|
Name |
Accession |
Description |
Interval |
E-value |
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-158 |
1.73e-90 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 263.87 E-value: 1.73e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEGVAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGG 80
Cdd:COG1116 63 PTSGEVLVDGKPVTGPGPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGG 142
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861249672 81 MRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRmpiKSVLIVTHNIEEAVFMCDRILVLSSNPG 158
Cdd:COG1116 143 MRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETG---KTVLFVTHDVDEAVFLADRVVVLSARPG 217
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1-158 |
1.60e-86 |
|
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: 252.39 E-value: 1.60e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEGVAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGG 80
Cdd:cd03293 56 PTSGEVLVDGEPVTGPGPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGG 135
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861249672 81 MRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRmpiKSVLIVTHNIEEAVFMCDRILVLSSNPG 158
Cdd:cd03293 136 MRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETG---KTVLLVTHDIDEAVFLADRVVVLSARPG 210
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-158 |
2.15e-63 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 195.08 E-value: 2.15e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEGVAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGG 80
Cdd:COG4525 59 PSSGEITLDGVPVTGPGADRGVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGG 138
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861249672 81 MRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRmpiKSVLIVTHNIEEAVFMCDRILVLSSNPG 158
Cdd:COG4525 139 MRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTG---KGVFLITHSVEEALFLATRLVVMSPGPG 213
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-153 |
3.08e-61 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 193.40 E-value: 3.08e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTG--PAE-------GVAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFEN 71
Cdd:COG4175 79 PTAGEVLIDGEDITKlsKKElrelrrkKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWED 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 72 AYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLtaetLRTD----LLDLwtQGRMPiKSVLIVTHNIEEAVFMC 147
Cdd:COG4175 159 SYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPL----IRREmqdeLLEL--QAKLK-KTIVFITHDLDEALRLG 231
|
....*.
gi 1861249672 148 DRILVL 153
Cdd:COG4175 232 DRIAIM 237
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1-154 |
2.58e-59 |
|
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: 183.10 E-value: 2.58e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTG-PAE--GVAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPREL 77
Cdd:cd03259 52 PDSGEILIDGRDVTGvPPErrNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHEL 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861249672 78 SGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRMPiksVLIVTHNIEEAVFMCDRILVLS 154
Cdd:cd03259 132 SGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGIT---TIYVTHDQEEALALADRIAVMN 205
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-154 |
2.76e-57 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 182.22 E-value: 2.76e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTG-PAE--GVAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPREL 77
Cdd:COG3842 57 PDSGRILLDGRDVTGlPPEkrNVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQL 136
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861249672 78 SGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLwtQGRMPIkSVLIVTHNIEEAVFMCDRILVLS 154
Cdd:COG3842 137 SGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRL--QRELGI-TFIYVTHDQEEALALADRIAVMN 210
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1-153 |
4.43e-57 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 179.38 E-value: 4.43e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEG---------VAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFEN 71
Cdd:cd03294 76 PTSGKVLIDGQDIAAMSRKelrelrrkkISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEH 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 72 AYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLwtQGRMPiKSVLIVTHNIEEAVFMCDRIL 151
Cdd:cd03294 156 KYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRL--QAELQ-KTIVFITHDLDEALRLGDRIA 232
|
..
gi 1861249672 152 VL 153
Cdd:cd03294 233 IM 234
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-158 |
2.74e-53 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 169.11 E-value: 2.74e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEGVAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGG 80
Cdd:PRK11248 53 YQHGSITLDGKPVEGPGAERGVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGG 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861249672 81 MRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRmpiKSVLIVTHNIEEAVFMCDRILVLSSNPG 158
Cdd:PRK11248 133 QRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETG---KQVLLITHDIEEAVFMATELVLLSPGPG 207
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
3-154 |
5.18e-49 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 160.70 E-value: 5.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 3 GGEVTYLGKPltgPAE-GVAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGM 81
Cdd:COG1118 62 NGRDLFTNLP---PRErRVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQ 138
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861249672 82 RQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTqgRMPIKSVLiVTHNIEEAVFMCDRILVLS 154
Cdd:COG1118 139 RQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHD--ELGGTTVF-VTHDQEEALELADRVVVMN 208
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1-154 |
5.29e-46 |
|
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: 149.18 E-value: 5.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEG---------VAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFEN 71
Cdd:cd03255 56 PTSGEVRVDGTDISKLSEKelaafrrrhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLN 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 72 AYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRmpiKSVLIVTHNiEEAVFMCDRIL 151
Cdd:cd03255 136 HYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAG---TTIVVVTHD-PELAEYADRII 211
|
...
gi 1861249672 152 VLS 154
Cdd:cd03255 212 ELR 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1-155 |
1.58e-45 |
|
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: 148.54 E-value: 1.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTG-PA--EGVAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPREL 77
Cdd:cd03300 52 PTSGEILLDGKDITNlPPhkRPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQL 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861249672 78 SGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLwtQGRMPIkSVLIVTHNIEEAVFMCDRILVLSS 155
Cdd:cd03300 132 SGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRL--QKELGI-TFVFVTHDQEEALTMSDRIAVMNK 206
|
|
| ABC_choXWV_ATP |
TIGR03415 |
choline ABC transporter, ATP-binding protein; Members of this protein family are the ... |
20-155 |
3.97e-45 |
|
choline ABC transporter, ATP-binding protein; Members of this protein family are the ATP-binding subunit of a three-protein transporter. This family belongs, more broadly, to the family of proline and glycine-betaine transporters, but members have been identified by direct characterization and by bioinformatic means as choline transporters. Many species have several closely-related members of this family, probably with variable abilities to act additionally on related quaternary amines. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 188317 [Multi-domain] Cd Length: 382 Bit Score: 151.85 E-value: 3.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 20 VAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILL 99
Cdd:TIGR03415 108 VSMVFQQFALLPWRTVEENVAFGLEMQGMPKAERRKRVDEQLELVGLAQWADRKPGELSGGMQQRVGLARAFATEAPILL 187
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1861249672 100 MDEPFSALDVLTAETLRTDLLDLwtQGRMPiKSVLIVTHNIEEAVFMCDRILVLSS 155
Cdd:TIGR03415 188 MDEPFSALDPLIRTQLQDELLEL--QSKLK-KTIVFVSHDLDEALKIGNRIAIMEG 240
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-154 |
1.21e-44 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 145.96 E-value: 1.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEG---------VAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFEN 71
Cdd:COG1136 60 PTSGEVLIDGQDISSLSERelarlrrrhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLD 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 72 AYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRMpikSVLIVTHNiEEAVFMCDRIL 151
Cdd:COG1136 140 HRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGT---TIVMVTHD-PELAARADRVI 215
|
...
gi 1861249672 152 VLS 154
Cdd:COG1136 216 RLR 218
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1-153 |
8.39e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 144.05 E-value: 8.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEG----VAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRE 76
Cdd:COG1131 52 PTSGEVRVLGEDVARDPAEvrrrIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGT 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVL 153
Cdd:COG1131 132 LSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEG----KTVLLSTHYLEEAERLCDRVAII 204
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-153 |
3.33e-43 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 145.99 E-value: 3.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTG--PAE-GVAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPREL 77
Cdd:COG3839 55 PTSGEILIGGRDVTDlpPKDrNIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQL 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861249672 78 SGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLwtQGRMPIkSVLIVTHNIEEAVFMCDRILVL 153
Cdd:COG3839 135 SGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRL--HRRLGT-TTIYVTHDQVEAMTLADRIAVM 207
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-154 |
1.20e-42 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 143.31 E-value: 1.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTG--PAE---GVAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLD--GFENAY 73
Cdd:COG1125 54 PTSGRILIDGEDIRDldPVElrrRIGYVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDpeEYRDRY 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 74 PRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLwtQGRMPiKSVLIVTHNIEEAVFMCDRILVL 153
Cdd:COG1125 134 PHELSGGQQQRVGVARALAADPPILLMDEPFGALDPITREQLQDELLRL--QRELG-KTIVFVTHDIDEALKLGDRIAVM 210
|
.
gi 1861249672 154 S 154
Cdd:COG1125 211 R 211
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1-158 |
8.31e-42 |
|
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: 139.14 E-value: 8.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEGVAMVFQTFALFPWLTVLQNVEAGLEALGVGAR--ERRERALAAIDLIGLDGFENAYPRELS 78
Cdd:TIGR01184 37 PTSGGVILEGKQITEPGPDRMVVFQNYSLLPWLTVRENIALAVDRVLPDLSksERRAIVEEHIALVGLTEAADKRPGQLS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 79 GGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVLSSNPG 158
Cdd:TIGR01184 117 GGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIWEEHRV---TVLMVTHDVDEALLLSDRVVMLTNGPA 193
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-153 |
1.09e-41 |
|
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: 138.96 E-value: 1.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEG--------VAMVFQTFALFPWLTVLQNVEAGL-EALGVGARERRERALAAIDLIGLDGFEN 71
Cdd:COG1127 57 PDSGEILVDGQDITGLSEKelyelrrrIGMLFQGGALFDSLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAAD 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 72 AYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLwtQGRMPIkSVLIVTHNIEEAVFMCDRIL 151
Cdd:COG1127 137 KMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIREL--RDELGL-TSVVVTHDLDSAFAIADRVA 213
|
..
gi 1861249672 152 VL 153
Cdd:COG1127 214 VL 215
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1-153 |
1.88e-40 |
|
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: 135.89 E-value: 1.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLT--GPAE---GVAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLD--GFENAY 73
Cdd:cd03295 53 PTSGEIFIDGEDIReqDPVElrrKIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRY 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 74 PRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRmpiKSVLIVTHNIEEAVFMCDRILVL 153
Cdd:cd03295 133 PHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELG---KTIVFVTHDIDEAFRLADRIAIM 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-153 |
2.09e-40 |
|
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: 141.58 E-value: 2.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEG--------VAMVFQ--TFALFPWLTVLQNVEAGLEALGVG-ARERRERALAAIDLIGLD-G 68
Cdd:COG1123 317 PTSGSILFDGKDLTKLSRRslrelrrrVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLsRAERRERVAELLERVGLPpD 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 69 FENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRMpikSVLIVTHNIEEAVFMCD 148
Cdd:COG1123 397 LADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGL---TYLFISHDLAVVRYIAD 473
|
....*
gi 1861249672 149 RILVL 153
Cdd:COG1123 474 RVAVM 478
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-153 |
2.38e-40 |
|
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: 134.73 E-value: 2.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 19 GVAMVFQTFALFPWLTVLQNVEAGLEalGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTIL 98
Cdd:cd03297 76 KIGLVFQQYALFPHLNVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELL 153
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1861249672 99 LMDEPFSALDVLTAETLRTDLLDLWTQGRMPiksVLIVTHNIEEAVFMCDRILVL 153
Cdd:cd03297 154 LLDEPFSALDRALRLQLLPELKQIKKNLNIP---VIFVTHDLSEAEYLADRIVVM 205
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-153 |
4.62e-40 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 134.74 E-value: 4.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPA-------EGVAMVFQTFALFPWLTVLQNV-EAGLEALGVGARERRERALAAIDLIGLDGFENA 72
Cdd:COG1126 53 PDSGTITVDGEDLTDSKkdinklrRKVGMVFQQFNLFPHLTVLENVtLAPIKVKKMSKAEAEERAMELLERVGLADKADA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 73 YPRELSGGMRQRVGFARALVVDPTILLMDEPFSALD-VLTAETLRTdLLDLWTQGR-MpiksvLIVTHNIEEAVFMCDRI 150
Cdd:COG1126 133 YPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDpELVGEVLDV-MRDLAKEGMtM-----VVVTHEMGFAREVADRV 206
|
...
gi 1861249672 151 LVL 153
Cdd:COG1126 207 VFM 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-153 |
7.12e-40 |
|
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: 133.79 E-value: 7.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEG--------VAMVFQ--TFALFPWLTVLQNVEAGLEALGV--GARERRERALAAIDLIGLD- 67
Cdd:cd03257 57 PTSGSIIFDGKDLLKLSRRlrkirrkeIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKlsKKEARKEAVLLLLVGVGLPe 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 68 GFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLT-AETLRTdLLDLWTQGRMpikSVLIVTHNIEEAVFM 146
Cdd:cd03257 137 EVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVqAQILDL-LKKLQEELGL---TLLFITHDLGVVAKI 212
|
....*..
gi 1861249672 147 CDRILVL 153
Cdd:cd03257 213 ADRVAVM 219
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1-153 |
5.06e-39 |
|
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: 131.86 E-value: 5.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTG--PAE------GVAMVFQTFALFPWLTVLQNVEAGL-EALGVGARERRERALAAIDLIGLDGFEN 71
Cdd:cd03261 52 PDSGEVLIDGEDISGlsEAElyrlrrRMGMLFQSGALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAED 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 72 AYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLwtqGRMPIKSVLIVTHNIEEAVFMCDRIL 151
Cdd:cd03261 132 LYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSL---KKELGLTSIMVTHDLDTAFAIADRIA 208
|
..
gi 1861249672 152 VL 153
Cdd:cd03261 209 VL 210
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-155 |
5.35e-38 |
|
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: 129.38 E-value: 5.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTG--PAE-GVAMVFQTFALFPWLTVLQNVEAGLEALGVGAR----ERRERALAAIDLIGLDGFENAY 73
Cdd:cd03296 54 PDSGTILFGGEDATDvpVQErNVGFVFQHYALFRHMTVFDNVAFGLRVKPRSERppeaEIRAKVHELLKLVQLDWLADRY 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 74 PRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLwtQGRMPIKSVLiVTHNIEEAVFMCDRILVL 153
Cdd:cd03296 134 PAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRL--HDELHVTTVF-VTHDQEEALEVADRVVVM 210
|
..
gi 1861249672 154 SS 155
Cdd:cd03296 211 NK 212
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-155 |
9.99e-38 |
|
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: 128.47 E-value: 9.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEG--------VAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENA 72
Cdd:cd03258 57 PTSGSVLVDGTDLTLLSGKelrkarrrIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 73 YPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLwtQGRMPIkSVLIVTHNIEEAVFMCDRILV 152
Cdd:cd03258 137 YPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDI--NRELGL-TIVLITHEMEVVKRICDRVAV 213
|
...
gi 1861249672 153 LSS 155
Cdd:cd03258 214 MEK 216
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1-154 |
2.03e-37 |
|
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: 127.83 E-value: 2.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLT--GPAEG---VAMVFQtfalFPWL-----TVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFE 70
Cdd:COG1122 53 PTSGEVLVDGKDITkkNLRELrrkVGLVFQ----NPDDqlfapTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 71 NAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRI 150
Cdd:COG1122 129 DRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEG----KTVIIVTHDLDLVAELADRV 204
|
....
gi 1861249672 151 LVLS 154
Cdd:COG1122 205 IVLD 208
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1-153 |
5.31e-37 |
|
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: 126.68 E-value: 5.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTG-PAE--GVAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPREL 77
Cdd:cd03299 51 PDSGKILLNGKDITNlPPEkrDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETL 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861249672 78 SGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRMPiksVLIVTHNIEEAVFMCDRILVL 153
Cdd:cd03299 131 SGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVT---VLHVTHDFEEAWALADKVAIM 203
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1-151 |
6.82e-37 |
|
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: 125.72 E-value: 6.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAE-------GVAMVFQTFALFPWLTVLQNV-EAGLEALGVGARERRERALAAIDLIGLDGFENA 72
Cdd:cd03262 52 PDSGTIIIDGLKLTDDKKninelrqKVGMVFQQFNLFPHLTVLENItLAPIKVKGMSKAEAEERALELLEKVGLADKADA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 73 YPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDV-LTAETLRTdLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRIL 151
Cdd:cd03262 132 YPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPeLVGEVLDV-MKDLAEEG----MTMVVVTHEMGFAREVADRVI 206
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1-155 |
7.10e-37 |
|
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: 124.61 E-value: 7.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEG-------VAMVFQTFALFPWLTVLQNVeaglealgvgarerreralaaidligldgfenAY 73
Cdd:cd03229 52 PDSGSILIDGEDLTDLEDElpplrrrIGMVFQDFALFPHLTVLENI--------------------------------AL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 74 PreLSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRMPiksVLIVTHNIEEAVFMCDRILVL 153
Cdd:cd03229 100 G--LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGIT---VVLVTHDLDEAARLADRVVVL 174
|
..
gi 1861249672 154 SS 155
Cdd:cd03229 175 RD 176
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-155 |
7.98e-37 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 130.54 E-value: 7.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 20 VAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILL 99
Cdd:PRK10070 108 IAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILL 187
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1861249672 100 MDEPFSALDVLTAETLRTDLLDLWTQGRmpiKSVLIVTHNIEEAVFMCDRILVLSS 155
Cdd:PRK10070 188 MDEAFSALDPLIRTEMQDELVKLQAKHQ---RTIVFISHDLDEAMRIGDRIAIMQN 240
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-153 |
7.98e-37 |
|
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: 126.84 E-value: 7.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEG-----VAMVFQ--TFALFPWLTVLQNVEAGLEALGVGarERRERALAAIDLIGLD-GFENA 72
Cdd:COG1124 57 PWSGEVTFDGRPVTRRRRKafrrrVQMVFQdpYASLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLPpSFLDR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 73 YPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLT-AETLRTdLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRIL 151
Cdd:COG1124 135 YPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVqAEILNL-LKDLREERGL---TYLFVSHDLAVVAHLCDRVA 210
|
..
gi 1861249672 152 VL 153
Cdd:COG1124 211 VM 212
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
1-154 |
1.08e-36 |
|
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: 128.38 E-value: 1.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTG-PAE--GVAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPREL 77
Cdd:TIGR01187 22 PDSGSIMLDGEDVTNvPPHlrHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPRVLEALRLVQLEEFADRKPHQL 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861249672 78 SGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLwtQGRMPIKSVLiVTHNIEEAVFMCDRILVLS 154
Cdd:TIGR01187 102 SGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTI--QEQLGITFVF-VTHDQEEAMTMSDRIAIMR 175
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-154 |
1.32e-36 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 128.27 E-value: 1.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTG--PAE------GVAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENA 72
Cdd:COG1135 57 PTSGSVLVDGVDLTAlsERElraarrKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 73 YPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDvltAETLRtDLLDLwtqgrmpIKS--------VLIVTHNIEEAV 144
Cdd:COG1135 137 YPSQLSGGQKQRVGIARALANNPKVLLCDEATSALD---PETTR-SILDL-------LKDinrelgltIVLITHEMDVVR 205
|
170
....*....|
gi 1861249672 145 FMCDRILVLS 154
Cdd:COG1135 206 RICDRVAVLE 215
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1-155 |
2.42e-36 |
|
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: 124.67 E-value: 2.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLT--GPAE-GVAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPREL 77
Cdd:cd03301 52 PTSGRIYIGGRDVTdlPPKDrDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQL 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861249672 78 SGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLwtQGRMPIkSVLIVTHNIEEAVFMCDRILVLSS 155
Cdd:cd03301 132 SGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRL--QQRLGT-TTIYVTHDQVEAMTMADRIAVMND 206
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-141 |
1.78e-35 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 122.47 E-value: 1.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTG-PAEGVA-------MVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENA 72
Cdd:COG2884 54 PTSGQVLVNGQDLSRlKRREIPylrrrigVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKA 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861249672 73 YPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAEtlrtDLLDLWTQ----GrmpiKSVLIVTHNIE 141
Cdd:COG2884 134 LPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSW----EIMELLEEinrrG----TTVLIATHDLE 198
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-153 |
6.82e-35 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 124.45 E-value: 6.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPA---EGVAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPREL 77
Cdd:PRK11432 58 PTEGQIFIDGEDVTHRSiqqRDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQI 137
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861249672 78 SGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLwtQGRMPIKSvLIVTHNIEEAVFMCDRILVL 153
Cdd:PRK11432 138 SGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIREL--QQQFNITS-LYVTHDQSEAFAVSDTVIVM 210
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-153 |
1.34e-34 |
|
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: 120.73 E-value: 1.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEG----VAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRE 76
Cdd:COG4555 53 PDSGSILIDGEDVRKEPREarrqIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGE 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRMpiksVLIVTHNIEEAVFMCDRILVL 153
Cdd:COG4555 133 LSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKT----VLFSSHIMQEVEALCDRVVIL 205
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1-154 |
1.57e-34 |
|
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: 119.88 E-value: 1.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGP-----AEGVAMVFQ-----TFALfpwlTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFE 70
Cdd:cd03225 53 PTSGEVLVDGKDLTKLslkelRRKVGLVFQnpddqFFGP----TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 71 NAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRI 150
Cdd:cd03225 129 DRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEG----KTIIIVTHDLDLLLELADRV 204
|
....
