFSAVFTDFHLF 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 89 EKRMHAlENQLSDPAIMnddQAYQQTLKTYDQVQtefqqkngygyqaeirgvLHGFQFdadvydkSVTELSGGQKTQLAL 168
Cdd:PRK10522 410 DQLLGP-EGKPANPALV---EKWLERLKMAHKLE------------------LEDGRI-------SNLKLSKGQKKRLAL 460
|
170
....*....|....*
gi 2269171783 169 AKLLLEKRDLLILDE 183
Cdd:PRK10522 461 LLALAEERDILLLDE 475
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
9-192 |
1.46e-03 |
|
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: 40.68 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 9 LFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI-------------SMRKglTIGYLAQDQGLdSQNTIW 75
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSIlidgqdirevtldSLRR--AIGVVPQDTVL-FNDTIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 76 EEMSsvFAELHAiekrmhalenqlsdpaimNDDQAYQQTLKtydqvqtefqqkngygyqAEIRGVLHGFQfdaDVYDKSV 155
Cdd:cd03253 93 YNIR--YGRPDA------------------TDEEVIEAAKA------------------AQIHDKIMRFP---DGYDTIV 131
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2269171783 156 TE----LSGGQKTQLALAKLLLEKRDLLILDEPTNHLDVET 192
Cdd:cd03253 132 GErglkLSGGEKQRVAIARAILKNPPILLLDEATSALDTHT 172
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-65 |
1.52e-03 |
|
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: 40.47 E-value: 1.52e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2269171783 3 RFGADV--LFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQIS-------------MRKGLTIgyLAQD 65
Cdd:cd03369 15 RYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEidgidistipledLRSSLTI--IPQD 90
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
11-73 |
1.52e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.95 E-value: 1.52e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISmRKGlTIGYLAQDQGLDSQNT 73
Cdd:PRK13546 41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD-RNG-EVSVIAISAGLSGQLT 101
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
11-220 |
1.58e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 40.87 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMrkgltigylaqDQGLDSQNTIWEEMssvfaelHAIEK 90
Cdd:PRK13650 24 NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIII-----------DGDLLTEENVWDIR-------HKIGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 91 RMHALENQLSDpAIMNDDQAyqqtlktydqvqteFQQKN-GYGYQAEIRGVLHGFQF--DADVYDKSVTELSGGQKTQLA 167
Cdd:PRK13650 86 VFQNPDNQFVG-ATVEDDVA--------------FGLENkGIPHEEMKERVNEALELvgMQDFKEREPARLSGGQKQRVA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2269171783 168 LAKLLLEKRDLLILDEPTNHLD----VETLTWLESYLQSYAGALLIVSHDryfLDRV 220
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD---LDEV 204
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
8-42 |
1.65e-03 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 41.33 E-value: 1.65e-03
10 20 30
....*....|....*....|....*....|....*
gi 2269171783 8 VLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAG 42
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG 411
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
7-42 |
1.80e-03 |
|
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: 39.44 E-value: 1.80e-03
10 20 30
....*....|....*....|....*....|....*.
gi 2269171783 7 DVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAG 42
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG 49
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
319-494 |
1.81e-03 |
|
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: 40.49 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 319 NIVLTVKDAAvgydG--HILSEPDnLNVKKHEAIAIVGPNGIGKSTFLkSIL--------GQIpFIKGQAVFGtgvvtgy 388
Cdd:COG4181 13 GLTKTVGTGA----GelTILKGIS-LEVEAGESVAIVGASGSGKSTLL-GLLagldrptsGTV-RLAGQDLFA------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 389 YDQEQR-------------------NLndkkTVLselwdEHPTTP-----EKDIRTILESFLFT---GADVDkpvHA--- 438
Cdd:COG4181 79 LDEDARarlrarhvgfvfqsfqllpTL----TAL-----ENVMLPlelagRRDARARARALLERvglGHRLD---HYpaq 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2269171783 439 LSGGER-----ARLLLTKLAMqndnfLILDEPTNHLDIDSREV---LEVALNDFDG-TLLFVSHD 494
Cdd:COG4181 147 LSGGEQqrvalARAFATEPAI-----LFADEPTGNLDAATGEQiidLLFELNRERGtTLVLVTHD 206
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
10-37 |
1.93e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 36.81 E-value: 1.93e-03
10 20
....*....|....*....|....*...
