|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
16-236 |
4.48e-121 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 344.33 E-value: 4.48e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 16 SEALRLVKVTRTYGSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELT 95
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 96 KFRRGRVGFVFQQYNLLETLTVAQNTVLPLKLAG--RRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVT 173
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPELTALENVALPLLLAGvsRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490075866 174 EPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDPVAASYADSVVFLADGRLAG 236
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
19-234 |
2.59e-110 |
|
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: 316.74 E-value: 2.59e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFR 98
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RGRVGFVFQQYNLLETLTVAQNTVLPLKLAG--RRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPR 176
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGvpKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490075866 177 VIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDPVAASYADSVVFLADGRL 234
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
12-241 |
7.58e-89 |
|
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: 263.14 E-value: 7.58e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 12 PGPASEALRLVKVTRTYGSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGE 91
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 92 AELTKFRRGRVGFVFQQYNLLETLTVAQNTVLPLKLAGRRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARAL 171
Cdd:COG4181 82 DARARLRARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAF 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 172 VTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDPVAASYADSVVFLADGRLAGRMDAP 241
Cdd:COG4181 162 ATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTAAT 231
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
19-234 |
2.72e-81 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 247.30 E-value: 2.72e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFR 98
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RgRVGFVFQQYNLLETLTVAQNTVLPLKLAG--RRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPR 176
Cdd:COG1135 82 R-KIGMIFQHFNLLSSRTVAENVALPLEIAGvpKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490075866 177 VIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHD-PVAASYADSVVFLADGRL 234
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEmDVVRRICDRVAVLENGRI 219
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
18-253 |
9.82e-80 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 240.34 E-value: 9.82e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 18 ALRLVKVTRTYgsaDNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKF 97
Cdd:COG3638 2 MLELRNLSKRY---PGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 98 RRgRVGFVFQQYNLLETLTVAQNtVLplklAGR---------------RVDRKRAREVLTSVGLGDRLGHRPDQLSGGQR 162
Cdd:COG3638 79 RR-RIGMIFQQFNLVPRLSVLTN-VL----AGRlgrtstwrsllglfpPEDRERALEALERVGLADKAYQRADQLSGGQQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 163 QRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDP-VAASYADSVVFLADGRLAgrMDAP 241
Cdd:COG3638 153 QRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVdLARRYADRIIGLRDGRVV--FDGP 230
|
250
....*....|..
gi 490075866 242 TPDAVAERLAHL 253
Cdd:COG3638 231 PAELTDAVLREI 242
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
14-243 |
4.87e-78 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 236.52 E-value: 4.87e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 14 PASEALRLVKVTRTYGSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGeae 93
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 94 ltkfrrGRVGFVFQQYNLLETLTVAQNTVLPLKLAG--RRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARAL 171
Cdd:COG1116 80 ------PDRGVVFQEPALLPWLTVLDNVALGLELRGvpKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 172 VTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDPvaasyaDSVVFLAD---------GRLAGRMDAPT 242
Cdd:COG1116 154 ANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDV------DEAVFLADrvvvlsarpGRIVEEIDVDL 227
|
.