gi 1861249672 151 LVLS 154
Cdd:cd03225 205 IVLE 208
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-153 |
5.31e-34 |
|
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: 124.25 E-value: 5.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 3 GGEVTYLGKPLTGPAEG-----VAMVFQTF--ALFPwLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPR 75
Cdd:COG1123 63 SGEVLLDGRDLLELSEAlrgrrIGMVFQDPmtQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPH 141
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861249672 76 ELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVL 153
Cdd:COG1123 142 QLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGT---TVLLITHDLGVVAEIADRVVVM 216
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-153 |
7.63e-34 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 118.70 E-value: 7.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTG--PAE-GVAMVFQTFALFPWLTVLQNVeagleALGVGA-----RERRERALAAIDLIGLDGFENA 72
Cdd:COG3840 51 PDSGRILWNGQDLTAlpPAErPVSMLFQENNLFPHLTVAQNI-----GLGLRPglkltAEQRAQVEQALERVGLAGLLDR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 73 YPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDvltaETLRTDLLDLWTQ-----GRmpikSVLIVTHNIEEAVFMC 147
Cdd:COG3840 126 LPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALD----PALRQEMLDLVDElcrerGL----TVLMVTHDPEDAARIA 197
|
....*.
gi 1861249672 148 DRILVL 153
Cdd:COG3840 198 DRVLLV 203
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2-153 |
7.97e-34 |
|
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: 120.54 E-value: 7.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 2 TGGEVTYLGKPLTG--PAE-------GVAMVFQ---TfALFPWLTVLQNVEAGLEA-LGVGARERRERALAAIDLIGLDG 68
Cdd:COG0444 61 TSGEILFDGEDLLKlsEKElrkirgrEIQMIFQdpmT-SLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPD 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 69 FE---NAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLT-AETLRTdLLDLWTQGRMpikSVLIVTHNIEEAV 144
Cdd:COG0444 140 PErrlDRYPHELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIqAQILNL-LKDLQRELGL---AILFITHDLGVVA 215
|
....*....
gi 1861249672 145 FMCDRILVL 153
Cdd:COG0444 216 EIADRVAVM 224
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-153 |
1.67e-32 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 118.51 E-value: 1.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTG-PAEG--VAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPREL 77
Cdd:PRK09452 66 PDSGRIMLDGQDITHvPAENrhVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQL 145
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861249672 78 SGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLwtQGRMPIKSVLiVTHNIEEAVFMCDRILVL 153
Cdd:PRK09452 146 SGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKAL--QRKLGITFVF-VTHDQEEALTMSDRIVVM 218
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-153 |
4.26e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 114.42 E-value: 4.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEGVAMVFQTFAL---FPwLTVLQNVEAGLEA----LGVGARERRERALAAIDLIGLDGFENAY 73
Cdd:COG1121 58 PTSGTVRLFGKPPRRARRRIGYVPQRAEVdwdFP-ITVRDVVLMGRYGrrglFRRPSRADREAVDEALERVGLEDLADRP 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 74 PRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLrTDLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVL 153
Cdd:COG1121 137 IGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEAL-YELLRELRREGK---TILVVTHDLGAVREYFDRVLLL 212
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1-153 |
8.97e-32 |
|
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: 112.63 E-value: 8.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEGVAMVFQTFAL---FPwLTVLQNVEAGLEA----LGVGARERRERALAAIDLIGLDGFENAY 73
Cdd:cd03235 51 PTSGSIRVFGKPLEKERKRIGYVPQRRSIdrdFP-ISVRDVVLMGLYGhkglFRRLSKADKAKVDEALERVGLSELADRQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 74 PRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLrTDLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVL 153
Cdd:cd03235 130 IGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDI-YELLRELRREGM---TILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1-153 |
9.34e-31 |
|
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: 110.60 E-value: 9.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTG--PAE----GVAMVFQTFALFPWLTVLQNVEAGLEALGVGA----------RERRERALAAIDLI 64
Cdd:cd03219 52 PTSGSVLFDGEDITGlpPHEiarlGIGRTFQIPRLFPELTVLENVMVAAQARTGSGlllararreeREARERAEELLERV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 65 GLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSAL-DVLTAETLRTdLLDLWTQGRmpikSVLIVTHNIeEA 143
Cdd:cd03219 132 GLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLnPEETEELAEL-IRELRERGI----TVLLVEHDM-DV 205
|
170
....*....|.
gi 1861249672 144 VF-MCDRILVL 153
Cdd:cd03219 206 VMsLADRVTVL 216
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1-155 |
1.01e-30 |
|
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: 110.74 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLT--GPAE------GVAMVFQTFALFPWLTVLQNVEAGLEA--------LGVGARERRERALAAIDLI 64
Cdd:cd03256 53 PTSGSVLIDGTDINklKGKAlrqlrrQIGMIFQQFNLIERLSVLENVLSGRLGrrstwrslFGLFPKEEKQRALAALERV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 65 GLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRMpikSVLIVTHNIEEAV 144
Cdd:cd03256 133 GLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGI---TVIVSLHQVDLAR 209
|
170
....*....|.
gi 1861249672 145 FMCDRILVLSS 155
Cdd:cd03256 210 EYADRIVGLKD 220
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-154 |
1.05e-30 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 110.92 E-value: 1.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLT--GPAE------GVAMVFQTFALFPWLTVLQNVEAGLEA--------LGVGARERRERALAAIDLI 64
Cdd:COG3638 55 PTSGEILVDGQDVTalRGRAlrrlrrRIGMIFQQFNLVPRLSVLTNVLAGRLGrtstwrslLGLFPPEDRERALEALERV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 65 GLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRMPiksVLIVTHNIEEAV 144
Cdd:COG3638 135 GLADKAYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGIT---VVVNLHQVDLAR 211
|
170
....*....|
gi 1861249672 145 FMCDRILVLS 154
Cdd:COG3638 212 RYADRIIGLR 221
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1-153 |
2.23e-30 |
|
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: 107.87 E-value: 2.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEG----VAMVFQTFALFPWLTVLQNVEaglealgvgarerreralaaidligldgfenaypre 76
Cdd:cd03230 52 PDSGEIKVLGKDIKKEPEEvkrrIGYLPEEPSLYENLTVRENLK------------------------------------ 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVL 153
Cdd:cd03230 96 LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKEG----KTILLSSHILEEAERLCDRVAIL 168
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
20-154 |
2.64e-30 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 112.10 E-value: 2.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 20 VAMVFQTFALFPWLTVLQNVEAGLEALgvgarERRERALAAI---------DLIGLDGFENAYPRELSGGMRQRVGFARA 90
Cdd:PRK10851 76 VGFVFQHYALFRHMTVFDNIAFGLTVL-----PRRERPNAAAikakvtqllEMVQLAHLADRYPAQLSGGQKQRVALARA 150
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861249672 91 LVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQgrMPIKSVLiVTHNIEEAVFMCDRILVLS 154
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEE--LKFTSVF-VTHDQEEAMEVADRVVVMS 211
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
20-154 |
7.20e-30 |
|
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: 110.96 E-value: 7.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 20 VAMVFQTFALFPWLTVLQNVEAGLEAlgVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILL 99
Cdd:COG4148 79 IGYVFQEARLFPHLSVRGNLLYGRKR--APRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLL 156
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1861249672 100 MDEPFSALDvltaETLRTDLLD----LWTQGRMPIksvLIVTHNIEEAVFMCDRILVLS 154
Cdd:COG4148 157 MDEPLAALD----LARKAEILPylerLRDELDIPI---LYVSHSLDEVARLADHVVLLE 208
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-153 |
9.77e-30 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 107.57 E-value: 9.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 4 GEVTYLGKPLTG-PAE--GVAMVFQTFALFPWLTVLQNVEAGLEAlGVGARERRERALAAIDLIGLDGFENAYPRELSGG 80
Cdd:COG4136 59 GEVLLNGRRLTAlPAEqrRIGILFQDDLLFPHLSVGENLAFALPP-TIGRAQRRARVEQALEEAGLAGFADRDPATLSGG 137
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861249672 81 MRQRVGFARALVVDPTILLMDEPFSALDVltaeTLRTDLLDL-WTQGRMPIKSVLIVTHNIEEAVFMcDRILVL 153
Cdd:COG4136 138 QRARVALLRALLAEPRALLLDEPFSKLDA----ALRAQFREFvFEQIRQRGIPALLVTHDEEDAPAA-GRVLDL 206
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1-153 |
1.16e-29 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 108.61 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEGVAMVFQTFALFPWLTVLQNVEAGLEAlgvgarERRERALAAIDLIGLDGFENAYPRELSGG 80
Cdd:PRK11247 64 PSAGELLAGTAPLAEAREDTRLMFQDARLLPWKKVIDNVGLGLKG------QWRDAALQALAAVGLADRANEWPAALSGG 137
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861249672 81 MRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVL 153
Cdd:PRK11247 138 QKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGF---TVLLVTHDVSEAVAMADRVLLI 207
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-153 |
1.41e-29 |
|
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: 108.20 E-value: 1.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTG--PAE----GVAMVFQTFALFPWLTVLQNVEAGLEA-------------LGVGARER--RERALA 59
Cdd:COG0411 56 PTSGRILFDGRDITGlpPHRiarlGIARTFQNPRLFPELTVLENVLVAAHArlgrgllaallrlPRARREEReaRERAEE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 60 AIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSAL-DVLTAETLRTdLLDLWTQGRMpikSVLIVTH 138
Cdd:COG0411 136 LLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLnPEETEELAEL-IRRLRDERGI---TILLIEH 211
|
170
....*....|....*.
gi 1861249672 139 NIeEAVF-MCDRILVL 153
Cdd:COG0411 212 DM-DLVMgLADRIVVL 226
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-152 |
1.88e-29 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 109.44 E-value: 1.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEG--------VAMVFQ-TFA-LFPWLTVLQNVEAGLEALGVG-ARERRERALAAIDLIGLD-G 68
Cdd:COG4608 70 PTSGEILFDGQDITGLSGRelrplrrrMQMVFQdPYAsLNPRMTVGDIIAEPLRIHGLAsKAERRERVAELLELVGLRpE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 69 FENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDV-LTAETLRTdLLDLwtQGRMPIkSVLIVTHNIeeAV--F 145
Cdd:COG4608 150 HADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVsIQAQVLNL-LEDL--QDELGL-TYLFISHDL--SVvrH 223
|
....*..
gi 1861249672 146 MCDRILV 152
Cdd:COG4608 224 ISDRVAV 230
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
2-143 |
6.21e-29 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 106.33 E-value: 6.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 2 TGGEVTYLGKPLTGPAEGV-------AMVFQTFALFPWLTVLQNVEAG-LEALGVGARERRERALAAIDLIGLDGFENAY 73
Cdd:PRK09493 54 TSGDLIVDGLKVNDPKVDErlirqeaGMVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHY 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1861249672 74 PRELSGGMRQRVGFARALVVDPTILLMDEPFSALDV-LTAETLRTdLLDLWTQGrMpikSVLIVTHNIEEA 143
Cdd:PRK09493 134 PSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPeLRHEVLKV-MQDLAEEG-M---TMVIVTHEIGFA 199
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1-153 |
1.03e-28 |
|
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: 104.88 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTG--PAE-GVAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPREL 77
Cdd:cd03298 50 PQSGRVLINGVDVTAapPADrPVSMLFQENNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGEL 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861249672 78 SGGMRQRVGFARALVVDPTILLMDEPFSALDvltaETLRTDLLDLWTQGRMPIK-SVLIVTHNIEEAVFMCDRILVL 153
Cdd:cd03298 130 SGGERQRVALARVLVRDKPVLLLDEPFAALD----PALRAEMLDLVLDLHAETKmTVLMVTHQPEDAKRLAQRVVFL 202
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1-105 |
2.99e-28 |
|
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: 101.96 E-value: 2.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAE-----GVAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFEN---- 71
Cdd:pfam00005 37 PTEGTILLDGQDLTDDERkslrkEIGYVFQDPQLFPRLTVRENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvg 116
|
90 100 110
....*....|....*....|....*....|....
gi 1861249672 72 AYPRELSGGMRQRVGFARALVVDPTILLMDEPFS 105
Cdd:pfam00005 117 ERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-155 |
5.96e-28 |
|
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: 103.53 E-value: 5.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEG--------VAMVFQTFALFPWLTVLQNVEAGLEA--------LGVGARERRERALAAIDLI 64
Cdd:TIGR02315 54 PSSGSILLEGTDITKLRGKklrklrrrIGMIFQHYNLIERLTVLENVLHGRLGykptwrslLGRFSEEDKERALSALERV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 65 GLDGFenAYPR--ELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLwtqGRMPIKSVLIVTHNIEE 142
Cdd:TIGR02315 134 GLADK--AYQRadQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRI---NKEDGITVIINLHQVDL 208
|
170
....*....|...
gi 1861249672 143 AVFMCDRILVLSS 155
Cdd:TIGR02315 209 AKKYADRIVGLKA 221
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
2-153 |
5.06e-27 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 103.38 E-value: 5.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 2 TGGEVTYLGKPLTG--PAE-GVAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELS 78
Cdd:PRK11650 57 TSGEIWIGGRVVNElePADrDIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELS 136
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861249672 79 GGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLwtQGRMPIKSvLIVTHNIEEAVFMCDRILVL 153
Cdd:PRK11650 137 GGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRL--HRRLKTTS-LYVTHDQVEAMTLADRVVVM 208
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-155 |
6.10e-27 |
|
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: 100.59 E-value: 6.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTG---------PAEGVAMVFQTFALFPWLTVLQNVEAGLEAlgVGARERRERALAAIDLIGLDGFEN 71
Cdd:COG4181 64 PTSGTVRLAGQDLFAldedararlRARHVGFVFQSFQLLPTLTALENVMLPLEL--AGRRDARARARALLERVGLGHRLD 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 72 AYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLrTDLL-DLWTQGRMpikSVLIVTHNIEEAVfMCDRI 150
Cdd:COG4181 142 HYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQI-IDLLfELNRERGT---TLVLVTHDPALAA-RCDRV 216
|
....*
gi 1861249672 151 LVLSS 155
Cdd:COG4181 217 LRLRA 221
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-154 |
6.70e-27 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 99.86 E-value: 6.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEG----VAMVFQTFALFPWLTVLQNVEAGLEALGVGARerRERALAAIDLIGLDGFENAYPRE 76
Cdd:COG4133 54 PSAGEVLWNGEPIRDAREDyrrrLAYLGHADGLKPELTVRENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQ 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRMpiksVLIVTHNIEEAVFmcDRILVLS 154
Cdd:COG4133 132 LSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGA----VLLTTHQPLELAA--ARVLDLG 203
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1-154 |
6.79e-27 |
|
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: 100.72 E-value: 6.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEG-------VAMVFQTFALFPwLTVLQNVEAGLEALGV-GARERRERALAAIDLIGLDGFEN- 71
Cdd:cd03260 57 PDEGEVLLDGKDIYDLDVDvlelrrrVGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKd 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 72 -AYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALD-VLTA--ETLRTDLLDLWTqgrmpiksVLIVTHNIEEAVFMC 147
Cdd:cd03260 136 rLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDpISTAkiEELIAELKKEYT--------IVIVTHNMQQAARVA 207
|
....*..
gi 1861249672 148 DRILVLS 154
Cdd:cd03260 208 DRTAFLL 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1-153 |
8.13e-27 |
|
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: 100.17 E-value: 8.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTG-PAEGVA-------MVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENA 72
Cdd:cd03292 53 PTSGTIRVNGQDVSDlRGRAIPylrrkigVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 73 YPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAetlrTDLLDLWTQGRMPIKSVLIVTHNIEEAVFMCDRILV 152
Cdd:cd03292 133 LPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTT----WEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIA 208
|
.
gi 1861249672 153 L 153
Cdd:cd03292 209 L 209
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
16-153 |
8.48e-27 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 103.19 E-value: 8.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 16 PAE-GVAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVD 94
Cdd:PRK11000 72 PAErGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAE 151
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 95 PTILLMDEPFSALDVLTAETLRTDLLDLWTQgrmpIKSVLI-VTHNIEEAVFMCDRILVL 153
Cdd:PRK11000 152 PSVFLLDEPLSNLDAALRVQMRIEISRLHKR----LGRTMIyVTHDQVEAMTLADKIVVL 207
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
20-153 |
1.59e-26 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 100.43 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 20 VAMVFQTFALFPWLTVLQNV-EAGLEALGVGARERRERALAAIDLIGLDGFENA-YPRELSGGMRQRVGFARALVVDPTI 97
Cdd:PRK10619 94 LTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGkYPVHLSGGQQQRVSIARALAMEPEV 173
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1861249672 98 LLMDEPFSALDV-LTAETLRTdLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVL 153
Cdd:PRK10619 174 LLFDEPTSALDPeLVGEVLRI-MQQLAEEG----KTMVVVTHEMGFARHVSSHVIFL 225
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
20-143 |
1.72e-26 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 99.70 E-value: 1.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 20 VAMVFQTFALFPWLTVLQN-VEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTIL 98
Cdd:PRK11124 84 VGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVL 163
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1861249672 99 LMDEPFSALDV-LTAETLRTdLLDLWTQGrmpIKSVlIVTHNIEEA 143
Cdd:PRK11124 164 LFDEPTAALDPeITAQIVSI-IRELAETG---ITQV-IVTHEVEVA 204
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-153 |
2.23e-26 |
|
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: 103.23 E-value: 2.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEG--------VAMVFQT-FA-LFPWLTVLQNVEAGLEALGVG--ARERRERALAAIDLIGLD- 67
Cdd:COG4172 337 PSEGEIRFDGQDLDGLSRRalrplrrrMQVVFQDpFGsLSPRMTVGQIIAEGLRVHGPGlsAAERRARVAEALEEVGLDp 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 68 GFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLT-AETLrtDLL-DLwtQGRMPIkSVLIVTHNIeeAV- 144
Cdd:COG4172 417 AARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVqAQIL--DLLrDL--QREHGL-AYLFISHDL--AVv 489
|
170
....*....|
gi 1861249672 145 -FMCDRILVL 153
Cdd:COG4172 490 rALAHRVMVM 499
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
1-154 |
2.48e-26 |
|
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: 98.78 E-value: 2.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPA---EGVAMVFQTFALFPWLTVLQNVEAGLE-ALGVGArERRERALAAIDLIGLDGFENAYPRE 76
Cdd:TIGR01277 50 PASGSIKVNDQSHTGLApyqRPVSMLFQENNLFAHLTVRQNIGLGLHpGLKLNA-EQQEKVVDAAQQVGIADYLDRLPEQ 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVLS 154
Cdd:TIGR01277 129 LSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSERQR---TLLMVTHHLSDARAIASQIAVVS 203
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-153 |
3.63e-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: 99.35 E-value: 3.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGP-----AEGVAMVFQTFALFPWLTVLQNVEAG----LEALGVGARERRERALAAIDLIGLDGFEN 71
Cdd:COG1120 53 PSSGEVLLDGRDLASLsrrelARRIAYVPQEPPAPFGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLAD 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 72 AYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVltaeTLRTDLLDL-----WTQGRmpikSVLIVTHNIEEAVFM 146
Cdd:COG1120 133 RPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDL----AHQLEVLELlrrlaRERGR----TVVMVLHDLNLAARY 204
|
....*..