gi 2269171783 10 FDNVQMDIQEHARVALVGRNGAGKSTLL 37
Cdd:pfam13555 12 FDGHTIPIDPRGNTLLTGPSGSGKSTLL 39
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
570-651 |
2.10e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 570 QASKQQQREKRKLERTVAALEEQMTTLDEQATKIQTEMAQpevsADVGRLTDLQKELDEISAQQEQVETEWTEQAEALEA 649
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRG----NGGDRLEQLEREIERLERELEERERRRARLEALLAA 370
|
..
gi 2269171783 650 FD 651
Cdd:COG4913 371 LG 372
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
27-212 |
2.13e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.85 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 27 GRNGAGKSTLLKMIAGETVPDEGQISMRKGLT-------IGYLAQDQGLDSQNTIWEEMsSVFAELhaiekrmhalenql 99
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNInniakpyCTYIGHNLGLKLEMTVFENL-KFWSEI-------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 100 sdpaimnddqayqqtlktYDQVQTefqqkngygyqaeIRGVLHGFQFDaDVYDKSVTELSGGQKTQLALAKLLLEKRDLL 179
Cdd:PRK13541 98 ------------------YNSAET-------------LYAAIHYFKLH-DLLDEKCYSLSSGMQKIVAIARLIACQSDLW 145
|
170 180 190
....*....|....*....|....*....|....*.
gi 2269171783 180 ILDEPTNHLDVETLTWLESYLQSYA---GALLIVSH 212
Cdd:PRK13541 146 LLDEVETNLSKENRDLLNNLIVMKAnsgGIVLLSSH 181
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
4-51 |
2.14e-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: 40.61 E-value: 2.14e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2269171783 4 FGADVLfDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI 51
Cdd:cd03291 48 VGAPVL-KNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI 94
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
321-520 |
2.30e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 40.16 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 321 VLTVKDAAVGYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSILG------------------------------- 369
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGredyevtggtvefkgkdllelspedragegi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 370 --------QIPFIKGQAVFGTGV--VTGYYDQEQRNLNDKKTVLSELWDEHPTTPEKDIRTILESFlftgadvdkpvhal 439
Cdd:PRK09580 81 fmafqypvEIPGVSNQFFLQTALnaVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGF-------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 440 SGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLEVALNDF-DGTLLF--VSHDRYFINQVATSVVEVSPEGTELF 516
Cdd:PRK09580 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLrDGKRSFiiVTHYQRILDYIKPDYVHVLYQGRIVK 226
|
....
gi 2269171783 517 LGDY 520
Cdd:PRK09580 227 SGDF 230
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
11-220 |
2.60e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 40.45 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGqismrkglTIGYLAQDQGLDSQNTIWEEM----------SS 80
Cdd:PRK13651 24 DNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTG--------TIEWIFKDEKNKKKTKEKEKVleklviqktrFK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 81 VFAELHAIEKRMHAL----ENQLSDPAIMND------------DQAYQQTLKTYDQVQtefqqkngygyqaeirgvlhgf 144
Cdd:PRK13651 96 KIKKIKEIRRRVGVVfqfaEYQLFEQTIEKDiifgpvsmgvskEEAKKRAAKYIELVG---------------------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 145 qFDADVYDKSVTELSGGQKTQLALAKLLLEKRDLLILDEPTNHLD----VETLTWLESyLQSYAGALLIVSHDryfLDRV 220
Cdd:PRK13651 154 -LDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgvKEILEIFDN-LNKQGKTIILVTHD---LDNV 228
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
24-51 |
2.62e-03 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 40.16 E-value: 2.62e-03
10 20
....*....|....*....|....*...