gi 490075866 243 P 243
Cdd:COG1116 228 P 228
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
19-234 |
2.22e-76 |
|
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: 231.32 E-value: 2.22e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFR 98
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RgRVGFVFQQYNLLETLTVAQNTVLPLKLAG--RRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPR 176
Cdd:cd03258 82 R-RIGMIFQHFNLLSSRTVFENVALPLEIAGvpKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490075866 177 VIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHD-PVAASYADSVVFLADGRL 234
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEmEVVKRICDRVAVMEKGEV 219
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
19-234 |
3.49e-74 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 225.32 E-value: 3.49e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGsadNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFR 98
Cdd:COG2884 2 IRFENVSKRYP---GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RgRVGFVFQQYNLLETLTVAQNTVLPLKLAG--RRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPR 176
Cdd:COG2884 79 R-RIGVVFQDFRLLPDRTVYENVALPLRVTGksRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490075866 177 VIFADEPTGALDTRSARQVLLLLQEAARVhGRTVVMVTHDP-VAASYADSVVFLADGRL 234
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLeLVDRMPKRVLELEDGRL 215
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
19-241 |
1.38e-73 |
|
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: 223.89 E-value: 1.38e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGggeaeltkfR 98
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG---------P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RGRVGFVFQQYNLLETLTVAQNTVLPLKLAG--RRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPR 176
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELQGvpKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490075866 177 VIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDpvaasyADSVVFLAD---------GRLAGRMDAP 241
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHD------IDEAVFLADrvvvlsarpGRIVAEVEVD 219
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
19-233 |
4.11e-72 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 220.64 E-value: 4.11e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSadnaVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGgEAELTKFR 98
Cdd:COG1126 2 IEIENLHKSFGD----LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDS-KKDINKLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RgRVGFVFQQYNLLETLTVAQNTVL-PLKLAGRRVD--RKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEP 175
Cdd:COG1126 77 R-KVGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAeaEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490075866 176 RVIFADEPTGALDTRSARQVLLLLQEAARvHGRTVVMVTHD-PVAASYADSVVFLADGR 233
Cdd:COG1126 156 KVMLFDEPTSALDPELVGEVLDVMRDLAK-EGMTMVVVTHEmGFAREVADRVVFMDGGR 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
19-253 |
4.89e-72 |
|
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: 220.52 E-value: 4.89e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGsadNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFR 98
Cdd:cd03256 1 IEVENLSKTYP---NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RgRVGFVFQQYNLLETLTVAQNtVLPLKLAGR-----------RVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAI 167
Cdd:cd03256 78 R-QIGMIFQQFNLIERLSVLEN-VLSGRLGRRstwrslfglfpKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 168 ARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDP-VAASYADSVVFLADGRLAgrMDAPTPDAV 246
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVdLAREYADRIVGLKDGRIV--FDGPPAELT 233
|
....*..
gi 490075866 247 AERLAHL 253
Cdd:cd03256 234 DEVLDEI 240
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
19-235 |
6.06e-70 |
|
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: 214.31 E-value: 6.06e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSadnaVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGggeaelTKFR 98
Cdd:cd03259 1 LELKGLSKTYGS----VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG------VPPE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RGRVGFVFQQYNLLETLTVAQNTVLPLKLAG--RRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPR 176
Cdd:cd03259 71 RRNIGMVFQDYALFPHLTVAENIAFGLKLRGvpKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 177 VIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDPV-AASYADSVVFLADGRLA 235
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEeALALADRIAVMNEGRIV 210
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
18-234 |
3.61e-68 |
|
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: 210.61 E-value: 3.61e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 18 ALRLVKVTRTYGsaDNAVtaLDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKF 97
Cdd:COG1127 5 MIEVRNLTKSFG--DRVV--LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 98 RRgRVGFVFQQYNLLETLTVAQNTVLPLKLAGR---RVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTE 174