gi 1861249672 147 CDRILVL 153
Cdd:COG1120 205 ADRLVLL 211
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
18-151 |
5.73e-26 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 98.75 E-value: 5.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 18 EGVAMVFQTFALFPWLTVLQNV-EAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPT 96
Cdd:TIGR03005 87 NKIGMVFQSFNLFPHKTVLDNVtEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARALAMRPK 166
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1861249672 97 ILLMDEPFSALDVLTAETLRTDLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRIL 151
Cdd:TIGR03005 167 VMLFDEVTSALDPELVGEVLNVIRRLASEHDL---TMLLVTHEMGFAREFADRVC 218
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
20-143 |
1.17e-25 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 97.78 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 20 VAMVFQTFALFPWLTVLQN-VEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTIL 98
Cdd:COG4161 84 VGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVL 163
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1861249672 99 LMDEPFSALD-VLTAETLRTdLLDLwtqGRMPIKSVlIVTHNIEEA 143
Cdd:COG4161 164 LFDEPTAALDpEITAQVVEI-IREL---SQTGITQV-IVTHEVEFA 204
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-154 |
1.80e-24 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 93.85 E-value: 1.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTG------PA--EGVAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENA 72
Cdd:TIGR02673 54 PSRGQVRIAGEDVNRlrgrqlPLlrRRIGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 73 YPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDvltaETLRTDLLDLWTQGRMPIKSVLIVTHNIEEAVFMCDRILV 152
Cdd:TIGR02673 134 FPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLD----PDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVII 209
|
..
gi 1861249672 153 LS 154
Cdd:TIGR02673 210 LD 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-153 |
2.12e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.78 E-value: 2.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKP--LTGPAE----GVAMVFQTFALFPWLTVLQNVEAGLEALGVGA---RERRERALAAIDLIGLDGFEN 71
Cdd:COG1129 56 PDSGEILLDGEPvrFRSPRDaqaaGIAIIHQELNLVPNLSVAENIFLGREPRRGGLidwRAMRRRARELLARLGLDIDPD 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 72 AYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEaVF-MCDRI 150
Cdd:COG1129 136 TPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQG----VAIIYISHRLDE-VFeIADRV 210
|
...
gi 1861249672 151 LVL 153
Cdd:COG1129 211 TVL 213
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1-153 |
4.05e-24 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 92.96 E-value: 4.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTG-PAEG----VAMVFQTFALFPwLTVLQNVEAGLEAlgVGARERRERALAAIDLIGLD-GFENAYP 74
Cdd:COG4619 52 PTSGEIYLDGKPLSAmPPPEwrrqVAYVPQEPALWG-GTVRDNLPFPFQL--RERKFDRERALELLERLGLPpDILDKPV 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1861249672 75 RELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVL 153
Cdd:COG4619 129 ERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGR---AVLWVSHDPEQIERVADRVLTL 204
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-152 |
1.20e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 92.34 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKP--LTGPAE-GVAMVFQTFALFPWLTVLQNVEAGLE-ALGVGARERRERALAAiDLIGLDGFENAYPRE 76
Cdd:PRK10771 51 PASGSLTLNGQDhtTTPPSRrPVSMLFQENNLFSHLTVAQNIGLGLNpGLKLNAAQREKLHAIA-RQMGIEDLLARLPGQ 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDvltaETLRTDLLDLWTQ-GRMPIKSVLIVTHNIEEAVFMCDRILV 152
Cdd:PRK10771 130 LSGGQRQRVALARCLVREQPILLLDEPFSALD----PALRQEMLTLVSQvCQERQLTLLMVSHSLEDAARIAPRSLV 202
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-154 |
1.27e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 94.52 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPA---EGVAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPREL 77
Cdd:PRK11607 71 PTAGQIMLDGVDLSHVPpyqRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQL 150
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861249672 78 SGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTqgRMPIKSVLiVTHNIEEAVFMCDRILVLS 154
Cdd:PRK11607 151 SGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILE--RVGVTCVM-VTHDQEEAMTMAGRIAIMN 224
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-154 |
1.29e-23 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 94.10 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEG--------VAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENA 72
Cdd:PRK11153 57 PTSGRVLVDGQDLTALSEKelrkarrqIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADR 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 73 YPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDvltAETLRTdLLDLWTQ--GRMPIKSVLIvTHNIEEAVFMCDRI 150
Cdd:PRK11153 137 YPAQLSGGQKQRVAIARALASNPKVLLCDEATSALD---PATTRS-ILELLKDinRELGLTIVLI-THEMDVVKRICDRV 211
|
....
gi 1861249672 151 LVLS 154
Cdd:PRK11153 212 AVID 215
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
20-151 |
1.35e-23 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 92.51 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 20 VAMVFQTFALFPWLTVLQNV-EAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTIL 98
Cdd:PRK11264 87 VGFVFQNFNLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVI 166
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1861249672 99 LMDEPFSALDV-LTAETLRTdLLDLWTQGRmpikSVLIVTHNIEEAVFMCDRIL 151
Cdd:PRK11264 167 LFDEPTSALDPeLVGEVLNT-IRQLAQEKR----TMVIVTHEMSFARDVADRAI 215
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
1-154 |
1.42e-23 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 93.61 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEGV----AMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRE 76
Cdd:TIGR01188 45 PTSGTARVAGYDVVREPRKVrrsiGIVPQYASVDEDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGT 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVLS 154
Cdd:TIGR01188 125 YSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYIRALKEEG----VTILLTTHYMEEADKLCDRIAIID 198
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1-155 |
1.73e-23 |
|
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: 91.41 E-value: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPL-TGPAE---GVAMVFQTFALFPWLTVLQNVE--AGLEalGVGARERRERALAAIDLIGLDGFENAYP 74
Cdd:cd03263 54 PTSGTAYINGYSIrTDRKAarqSLGYCPQFDALFDELTVREHLRfyARLK--GLPKSEIKEEVELLLRVLGLTDKANKRA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 75 RELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTaetlRTDLLDLwTQGRMPIKSVLIVTHNIEEAVFMCDRILVLS 154
Cdd:cd03263 132 RTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPAS----RRAIWDL-ILEVRKGRSIILTTHSMDEAEALCDRIAIMS 206
|
.
gi 1861249672 155 S 155
Cdd:cd03263 207 D 207
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
76-153 |
2.01e-23 |
|
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: 89.61 E-value: 2.01e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861249672 76 ELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRMpiksVLIVTHNIEEAVFMCDRILVL 153
Cdd:cd00267 80 QLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRT----VIIVTHDPELAELAADRVIVL 153
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
1-153 |
5.23e-23 |
|
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: 90.49 E-value: 5.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEG---------VAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFEN 71
Cdd:TIGR02211 57 PTSGEVLFNGQSLSKLSSNeraklrnkkLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRIN 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 72 AYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRMpikSVLIVTHNIEEAVFMcDRIL 151
Cdd:TIGR02211 137 HRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNT---SFLVVTHDLELAKKL-DRVL 212
|
..
gi 1861249672 152 VL 153
Cdd:TIGR02211 213 EM 214
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-153 |
8.92e-23 |
|
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: 92.10 E-value: 8.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 20 VAMVFQTFALFPWLTVLQNVEAGLEAlgVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILL 99
Cdd:TIGR02142 77 IGYVFQEARLFPHLSVRGNLRYGMKR--ARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLL 154
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1861249672 100 MDEPFSALDVLTAETLRTDLLDLWTQGRMPIksvLIVTHNIEEAVFMCDRILVL 153
Cdd:TIGR02142 155 MDEPLAALDDPRKYEILPYLERLHAEFGIPI---LYVSHSLQEVLRLADRVVVL 205
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
23-153 |
9.11e-23 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 89.21 E-value: 9.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 23 VFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDE 102
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1861249672 103 PFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVfMCDRILVL 153
Cdd:TIGR03608 161 PTGSLDPKNRDEVLDLLLELNDEG----KTIIIVTHDPEVAK-QADRVIEL 206
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-153 |
1.24e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 92.78 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLT--GPAE----GVAMVFQTFALFPWLTVLQNVEAGLEALGvGARERRERALAAI-DLIGLDGFE--- 70
Cdd:COG3845 57 PDSGEILIDGKPVRirSPRDaialGIGMVHQHFMLVPNLTVAENIVLGLEPTK-GGRLDRKAARARIrELSERYGLDvdp 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 71 NAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSaldVLT---AETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMC 147
Cdd:COG3845 136 DAKVEDLSVGEQQRVEILKALYRGARILILDEPTA---VLTpqeADELFEILRRLAAEG----KSIIFITHKLREVMAIA 208
|
....*.
gi 1861249672 148 DRILVL 153
Cdd:COG3845 209 DRVTVL 214
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1-154 |
7.74e-22 |
|
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: 87.43 E-value: 7.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEGV----AMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRE 76
Cdd:cd03265 52 PTSGRATVAGHDVVREPREVrrriGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKT 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVLS 154
Cdd:cd03265 132 YSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGM---TILLTTHYMEEAEQLCDRVAIID 206
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1-153 |
1.12e-21 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 85.51 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEG-----VAMVFQTFALFPwLTVLQNVeaglealgvgarerreralaaidligldgfenaypr 75
Cdd:cd03228 54 PTSGEILIDGVDLRDLDLEslrknIAYVPQDPFLFS-GTIRENI------------------------------------ 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861249672 76 eLSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLwtqgrMPIKSVLIVTHNIeEAVFMCDRILVL 153
Cdd:cd03228 97 -LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRAL-----AKGKTVIVIAHRL-STIRDADRIIVL 167
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1-153 |
1.49e-21 |
|
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: 86.18 E-value: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEgvamvfQTFA-------LFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAY 73
Cdd:cd03269 52 PDSGEVLFDGKPLDIAAR------NRIGylpeergLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 74 PRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVL 153
Cdd:cd03269 126 VEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAG----KTVILSTHQMELVEELCDRVLLL 201
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-153 |
2.52e-21 |
|
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: 85.88 E-value: 2.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLG-KPLTGPAE---GVAMVFQTFALFPWLTVLQNVE--AGLEALgvgareRRERALAAID-LIGLDGFENAY 73
Cdd:cd03266 57 PDAGFATVDGfDVVKEPAEarrRLGFVSDSTGLYDRLTARENLEyfAGLYGL------KGDELTARLEeLADRLGMEELL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 74 PR---ELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRI 150
Cdd:cd03266 131 DRrvgGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALG----KCILFSTHIMQEVERLCDRV 206
|
...
gi 1861249672 151 LVL 153
Cdd:cd03266 207 VVL 209
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-153 |
2.79e-21 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 85.99 E-value: 2.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 2 TGGEVTYLGKPLTG---------PAEGVAMVFQTFALFPWLTVLQNVEagLEALGVGARER--RERALAAIDLIGLDGFE 70
Cdd:PRK10584 63 SSGEVSLVGQPLHQmdeearaklRAKHVGFVFQSFMLIPTLNALENVE--LPALLRGESSRqsRNGAKALLEQLGLGKRL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 71 NAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLrTDLldLWTQGRMPIKSVLIVTHNIEEAVfMCDRI 150
Cdd:PRK10584 141 DHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI-ADL--LFSLNREHGTTLILVTHDLQLAA-RCDRR 216
|
...
gi 1861249672 151 LVL 153
Cdd:PRK10584 217 LRL 219
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
33-149 |
1.86e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 83.93 E-value: 1.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 33 LTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTA 112
Cdd:COG1137 93 LTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAV 172
|
90 100 110
....*....|....*....|....*....|....*..
gi 1861249672 113 ETLRTDLLDLWTQGrmpIkSVLIVTHNIEEAVFMCDR 149
Cdd:COG1137 173 ADIQKIIRHLKERG---I-GVLITDHNVRETLGICDR 205
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-154 |
1.87e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 85.16 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTG---------PAE-GvamvfqtfaLFPWLTVLqnveaglEAL-------GVGARERRERALAAIDL 63
Cdd:COG4152 53 PDSGEVLWDGEPLDPedrrrigylPEErG---------LYPKMKVG-------EQLvylarlkGLSKAEAKRRADEWLER 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 64 IGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEA 143
Cdd:COG4152 117 LGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKG----TTVIFSSHQMELV 192
|
170
....*....|.
gi 1861249672 144 VFMCDRILVLS 154
Cdd:COG4152 193 EELCDRIVIIN 203
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1-153 |
2.29e-20 |
|
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: 86.43 E-value: 2.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLT--GPAE---GVAMVFQTFALFPwLTVLQNVEAGLEALGvgarerRERALAAIDLIGLDGFENAYP- 74
Cdd:COG2274 527 PTSGRILIDGIDLRqiDPASlrrQIGVVLQDVFLFS-GTIRENITLGDPDAT------DEEIIEAARLAGLHDFIEALPm 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 75 ----------RELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLrTDLLDLWTQGRmpikSVLIVTHNiEEAV 144
Cdd:COG2274 600 gydtvvgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAII-LENLRRLLKGR----TVIIIAHR-LSTI 673
|
....*....
gi 1861249672 145 FMCDRILVL 153
Cdd:COG2274 674 RLADRIIVL 682
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-109 |
2.80e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 85.02 E-value: 2.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEG--------VAMVFQT-FA-LFPWLTVLQNVEAGLEA-LGVGARERRERALAAIDLIGLDG- 68
Cdd:PRK11308 67 PTGGELYYQGQDLLKADPEaqkllrqkIQIVFQNpYGsLNPRKKVGQILEEPLLInTSLSAAERREKALAMMAKVGLRPe 146
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1861249672 69 FENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDV 109
Cdd:PRK11308 147 HYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDV 187
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-153 |
3.88e-20 |
|
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: 85.89 E-value: 3.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 2 TGGEVTYLGKPLTGPAEG---------VAMVFQ---TfALFPWLTVLQNVEAGLEA-LGVGARERRERALAAIDLIGLDG 68
Cdd:COG4172 67 PSGSILFDGQDLLGLSERelrrirgnrIAMIFQepmT-SLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPD 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 69 FE---NAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLT-AETLrtDLL-DLWTQGRMpikSVLIVTHNIeeA 143
Cdd:COG4172 146 PErrlDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVqAQIL--DLLkDLQRELGM---ALLLITHDL--G 218
|
170
....*....|..
gi 1861249672 144 VF--MCDRILVL 153
Cdd:COG4172 219 VVrrFADRVAVM 230
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
29-155 |
4.05e-20 |
|
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: 82.98 E-value: 4.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 29 LFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALD 108
Cdd:cd03218 86 IFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1861249672 109 VLTAETLRTDLLDLWTQGrmpIkSVLIVTHNIEEAVFMCDRILVLSS 155
Cdd:cd03218 166 PIAVQDIQKIIKILKDRG---I-GVLITDHNVRETLSITDRAYIIYE 208
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
25-155 |
4.51e-20 |
|
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: 82.24 E-value: 4.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 25 QTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPF 104
Cdd:cd03264 79 QEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1861249672 105 SALDVLTAETLRTDLLDLWTQgrmpiKSVLIVTHNIEEAVFMCDRILVLSS 155
Cdd:cd03264 159 AGLDPEERIRFRNLLSELGED-----RIVILSTHIVEDVESLCNQVAVLNK 204
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-143 |
8.24e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 82.17 E-value: 8.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEG---------VAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFEN 71
Cdd:PRK11629 61 PTSGDVIFNGQPMSKLSSAakaelrnqkLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRAN 140
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861249672 72 AYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDL-WTQGrmpiKSVLIVTHNIEEA 143
Cdd:PRK11629 141 HRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQG----TAFLVVTHDLQLA 209
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
53-153 |
8.76e-20 |
|
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: 80.94 E-value: 8.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 53 RRERA--LA----AIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVltaeTLRTDLLDLWTQ- 125
Cdd:cd03214 68 PKELArkIAyvpqALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDI----AHQIELLELLRRl 143
|
90 100
....*....|....*....|....*...
gi 1861249672 126 GRMPIKSVLIVTHNIEEAVFMCDRILVL 153
Cdd:cd03214 144 ARERGKTVVMVLHDLNLAARYADRVILL 171
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-153 |
9.42e-20 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 82.47 E-value: 9.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTG--PAE---GVAMVFQTFAL-FPWlTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYP 74
Cdd:COG4559 53 PSSGEVRLNGRPLAAwsPWElarRRAVLPQHSSLaFPF-TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 75 RELSGGMRQRVGFARALV-----VDPT--ILLMDEPFSALDVL----TAETLRTdlldlWTQGRMpikSVLIVTHNIEEA 143
Cdd:COG4559 132 QTLSGGEQQRVQLARVLAqlwepVDGGprWLFLDEPTSALDLAhqhaVLRLARQ-----LARRGG---GVVAVLHDLNLA 203
|
170
....*....|
gi 1861249672 144 VFMCDRILVL 153
Cdd:COG4559 204 AQYADRILLL 213
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-154 |
1.29e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 82.13 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTG--PAE---GVAMVFQTFAL-FPWlTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYP 74
Cdd:PRK13548 54 PDSGEVRLNGRPLADwsPAElarRRAVLPQHSSLsFPF-TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDY 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 75 RELSGGMRQRVGFARALV------VDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRMpikSVLIVTHNIEEAVFMCD 148
Cdd:PRK13548 133 PQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGL---AVIVVLHDLNLAARYAD 209
|
....*.
gi 1861249672 149 RILVLS 154
Cdd:PRK13548 210 RIVLLH 215
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
20-153 |
4.04e-19 |
|
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 upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 80.94 E-value: 4.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 20 VAMVFQ--------TfalfpwlTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARAL 91
Cdd:TIGR04520 79 VGMVFQnpdnqfvgA-------TVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVL 151
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1861249672 92 VVDPTILLMDEPFSALD------VL-TAETLRTDlldlwtQGrmpiKSVLIVTHNIEEAVfMCDRILVL 153
Cdd:TIGR04520 152 AMRPDIIILDEATSMLDpkgrkeVLeTIRKLNKE------EG----ITVISITHDMEEAV-LADRVIVM 209
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
23-153 |
5.37e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 81.84 E-value: 5.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 23 VFQTFALFPWLTVLQNVEAGLealgvgARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDE 102
Cdd:PRK11144 81 VFQDARLFPHYKVRGNLRYGM------AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDE 154
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1861249672 103 PFSALDVLTAETLRTDLLDLWTQGRMPIksvLIVTHNIEEAVFMCDRILVL 153
Cdd:PRK11144 155 PLASLDLPRKRELLPYLERLAREINIPI---LYVSHSLDEILRLADRVVVL 202
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1-153 |
7.88e-19 |
|
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: 82.12 E-value: 7.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEG-----VAMVFQTFALFPwLTVLQNV-----EAGLEALgvgarerreraLAAIDLIGLDGFE 70
Cdd:COG4987 387 PQSGSITLGGVDLRDLDEDdlrrrIAVVPQRPHLFD-TTLRENLrlarpDATDEEL-----------WAALERVGLGDWL 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 71 NAYP-----------RELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDlWTQGRmpikSVLIVTHN 139
Cdd:COG4987 455 AALPdgldtwlgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLE-ALAGR----TVLLITHR 529
|
170
....*....|....