gi 2269171783 24 ALVGRNGAGKSTLLKMIAGETVPDEGQI 51
Cdd:PRK10575 41 GLIGHNGSGKSTLLKMLGRHQPPSEGEI 68
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
322-494 |
2.65e-03 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 40.44 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 322 LTVKDAAVGYDGHILSEPDNLNVKKHEAIAIVGPNGIGKSTFLKSI--L-----GQIpFIKGQAVfgTGVVTgyydqEQR 394
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIagLedptsGEI-LIGGRDV--TDLPP-----KDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 395 N---------LNDKKTV---------LSELwdehpttPEKDIRTI---------LESFLftgadvDKPVHALSGGER--- 444
Cdd:COG3839 76 NiamvfqsyaLYPHMTVyeniafplkLRKV-------PKAEIDRRvreaaellgLEDLL------DRKPKQLSGGQRqrv 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2269171783 445 --ARllltKLAMQNDNFLiLDEPTNHLDIDSREVLEVAL----NDFDGTLLFVSHD 494
Cdd:COG3839 143 alGR----ALVREPKVFL-LDEPLSNLDAKLRVEMRAEIkrlhRRLGTTTIYVTHD 193
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
438-517 |
2.65e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.17 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 438 ALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLEVALNDF----DGTLLFVSHDRYFINQVATSVVEVSPEGT 513
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdkaDKTIITIAHRIASIKRSDKIVVFNNPDRT 1437
|
....
gi 2269171783 514 ELFL 517
Cdd:PTZ00265 1438 GSFV 1441
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
342-505 |
2.80e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 40.03 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 342 LNVKKHEAIAIVGPNGIGKSTFLKsILGQIPFIKGQAVFGTGVVTgYYDQEQRNLNDKK------TVLSE--------LW 407
Cdd:PRK14246 31 IKIPNNSIFGIMGPSGSGKSTLLK-VLNRLIEIYDSKIKVDGKVL-YFGKDIFQIDAIKlrkevgMVFQQpnpfphlsIY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 408 D-------EHPTTPEKDIRTILESFLFTGA-------DVDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDS 473
Cdd:PRK14246 109 DniayplkSHGIKEKREIKKIVEECLRKVGlwkevydRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVN 188
|
170 180 190
....*....|....*....|....*....|....
gi 2269171783 474 REVLEVALNDF--DGTLLFVSHDRYFINQVATSV 505
Cdd:PRK14246 189 SQAIEKLITELknEIAIVIVSHNPQQVARVADYV 222
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
11-189 |
2.83e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 40.17 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISM--RKGLTIGylaqdqgldsQNTIW---EEMSSVFAEL 85
Cdd:PRK13640 24 NDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKitVDGITLT----------AKTVWdirEKVGIVFQNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 86 haiekrmhalENQLSDpAIMNDDQAyqqtlktydqvqteFQQKNGYGYQAEIRGVLHGFQFDADVYDKSVTE---LSGGQ 162
Cdd:PRK13640 94 ----------DNQFVG-ATVGDDVA--------------FGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEpanLSGGQ 148
|
170 180
....*....|....*....|....*..
gi 2269171783 163 KTQLALAKLLLEKRDLLILDEPTNHLD 189
Cdd:PRK13640 149 KQRVAIAGILAVEPKIIILDESTSMLD 175
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
264-495 |
3.17e-03 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 40.71 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 264 ISKLE---DFVNRNIVrasttkrAQARRKQLAKM-----DRIDRPDsdektahfgfhaAKQSGNIVLTV--KDAAVGYDG 333
Cdd:PRK13657 286 IGRLDqvvAFINQVFM-------AAPKLEEFFEVedavpDVRDPPG------------AIDLGRVKGAVefDDVSFSYDN 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 334 hilSEP--DNLN--VKKHEAIAIVGPNGIGKSTFLkSIL--------GQIpFIKGQAVFGT---------GVVTgyydQE 392
Cdd:PRK13657 347 ---SRQgvEDVSfeAKPGQTVAIVGPTGAGKSTLI-NLLqrvfdpqsGRI-LIDGTDIRTVtraslrrniAVVF----QD 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 393 QRNLNdkKTVLSELWDEHPTTPEKDIRTILES-----FLFTGAD-----VDKPVHALSGGERARLLLTKLAMQNDNFLIL 462
Cdd:PRK13657 418 AGLFN--RSIEDNIRVGRPDATDEEMRAAAERaqahdFIERKPDgydtvVGERGRQLSGGERQRLAIARALLKDPPILIL 495
|
250 260 270
....*....|....*....|....*....|...