Cdd:COG1127 81 RR-RIGMLFQGGALFDSLTVFENVAFPLREHTDlseAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490075866 175 PRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHD-PVAASYADSVVFLADGRL 234
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDlDSAFAIADRVAVLADGKI 220
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
28-235 |
6.30e-67 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 206.79 E-value: 6.30e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 28 YGSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFRRgRVGFVFQ 107
Cdd:TIGR02982 11 YGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQLRR-RIGYIFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 108 QYNLLETLTVAQNTVLPLKLA---GRRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPT 184
Cdd:TIGR02982 90 AHNLLGFLTARQNVQMALELQpnlSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490075866 185 GALDTRSARQVLLLLQEAARVHGRTVVMVTHDPVAASYADSVVFLADGRLA 235
Cdd:TIGR02982 170 AALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGKLL 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-234 |
7.44e-67 |
|
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: 215.54 E-value: 7.44e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 5 GARGNHDPGPASEALRLVKVTRTYGS-ADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDG 83
Cdd:COG1123 247 RGRAAPAAAAAEPLLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDG 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 84 KELTGGGEAELTKFRRgRVGFVFQQYN--LLETLTVAQNTVLPLKLAG---RRVDRKRAREVLTSVGLGDRLGHR-PDQL 157
Cdd:COG1123 327 KDLTKLSRRSLRELRR-RVQMVFQDPYssLNPRMTVGDIIAEPLRLHGllsRAERRERVAELLERVGLPPDLADRyPHEL 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490075866 158 SGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHD-PVAASYADSVVFLADGRL 234
Cdd:COG1123 406 SGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDlAVVRYIADRVAVMYDGRI 483
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
19-235 |
7.46e-66 |
|
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: 204.12 E-value: 7.46e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFR 98
Cdd:TIGR02211 2 LKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RGRVGFVFQQYNLLETLTVAQNTVLPLKLAGRRVD--RKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPR 176
Cdd:TIGR02211 82 NKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKeaKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPS 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490075866 177 VIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDPVAASYADSVVFLADGRLA 235
Cdd:TIGR02211 162 LVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQLF 220
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
15-235 |
5.35e-65 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 206.10 E-value: 5.35e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 15 ASEALRLVKVTRTYGSadnaVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGggeaeL 94
Cdd:COG3842 2 AMPALELENVSKRYGD----VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG-----L 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 95 TKFRRGrVGFVFQQYNLLETLTVAQNTVLPLKLAG--RRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALV 172
Cdd:COG3842 73 PPEKRN-VGMVFQDYALFPHLTVAENVAFGLRMRGvpKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490075866 173 TEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDPV-AASYADSVVFLADGRLA 235
Cdd:COG3842 152 PEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEeALALADRIAVMNDGRIE 215
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
19-234 |
6.52e-65 |
|
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: 202.35 E-value: 6.52e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSAdnavTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFR 98
Cdd:cd03261 1 IELRGLTKSFGGR----TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RgRVGFVFQQYNLLETLTVAQNTVLPLKLAGRRVD---RKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEP 175
Cdd:cd03261 77 R-RMGMLFQSGALFDSLTVFENVAFPLREHTRLSEeeiREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 176 RVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHD-PVAASYADSVVFLADGRL 234
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDlDTAFAIADRIAVLYDGKI 215
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
18-240 |
2.31e-64 |
|
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: 201.18 E-value: 2.31e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 18 ALRLVKVTRTYGSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGggeAELTKF 97
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTR---RRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 98 RRgRVGFVFQQY--------NLLETLTvaqntvLPLKLAGRRVDRKRAREVLTSVGLGDRLGHR-PDQLSGGQRQRVAIA 168
Cdd:COG1124 78 RR-RVQMVFQDPyaslhprhTVDRILA------EPLRIHGLPDREERIAELLEQVGLPPSFLDRyPHQLSGGQRQRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490075866 169 RALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDPVAASY-ADSVVFLADGRLAGRMDA 240
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTV 223
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
19-234 |
3.42e-64 |
|
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: 200.04 E-value: 3.42e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELtKFR 98