gi 1861249672 140 iEEAVFMCDRILVL 153
Cdd:COG4987 530 -LAGLERMDRILVL 542
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1-143 |
8.08e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 78.81 E-value: 8.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTylgkplTGPAEGVAMVFQTFAL---FPwLTVLQNVEAGLEA----LGVGARERRERALAAIDLIGLDGFENAY 73
Cdd:NF040873 44 PTSGTVR------RAGGARVAYVPQRSEVpdsLP-LTVRDLVAMGRWArrglWRRLTRDDRAAVDDALERVGLADLAGRQ 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1861249672 74 PRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRtDLLDLWT-QGRmpikSVLIVTHNIEEA 143
Cdd:NF040873 117 LGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERII-ALLAEEHaRGA----TVVVVTHDLELV 182
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1-155 |
8.30e-19 |
|
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: 79.40 E-value: 8.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTG------PAEGVAMVFQTFALFPWLTVLQNVEAGLEALGVGARERR-ERALAAIDLigLDGFENAY 73
Cdd:cd03224 52 PRSGSIRFDGRDITGlppherARAGIGYVPEGRRIFPELTVEENLLLGAYARRRAKRKARlERVYELFPR--LKERRKQL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 74 PRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRmpikSVLIVTHNIEEAVFMCDRILVL 153
Cdd:cd03224 130 AGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGV----TILLVEQNARFALEIADRAYVL 205
|
..
gi 1861249672 154 SS 155
Cdd:cd03224 206 ER 207
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-155 |
1.13e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 80.65 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAE----GVAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRE 76
Cdd:PRK13536 93 PDAGKITVLGVPVPARARlaraRIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSD 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDV----LTAETLRTdlldLWTQGrmpiKSVLIVTHNIEEAVFMCDRILV 152
Cdd:PRK13536 173 LSGGMKRRLTLARALINDPQLLILDEPTTGLDPharhLIWERLRS----LLARG----KTILLTTHFMEEAERLCDRLCV 244
|
...
gi 1861249672 153 LSS 155
Cdd:PRK13536 245 LEA 247
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1-153 |
1.30e-18 |
|
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: 78.41 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEGVAMV---FQTFALFPWLTVLQNveagLEALGVGARERRERALAAIDLIGLDGFENAYPREL 77
Cdd:cd03268 52 PDSGEITFDGKSYQKNIEALRRIgalIEAPGFYPNLTAREN----LRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGF 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861249672 78 SGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVL 153
Cdd:cd03268 128 SLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQG----ITVLISSHLLSEIQKVADRIGII 199
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-153 |
1.46e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 79.67 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPA-----EGVAMVFQT-FALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYP 74
Cdd:PRK13635 59 PEAGTITVGGMVLSEETvwdvrRQVGMVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREP 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 75 RELSGGMRQRVGFARALVVDPTILLMDEPFSALD------VLtaETLRtdllDLWTQGRMpikSVLIVTHNIEEAVFmCD 148
Cdd:PRK13635 139 HRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDprgrreVL--ETVR----QLKEQKGI---TVLSITHDLDEAAQ-AD 208
|
....*
gi 1861249672 149 RILVL 153
Cdd:PRK13635 209 RVIVM 213
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
18-139 |
1.71e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 81.31 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 18 EGVAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTI 97
Cdd:PRK10535 86 EHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQV 165
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1861249672 98 LLMDEPFSALDVLTAETLRTDLLDLWTQGRmpikSVLIVTHN 139
Cdd:PRK10535 166 ILADEPTGALDSHSGEEVMAILHQLRDRGH----TVIIVTHD 203
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-153 |
2.68e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 80.59 E-value: 2.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLT--GPAE---GVAMVFQTFALFPwLTVLQNVeagleALGvgaRER--RERALAAIDLIGLDGFENAY 73
Cdd:COG1132 392 PTSGRILIDGVDIRdlTLESlrrQIGVVPQDTFLFS-GTIRENI-----RYG---RPDatDEEVEEAAKAAQAHEFIEAL 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 74 P-----------RELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLwTQGRMpiksVLIVTHNIeE 142
Cdd:COG1132 463 PdgydtvvgergVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERL-MKGRT----TIVIAHRL-S 536
|
170
....*....|.
gi 1861249672 143 AVFMCDRILVL 153
Cdd:COG1132 537 TIRNADRILVL 547
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-155 |
4.35e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 78.69 E-value: 4.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPA----EGVAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRE 76
Cdd:PRK13537 59 PDAGSISLCGEPVPSRArharQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGE 138
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVLSS 155
Cdd:PRK13537 139 LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARG----KTILLTTHFMEEAERLCDRLCVIEE 213
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-143 |
6.45e-18 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 77.38 E-value: 6.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 4 GEVTYLGKPLTGPAEG-------VAMVFQTFALFPwLTVLQNVEAGLEALGVGAR----ERRERAL--AAI------DLi 64
Cdd:COG1117 71 GEILLDGEDIYDPDVDvvelrrrVGMVFQKPNPFP-KSIYDNVAYGLRLHGIKSKseldEIVEESLrkAALwdevkdRL- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 65 gldgfeNAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALD-VLTA------ETLRTDLldlwtqgrmpikSVLIVT 137
Cdd:COG1117 149 ------KKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpISTAkieeliLELKKDY------------TIVIVT 210
|
....*.
gi 1861249672 138 HNIEEA 143
Cdd:COG1117 211 HNMQQA 216
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-149 |
9.54e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 77.12 E-value: 9.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 4 GEVTYLGKPLTGPA-------EGVAMVFQTFALFPwLTVLQNVEAGLEALGVGARERRERALAAiDLIGLDGFENAYPR- 75
Cdd:PRK14239 65 GSIVYNGHNIYSPRtdtvdlrKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEK-SLKGASIWDEVKDRl 142
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1861249672 76 -----ELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRMpiksvLIVTHNIEEAVFMCDR 149
Cdd:PRK14239 143 hdsalGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTM-----LLVTRSMQQASRISDR 216
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
52-142 |
1.59e-17 |
|
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: 76.28 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 52 ERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRtDLLDLWTQGRMPik 131
Cdd:COG1119 118 EQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLL-ALLDKLAAEGAP-- 194
|
90
....*....|.
gi 1861249672 132 SVLIVTHNIEE 142
Cdd:COG1119 195 TLVLVTHHVEE 205
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-154 |
1.80e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 76.65 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEG-------VAMVFQT-----FAlfPwlTVLQNVEAGLEALGVGARERRERALAAIDLIGLDG 68
Cdd:PRK13639 54 PTSGEVLIKGEPIKYDKKSllevrktVGIVFQNpddqlFA--P--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 69 FENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCD 148
Cdd:PRK13639 130 FENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEG----ITIIISTHDVDLVPVYAD 205
|
....*.
gi 1861249672 149 RILVLS 154
Cdd:PRK13639 206 KVYVMS 211
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
59-154 |
2.59e-17 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 75.27 E-value: 2.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 59 AAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLrTDLLDLWTQGRMpikSVLIVTH 138
Cdd:TIGR03771 96 DALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELL-TELFIELAGAGT---AILMTTH 171
|
90
....*....|....*.
gi 1861249672 139 NIEEAVFMCDRILVLS 154
Cdd:TIGR03771 172 DLAQAMATCDRVVLLN 187
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
23-153 |
2.64e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 76.20 E-value: 2.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 23 VFQTFALFPWLTVLQNVEAGleALGVG----------ARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALV 92
Cdd:PRK09984 91 IFQQFNLVNRLSVLENVLIG--ALGSTpfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALM 168
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1861249672 93 VDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVL 153
Cdd:PRK09984 169 QQAKVILADEPIASLDPESARIVMDTLRDINQNDGI---TVVVTLHQVDYALRYCERIVAL 226
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
20-154 |
2.66e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 75.30 E-value: 2.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 20 VAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILL 99
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1861249672 100 MDEPFSALDvltaETLRTDLLDLWTQGRMPIKSVLIVTHNIEEAVFMCDRILVLS 154
Cdd:PRK10908 161 ADEPTGNLD----DALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLS 211
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
35-156 |
3.62e-17 |
|
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: 3.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 35 VLQNVEAGL------EALGVGAR---ERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFS 105
Cdd:cd03226 76 VMQDVDYQLftdsvrEELLLGLKeldAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1861249672 106 ALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVLSSN 156
Cdd:cd03226 156 GLDYKNMERVGELIRELAAQG----KAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-154 |
3.77e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 75.64 E-value: 3.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGP-----AEGVAMVFQ--TFALFPWLTVLQNVEAGLE-ALGVGARERRERALAAIDLIGLDGfENA 72
Cdd:COG4167 65 PTSGEILINGHKLEYGdykyrCKHIRMIFQdpNTSLNPRLNIGQILEEPLRlNTDLTAEEREERIFATLRLVGLLP-EHA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 73 --YPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVltaeTLRTD----LLDLwtQGRMPIkSVLIVTHNIEEAVFM 146
Cdd:COG4167 144 nfYPHMLSSGQKQRVALARALILQPKIIIADEALAALDM----SVRSQiinlMLEL--QEKLGI-SYIYVSQHLGIVKHI 216
|
....*...
gi 1861249672 147 CDRILVLS 154
Cdd:COG4167 217 SDKVLVMH 224
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
2-154 |
3.95e-17 |
|
nickel import ATP-binding protein NikD; This family represents the NikD 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. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 75.10 E-value: 3.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 2 TGGEVTYLGKPLTGPA---EGVAMVFQT--FALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFE---NAY 73
Cdd:TIGR02770 43 TSGEILLDGRPLLPLSirgRHIATIMQNprTAFNPLFTMGNHAIETLRSLGKLSKQARALILEALEAVGLPDPEevlKKY 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 74 PRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLrTDLLDLWTQGRMPikSVLIVTHNIEEAVFMCDRILVL 153
Cdd:TIGR02770 123 PFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQARV-LKLLRELRQLFGT--GILLITHDLGVVARIADEVAVM 199
|
.
gi 1861249672 154 S 154
Cdd:TIGR02770 200 D 200
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-153 |
6.36e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 75.25 E-value: 6.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTgPAEG----------VAMVFQtfalFPWL-----TVLQNVEAGLEALGVGARERRERALAAIDLIG 65
Cdd:PRK13641 59 PSSGTITIAGYHIT-PETGnknlkklrkkVSLVFQ----FPEAqlfenTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 66 L-DGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTaetlRTDLLDLWTQGRMPIKSVLIVTHNIEEAV 144
Cdd:PRK13641 134 LsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG----RKEMMQLFKDYQKAGHTVILVTHNMDDVA 209
|
....*....
gi 1861249672 145 FMCDRILVL 153
Cdd:PRK13641 210 EYADDVLVL 218
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
2-153 |
8.16e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 75.51 E-value: 8.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 2 TGGEVTYLGKPLTGPAEG--------VAMVFQT--FALFPWLTVLQNVEAGLEAL--GVGARERRERALAAIDLIGL-DG 68
Cdd:PRK15079 74 TDGEVAWLGKDLLGMKDDewravrsdIQMIFQDplASLNPRMTIGEIIAEPLRTYhpKLSRQEVKDRVKAMMLKVGLlPN 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 69 FENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLwtQGRMPIkSVLIVTHNIEEAVFMCD 148
Cdd:PRK15079 154 LINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQL--QREMGL-SLIFIAHDLAVVKHISD 230
|
....*
gi 1861249672 149 RILVL 153
Cdd:PRK15079 231 RVLVM 235
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
77-153 |
1.05e-16 |
|
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: 72.46 E-value: 1.05e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVL 153
Cdd:cd03216 83 LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQG----VAVIFISHRLDEVFEIADRVTVL 155
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-153 |
1.11e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.90 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 4 GEVTYLGKPLTG-------PAEG-VAMVFQ--TFALFPWLTVLQNVEAGLEA--LGVGARERRERALAAIDLIGLD-GFE 70
Cdd:PRK15134 340 GEIWFDGQPLHNlnrrqllPVRHrIQVVFQdpNSSLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDpETR 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 71 NAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRI 150
Cdd:PRK15134 420 HRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQL---AYLFISHDLHVVRALCHQV 496
|
...
gi 1861249672 151 LVL 153
Cdd:PRK15134 497 IVL 499
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
55-153 |
1.64e-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: 73.01 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 55 ERALAAIDLIGLDGFENAYP-----------RELSGGMRQRVGFARALVVDPTILLMDEPFSALDvLTAETLRTDLLDLW 123
Cdd:cd03245 108 ERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLLDEPTSAMD-MNSEERLKERLRQL 186
|
90 100 110
....*....|....*....|....*....|
gi 1861249672 124 TQGrmpiKSVLIVTHNIeEAVFMCDRILVL 153
Cdd:cd03245 187 LGD----KTLIIITHRP-SLLDLVDRIIVM 211
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-153 |
2.77e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 73.57 E-value: 2.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEG--------VAMVFQTF--ALFPWLTVLQNVEAGLEAL-GVGARERRERALAAIDLIGLD-G 68
Cdd:PRK10419 64 PSQGNVSWRGEPLAKLNRAqrkafrrdIQMVFQDSisAVNPRKTVREIIREPLRHLlSLDKAERLARASEMLRAVDLDdS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 69 FENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALD-VLTAETLRTdLLDLWTQGRMpikSVLIVTHNIEEAVFMC 147
Cdd:PRK10419 144 VLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDlVLQAGVIRL-LKKLQQQFGT---ACLFITHDLRLVERFC 219
|
....*.
gi 1861249672 148 DRILVL 153
Cdd:PRK10419 220 QRVMVM 225
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1-153 |
3.67e-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: 74.41 E-value: 3.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTG-----PAEGVAMVFQTFALFPWlTVLQNveagleaLGVGARERRERAL-AAIDLIGLDGFENAYP 74
Cdd:COG4988 389 PYSGSILINGVDLSDldpasWRRQIAWVPQNPYLFAG-TIREN-------LRLGRPDASDEELeAALEAAGLDEFVAALP 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 75 -----------RELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWtQGRMpiksVLIVTHNIEEA 143
Cdd:COG4988 461 dgldtplgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRT----VILITHRLALL 535
|
170
....*....|
gi 1861249672 144 VFMcDRILVL 153
Cdd:COG4988 536 AQA-DRILVL 544
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
20-153 |
4.52e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 72.84 E-value: 4.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 20 VAMVFQT-FALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTIL 98
Cdd:PRK13650 83 IGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKII 162
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1861249672 99 LMDEPFSALDVLTAETLRTDLLDLWTQGRMpikSVLIVTHNIEEaVFMCDRILVL 153
Cdd:PRK13650 163 ILDEATSMLDPEGRLELIKTIKGIRDDYQM---TVISITHDLDE-VALSDRVLVM 213
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-155 |
5.13e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 72.85 E-value: 5.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAE-----GVAMVFQ-----TFALfpwlTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFE 70
Cdd:PRK13647 57 PQRGRVKVMGREVNAENEkwvrsKVGLVFQdpddqVFSS----TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 71 NAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRI 150
Cdd:PRK13647 133 DKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQG----KTVIVATHDVDLAAEWADQV 208
|
....*
gi 1861249672 151 LVLSS 155
Cdd:PRK13647 209 IVLKE 213
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-153 |
5.42e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 72.77 E-value: 5.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 20 VAMVFQ--TFALFPwLTVLQNVEAGLEALGVGARERRERALAAIDLIGLD--GFENAYPRELSGGMRQRVGFARALVVDP 95
Cdd:PRK13637 85 VGLVFQypEYQLFE-ETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEP 163
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1861249672 96 TILLMDEPFSALDVLTAETLRTDLLDLWTQGRMPIksvLIVTHNIEEAVFMCDRILVL 153
Cdd:PRK13637 164 KILILDEPTAGLDPKGRDEILNKIKELHKEYNMTI---ILVSHSMEDVAKLADRIIVM 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-138 |
7.57e-16 |
|
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: 73.30 E-value: 7.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 20 VAMVFQ-TFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTIL 98
Cdd:TIGR03269 111 IAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLF 190
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1861249672 99 LMDEPFSALDVLTAETLRTDLLDLWTQGRMpikSVLIVTH 138
Cdd:TIGR03269 191 LADEPTGTLDPQTAKLVHNALEEAVKASGI---SMVLTSH 227
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
20-153 |
7.72e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 72.85 E-value: 7.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 20 VAMVFQ--TFALFPWLTV-LQNVEAGLEALGVGARERRERALAAIDLIGLDGFE---NAYPRELSGGMRQRVGFARALVV 93
Cdd:PRK11022 91 VAMIFQdpMTSLNPCYTVgFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQRVMIAMAIAC 170
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 94 DPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVL 153
Cdd:PRK11022 171 RPKLLIADEPTTALDVTIQAQIIELLLELQQKENM---ALVLITHDLALVAEAAHKIIVM 227
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
20-153 |
1.18e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 72.04 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 20 VAMVFQtFA---LFPwLTVLQNVEAGLEALGVGARERRERALAAIDLIGLD-GFENAYPRELSGGMRQRVGFARALVVDP 95
Cdd:PRK13651 107 VGVVFQ-FAeyqLFE-QTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDeSYLQRSPFELSGGQKRRVALAGILAMEP 184
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 96 TILLMDEPFSALD-VLTAETLrtDLLD-LWTQGrmpiKSVLIVTHNIEEAVFMCDRILVL 153
Cdd:PRK13651 185 DFLVFDEPTAGLDpQGVKEIL--EIFDnLNKQG----KTIILVTHDLDNVLEWTKRTIFF 238
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-153 |
3.66e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 70.46 E-value: 3.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 4 GEVTYLGKPL-----TGPAEGVAMVFQTFALFPWLTVLQNVEAGLEALGVG-ARERRERALAAIDLIGLdgFENAYPR-- 75
Cdd:PRK14246 71 GKVLYFGKDIfqidaIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGL--WKEVYDRln 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 76 ----ELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQgrmpiKSVLIVTHNIEEAVFMCDRIL 151
Cdd:PRK14246 149 spasQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-----IAIVIVSHNPQQVARVADYVA 223
|
..
gi 1861249672 152 VL 153
Cdd:PRK14246 224 FL 225
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
20-154 |
4.38e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 70.65 E-value: 4.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 20 VAMVFQ--TFALFPwLTVLQNVEAGLEALGVGARERRERALAAIDLIGLD-GFENAYPRELSGGMRQRVGFARALVVDPT 96
Cdd:PRK13631 118 VSMVFQfpEYQLFK-DTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDdSYLERSPFGLSGGQKRRVAIAGILAIQPE 196
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1861249672 97 ILLMDEPFSALDVLTAETLRTDLLDLWTQGRmpikSVLIVTHNIEEAVFMCDRILVLS 154
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLILDAKANNK----TVFVITHTMEHVLEVADEVIVMD 250
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-154 |
4.50e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 70.26 E-value: 4.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEG-------VAMVFQT--FALFPwLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFEN 71
Cdd:PRK13636 58 PSSGRILFDGKPIDYSRKGlmklresVGMVFQDpdNQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKD 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 72 AYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALD-VLTAETLRtdlLDLWTQGRMPIkSVLIVTHNIEEAVFMCDRI 150
Cdd:PRK13636 137 KPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDpMGVSEIMK---LLVEMQKELGL-TIIIATHDIDIVPLYCDNV 212
|
....