gi 2269171783 463 DEPTNHLDIDSREVLEVALNDfdgtllfVSHDR 495
Cdd:PRK13657 496 DEATSALDVETEAKVKAALDE-------LMKGR 521
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
4-189 |
3.44e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 40.00 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 4 FGADVLFDnVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQIsmrkglTIGylaqdqgldsQNTIWEEMSSvfA 83
Cdd:PRK13634 18 FERRALYD-VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTV------TIG----------ERVITAGKKN--K 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 84 ELHAIEKRMHAL----ENQLSDPAIMNDdqayqqtlktydqvqTEFQQKNgYGYQAE-----IRGVLHGFQFDADVYDKS 154
Cdd:PRK13634 79 KLKPLRKKVGIVfqfpEHQLFEETVEKD---------------ICFGPMN-FGVSEEdakqkAREMIELVGLPEELLARS 142
|
170 180 190
....*....|....*....|....*....|....*
gi 2269171783 155 VTELSGGQKTQLALAKLLLEKRDLLILDEPTNHLD 189
Cdd:PRK13634 143 PFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
439-486 |
3.72e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.78 E-value: 3.72e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2269171783 439 LSGGERARLLLTKLAMQNDNFLILDEPTNHLDIDSREVLEVALNDFDG 486
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKG 627
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-257 |
3.73e-03 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 39.61 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 4 FGAD-VLFDnVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISmrkgltigyLAQDQGLDSQNTIWEEMSS-- 80
Cdd:PRK11124 12 YGAHqALFD-ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLN---------IAGNHFDFSKTPSDKAIRElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 81 -----VFAELHaIEKRMHALENQLSDP---AIMNDDQAYQQTLKTYDQVQ-TEFQQkngygyqaeiRGVLHgfqfdadvy 151
Cdd:PRK11124 82 rnvgmVFQQYN-LWPHLTVQQNLIEAPcrvLGLSKDQALARAEKLLERLRlKPYAD----------RFPLH--------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 152 dksvteLSGGQKTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLESYLQSYAG---ALLIVSHDRYFLDRVVNEVYDLS 228
Cdd:PRK11124 142 ------LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtgiTQVIVTHEVEVARKTASRVVYME 215
|
250 260
....*....|....*....|....*....
gi 2269171783 229 HHEMVHyTGNYDQFVQEKAariqAQWKHY 257
Cdd:PRK11124 216 NGHIVE-QGDASCFTQPQT----EAFKNY 239
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
11-233 |
3.84e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 39.68 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQIsMRKGLTIGY-------LAQDQGLDSQNTiweemssvfa 83
Cdd:PRK13639 19 KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEV-LIKGEPIKYdkkslleVRKTVGIVFQNP---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 84 elhaiekrmhalENQLSDPAIMNDDQAYQQTLK-TYDQVQTEFQQkngygyqAEIRGVLHGFQfdadvyDKSVTELSGGQ 162
Cdd:PRK13639 88 ------------DDQLFAPTVEEDVAFGPLNLGlSKEEVEKRVKE-------ALKAVGMEGFE------NKPPHHLSGGQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2269171783 163 KTQLALAKLLLEKRDLLILDEPTNHLD---VETLTWLESYLQSYAGALLIVSHDRYFLDRVVNEVYDLSHHEMV 233
Cdd:PRK13639 143 KKRVAIAGILAMKPEIIVLDEPTSGLDpmgASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKII 216
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
351-475 |
3.91e-03 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 38.83 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 351 AIVGPNGIGKSTFLKSILgqipfikgqavfgtgVVTGYYDQEQRNlNDKKTVLSElwDEHPTTPEKDIRTILES--FLFT 428
Cdd:cd03239 26 AIVGPNGSGKSNIVDAIC---------------FVLGGKAAKLRR-GSLLFLAGG--GVKAGINSASVEITFDKsyFLVL 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2269171783 429 GADVDKpvhALSGGERARL-LLTKLAMQNDN---FLILDEPTNHLDIDSRE 475
Cdd:cd03239 88 QGKVEQ---ILSGGEKSLSaLALIFALQEIKpspFYVLDEIDAALDPTNRR 135
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
10-41 |
3.93e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 39.60 E-value: 3.93e-03
10 20 30
....*....|....*....|....*....|...