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLR-KIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RGRVGFVFQQY--NLLETLTVAQNTVLPLKLAGRRVDRKRAREV----LTSVGLGDRLGHR-PDQLSGGQRQRVAIARAL 171
Cdd:cd03257 81 RKEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAvlllLVGVGLPEEVLNRyPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490075866 172 VTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHD-PVAASYADSVVFLADGRL 234
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDlGVVAKIADRVAVMYAGKI 224
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
19-249 |
9.59e-64 |
|
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: 199.10 E-value: 9.59e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYgsaDNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTgggEAELTKFR 98
Cdd:COG1122 1 IELENLSFSY---PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT---KKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RgRVGFVFQQYN--LLETlTVAQNTVLPLKLAGRRVD--RKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTE 174
Cdd:COG1122 75 R-KVGLVFQNPDdqLFAP-TVEEDVAFGPENLGLPREeiRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490075866 175 PRVIFADEPTGALDTRSARQVLLLLQEAARvHGRTVVMVTHDP-VAASYADSVVFLADGRLAgrMDAPTPDAVAER 249
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNK-EGKTVIIVTHDLdLVAELADRVIVLDDGRIV--ADGTPREVFSDY 225
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
19-234 |
1.32e-63 |
|
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: 198.14 E-value: 1.32e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGsaDNAVtaLDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEaELTKFR 98
Cdd:cd03262 1 IEIKNLHKSFG--DFHV--LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKK-NINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RgRVGFVFQQYNLLETLTVAQNTVL-PLKLAGRRVD--RKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEP 175
Cdd:cd03262 76 Q-KVGMVFQQFNLFPHLTVLENITLaPIKVKGMSKAeaEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 176 RVIFADEPTGALDTRSARQVLLLLQEAARvHGRTVVMVTHD-PVAASYADSVVFLADGRL 234
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAE-EGMTMVVVTHEmGFAREVADRVIFMDDGRI 213
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
20-234 |
9.07e-63 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 200.03 E-value: 9.07e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 20 RLVKVTRTYGSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFRR 99
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 100 gRVGFVFQQYNLLETLTVAQNTVLPLKLAGRRVD--RKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRV 177
Cdd:PRK11153 83 -QIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAeiKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490075866 178 IFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHD-PVAASYADSVVFLADGRL 234
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEmDVVKRICDRVAVIDAGRL 219
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
21-229 |
1.56e-62 |
|
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: 195.14 E-value: 1.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 21 LVKVTRTYGSAdnavTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFRRG 100
Cdd:TIGR03608 1 LKNISKKFGDK----VILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 101 RVGFVFQQYNLLETLTVAQNTVLPLKLAGR--RVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVI 178
Cdd:TIGR03608 77 KLGYLFQNFALIENETVEENLDLGLKYKKLskKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490075866 179 FADEPTGALDTRSARQVLLLLQEAARvHGRTVVMVTHDPVAASYADSVVFL 229
Cdd:TIGR03608 157 LADEPTGSLDPKNRDEVLDLLLELND-EGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
19-253 |
1.57e-62 |
|
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: 196.37 E-value: 1.57e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGsadNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFR 98
Cdd:TIGR02315 2 LEVENLSKVYP---NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RgRVGFVFQQYNLLETLTVAQNtVLPLKLA---------GR--RVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAI 167
Cdd:TIGR02315 79 R-RIGMIFQHYNLIERLTVLEN-VLHGRLGykptwrsllGRfsEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 168 ARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHD-PVAASYADSVVFLADGRLAgrMDAPTPDAV 246
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQvDLAKKYADRIVGLKAGEIV--FDGAPSELD 234
|
....*..
gi 490075866 247 AERLAHL 253
Cdd:TIGR02315 235 DEVLRHI 241
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
19-250 |
2.03e-60 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 190.66 E-value: 2.03e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSadnaVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTgggeAELTKFR 98
Cdd:COG1131 1 IEVRGLTKRYGD----KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA----RDPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RgRVGFVFQQYNLLETLTVAQNtvlpLKLAGR------RVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALV 172
Cdd:COG1131 73 R-RIGYVPQEPALYPDLTVREN----LRFFARlyglprKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490075866 173 TEPRVIFADEPTGALDTRSARQVLLLLQEAARvHGRTVVMVTHD-PVAASYADSVVFLADGRLAGRMdapTPDAVAERL 250