gi 1861249672 151 LVLS 154
Cdd:PRK13636 213 FVMK 216
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-153 |
5.94e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 69.49 E-value: 5.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 4 GEVTYLGKPLTGPA-------EGVAMVFQTFALFPWLTVLQNVEAGLE--ALGVGARERRERALAAIDLIGL-DGFE--- 70
Cdd:PRK14267 64 GEVRLFGRNIYSPDvdpievrREVGMVFQYPNPFPHLTIYDNVAIGVKlnGLVKSKKELDERVEWALKKAALwDEVKdrl 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 71 NAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQgrmpiKSVLIVTHNIEEAVFMCDRI 150
Cdd:PRK14267 144 NDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-----YTIVLVTHSPAQAARVSDYV 218
|
...
gi 1861249672 151 LVL 153
Cdd:PRK14267 219 AFL 221
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-154 |
7.68e-15 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 67.84 E-value: 7.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEGVAMvfqtfalfpwltvlqnveagleALGVG--ARERRERALaaidLIGLDGFEN-AYPREL 77
Cdd:cd03215 52 PASGEITLDGKPVTRRSPRDAI----------------------RAGIAyvPEDRKREGL----VLDLSVAENiALSSLL 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861249672 78 SGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVLS 154
Cdd:cd03215 106 SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAG----KAVLLISSELDELLGLCDRILVMY 178
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-149 |
1.07e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 69.35 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 20 VAMVFQTFALFPwLTVLQNVEAGLEALG-VGARERRERALAAIDLIGL-DGFENAY---PRELSGGMRQRVGFARALVVD 94
Cdd:PRK14271 103 VGMLFQRPNPFP-MSIMDNVLAGVRAHKlVPRKEFRGVAQARLTEVGLwDAVKDRLsdsPFRLSGGQQQLLCLARTLAVN 181
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1861249672 95 PTILLMDEPFSALDVLTAETLRTDLLDLwtQGRMpikSVLIVTHNIEEAVFMCDR 149
Cdd:PRK14271 182 PEVLLLDEPTSALDPTTTEKIEEFIRSL--ADRL---TVIIVTHNLAQAARISDR 231
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
77-153 |
1.28e-14 |
|
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: 67.88 E-value: 1.28e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLdlwtQGR-MPIKSVLIVTHNIeEAVFMCDRILVL 153
Cdd:cd03250 128 LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCI----LGLlLNNKTRILVTHQL-QLLPHADQIVVL 200
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1-153 |
1.30e-14 |
|
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: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGK--PLTGPAEGvamvFQtfalfPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELS 78
Cdd:cd03220 74 PDSGTVTVRGRvsSLLGLGGG----FN-----PELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYS 144
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861249672 79 GGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRmpikSVLIVTHNIEEAVFMCDRILVL 153
Cdd:cd03220 145 SGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGK----TVILVSHDPSSIKRLCDRALVL 215
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1-153 |
1.39e-14 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 70.01 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAE-----GVAMVFQTFALFPWlTVLQNVeaGLEALGVGARERREralaAIDLIGLDGFENAYP- 74
Cdd:TIGR02857 374 PTEGSIAVNGVPLADADAdswrdQIAWVPQHPFLFAG-TIAENI--RLARPDASDAEIRE----ALERAGLDEFVAALPq 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 75 ----------RELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLwTQGRmpikSVLIVTHNIEEAV 144
Cdd:TIGR02857 447 gldtpigeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGR----TVLLVTHRLALAA 521
|
....*....
gi 1861249672 145 fMCDRILVL 153
Cdd:TIGR02857 522 -LADRIVVL 529
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
17-153 |
1.89e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 68.98 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 17 AEGVAMVFQ--TFALFPWLTV-LQNVEAGLEALGVGARERRE---RALAAIDLIGLDGFENAYPRELSGGMRQRVGFARA 90
Cdd:PRK09473 96 AEQISMIFQdpMTSLNPYMRVgEQLMEVLMLHKGMSKAEAFEesvRMLDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMA 175
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861249672 91 LVVDPTILLMDEPFSALDVLTAETLRTDLLDLwtqGRMPIKSVLIVTHNIEEAVFMCDRILVL 153
Cdd:PRK09473 176 LLCRPKLLIADEPTTALDVTVQAQIMTLLNEL---KREFNTAIIMITHDLGVVAGICDKVLVM 235
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-156 |
2.25e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 68.14 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 20 VAMVFQTFALFPwLTVLQNVEAGLEALG----VGARERRERALAAIDLigLDGFENAYPR---ELSGGMRQRVGFARALV 92
Cdd:PRK14258 90 VSMVHPKPNLFP-MSVYDNVAYGVKIVGwrpkLEIDDIVESALKDADL--WDEIKHKIHKsalDLSGGQQQRLCIARALA 166
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861249672 93 VDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVLSSN 156
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSEL---TMVIVSHNLHQVSRLSDFTAFFKGN 227
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-153 |
3.69e-14 |
|
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: 66.93 E-value: 3.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTG-PAE-----GVAMVFQTFALFPWLTVLQNVEAGleALGVGARERRERALAAIdligLDGFENAYP 74
Cdd:COG0410 55 PRSGSIRFDGEDITGlPPHriarlGIGYVPEGRRIFPSLTVEENLLLG--AYARRDRAEVRADLERV----YELFPRLKE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 75 R------ELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCD 148
Cdd:COG0410 129 RrrqragTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREG----VTILLVEQNARFALEIAD 204
|
....*
gi 1861249672 149 RILVL 153
Cdd:COG0410 205 RAYVL 209
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
77-153 |
5.83e-14 |
|
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: 65.32 E-value: 5.83e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLwtqgRMPIKSVLIVTHNIeEAVFMCDRILVL 153
Cdd:cd03246 97 LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAAL----KAAGATRIVIAHRP-ETLASADRILVL 168
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1-155 |
6.85e-14 |
|
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: 66.34 E-value: 6.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPA-----EGVAMVFQTFALFPwLTVLQNVEAGLEALGVGARERRERALAAIDLIglDGFENAYPR 75
Cdd:cd03248 66 PQGGQVLLDGKPISQYEhkylhSKVSLVGQEPVLFA-RSLQDNIAYGLQSCSFECVKEAAQKAHAHSFI--SELASGYDT 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 76 E-------LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDlWTQGRmpikSVLIVTHNIeEAVFMCD 148
Cdd:cd03248 143 EvgekgsqLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYD-WPERR----TVLVIAHRL-STVERAD 216
|
....*..
gi 1861249672 149 RILVLSS 155
Cdd:cd03248 217 QILVLDG 223
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
4-148 |
7.35e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 66.73 E-value: 7.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 4 GEVTYLGKPLTG----PAE---GVAMVFQTFALFPwLTVLQNVEAGLEALG--VGARERRERAL--AAI-----DLIGLD 67
Cdd:PRK14243 70 GKVTFHGKNLYApdvdPVEvrrRIGMVFQKPNPFP-KSIYDNIAYGARINGykGDMDELVERSLrqAALwdevkDKLKQS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 68 GFEnaypreLSGGMRQRVGFARALVVDPTILLMDEPFSALD---VLTAETLRTDLLDLWTqgrmpiksVLIVTHNIEEAV 144
Cdd:PRK14243 149 GLS------LSGGQQQRLCIARAIAVQPEVILMDEPCSALDpisTLRIEELMHELKEQYT--------IIIVTHNMQQAA 214
|
....
gi 1861249672 145 FMCD 148
Cdd:PRK14243 215 RVSD 218
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
19-154 |
9.77e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.07 E-value: 9.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 19 GVAMVFQTFALFPWLTVLQNVEAGLEAL-GVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTI 97
Cdd:PRK10895 79 GIGYLPQEASIFRRLSVYDNLMAVLQIRdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKF 158
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1861249672 98 LLMDEPFSALDVLTAETLRTDLLDLWTQGRmpikSVLIVTHNIEEAVFMCDRILVLS 154
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRIIEHLRDSGL----GVLITDHNVRETLAVCERAYIVS 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-149 |
1.05e-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: 67.13 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEV-----------TYLGKPLTGPAEG-VAMVFQTFALFPWLTVLQNVEaglEALGVGARERRERALAAIDLIGLdG 68
Cdd:TIGR03269 336 PTSGEVnvrvgdewvdmTKPGPDGRGRAKRyIGILHQEYDLYPHRTVLDNLT---EAIGLELPDELARMKAVITLKMV-G 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 69 FE--------NAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLdlwtQGRMPI-KSVLIVTHN 139
Cdd:TIGR03269 412 FDeekaeeilDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIL----KAREEMeQTFIIVSHD 487
|
170
....*....|
gi 1861249672 140 IEEAVFMCDR 149
Cdd:TIGR03269 488 MDFVLDVCDR 497
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
18-153 |
1.22e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 66.36 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 18 EGVAMVFQT-FALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPT 96
Cdd:PRK13640 84 EKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPK 163
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1861249672 97 ILLMDEPFSALDVLTAETLRTDLLDLWTQGRMPIKSvliVTHNIEEAVfMCDRILVL 153
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVIS---ITHDIDEAN-MADQVLVL 216
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
77-154 |
2.27e-13 |
|
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: 64.94 E-value: 2.27e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLwTQGRmpikSVLIVTHNIEEAVfMCDRILVLS 154
Cdd:cd03253 138 LSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDV-SKGR----TTIVIAHRLSTIV-NADKIIVLK 209
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-153 |
3.61e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.70 E-value: 3.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGP------AEGVAMVFQTFALFPWLTVLQNVEAGL--EALGVGARER-RERALAAIDLIGLDGFEN 71
Cdd:PRK11288 56 PDAGSILIDGQEMRFAsttaalAAGVAIIYQELHLVPEMTVAENLYLGQlpHKGGIVNRRLlNYEAREQLEHLGVDIDPD 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 72 AYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRMpiksVLIVTHNIEEAVFMCDRIL 151
Cdd:PRK11288 136 TPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRV----ILYVSHRMEEIFALCDAIT 211
|
..
gi 1861249672 152 VL 153
Cdd:PRK11288 212 VF 213
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
64-154 |
4.55e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 64.63 E-value: 4.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 64 IGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRmpiKSVLIVTHNIEEA 143
Cdd:PRK13632 130 VGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRK---KTLISITHDMDEA 206
|
90
....*....|.
gi 1861249672 144 VfMCDRILVLS 154
Cdd:PRK13632 207 I-LADKVIVFS 216
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-155 |
4.61e-13 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 63.34 E-value: 4.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 2 TGGEVTYLGKPLT--GPAEGVAMVFQTFALFPWLTVLqnveaglEALGVGARERReralaaidligldgfenaypreLSG 79
Cdd:cd03213 64 VSGEVLINGRPLDkrSFRKIIGYVPQDDILHPTLTVR-------ETLMFAAKLRG----------------------LSG 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861249672 80 GMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRmpikSVLIVTHNIEEAVF-MCDRILVLSS 155
Cdd:cd03213 115 GERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGR----TIICSIHQPSSEIFeLFDKLLLLSQ 187
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
20-115 |
5.53e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 64.40 E-value: 5.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 20 VAMVFQTFALFPWLTVLQNVEAGL-EALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTIL 98
Cdd:PRK11831 86 MSMLFQSGALFTDMNVFDNVAYPLrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLI 165
|
90
....*....|....*..
gi 1861249672 99 LMDEPFSALDVLTAETL 115
Cdd:PRK11831 166 MFDEPFVGQDPITMGVL 182
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
46-153 |
7.61e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 63.79 E-value: 7.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 46 LGVGARE-RRERALAA-------IDLIGLDGFenayPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVltaeTLRT 117
Cdd:PRK11701 117 MAVGARHyGDIRATAGdwlerveIDAARIDDL----PTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDV----SVQA 188
|
90 100 110
....*....|....*....|....*....|....*...
gi 1861249672 118 DLLDLWTQ--GRMPIkSVLIVTHNIEEAVFMCDRILVL 153
Cdd:PRK11701 189 RLLDLLRGlvRELGL-AVVIVTHDLAVARLLAHRLLVM 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-154 |
1.12e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 64.27 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLT--GPAE----GVAMV---FQTFALFPWLTVLQNVE-AGLEALGVGA--RERRERALAA--IDLIGL 66
Cdd:COG1129 304 ADSGEIRLDGKPVRirSPRDairaGIAYVpedRKGEGLVLDLSIRENITlASLDRLSRGGllDRRRERALAEeyIKRLRI 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 67 ---DGFENAypRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLT-AETLRTdLLDLWTQGrmpiKSVLIVTHNIEE 142
Cdd:COG1129 384 ktpSPEQPV--GNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAkAEIYRL-IRELAAEG----KAVIVISSELPE 456
|
170
....*....|..
gi 1861249672 143 AVFMCDRILVLS 154
Cdd:COG1129 457 LLGLSDRILVMR 468
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
2-155 |
1.28e-12 |
|
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: 62.67 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 2 TGGEVTYLGKPLTgPAE---GVAMVFQTFALFPWLTVLQNVE-AGLEALGVGARERRERALAAIDLIGLDGFE---NAYP 74
Cdd:cd03234 63 TSGQILFNGQPRK-PDQfqkCVAYVRQDDILLPGLTVRETLTyTAILRLPRKSSDAIRKKRVEDVLLRDLALTrigGNLV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 75 RELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRMpiksVLIVTHNIEEAVF-MCDRILVL 153
Cdd:cd03234 142 KGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRI----VILTIHQPRSDLFrLFDRILLL 217
|
..
gi 1861249672 154 SS 155
Cdd:cd03234 218 SS 219
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
20-153 |
1.62e-12 |
|
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: 62.63 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 20 VAMVFQTFALFPWlTVLQNVEAGLEALGVGARERRERALAAIDLIglDGFENAYPRE-------LSGGMRQRVGFARALV 92
Cdd:cd03251 78 IGLVSQDVFLFND-TVAENIAYGRPGATREEVEEAARAANAHEFI--MELPEGYDTVigergvkLSGGQRQRIAIARALL 154
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861249672 93 VDPTILLMDEPFSALDVLTaETLRTDLLDLWTQGRmpikSVLIVTH---NIEEAvfmcDRILVL 153
Cdd:cd03251 155 KDPPILILDEATSALDTES-ERLVQAALERLMKNR----TTFVIAHrlsTIENA----DRIVVL 209
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-153 |
1.69e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.96 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 20 VAMVFQ--TFALFPwltvLQNVEAGL-EALGVGARERRERALAAIdLIGLD--GFENA------YPRELSGGMRQRVGFA 88
Cdd:PRK15134 94 IAMIFQepMVSLNP----LHTLEKQLyEVLSLHRGMRREAARGEI-LNCLDrvGIRQAakrltdYPHQLSGGERQRVMIA 168
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861249672 89 RALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVL 153
Cdd:PRK15134 169 MALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNM---GLLFITHNLSIVRKLADRVAVM 230
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-153 |
2.07e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 62.41 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGK---PLtgpaeGVAMVFQtfalfPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPREL 77
Cdd:COG1134 78 PTSGRVEVNGRvsaLL-----ELGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTY 147
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861249672 78 SGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRmpikSVLIVTHNIEEAVFMCDRILVL 153
Cdd:COG1134 148 SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGR----TVIFVSHSMGAVRRLCDRAIWL 219
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
13-153 |
2.10e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 63.08 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 13 LTGPAEGVAMVFQT-FALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARAL 91
Cdd:PRK13644 72 LQGIRKLVGIVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGIL 151
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861249672 92 VVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEaVFMCDRILVL 153
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKG----KTIVYITHNLEE-LHDADRIIVM 208
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-153 |
2.13e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 63.21 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 19 GVAMVFQTFALFPWlTVLQNVEAGLEALGVGARERRERALAAIDLIGLDG-FENAYPRELSGGMRQRVGFARALVVDPTI 97
Cdd:PRK13643 87 GVVFQFPESQLFEE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEV 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1861249672 98 LLMDEPFSALDvltaETLRTDLLDLWTQGRMPIKSVLIVTHNIEEAVFMCDRILVL 153
Cdd:PRK13643 166 LVLDEPTAGLD----PKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLL 217
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-153 |
2.40e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 62.73 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTyLG-------------KPLTgpaEGVAMVFQtFA---LFPwLTVLQNVEAGLEALGVGARERRERALAAIDLI 64
Cdd:PRK13634 59 PTSGTVT-IGervitagkknkklKPLR---KKVGIVFQ-FPehqLFE-ETVEKDICFGPMNFGVSEEDAKQKAREMIELV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 65 GLD-GFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDvltaETLRTDLLD----LWTQGRMpikSVLIVTHN 139
Cdd:PRK13634 133 GLPeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD----PKGRKEMMEmfykLHKEKGL---TTVLVTHS 205
|
170
....*....|....
gi 1861249672 140 IEEAVFMCDRILVL 153
Cdd:PRK13634 206 MEDAARYADQIVVM 219
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1-153 |
3.17e-12 |
|
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: 61.86 E-value: 3.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPA-----EGVAMVFQTFALFPWlTVLQNVEAGlealgvGARERRERALAAIDLIGLDGF----EN 71
Cdd:cd03254 55 PQKGQILIDGIDIRDISrkslrSMIGVVLQDTFLFSG-TIMENIRLG------RPNATDEEVIEAAKEAGAHDFimklPN 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 72 AY---PRE----LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLwtqgrMPIKSVLIVTHN---IE 141
Cdd:cd03254 128 GYdtvLGEnggnLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKL-----MKGRTSIIIAHRlstIK 202
|
170
....*....|..
gi 1861249672 142 EAvfmcDRILVL 153
Cdd:cd03254 203 NA----DKILVL 210
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-138 |
3.47e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 61.36 E-value: 3.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLT-------------GPAEGVAmvfqtfalfPWLTVLQNVEAGLEALGVGARERRERALAAIdliGLD 67
Cdd:PRK13538 53 PDAGEVLWQGEPIRrqrdeyhqdllylGHQPGIK---------TELTALENLRFYQRLHGPGDDEALWEALAQV---GLA 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1861249672 68 GFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRMpiksVLIVTH 138
Cdd:PRK13538 121 GFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGM----VILTTH 187
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
31-154 |
4.09e-12 |
|
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: 61.68 E-value: 4.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 31 PWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDgfEN---AYPRELSGGMRQRVGFARALVVDPTILLMDEPFSAL 107
Cdd:COG4778 106 PRVSALDVVAEPLLERGVDREEARARARELLARLNLP--ERlwdLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASL 183
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1861249672 108 DVLTAETLRTDLLDLWTQGRmpikSVLIVTHNIE--EAVfmCDRILVLS 154
Cdd:COG4778 184 DAANRAVVVELIEEAKARGT----AIIGIFHDEEvrEAV--ADRVVDVT 226
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-139 |
4.10e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.04 E-value: 4.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKP--LTGPAEGVAMVFQTFALFPWLTVLQNVEAGLEALGvgarERRERALAAIDLIGLDGFENAYPRELS 78
Cdd:PRK13539 54 PAAGTIKLDGGDidDPDVAEACHYLGHRNAMKPALTVAENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLS 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861249672 79 GGMRQRVGFARALVVDPTILLMDEPFSALDV----LTAETLRTDLldlwTQGRMpiksVLIVTHN 139
Cdd:PRK13539 130 AGQKRRVALARLLVSNRPIWILDEPTAALDAaavaLFAELIRAHL----AQGGI----VIAATHI 186
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-154 |
5.83e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 62.34 E-value: 5.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKP----LTGPAEGVAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRE 76
Cdd:TIGR01257 982 PTSGTVLVGGKDietnLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQD 1061
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLrTDLLDLWTQGRmpikSVLIVTHNIEEAVFMCDRILVLS 154
Cdd:TIGR01257 1062 LSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI-WDLLLKYRSGR----TIIMSTHHMDEADLLGDRIAIIS 1134
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-153 |
7.76e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.80 E-value: 7.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 20 VAMVFQ--TFALFPWLTVLQNVEaglEALGVGARERRERALAA----IDLIGLDGFE---NAYPRELSGGMRQRVGFARA 90
Cdd:PRK10261 106 MAMIFQepMTSLNPVFTVGEQIA---ESIRLHQGASREEAMVEakrmLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMA 182
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861249672 91 LVVDPTILLMDEPFSALDVltaeTLRTDLLDLWT--QGRMPIkSVLIVTHNIEEAVFMCDRILVL 153
Cdd:PRK10261 183 LSCRPAVLIADEPTTALDV----TIQAQILQLIKvlQKEMSM-GVIFITHDMGVVAEIADRVLVM 242
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1-109 |
8.17e-12 |
|
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: 60.45 E-value: 8.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTG----PAEGVAMVFQTFALFPWLTVLQNVEAgLEALGVGARERRERALAAIdliGLDGFENAYPRE 76
Cdd:TIGR01189 52 PDSGEVRWNGTPLAEqrdePHENILYLGHLPGLKPELSALENLHF-WAAIHGGAQRTIEDALAAV---GLTGFEDLPAAQ 127
|
90 100 110
....*....|....*....|....*....|...