gi 2269171783 10 FDNVQMDIQEHARV-ALVGRNGAGKSTLLKMIA 41
Cdd:COG3950 14 FEDLEIDFDNPPRLtVLVGENGSGKTTLLEAIA 46
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
436-495 |
4.11e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 4.11e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2269171783 436 VHALSGGERA------RLLLTKLAMQNDNFLILDEPTNHLDIDSR----EVLEVALNDFDG--TLLFVSHDR 495
Cdd:PRK01156 799 IDSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRtnlkDIIEYSLKDSSDipQVIMISHHR 870
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
12-54 |
4.47e-03 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 39.25 E-value: 4.47e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2269171783 12 NVQMDIQEHARVALVGRNGAGKSTLLK----MIagETVPD---EGQISMR 54
Cdd:COG1117 29 DINLDIPENKVTALIGPSGCGKSTLLRclnrMN--DLIPGarvEGEILLD 76
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
11-42 |
5.64e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.77 E-value: 5.64e-03
10 20 30
....*....|....*....|....*....|....*
gi 2269171783 11 DNVQMDIQE---HArvaLVGRNGAGKSTLLKMIAG 42
Cdd:NF040905 18 DDVNLSVREgeiHA---LCGENGAGKSTLMKVLSG 49
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
342-512 |
5.95e-03 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 38.90 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 342 LNVKKHEAIAIVGPNGIGKSTFLKSILGQIPFIKGQaVFGTGVVTGYYDQEQRN----------------LNDKKTV--- 402
Cdd:PRK10419 33 LSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGN-VSWRGEPLAKLNRAQRKafrrdiqmvfqdsisaVNPRKTVrei 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 403 ----LSELWDEHPTTPEKDIRTILESFLFTGADVDKPVHALSGGERARLLLTKLAMQNDNFLILDEPTNHLDIdsreVLE 478
Cdd:PRK10419 112 irepLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDL----VLQ 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2269171783 479 VALND--------FDGTLLFVSHD----RYFINQVAT----SVVEVSPEG 512
Cdd:PRK10419 188 AGVIRllkklqqqFGTACLFITHDlrlvERFCQRVMVmdngQIVETQPVG 237
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-51 |
6.86e-03 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 39.16 E-value: 6.86e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2269171783 2 RRFGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQI 51
Cdd:PRK09452 22 KSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRI 71
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-198 |
6.90e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 38.74 E-value: 6.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 4 FGADVLFDNVQMDIQEHARVALVGRNGAGKSTLLKMIAG--ETVPDegqismrkgltiGYLAQDQGLDSQNTIWEEMSsv 81
Cdd:PRK14247 13 FGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPE------------ARVSGEVYLDGQDIFKMDVI-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 82 faELHAIEKRMHALENQLSDPAIMnDDQAYQQTLKTYDQVQTEFQQKngygyqaeIRGVLHGFQFDADVYDK---SVTEL 158
Cdd:PRK14247 79 --ELRRRVQMVFQIPNPIPNLSIF-ENVALGLKLNRLVKSKKELQER--------VRWALEKAQLWDEVKDRldaPAGKL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2269171783 159 SGGQKTQLALAKLLLEKRDLLILDEPTNHLDVETLTWLES 198
Cdd:PRK14247 148 SGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIES 187
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
433-506 |
7.76e-03 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 38.93 E-value: 7.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 433 DKPVHALSGGER-----ARLLLTKLAMqndnfLILDEPTNHLDIDSR-EVLEV--ALND-FDGTLLFVSHDRYFINQVAT 503
Cdd:COG4148 128 DRRPATLSGGERqrvaiGRALLSSPRL-----LLMDEPLAALDLARKaEILPYleRLRDeLDIPILYVSHSLDEVARLAD 202
|
...