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRELAA-EGKTVLLSTHYlEEAERLCDRVAIIDKGRIVADG---TPDELKARL 222
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
18-235 |
2.96e-60 |
|
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: 191.03 E-value: 2.96e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 18 ALRLVKVTRTYGSAdnavTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKf 97
Cdd:COG1120 1 MLEAENLSVGYGGR----PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELAR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 98 rrgRVGFVFQQYNLLETLTVAQnTVL----P-LKLAGR--RVDRKRAREVLTSVGLGDrLGHRP-DQLSGGQRQRVAIAR 169
Cdd:COG1120 76 ---RIAYVPQEPPAPFGLTVRE-LVAlgryPhLGLFGRpsAEDREAVEEALERTGLEH-LADRPvDELSGGERQRVLIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490075866 170 ALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDP-VAASYADSVVFLADGRLA 235
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLnLAARYADRLVLLKDGRIV 217
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
19-234 |
4.38e-60 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 200.72 E-value: 4.38e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFR 98
Cdd:PRK10535 5 LELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RGRVGFVFQQYNLLETLTVAQNTVLPLKLAG--RRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPR 176
Cdd:PRK10535 85 REHFGFIFQRYHLLSHLTAAQNVEVPAVYAGleRKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQ 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490075866 177 VIFADEPTGALDTRSARQVLLLLQEaARVHGRTVVMVTHDPVAASYADSVVFLADGRL 234
Cdd:PRK10535 165 VILADEPTGALDSHSGEEVMAILHQ-LRDRGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
19-233 |
7.02e-60 |
|
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: 187.39 E-value: 7.02e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSadnaVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGgEAELTKFR 98
Cdd:cd03229 1 LELKNVSKRYGQ----KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL-EDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RgRVGFVFQQYNLLETLTVAQNTVLPLklagrrvdrkrarevltsvglgdrlghrpdqlSGGQRQRVAIARALVTEPRVI 178
Cdd:cd03229 76 R-RIGMVFQDFALFPHLTVLENIALGL--------------------------------SGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490075866 179 FADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDP-VAASYADSVVFLADGR 233
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLdEAARLADRVVVLRDGK 178
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
18-234 |
1.67e-59 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 192.21 E-value: 1.67e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 18 ALRLVKVTRTYGsadnAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAEltkf 97
Cdd:COG3839 3 SLELENVSKSYG----GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 98 rRGrVGFVFQQYNLLETLTVAQNTVLPLKLAGRRVD--RKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEP 175
Cdd:COG3839 75 -RN-IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAeiDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490075866 176 RVIFADEPTGALDTRSARQvllLLQEAARVH---GRTVVMVTHDPV-AASYADSVVFLADGRL 234
Cdd:COG3839 153 KVFLLDEPLSNLDAKLRVE---MRAEIKRLHrrlGTTTIYVTHDQVeAMTLADRIAVMNDGRI 212
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
38-234 |
1.77e-59 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 187.33 E-value: 1.77e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTgggEAELTKFRRgRVGFVFQQYNLLETlTV 117
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLS---AMPPPEWRR-QVAYVPQEPALWGG-TV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 118 AQNTVLPLKLAGRRVDRKRAREVLTSVGLGDR-LGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQVL 196
Cdd:COG4619 91 RDNLPFPFQLRERKFDRERALELLERLGLPPDiLDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVE 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 490075866 197 LLLQEAARVHGRTVVMVTHDP-VAASYADSVVFLADGRL 234
Cdd:COG4619 171 ELLREYLAEEGRAVLWVSHDPeQIERVADRVLTLEAGRL 209
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
19-234 |
2.77e-57 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 186.12 E-value: 2.77e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSadnaVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAeltkfR 98
Cdd:COG1118 3 IEVRNISKRFGS----FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPP-----R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RGRVGFVFQQYNLLETLTVAQN-----TVLPLklaGRRVDRKRAREVLTSVGLGDrLGHR-PDQLSGGQRQRVAIARALV 172
Cdd:COG1118 74 ERRVGFVFQHYALFPHMTVAENiafglRVRPP---SKAEIRARVEELLELVQLEG-LADRyPSQLSGGQRQRVALARALA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490075866 173 TEPRVIFADEPTGALDTRSARQVLLLLQeaaRVH---GRTVVMVTHDPV-AASYADSVVFLADGRL 234
Cdd:COG1118 150 VEPEVLLLDEPFGALDAKVRKELRRWLR---RLHdelGGTTVFVTHDQEeALELADRVVVMNQGRI 212
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
20-233 |
4.46e-57 |
|
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: 181.51 E-value: 4.46e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 20 RLVKVTRTYGSADNAvtALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELtkfrR 99