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDV 109
Cdd:TIGR01189 128 LSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-153 |
8.29e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 61.16 E-value: 8.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTG-PAE-----GVAMVFQTFALFPWLTVLQN--------VEAGL-------EALGVGARERRERALA 59
Cdd:PRK11300 57 PTGGTILLRGQHIEGlPGHqiarmGVVRTFQHVRLFREMTVIENllvaqhqqLKTGLfsgllktPAFRRAESEALDRAAT 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 60 AIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDvlTAETlrTDLLDLWTQGRMPIK-SVLIVTH 138
Cdd:PRK11300 137 WLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLN--PKET--KELDELIAELRNEHNvTVLLIEH 212
|
170
....*....|....*
gi 1861249672 139 NIEEAVFMCDRILVL 153
Cdd:PRK11300 213 DMKLVMGISDRIYVV 227
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-154 |
8.90e-12 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 60.63 E-value: 8.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 20 VAMVFQTFALFPwLTVLQNVEAGLEALGVGARERRERALAAIDLIglDGFENAY-----PR--ELSGGMRQRVGFARALV 92
Cdd:cd03249 79 IGLVSQEPVLFD-GTIAENIRYGKPDATDEEVEEAAKKANIHDFI--MSLPDGYdtlvgERgsQLSGGQKQRIAIARALL 155
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861249672 93 VDPTILLMDEPFSALDVLTaETLRTDLLDLWTQGRMpiksVLIVTHNIeEAVFMCDRILVLS 154
Cdd:cd03249 156 RNPKILLLDEATSALDAES-EKLVQEALDRAMKGRT----TIVIAHRL-STIRNADLIAVLQ 211
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
74-153 |
9.24e-12 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 61.00 E-value: 9.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 74 PRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVltaeTLRTDLLDLwTQG--RMPIKSVLIVTHNIEEAVFMCDRIL 151
Cdd:TIGR02323 146 PRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDV----SVQARLLDL-LRGlvRDLGLAVIIVTHDLGVARLLAQRLL 220
|
..
gi 1861249672 152 VL 153
Cdd:TIGR02323 221 VM 222
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1-153 |
9.88e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 60.96 E-value: 9.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGP-----AEGVAMVFQTFALFPWLTVLQNVEAGLE----ALGVGARERRERALAAIDLIGLDGFEN 71
Cdd:PRK10575 63 PSEGEILLDAQPLESWsskafARKVAYLPQQLPAAEGMTVRELVAIGRYpwhgALGRFGAADREKVEEAISLVGLKPLAH 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 72 AYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVltaeTLRTDLLDLWTQ-GRMPIKSVLIVTHNIEEAVFMCDRI 150
Cdd:PRK10575 143 RLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI----AHQVDVLALVHRlSQERGLTVIAVLHDINMAARYCDYL 218
|
...
gi 1861249672 151 LVL 153
Cdd:PRK10575 219 VAL 221
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-153 |
1.30e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 61.28 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPA-----EGVAMVFQTFALFPWlTVLQNVEAGLEALGVGARERRERALAAIDLIGldGFENAYPR 75
Cdd:TIGR00958 533 PTGGQVLLDGVPLVQYDhhylhRQVALVGQEPVLFSG-SVRENIAYGLTDTPDEEIMAAAKAANAHDFIM--EFPNGYDT 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 76 E-------LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLldlwTQGRMPiksVLIVTHNIeEAVFMCD 148
Cdd:TIGR00958 610 EvgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESR----SRASRT---VLLIAHRL-STVERAD 681
|
....*
gi 1861249672 149 RILVL 153
Cdd:TIGR00958 682 QILVL 686
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
20-153 |
2.00e-11 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 60.89 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 20 VAMVFQTFALFPwLTVLQNVEAGleALGVGARERRERALAAIDLIGL-----DGF-----ENAypRELSGGMRQRVGFAR 89
Cdd:TIGR02203 408 VALVSQDVVLFN-DTIANNIAYG--RTEQADRAEIERALAAAYAQDFvdklpLGLdtpigENG--VLLSGGQRQRLAIAR 482
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861249672 90 ALVVDPTILLMDEPFSALDVlTAETLRTDLLDLWTQGRmpikSVLIVTH---NIEEAvfmcDRILVL 153
Cdd:TIGR02203 483 ALLKDAPILILDEATSALDN-ESERLVQAALERLMQGR----TTLVIAHrlsTIEKA----DRIVVM 540
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
20-153 |
2.34e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 60.36 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 20 VAMVFQTFALFPwLTVLQNVEAGLE-ALGVGARERRERAlAAIDLI-----GLDGFENAYPRELSGGMRQRVGFARALVV 93
Cdd:PRK13657 411 IAVVFQDAGLFN-RSIEDNIRVGRPdATDEEMRAAAERA-QAHDFIerkpdGYDTVVGERGRQLSGGERQRLAIARALLK 488
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861249672 94 DPTILLMDEPFSALDVLTAETLRtDLLDLWTQGRmpikSVLIVTH---NIEEAvfmcDRILVL 153
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVK-AALDELMKGR----TTFIIAHrlsTVRNA----DRILVF 542
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-154 |
2.49e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 59.64 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTG-PAEGVAmvfQTFALFPW-------LTVLQNVEAG----LEALGVGARERRERALAAIDLIGLDG 68
Cdd:PRK11231 54 PQSGTVFLGDKPISMlSSRQLA---RRLALLPQhhltpegITVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINH 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 69 FENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVltaeTLRTDLLDLWTQGRMPIKSVLIVTHNIEEAVFMCD 148
Cdd:PRK11231 131 LADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDI----NHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCD 206
|
....*.
gi 1861249672 149 RILVLS 154
Cdd:PRK11231 207 HLVVLA 212
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
77-153 |
3.33e-11 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 60.15 E-value: 3.33e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIeEAVFMCDRILVL 153
Cdd:COG4618 468 LSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARG----ATVVVITHRP-SLLAAVDKLLVL 539
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-153 |
3.44e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 59.43 E-value: 3.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGP-----AEGVAMVFQT-----FALfpwlTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFE 70
Cdd:PRK13652 56 PTSGSVLIRGEPITKEnirevRKFVGLVFQNpddqiFSP----TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 71 NAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRI 150
Cdd:PRK13652 132 DRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGM---TVIFSTHQLDLVPEMADYI 208
|
...
gi 1861249672 151 LVL 153
Cdd:PRK13652 209 YVM 211
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1-153 |
3.76e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 59.37 E-value: 3.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEG---------VAMVFQtfalFPWL-----TVLQNVEAGLEALGVGARERRERALAAIDLIGL 66
Cdd:PRK13649 59 PTQGSVRVDDTLITSTSKNkdikqirkkVGLVFQ----FPESqlfeeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 67 D-GFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTaetlRTDLLDLWTQGRMPIKSVLIVTHNIEEAVF 145
Cdd:PRK13649 135 SeSLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG----RKELMTLFKKLHQSGMTIVLVTHLMDDVAN 210
|
....*...
gi 1861249672 146 MCDRILVL 153
Cdd:PRK13649 211 YADFVYVL 218
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
77-154 |
4.12e-11 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 59.67 E-value: 4.12e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRmpikSVLIVTHNIeeAVFMC-DRILVLS 154
Cdd:TIGR01842 455 LSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGI----TVVVITHRP--SLLGCvDKILVLQ 527
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-153 |
5.61e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 58.77 E-value: 5.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 20 VAMVFQTFALFPWLTVLQNVEAGLE--ALGVGARERRERALAAIDLIGL-DGFEN---AYPRELSGGMRQRVGFARALVV 93
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKlnRLVKSKKELQERVRWALEKAQLwDEVKDrldAPAGKLSGGQQQRLCIARALAF 163
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 94 DPTILLMDEPFSALDVLTAETLRTDLLDLwtQGRMPIksvLIVTHNIEEAVFMCDRILVL 153
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLFLEL--KKDMTI---VLVTHFPQQAARISDYVAFL 218
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
35-155 |
5.81e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 58.95 E-value: 5.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 35 VLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAET 114
Cdd:PRK13633 103 VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRRE 182
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1861249672 115 LRTDLLDLwtQGRMPIKSVLIvTHNIEEAVfMCDRILVLSS 155
Cdd:PRK13633 183 VVNTIKEL--NKKYGITIILI-THYMEEAV-EADRIIVMDS 219
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1-139 |
6.02e-11 |
|
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: 59.30 E-value: 6.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEG-VAMVFQTFALFPWL---TVLQNVeagLEALGVGARERRERALAAIDLI--------GLDG 68
Cdd:TIGR02868 387 PLQGEVTLDGVPVSSLDQDeVRRRVSVCAQDAHLfdtTVRENL---RLARPDATDEELWAALERVGLAdwlralpdGLDT 463
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1861249672 69 FENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLwtqgrMPIKSVLIVTHN 139
Cdd:TIGR02868 464 VLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAA-----LSGRTVVLITHH 529
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
77-153 |
7.44e-11 |
|
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: 58.27 E-value: 7.44e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLwTQGRmpikSVLIVTHNIeEAVFMCDRILVL 153
Cdd:cd03252 139 LSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDI-CAGR----TVIIIAHRL-STVKNADRIIVM 209
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
51-157 |
1.28e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 57.97 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 51 RERRERALAAIDLIGldgFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRmpi 130
Cdd:PRK15056 120 RQIVTAALARVDMVE---FRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGK--- 193
|
90 100 110
....*....|....*....|....*....|..
gi 1861249672 131 kSVLIVTHNIEEAVFMCDRIL-----VLSSNP 157
Cdd:PRK15056 194 -TMLVSTHNLGSVTEFCDYTVmvkgtVLASGP 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-138 |
1.46e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 58.15 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYlgkpltGPAEGVAMVFQTFALFPWLTVLQNVEAGLEALGvGARERRERALAAID------------------ 62
Cdd:COG0488 50 PDSGEVSI------PKGLRIGYLPQEPPLDDDLTVLDTVLDGDAELR-ALEAELEELEAKLAepdedlerlaelqeefea 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 63 -------------LIGLdGFENAYP----RELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLwtQ 125
Cdd:COG0488 123 lggweaearaeeiLSGL-GFPEEDLdrpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNY--P 199
|
170
....*....|...
gi 1861249672 126 GrmpikSVLIVTH 138
Cdd:COG0488 200 G-----TVLVVSH 207
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
72-156 |
1.64e-10 |
|
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: 55.53 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 72 AYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLwtQGrmpikSVLIVTHNIEeavFM---CD 148
Cdd:cd03221 66 GYFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEY--PG-----TVILVSHDRY---FLdqvAT 135
|
....*...
gi 1861249672 149 RILVLSSN 156
Cdd:cd03221 136 KIIELEDG 143
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
11-150 |
1.67e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.21 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 11 KPLTG---PAEGVAMVF-------------------QTFALFPWLTVLQNVEagLEA--LGVGARERRERALAAIDLIGL 66
Cdd:NF033858 310 KMLTGllpASEGEAWLFgqpvdagdiatrrrvgymsQAFSLYGELTVRQNLE--LHArlFHLPAAEIAARVAEMLERFDL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 67 DGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRMPIksvLIVTHnieeavFM 146
Cdd:NF033858 388 ADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTI---FISTH------FM 458
|
....*....
gi 1861249672 147 -----CDRI 150
Cdd:NF033858 459 neaerCDRI 467
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
21-157 |
1.89e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.12 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 21 AMVFQTFALFPwLTVLQNVEAGLEAlgvGARERRERA--LAAIDLIgLDGFENAYP-------RELSGGMRQRVGFARAL 91
Cdd:PTZ00265 1299 SIVSQEPMLFN-MSIYENIKFGKED---ATREDVKRAckFAAIDEF-IESLPNKYDtnvgpygKSLSGGQKQRIAIARAL 1373
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861249672 92 VVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRmpiKSVLIVTHNIeEAVFMCDRILVLsSNP 157
Cdd:PTZ00265 1374 LREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAD---KTIITIAHRI-ASIKRSDKIVVF-NNP 1434
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-154 |
1.90e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 57.40 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 2 TGGEVTYLGKPLTG---PAEGVAMVFQT--FALFPWLTVLQNVEAGLEALGVGARERRerALAAIDLIGLDGFE---NAY 73
Cdd:PRK10418 60 TAGRVLLDGKPVAPcalRGRKIATIMQNprSAFNPLHTMHTHARETCLALGKPADDAT--LTAALEAVGLENAArvlKLY 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 74 PRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLtAETLRTDLLDLWTQGRMPikSVLIVTHNIEEAVFMCDRILVL 153
Cdd:PRK10418 138 PFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVV-AQARILDLLESIVQKRAL--GMLLVTHDMGVVARLADDVAVM 214
|
.
gi 1861249672 154 S 154
Cdd:PRK10418 215 S 215
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-153 |
1.93e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 57.49 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLT-----GPAEGVAMVFQ--TFALFPWLTVLQNVEAGLEA-LGVGARERRERALAAIDLIGL-DGFEN 71
Cdd:PRK15112 65 PTSGELLIDDHPLHfgdysYRSQRIRMIFQdpSTSLNPRQRISQILDFPLRLnTDLEPEQREKQIIETLRQVGLlPDHAS 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 72 AYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVltaeTLRTDLLDLW--TQGRMPIkSVLIVTHNIEEAVFMCDR 149
Cdd:PRK15112 145 YYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM----SMRSQLINLMleLQEKQGI-SYIYVTQHLGMMKHISDQ 219
|
....
gi 1861249672 150 ILVL 153
Cdd:PRK15112 220 VLVM 223
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
1-153 |
2.94e-10 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 57.26 E-value: 2.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPL-----TGPAEGVAMVFQTFALFPWlTVLQNV--------EAGLEalgvgarerreRAL--AAI-DLI 64
Cdd:TIGR03796 531 PWSGEILFDGIPReeiprEVLANSVAMVDQDIFLFEG-TVRDNLtlwdptipDADLV-----------RACkdAAIhDVI 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 65 -----GLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDvltAETLRTDLLDLWTQGrmpiKSVLIVTHN 139
Cdd:TIGR03796 599 tsrpgGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALD---PETEKIIDDNLRRRG----CTCIIVAHR 671
|
170
....*....|....
gi 1861249672 140 IeEAVFMCDRILVL 153
Cdd:TIGR03796 672 L-STIRDCDEIIVL 684
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
20-155 |
3.05e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 57.03 E-value: 3.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 20 VAMVFQT-FALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTIL 98
Cdd:PRK13642 83 IGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEII 162
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1861249672 99 LMDEPFSALDvltaETLRTDLLDLWTQGRMPIK-SVLIVTHNIEEAVfMCDRILVLSS 155
Cdd:PRK13642 163 ILDESTSMLD----PTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAA-SSDRILVMKA 215
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
48-155 |
3.13e-10 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 56.35 E-value: 3.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 48 VGARERRERALAAIDLIGLDGFENaypreLSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTA----ETLRTdlldlw 123
Cdd:cd03244 116 VGLKEFVESLPGGLDTVVEEGGEN-----LSVGQRQLLCLARALLRKSKILVLDEATASVDPETDaliqKTIRE------ 184
|
90 100 110
....*....|....*....|....*....|..
gi 1861249672 124 tqgRMPIKSVLIVTHNIeEAVFMCDRILVLSS 155
Cdd:cd03244 185 ---AFKDCTVLTIAHRL-DTIIDSDRILVLDK 212
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-153 |
3.16e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 56.94 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEG-------VAMVFQ--TFALFpWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFEN 71
Cdd:PRK13638 53 PQKGAVLWQGKPLDYSKRGllalrqqVATVFQdpEQQIF-YTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 72 AYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRmpikSVLIVTHNIEEAVFMCDRIL 151
Cdd:PRK13638 132 QPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGN----HVIISSHDIDLIYEISDAVY 207
|
..
gi 1861249672 152 VL 153
Cdd:PRK13638 208 VL 209
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
20-153 |
3.32e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 56.94 E-value: 3.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 20 VAMVFQ--TFALFPwLTVLQNVEAGLEALGVGARERRERALAAIDLIGL-DGFENAYPRELSGGMRQRVGFARALVVDPT 96
Cdd:PRK13645 92 IGLVFQfpEYQLFQ-ETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGN 170
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1861249672 97 ILLMDEPFSALDVLTAEtlrtDLLDLWTQ-GRMPIKSVLIVTHNIEEAVFMCDRILVL 153
Cdd:PRK13645 171 TLVLDEPTGGLDPKGEE----DFINLFERlNKEYKKRIIMVTHNMDQVLRIADEVIVM 224
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
54-158 |
3.85e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 57.12 E-value: 3.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 54 RERALAAIDLIGLDGF------ENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDlwtqgR 127
Cdd:COG4178 457 DAELREALEAVGLGHLaerldeEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-----E 531
|
90 100 110
....*....|....*....|....*....|.
gi 1861249672 128 MPIKSVLIVTHNIEEAVFmCDRILVLSSNPG 158
Cdd:COG4178 532 LPGTTVISVGHRSTLAAF-HDRVLELTGDGS 561
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-153 |
4.09e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.10 E-value: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGK------PLTGPAEGVAMVFQTFALFPWLTVLQNVEAGL----EALGVGA---RERRERALAAIDLIGLD 67
Cdd:PRK09700 57 PTKGTITINNInynkldHKLAAQLGIGIIYQELSVIDELTVLENLYIGRhltkKVCGVNIidwREMRVRAAMMLLRVGLK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 68 GFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMC 147
Cdd:PRK09700 137 VDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEG----TAIVYISHKLAEIRRIC 212
|
....*.
gi 1861249672 148 DRILVL 153
Cdd:PRK09700 213 DRYTVM 218
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
75-153 |
5.46e-10 |
|
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: 55.01 E-value: 5.46e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1861249672 75 RELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLwtqgrMPIKSVLIVTHNIeEAVFMCDRILVL 153
Cdd:cd03247 97 RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEV-----LKDKTLIWITHHL-TGIEHMDKILFL 169
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
2-154 |
9.08e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.04 E-value: 9.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 2 TGGEVTYLGKPLTGPAEGVAMVFQTFALFPWLTVLQN-VEAGLEAL--GVGARERRERALAAIDLIGLDGFEN-----AY 73
Cdd:PLN03211 124 TGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRETlVFCSLLRLpkSLTKQEKILVAESVISELGLTKCENtiignSF 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 74 PRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVF-MCDRILV 152
Cdd:PLN03211 204 IRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKG----KTIVTSMHQPSSRVYqMFDSVLV 279
|
..