gi 2269171783 504 SVV 506
Cdd:COG4148 203 HVV 205
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
564-649 |
8.02e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.37 E-value: 8.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 564 KGQQDYQAskqQQREKRKLERTVAALEEQMTTLDEQATKIQTEM--AQPEVSADVGRLTDLQKELDEISAQQEQVETEWT 641
Cdd:COG1579 86 RNNKEYEA---LQKEIESLKRRISDLEDEILELMERIEELEEELaeLEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
....*...
gi 2269171783 642 EQAEALEA 649
Cdd:COG1579 163 AEREELAA 170
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
11-191 |
8.37e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 38.68 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 11 DNVQMDIQEHARVALVGRNGAGKSTLLKMIAGETVPDEGQISMRKgLTIGylaqdQGLDSQNTIWEEMSSVFAELHAIEK 90
Cdd:PRK13631 43 NNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGD-IYIG-----DKKNNHELITNPYSKKIKNFKELRR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 91 RMHAL----ENQLSDPAIMNDDQAYQQTLKtydQVQTEFQQKNGYgyqaeirgVLHGFQFDADVYDKSVTELSGGQKTQL 166
Cdd:PRK13631 117 RVSMVfqfpEYQLFKDTIEKDIMFGPVALG---VKKSEAKKLAKF--------YLNKMGLDDSYLERSPFGLSGGQKRRV 185
|
170 180
....*....|....*....|....*
gi 2269171783 167 ALAKLLLEKRDLLILDEPTNHLDVE 191
Cdd:PRK13631 186 AIAGILAIQPEILIFDEPTAGLDPK 210
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
24-51 |
9.45e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 38.83 E-value: 9.45e-03
10 20
....*....|....*....|....*...
gi 2269171783 24 ALVGRNGAGKSTLLKMIAGETVPDEGQI 51
Cdd:PRK10762 34 ALVGENGAGKSTMMKVLTGIYTRDAGSI 61
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
25-189 |
9.48e-03 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 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. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 38.63 E-value: 9.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 25 LVGRNGAGKSTLLKMIAGETVPDEGQISM-----------RKGltIGYLAQDQGLDSQNTIWEEMssvfaelhAIEKRMH 93
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLdgedvtnvpphLRH--INMVFQSYALFPHMTVEENV--------AFGLKMR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 94 ALENQLSDPAIMnddqayqQTLKTydqVQTEfqqknGYGyqaeirgvlhgfqfdadvyDKSVTELSGGQKTQLALAKLLL 173
Cdd:TIGR01187 71 KVPRAEIKPRVL-------EALRL---VQLE-----EFA-------------------DRKPHQLSGGQQQRVALARALV 116
|
170
....*....|....*.
gi 2269171783 174 EKRDLLILDEPTNHLD 189
Cdd:TIGR01187 117 FKPKILLLDEPLSALD 132
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
24-192 |
9.53e-03 |
|
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: 38.22 E-value: 9.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 24 ALVGRNGAGKSTLLKMIAGETVPDEGQISMR-KGLTigyLAQDQGLDSQntiweeMSSVfaelhaiekrmhALENQLSDP 102
Cdd:cd03248 44 ALVGPSGSGKSTVVALLENFYQPQGGQVLLDgKPIS---QYEHKYLHSK------VSLV------------GQEPVLFAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2269171783 103 AImNDDQAYQQTLKTYDQVqTEFQQKngYGYQAEIRGVLHGFQFDADvydKSVTELSGGQKTQLALAKLLLEKRDLLILD 182
Cdd:cd03248 103 SL-QDNIAYGLQSCSFECV-KEAAQK--AHAHSFISELASGYDTEVG---EKGSQLSGGQKQRVAIARALIRNPQVLILD 175
|
170
....*....|
gi 2269171783 183 EPTNHLDVET 192
Cdd:cd03248 176 EATSALDAES 185
|
|
| |