gi 1861249672 153 LS 154
Cdd:PLN03211 280 LS 281
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
63-158 |
9.27e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.11 E-value: 9.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 63 LIGLDGfeNAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLwtQGrmpikSVLIVTHNIEE 142
Cdd:PRK11147 145 QLGLDP--DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF--QG-----SIIFISHDRSF 215
|
90 100
....*....|....*....|.
gi 1861249672 143 AVFMCDRIL-----VLSSNPG 158
Cdd:PRK11147 216 IRNMATRIVdldrgKLVSYPG 236
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-154 |
1.00e-09 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 55.62 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPL-----TGPAEGVAMVFQTFALFPWLTVLQNVEAG----LEALGvGARERRERAL-AAIDLIGLDGFE 70
Cdd:PRK09536 55 PTAGTVLVAGDDVealsaRAASRRVASVPQDTSLSFEFDVRQVVEMGrtphRSRFD-TWTETDRAAVeRAMERTGVAQFA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 71 NAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALD----VLTAETLRtdllDLWTQGrmpiKSVLIVTHNIEEAVFM 146
Cdd:PRK09536 134 DRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDinhqVRTLELVR----RLVDDG----KTAVAAIHDLDLAARY 205
|
....*...
gi 1861249672 147 CDRILVLS 154
Cdd:PRK09536 206 CDELVLLA 213
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
50-154 |
1.56e-09 |
|
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: 54.65 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 50 ARERRERaLAaiDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRtDLLDLWTQGRMP 129
Cdd:cd03267 130 FKKRLDE-LS--ELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIR-NFLKEYNRERGT 205
|
90 100
....*....|....*....|....*
gi 1861249672 130 ikSVLIVTHNIEEAVFMCDRILVLS 154
Cdd:cd03267 206 --TVLLTSHYMKDIEALARRVLVID 228
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-153 |
2.31e-09 |
|
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: 54.83 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 4 GEVTYLGKPLTG------PAEGVAMVFQTFALFPWLTVLQNVEAGLEALGVGAR----ERRERALAAIDLIGLDGFENAY 73
Cdd:TIGR02633 58 GEIYWSGSPLKAsnirdtERAGIVIIHQELTLVPELSVAENIFLGNEITLPGGRmaynAMYLRAKNLLRELQLDADNVTR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 74 P-RELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpIKSVLIvTHNIEEAVFMCDRILV 152
Cdd:TIGR02633 138 PvGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHG---VACVYI-SHKLNEVKAVCDTICV 213
|
.
gi 1861249672 153 L 153
Cdd:TIGR02633 214 I 214
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
3-154 |
3.08e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 54.28 E-value: 3.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 3 GGEVTYLGKPLTGPAEGV--AMVFQTFALFPWLTVLqnveaglEALGVGAR----------ERRERALAAIDLIGLD--- 67
Cdd:TIGR00955 82 SGSVLLNGMPIDAKEMRAisAYVQQDDLFIPTLTVR-------EHLMFQAHlrmprrvtkkEKRERVDEVLQALGLRkca 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 68 ----GFENAYpRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRmpikSVLIVTHNIEEA 143
Cdd:TIGR00955 155 ntriGVPGRV-KGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGK----TIICTIHQPSSE 229
|
170
....*....|..
gi 1861249672 144 VF-MCDRILVLS 154
Cdd:TIGR00955 230 LFeLFDKIILMA 241
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-153 |
3.09e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 54.63 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 2 TGGEVTYLGKPLTgpaEGVAMVFQTFALFPWLTVLQNVEAGLEAL-------GVGARERRERALAAIDLIGLDGFENAYP 74
Cdd:TIGR01257 1992 TSGDATVAGKSIL---TNISDVHQNMGYCPQFDAIDDLLTGREHLylyarlrGVPAEEIEKVANWSIQSLGLSLYADRLA 2068
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1861249672 75 RELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRmpikSVLIVTHNIEEAVFMCDRILVL 153
Cdd:TIGR01257 2069 GTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGR----AVVLTSHSMEECEALCTRLAIM 2143
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
18-152 |
4.52e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 53.87 E-value: 4.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 18 EGVAMVFQTFALFPwLTVLQNVEAGLEalGVGARERRERA--LA-AIDLI-----GLDGF--ENAYprELSGGMRQRVGF 87
Cdd:PRK11176 417 NQVALVSQNVHLFN-DTIANNIAYART--EQYSREQIEEAarMAyAMDFInkmdnGLDTVigENGV--LLSGGQRQRIAI 491
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861249672 88 ARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQgrmpiKSVLIVTH---NIEEAvfmcDRILV 152
Cdd:PRK11176 492 ARALLRDSPILILDEATSALDTESERAIQAALDELQKN-----RTSLVIAHrlsTIEKA----DEILV 550
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
60-153 |
5.91e-09 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 53.16 E-value: 5.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 60 AIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTA----ETLR--TDLLDlwtqgrmpiKSV 133
Cdd:COG4604 119 AIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSvqmmKLLRrlADELG---------KTV 189
|
90 100
....*....|....*....|
gi 1861249672 134 LIVTHNIEEAVFMCDRILVL 153
Cdd:COG4604 190 VIVLHDINFASCYADHIVAM 209
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
50-153 |
5.92e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 53.37 E-value: 5.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 50 ARERRERALAAIDLIGLDGFE---NAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLT-AETLRtdLLDLWTQ 125
Cdd:COG4170 129 FKWRKKRAIELLHRVGIKDHKdimNSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTqAQIFR--LLARLNQ 206
|
90 100
....*....|....*....|....*....
gi 1861249672 126 GR-MpikSVLIVTHNIEEAVFMCDRILVL 153
Cdd:COG4170 207 LQgT---SILLISHDLESISQWADTITVL 232
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
77-153 |
8.17e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 53.31 E-value: 8.17e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQgrmpiKSVLIVTHNIEEaVFMCDRILVL 153
Cdd:PRK11174 486 LSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRR-----QTTLMVTHQLED-LAQWDQIWVM 556
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
77-141 |
1.09e-08 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 51.95 E-value: 1.09e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDV-LTAETLRTDLLDLWTQGRmpiKSVLIVTHNIE 141
Cdd:cd03290 141 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIhLSDHLMQEGILKFLQDDK---RTLVLVTHKLQ 203
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
72-115 |
1.16e-08 |
|
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: 51.39 E-value: 1.16e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1861249672 72 AYP--RELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETL 115
Cdd:cd03223 85 IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRL 130
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
34-153 |
1.31e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 52.06 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 34 TVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDvltaE 113
Cdd:PRK13648 100 IVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLD----P 175
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1861249672 114 TLRTDLLDLWTQGRMPiKSVLI--VTHNIEEAVfMCDRILVL 153
Cdd:PRK13648 176 DARQNLLDLVRKVKSE-HNITIisITHDLSEAM-EADHVIVM 215
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
54-144 |
1.33e-08 |
|
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: 51.72 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 54 RERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRMpiksV 133
Cdd:cd03231 103 DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGM----V 178
|
90
....*....|....
gi 1861249672 134 LIVTH---NIEEAV 144
Cdd:cd03231 179 VLTTHqdlGLSEAG 192
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
73-140 |
1.51e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.55 E-value: 1.51e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861249672 73 YPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLwtQGRMPIkSVLIVTHNI 140
Cdd:PRK10261 460 YPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDL--QRDFGI-AYLFISHDM 524
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
29-143 |
2.07e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.05 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 29 LFPWLTVLQNVE--AGLeaLGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSA 106
Cdd:NF033858 89 LYPTLSVFENLDffGRL--FGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTG 166
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1861249672 107 LDVLT-------AETLRTdlldlwtqgRMPIKSVLIVTHNIEEA 143
Cdd:NF033858 167 VDPLSrrqfwelIDRIRA---------ERPGMSVLVATAYMEEA 201
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-154 |
2.40e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.95 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTG--PAE----GVAMV---FQTFALFPWLTVLQNV---EAGLEALGVGARERRERALA-AIDLIglD 67
Cdd:COG3845 310 PASGSIRLDGEDITGlsPRErrrlGVAYIpedRLGRGLVPDMSVAENLilgRYRRPPFSRGGFLDRKAIRAfAEELI--E 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 68 GF------ENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIE 141
Cdd:COG3845 388 EFdvrtpgPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAG----AAVLLISEDLD 463
|
170
....*....|...
gi 1861249672 142 EAVFMCDRILVLS 154
Cdd:COG3845 464 EILALSDRIAVMY 476
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
76-154 |
2.98e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 51.71 E-value: 2.98e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1861249672 76 ELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVLS 154
Cdd:PRK09700 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDG----KVILMVSSELPEIITVCDRIAVFC 483
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
77-153 |
4.81e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 50.97 E-value: 4.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLT-AETLRTdlLDLWTQGRmpikSVLIVTH---NIEEAvfmcDRILV 152
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTeRAIQAA--LREVARGR----TTLVIAHrlsTIVDA----DEILV 564
|
.
gi 1861249672 153 L 153
Cdd:COG5265 565 L 565
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-153 |
5.28e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.77 E-value: 5.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 4 GEVTYLGKPLT--GPAE----GVAMVFQTFALFPWLTVLQNVEAGLE---ALG-VGARERRERALAAIDLIGLDGFENAY 73
Cdd:PRK10762 59 GSILYLGKEVTfnGPKSsqeaGIGIIHQELNLIPQLTIAENIFLGREfvnRFGrIDWKKMYAEADKLLARLNLRFSSDKL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 74 PRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRmpikSVLIVTHNIEEAVFMCDRILVL 153
Cdd:PRK10762 139 VGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGR----GIVYISHRLKEIFEICDDVTVF 214
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
50-153 |
6.45e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 50.43 E-value: 6.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 50 ARERR--ERALAAIDlIGLDGFENAYpRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVltaeTLRTDLLDLwtqgr 127
Cdd:PRK15439 377 ARENAvlERYRRALN-IKFNHAEQAA-RTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV----SARNDIYQL----- 445
|
90 100 110
....*....|....*....|....*....|...
gi 1861249672 128 mpIKS-------VLIVTHNIEEAVFMCDRILVL 153
Cdd:PRK15439 446 --IRSiaaqnvaVLFISSDLEEIEQMADRVLVM 476
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-158 |
8.03e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 49.71 E-value: 8.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTG-PAEG----VAMVFQTFALF----------PWLTVLQNVEaglealgvgarerrERALAAidliG 65
Cdd:PRK10247 59 PTSGTLLFEGEDISTlKPEIyrqqVSYCAQTPTLFgdtvydnlifPWQIRNQQPD--------------PAIFLD----D 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 66 LDGFE------NAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDvltaETLRTDLLDLWTQ-GRMPIKSVLIVTH 138
Cdd:PRK10247 121 LERFAlpdtilTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD----ESNKHNVNEIIHRyVREQNIAVLWVTH 196
|
170 180
....*....|....*....|
gi 1861249672 139 NIEEaVFMCDRILVLSSNPG 158
Cdd:PRK10247 197 DKDE-INHADKVITLQPHAG 215
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
75-153 |
8.18e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 50.21 E-value: 8.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 75 RELSGGMRQRVGFARALVVDPTILLMDEPFSALDvltAETLRT--DLLDLWTQGrmpiKSVLIVTHNIEEAVFMcDRILV 152
Cdd:PRK11160 474 RQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLD---AETERQilELLAEHAQN----KTVLMITHRLTGLEQF-DRICV 545
|
.
gi 1861249672 153 L 153
Cdd:PRK11160 546 M 546
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
77-153 |
9.74e-08 |
|
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: 50.29 E-value: 9.74e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLT-AETLRTDLLDLwtqgrMPIKSVLIVTHNIEEaVFMCDRILVL 153
Cdd:TIGR01271 549 LSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTeKEIFESCLCKL-----MSNKTRILVTSKLEH-LKKADKILLL 620
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-153 |
1.08e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.93 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 4 GEVTYLGKPLTG------PAEGVAMVFQTFALFPWLTVLQNVEAGLEaLGVGAR-------ERRERALAAIdliGLDGFE 70
Cdd:PRK13549 62 GEIIFEGEELQAsnirdtERAGIAIIHQELALVKELSVLENIFLGNE-ITPGGImdydamyLRAQKLLAQL---KLDINP 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 71 NAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpIKSVLIvTHNIEEAVFMCDRI 150
Cdd:PRK13549 138 ATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHG---IACIYI-SHKLNEVKAISDTI 213
|
...
gi 1861249672 151 LVL 153
Cdd:PRK13549 214 CVI 216
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
77-154 |
1.41e-07 |
|
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: 48.95 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLT----AETLRTDLLDlwtqgrmpiKSVLIVTHNIeEAVFMCDRILV 152
Cdd:cd03369 126 LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATdaliQKTIREEFTN---------STILTIAHRL-RTIIDYDKILV 195
|
..
gi 1861249672 153 LS 154
Cdd:cd03369 196 MD 197
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1-150 |
1.51e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.04 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKpltgpaegVAMVFQTFALFPWLTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGG 80
Cdd:PRK13546 76 PTVGKVDRNGE--------VSVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSG 147
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 81 MRQRVGFARALVVDPTILLMDEPFSALDvltaETLRTDLLDLWTQGRMPIKSVLIVTHNIEEAVFMCDRI 150
Cdd:PRK13546 148 MRAKLGFSINITVNPDILVIDEALSVGD----QTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKI 213
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
77-153 |
1.67e-07 |
|
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: 49.08 E-value: 1.67e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAEtlrtDLLDLWTQGRMPIKSVLIVTHNIEEaVFMCDRILVL 153
Cdd:cd03291 160 LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEK----EIFESCVCKLMANKTRILVTSKMEH-LKKADKILIL 231
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-153 |
2.46e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.89 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTG--PAE----GVAMVFQTFALFPWLTVLQNVEAGLEAlGVGARERRERALAAIDlIGLDGFENAYP 74
Cdd:PRK15439 63 PDSGTLEIGGNPCARltPAKahqlGIYLVPQEPLLFPNLSVKENILFGLPK-RQASMQKMKQLLAALG-CQLDLDSSAGS 140
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1861249672 75 RELSGgmRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVL 153
Cdd:PRK15439 141 LEVAD--RQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQG----VGIVFISHKLPEIRQLADRISVM 213
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
76-158 |
2.48e-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: 47.95 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 76 ELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRmpiKSVLIVTHNIEEAVFMCDRILVLSS 155
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGK---KTALVVEHDLAVLDYLSDRIHVFEG 147
|
...
gi 1861249672 156 NPG 158
Cdd:cd03222 148 EPG 150
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-116 |
2.51e-07 |
|
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: 48.78 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 2 TGGEVTYLGKPLTGPAEGVAMVFQTF-ALFPWLTVLQNVEAGLEALGVGARERRERA-LAAIDLIGLDgfENAYPRELSG 79
Cdd:TIGR03719 369 TGQEQPDSGTIEIGETVKLAYVDQSRdALDPNKTVWEEISGGLDIIKLGKREIPSRAyVGRFNFKGSD--QQKKVGQLSG 446
|
90 100 110
....*....|....*....|....*....|....*..
gi 1861249672 80 GMRQRVGFARALVVDPTILLMDEPFSALDVltaETLR 116
Cdd:TIGR03719 447 GERNRVHLAKTLKSGGNVLLLDEPTNDLDV---ETLR 480
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
77-154 |
2.74e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.57 E-value: 2.74e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVLS 154
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKD----KGIIIISSEMPELLGITDRILVMS 465
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-153 |
2.89e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 48.16 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEG-----VAMVFQ-----TFalfPWLTVLQNV--------EAGLeALGVGARER---RERaLA 59
Cdd:COG1101 58 PDSGSILIDGKDVTKLPEYkrakyIGRVFQdpmmgTA---PSMTIEENLalayrrgkRRGL-RRGLTKKRRelfREL-LA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 60 AIDLigldGFENaypR------ELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETlrtdLLDLwTQGRmpIK-- 131
Cdd:COG1101 133 TLGL----GLEN---RldtkvgLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAAL----VLEL-TEKI--VEen 198
|
170 180
....*....|....*....|....
gi 1861249672 132 --SVLIVTHNIEEAVFMCDRILVL 153
Cdd:COG1101 199 nlTTLMVTHNMEQALDYGNRLIMM 222
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
75-158 |
3.50e-07 |
|
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: 48.17 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 75 RELSGGMRQRVGFARALVVDPTILLMDEPFSALDV----LTAETLRTDLLDlwTQgrmpiKSVLIVTHNIEEAVFMCDRI 150
Cdd:cd03237 114 PELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrlMASKVIRRFAEN--NE-----KTAFVVEHDIIMIDYLADRL 186
|
....*...
gi 1861249672 151 LVLSSNPG 158
Cdd:cd03237 187 IVFEGEPS 194
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
77-153 |
3.63e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 48.56 E-value: 3.63e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDlLDLWTQGRmpikSVLIVTHNIeEAVFMCDRILVL 153
Cdd:PRK10789 452 LSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHN-LRQWGEGR----TVIISAHRL-SALTEASEILVM 522
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
77-154 |
4.17e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 48.40 E-value: 4.17e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDlwTQGRMPIKSVLIVTHNIeEAVFMCDRILVLS 154
Cdd:TIGR00957 761 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIG--PEGVLKNKTRILVTHGI-SYLPQVDVIIVMS 835
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
54-143 |
5.51e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.70 E-value: 5.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 54 RERALAA--IDLIGLDGFENAYP-RELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRmpi 130
Cdd:PRK10938 376 RQQKLAQqwLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGE--- 452
|
90
....*....|...
gi 1861249672 131 KSVLIVTHNIEEA 143
Cdd:PRK10938 453 TQLLFVSHHAEDA 465
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
75-158 |
8.14e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.50 E-value: 8.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 75 RELSGGMRQRVGFARALVVDPTILLMDEPFSALDV----LTAETLRtdlldlwtqgRMpI----KSVLIVTHNIEEAVFM 146
Cdd:PRK13409 452 KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlAVAKAIR----------RI-AeereATALVVDHDIYMIDYI 520
|
90
....*....|..
gi 1861249672 147 CDRILVLSSNPG 158
Cdd:PRK13409 521 SDRLMVFEGEPG 532
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
75-138 |
8.91e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.55 E-value: 8.91e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861249672 75 RELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDlWTqgrmpiKSVLIVTH 138
Cdd:PLN03073 343 KTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLK-WP------KTFIVVSH 399
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
75-158 |
9.73e-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: 47.09 E-value: 9.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 75 RELSGGMRQRVGFARALVVDPTILLMDEPFSALDV----LTAETLRTdlldlWTQGRMpiKSVLIVTHNIEEAVFMCDRI 150
Cdd:COG1245 454 KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlAVAKAIRR-----FAENRG--KTAMVVDHDIYLIDYISDRL 526
|
....*...
gi 1861249672 151 LVLSSNPG 158
Cdd:COG1245 527 MVFEGEPG 534
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-138 |
1.07e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 46.49 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTGPAEGVAMvfQTFALFPWLTVLQNVeAGLEALGvgareRRERALAAIDLIGLDGFENAY-----PR 75
Cdd:COG2401 64 ASGSGKSTLLRLLAGALKGTPV--AGCVDVPDNQFGREA-SLIDAIG-----RKGDFKDAVELLNAVGLSDAVlwlrrFK 135
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861249672 76 ELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRmpiKSVLIVTH 138
Cdd:COG2401 136 ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAG---ITLVVATH 195
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
47-153 |
1.12e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 46.62 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 47 GVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQG 126
Cdd:COG4586 125 RIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRER 204
|
90 100 110
....*....|....*....|....*....|
gi 1861249672 127 RMpikSVLIVTHN---IEEavfMCDRILVL 153
Cdd:COG4586 205 GT---TILLTSHDmddIEA---LCDRVIVI 228
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
77-153 |
1.39e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.54 E-value: 1.39e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVlTAETLRTDLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVL 153
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDV-GAKKEIYQLINQFKAEGL---SIILVSSEMPEVLGMSDRILVM 468
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
33-153 |
1.48e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.81 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 33 LTVLQNVEAGLEALGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDvlta 112
Cdd:PRK13545 100 LTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD---- 175
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1861249672 113 ETLRTDLLDLWTQGRMPIKSVLIVTHNIEEAVFMCDRILVL 153
Cdd:PRK13545 176 QTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWL 216
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
47-154 |
4.13e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 45.20 E-value: 4.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 47 GVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARAL---------VVDPTILLMDEPFSALDVLTAETLRT 117
Cdd:PRK13547 116 GALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLD 195
|
90 100 110
....*....|....*....|....*....|....*..
gi 1861249672 118 DLLDLWTQGRMpikSVLIVTHNIEEAVFMCDRILVLS 154
Cdd:PRK13547 196 TVRRLARDWNL---GVLAIVHDPNLAARHADRIAMLA 229
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
65-155 |
4.57e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 45.35 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 65 GLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVltaetlRTDLLDLWTQgRMPIKS--VLIVTHNIeE 142
Cdd:PLN03232 1360 GLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDV------RTDSLIQRTI-REEFKSctMLVIAHRL-N 1431
|
90
....*....|...
gi 1861249672 143 AVFMCDRILVLSS 155
Cdd:PLN03232 1432 TIIDCDKILVLSS 1444
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
46-153 |
7.40e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 44.34 E-value: 7.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 46 LGVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAEtlrtdllDLWTQ 125
Cdd:NF000106 114 LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRN-------EVWDE 186
|
90 100 110
....*....|....*....|....*....|.
gi 1861249672 126 GRMPIK---SVLIVTHNIEEAVFMCDRILVL 153
Cdd:NF000106 187 VRSMVRdgaTVLLTTQYMEEAEQLAHELTVI 217
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
61-158 |
7.95e-06 |
|
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: 44.28 E-value: 7.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 61 IDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDV---LTAETLRTDLLDlwtqgrmPIKSVLIVT 137
Cdd:cd03236 124 VDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIkqrLNAARLIRELAE-------DDNYVLVVE 196
|
90 100
....*....|....*....|.
gi 1861249672 138 HNIEEAVFMCDRILVLSSNPG 158
Cdd:cd03236 197 HDLAVLDYLSDYIHCLYGEPG 217
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
54-158 |
1.04e-05 |
|
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: 44.00 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 54 RERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDV---LTAETLRTDLLDlwtqgrmPI 130
Cdd:COG1245 190 RGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIyqrLNVARLIRELAE-------EG 262
|
90 100 110
....*....|....*....|....*....|
gi 1861249672 131 KSVLIVTHNIeeAV--FMCDRILVLSSNPG 158
Cdd:COG1245 263 KYVLVVEHDL--AIldYLADYVHILYGEPG 290
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
76-108 |
1.12e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.25 E-value: 1.12e-05
10 20 30
....*....|....*....|....*....|...
gi 1861249672 76 ELSGGMRQRVGFARALVVDPTILLMDEPFSALD 108
Cdd:PTZ00265 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
78-155 |
1.20e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.96 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 78 SGGMRQRVGFARALVVDPTILLMDEPFSALDVltaetlRTDLLDLWTQgRMPIKS--VLIVTHNIeEAVFMCDRILVLSS 155
Cdd:PLN03130 1376 SVGQRQLLSLARALLRRSKILVLDEATAAVDV------RTDALIQKTI-REEFKSctMLIIAHRL-NTIIDCDRILVLDA 1447
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
75-153 |
1.32e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 43.56 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 75 RELSGGMRQRVGFARALVVDPTILLMDEPFSALDVltaeTLRTDLLDLWTQGRMPIK-SVLIVTHNIEEAVFMCDRILVL 153
Cdd:PRK09544 119 QKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDV----NGQVALYDLIDQLRRELDcAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
77-153 |
1.43e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 43.76 E-value: 1.43e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVL 153
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQG----VAIIVISSELPEVLGLSDRVLVM 478
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
49-154 |
1.74e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.81 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 49 GARERRERALAAIDLIGLDGFENAYP-REL----------SGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRT 117
Cdd:PLN03232 702 GSDFESERYWRAIDVTALQHDLDLLPgRDLteigergvniSGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFD 781
|
90 100 110
....*....|....*....|....*....|....*..
gi 1861249672 118 DLLDLWTQGrmpiKSVLIVTHNIEEAVFMcDRILVLS 154
Cdd:PLN03232 782 SCMKDELKG----KTRVLVTNQLHFLPLM-DRIILVS 813
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
2-153 |
1.75e-05 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 42.94 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 2 TGGEVTYLGKPLTG------PAEGVAMVFQTFALFPWLTVLQNVEAGlealgvGARERRERALAAIDLIgLDGFENAYPR 75
Cdd:PRK11614 58 TSGRIVFDGKDITDwqtakiMREAVAIVPEGRRVFSRMTVEENLAMG------GFFAERDQFQERIKWV-YELFPRLHER 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 76 E------LSGGMRQRVGFARALVVDPTILLMDEPFSALdvltAETLRTDLLDLWTQGRMPIKSVLIVTHNIEEAVFMCDR 149
Cdd:PRK11614 131 RiqragtMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL----APIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADR 206
|
....
gi 1861249672 150 ILVL 153
Cdd:PRK11614 207 GYVL 210
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
77-154 |
2.09e-05 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 42.91 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 77 LSGGMRQRVGFARALV-VDPTI------LLMDEPFSALDVLTAETLRTDLLDLWTQGRmpikSVLIVTHNIEEAVFMCDR 149
Cdd:COG4138 127 LSGGEWQRVRLAAVLLqVWPTInpegqlLLLDEPMNSLDVAQQAALDRLLRELCQQGI----TVVMSSHDLNHTLRHADR 202
|
....*
gi 1861249672 150 ILVLS 154
Cdd:COG4138 203 VWLLK 207
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
49-139 |
2.86e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.92 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 49 GARERRERA-LAAIDLIGLDGFENAYprELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLwtQGr 127
Cdd:PLN03073 601 GVPEQKLRAhLGSFGVTGNLALQPMY--TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLF--QG- 675
|
90
....*....|..
gi 1861249672 128 mpikSVLIVTHN 139
Cdd:PLN03073 676 ----GVLMVSHD 683
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
34-116 |
3.03e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.80 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 34 TVLQNVEAGLEALGVGARERRERA-LAAIDLIGLDgfENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVlta 112
Cdd:PRK11819 404 TVWEEISGGLDIIKVGNREIPSRAyVGRFNFKGGD--QQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV--- 478
|
....
gi 1861249672 113 ETLR 116
Cdd:PRK11819 479 ETLR 482
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
47-157 |
3.24e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 42.14 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 47 GVGARERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDvLTAETLRTDLLD--LWT 124
Cdd:PRK13543 108 GLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD-LEGITLVNRMISahLRG 186
|
90 100 110
....*....|....*....|....*....|...
gi 1861249672 125 QGrmpikSVLIVTHNIEEAVFMCDRILVLSSNP 157
Cdd:PRK13543 187 GG-----AALVTTHGAYAAPPVRTRMLTLEAAA 214
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
77-138 |
3.46e-05 |
|
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: 42.61 E-value: 3.46e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLwtQGrmpikSVLIVTH 138
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY--PG-----TVVAVTH 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
75-153 |
3.75e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 42.36 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 75 RELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLrTDLLDLWtQGrmpikSVLIVTHNIEeavFM---CDRIL 151
Cdd:COG0488 431 GVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEAL-EEALDDF-PG-----TVLLVSHDRY---FLdrvATRIL 500
|
..
gi 1861249672 152 VL 153
Cdd:COG0488 501 EF 502
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
48-153 |
4.63e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 42.10 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 48 VGARERReralaAIDLIGLDGFEN------AYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLT-AETLRtdLL 120
Cdd:PRK15093 129 FGWRKRR-----AIELLHRVGIKDhkdamrSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTqAQIFR--LL 201
|
90 100 110
....*....|....*....|....*....|...
gi 1861249672 121 DLWTQGRMpiKSVLIVTHNIEEAVFMCDRILVL 153
Cdd:PRK15093 202 TRLNQNNN--TTILLISHDLQMLSQWADKINVL 232
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
77-156 |
5.09e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; 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: 213256 [Multi-domain] Cd Length: 275 Bit Score: 41.76 E-value: 5.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpikSVLIVTHNIeEAVFMCDRILVLSSN 156
Cdd:cd03289 139 LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADC-----TVILSEHRI-EAMLECQRFLVIEEN 212
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
77-154 |
5.29e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.08 E-value: 5.29e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVLS 154
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEG----KGVIVISSELPELLGMCDRIYVMN 478
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
77-139 |
6.01e-05 |
|
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: 41.36 E-value: 6.01e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDV----LTAETLRTdLLDlwtqgrmPIKSVLIVTHN 139
Cdd:cd03217 105 FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIdalrLVAEVINK-LRE-------EGKSVLIITHY 163
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
77-140 |
6.12e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.07 E-value: 6.12e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLdlwtQGRMPIKSVLIVTHNI 140
Cdd:PTZ00243 783 LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECF----LGALAGKTRVLATHQV 842
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
77-137 |
6.22e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.92 E-value: 6.22e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpIKSVLIVT 137
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSG---ITLVLVLN 193
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-153 |
6.50e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.64 E-value: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 4 GEVTYLGKPLTGPA------EGVAMVFQTFALFPWLTVLQNVEAG---LEALGVGARERRERALAAIDLIGLDgfenAYP 74
Cdd:PRK10982 53 GSILFQGKEIDFKSskealeNGISMVHQELNLVLQRSVMDNMWLGrypTKGMFVDQDKMYRDTKAIFDELDID----IDP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 75 RE----LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRI 150
Cdd:PRK10982 129 RAkvatLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERG----CGIVYISHKMEEIFQLCDEI 204
|
...
gi 1861249672 151 LVL 153
Cdd:PRK10982 205 TIL 207
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
77-153 |
6.78e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 41.73 E-value: 6.78e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEEAVFMCDRILVL 153
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEG----VAIIVVSSELAEVLGLSDRVLVI 476
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
4-112 |
7.21e-05 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 41.09 E-value: 7.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 4 GEVTYLGKPLTGPAE----GVAMVFQTFALFPWLTVLQNVEAGLEALGvgarerreralaaidligldgfeNAYPRELSG 79
Cdd:cd03233 65 GDIHYNGIPYKEFAEkypgEIIYVSEEDVHFPTLTVRETLDFALRCKG-----------------------NEFVRGISG 121
|
90 100 110
....*....|....*....|....*....|...
gi 1861249672 80 GMRQRVGFARALVVDPTILLMDEPFSALDVLTA 112
Cdd:cd03233 122 GERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
20-153 |
7.55e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 41.30 E-value: 7.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 20 VAMVFQtfalFPWL-----TVLQNVEAGLEALGVGARERRERALaaiDLIGLDGFE----NAYPRELSGGMRQRVGFARA 90
Cdd:PRK13646 87 IGMVFQ----FPESqlfedTVEREIIFGPKNFKMNLDEVKNYAH---RLLMDLGFSrdvmSQSPFQMSGGQMRKIAIVSI 159
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1861249672 91 LVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRmpiKSVLIVTHNIEEAVFMCDRILVL 153
Cdd:PRK13646 160 LAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDEN---KTIILVSHDMNEVARYADEVIVM 219
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
75-158 |
8.90e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 41.33 E-value: 8.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 75 RELSGGMRQRVGFARALVVDPTILLMDEPFSALDV---LTAETLRTDLldlwTQGrmpiKSVLIVTHNIeeAV--FMCDR 149
Cdd:PRK13409 211 SELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIrqrLNVARLIREL----AEG----KYVLVVEHDL--AVldYLADN 280
|
....*....
gi 1861249672 150 ILVLSSNPG 158
Cdd:PRK13409 281 VHIAYGEPG 289
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
77-108 |
9.04e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 41.65 E-value: 9.04e-05
10 20 30
....*....|....*....|....*....|..
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALD 108
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
51-143 |
9.21e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 41.13 E-value: 9.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 51 RERRERALAAIDLIGLDGFENAYPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVltaeTLRTDLLDLWTQ-GRMP 129
Cdd:PRK10253 118 KEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI----SHQIDLLELLSElNREK 193
|
90
....*....|....
gi 1861249672 130 IKSVLIVTHNIEEA 143
Cdd:PRK10253 194 GYTLAAVLHDLNQA 207
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1-139 |
1.04e-04 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 40.82 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 1 PTGGEVTYLGKPLTG--PAE----GVAMVFQTFALFPWLTVLQNVEAGLEALG---VGARERRERALAAIDLIGLD---- 67
Cdd:COG0396 54 VTSGSILLDGEDILElsPDEraraGIFLAFQYPVEIPGVSVSNFLRTALNARRgeeLSAREFLKLLKEKMKELGLDedfl 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 68 ------GFenayprelSGGMRQRVGFARALVVDPTILLMDEPFSALDVltaetlrtDLLDLWTQG----RMPIKSVLIVT 137
Cdd:COG0396 134 dryvneGF--------SGGEKKRNEILQMLLLEPKLAILDETDSGLDI--------DALRIVAEGvnklRSPDRGILIIT 197
|
..
gi 1861249672 138 HN 139
Cdd:COG0396 198 HY 199
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
75-138 |
2.12e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 40.32 E-value: 2.12e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861249672 75 RELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRtDLLDLWtQGrmpikSVLIVTH 138
Cdd:PRK11147 439 KALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLE-ELLDSY-QG-----TVLLVSH 495
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
77-156 |
2.24e-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: 40.28 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpikSVLIVTHNIeEAVFMCDRILVLSSN 156
Cdd:TIGR01271 1354 LSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNC-----TVILSEHRV-EALLECQQFLVIEGS 1427
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
3-155 |
3.33e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 40.09 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 3 GGEVTYLGkplTGPAE-------GVAMVFQTFALFPWLTVLQNVEAGLEALGVGAR----ERRERALAAIDLI----GLD 67
Cdd:TIGR00956 119 EGVITYDG---ITPEEikkhyrgDVVYNAETDVHFPHLTVGETLDFAARCKTPQNRpdgvSREEYAKHIADVYmatyGLS 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 68 GFENA-----YPRELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTA-ETLRTdlldLWTQGRMPIKSVLIVTHNIE 141
Cdd:TIGR00956 196 HTRNTkvgndFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATAlEFIRA----LKTSANILDTTPLVAIYQCS 271
|
170
....*....|....*
gi 1861249672 142 EAVF-MCDRILVLSS 155
Cdd:TIGR00956 272 QDAYeLFDKVIVLYE 286
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
75-154 |
3.52e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 39.51 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 75 RELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRmpikSVLIVTHNIEEAVFMCDRILVLS 154
Cdd:PRK11288 395 MNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGV----AVLFVSSDLPEVLGVADRIVVMR 470
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
77-138 |
4.21e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 39.33 E-value: 4.21e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDvltAETLrtdlldLWTQG---RMPiKSVLIVTH 138
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD---AESV------AWLEQflhDYP-GTVVAVTH 218
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
55-153 |
5.06e-04 |
|
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: 39.54 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 55 ERALAAIDLIGLDGFENAYP-----------RELSGGMRQRVGFARALVVDPTILLMDEPFSALDV----LTAETLRTDL 119
Cdd:TIGR00957 1389 EEVWWALELAHLKTFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLetdnLIQSTIRTQF 1468
|
90 100 110
....*....|....*....|....*....|....
gi 1861249672 120 LDLwtqgrmpikSVLIVTHNIeEAVFMCDRILVL 153
Cdd:TIGR00957 1469 EDC---------TVLTIAHRL-NTIMDYTRVIVL 1492
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
77-154 |
5.06e-04 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 38.76 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 77 LSGGMRQRVGFARA-LVVDPTI------LLMDEPFSALDVLTAETLRTDLLDLWTQGRmpikSVLIVTHNIEEAVFMCDR 149
Cdd:PRK03695 127 LSGGEWQRVRLAAVvLQVWPDInpagqlLLLDEPMNSLDVAQQAALDRLLSELCQQGI----AVVMSSHDLNHTLRHADR 202
|
....*
gi 1861249672 150 ILVLS 154
Cdd:PRK03695 203 VWLLK 207
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-153 |
7.77e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 38.62 E-value: 7.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 17 AEGVAMVFQTFALFPWLTVLQNVEAGLEALGVGA---RERRERALAAIDLIGLDgfENayPRELSG----GMRQRVGFAR 89
Cdd:NF040905 77 ALGIVIIHQELALIPYLSIAENIFLGNERAKRGVidwNETNRRARELLAKVGLD--ES--PDTLVTdigvGKQQLVEIAK 152
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1861249672 90 ALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpIKSVLIvTHNIEEAVFMCDRILVL 153
Cdd:NF040905 153 ALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQG---ITSIII-SHKLNEIRRVADSITVL 212
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
44-155 |
1.75e-03 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 37.58 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 44 EALGVGARERRERAL-AAIDLIGLDGFENaypreLSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDL 122
Cdd:cd03288 128 EALEIAQLKNMVKSLpGGLDAVVTEGGEN-----FSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTA 202
|
90 100 110
....*....|....*....|....*....|...
gi 1861249672 123 WTQgrmpiKSVLIVTHNIeEAVFMCDRILVLSS 155
Cdd:cd03288 203 FAD-----RTVVTIAHRV-STILDADLVLVLSR 229
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
77-158 |
1.88e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.89 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 77 LSGGMRQRVGFARAL---VVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGRmpikSVLIVTHNIeEAVFMCDRILVL 153
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGH----TVVIIEHNM-HVVKVADYVLEL 884
|
....*
gi 1861249672 154 SSNPG 158
Cdd:PRK00635 885 GPEGG 889
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
77-112 |
2.14e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 37.52 E-value: 2.14e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTA 112
Cdd:PLN03140 1020 LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAA 1055
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
56-109 |
2.58e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 37.07 E-value: 2.58e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1861249672 56 RALAAIDLIGLdGFEN---AYP-RELSGGMRQRVGFARALVVDPTILLMDEPFSALDV 109
Cdd:PRK10636 126 RSRAASLLHGL-GFSNeqlERPvSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDL 182
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
77-138 |
2.67e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 36.47 E-value: 2.67e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTH 138
Cdd:PRK13540 128 LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKG----GAVLLTSH 185
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
77-119 |
7.92e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 35.64 E-value: 7.92e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1861249672 77 LSGGMRQRVGFARALVVDPTILLMDEPFSALDVLTAETLRTDL 119
Cdd:PRK15064 439 LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMAL 481
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
77-158 |
8.43e-03 |
|
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: 34.99 E-value: 8.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861249672 77 LSGGMRQRVGFARALVVDP--TILLMDEPFSALDVLTAETLRTDLLDLWTQGrmpiKSVLIVTHNIEeavFMC--DRILV 152
Cdd:cd03238 88 LSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKGLIDLG----NTVILIEHNLD---VLSsaDWIID 160
|
....*.
gi 1861249672 153 LSSNPG 158
Cdd:cd03238 161 FGPGSG 166
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
76-111 |
8.61e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 35.64 E-value: 8.61e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1861249672 76 ELSGGMRQRVGFARALVVDPTILLMDEPFSALDVLT 111
Cdd:PRK15064 155 EVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINT 190
|
|
| |