Cdd:cd03225 1 ELKNLSFSYPDGARP--ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL----R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 100 GRVGFVFQQYNL-LETLTVAQNTVLPLKLAG--RRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPR 176
Cdd:cd03225 75 RKVGLVFQNPDDqFFGPTVEEEVAFGLENLGlpEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490075866 177 VIFADEPTGALDTRSARQVLLLLQEAARvHGRTVVMVTHDP-VAASYADSVVFLADGR 233
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLdLLLELADRVIVLEDGK 211
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
19-233 |
4.78e-56 |
|
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: 178.98 E-value: 4.78e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGsadNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFR 98
Cdd:TIGR02673 2 IEFHNVSKAYP---GGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RgRVGFVFQQYNLLETLTVAQNTVLPLKLAGR--RVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPR 176
Cdd:TIGR02673 79 R-RIGVVFQDFRLLPDRTVYENVALPLEVRGKkeREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490075866 177 VIFADEPTGALDTRSARQVLLLLQEAARvHGRTVVMVTHDP-VAASYADSVVFLADGR 233
Cdd:TIGR02673 158 LLLADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLsLVDRVAHRVIILDDGR 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
19-234 |
9.58e-56 |
|
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: 178.58 E-value: 9.58e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSadnaVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGggeaeLTKFR 98
Cdd:cd03300 1 IELENVSKFYGG----FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN-----LPPHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RGrVGFVFQQYNLLETLTVAQNTVLPLKLAGRRVD--RKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPR 176
Cdd:cd03300 72 RP-VNTVFQNYALFPHLTVFENIAFGLRLKKLPKAeiKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490075866 177 VIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDPVAA-SYADSVVFLADGRL 234
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEAlTMSDRIAVMNKGKI 209
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
19-258 |
2.42e-55 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 179.18 E-value: 2.42e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTY--GSAdNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTK 96
Cdd:TIGR04521 1 IKLKNVSYIYqpGTP-FEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 97 FRRgRVGFVFQ--QYNLLETlTVA-------QNtvlpLKLAGRRVDrKRAREVLTSVGLGDRLGHR-PDQLSGGQRQRVA 166
Cdd:TIGR04521 80 LRK-KVGLVFQfpEHQLFEE-TVYkdiafgpKN----LGLSEEEAE-ERVKEALELVGLDEEYLERsPFELSGGQMRRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 167 IARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHD-PVAASYADSVVFLADGRLAgrMDApTPDA 245
Cdd:TIGR04521 153 IAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSmEDVAEYADRVIVMHKGKIV--LDG-TPRE 229
|
250
....*....|....*.
gi 490075866 246 V---AERLAHLGDDVP 258
Cdd:TIGR04521 230 VfsdVDELEKIGLDVP 245
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
19-234 |
2.70e-55 |
|
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: 177.37 E-value: 2.70e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSadnaVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGL-----DRPDSGIVCVDGKELTGGGEaE 93
Cdd:cd03260 1 IELRDLNVYYGD----KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDV-D 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 94 LTKFRRgRVGFVFQQYNLLEtLTVAQNTVLPLKLAG---RRVDRKRAREVLTSVGLGDRLGHRPD--QLSGGQRQRVAIA 168
Cdd:cd03260 76 VLELRR-RVGMVFQKPNPFP-GSIYDNVAYGLRLHGiklKEELDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490075866 169 RALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHgrTVVMVTHDPV-AASYADSVVFLADGRL 234
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQqAARVADRTAFLLNGRL 218
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
14-235 |
5.09e-55 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 177.20 E-value: 5.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 14 PASEALRLVKVTRTYGSadnaVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGggeae 93
Cdd:COG1121 2 MMMPAIELENLTVSYGG----RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 94 ltkfRRGRVGFVFQQYNLLETL------TVAQNTVLPLKLAGR--RVDRKRAREVLTSVGLGDrLGHRP-DQLSGGQRQR 164
Cdd:COG1121 73 ----ARRRIGYVPQRAEVDWDFpitvrdVVLMGRYGRRGLFRRpsRADREAVDEALERVGLED-LADRPiGELSGGQQQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490075866 165 VAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARvHGRTVVMVTHDP-VAASYADSVVFLADGRLA 235
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDLgAVREYFDRVLLLNRGLVA 218
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
17-241 |
1.12e-54 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 176.98 E-value: 1.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 17 EALRLVKVTRTYGSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGeaeltk 96
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 97 frrGRVGFVFQQYNLLETLTVAQNTVLPLKLAG--RRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTE 174
Cdd:COG4525 76 ---ADRGVVFQKDALLPWLNVLDNVAFGLRLRGvpKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAAD 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490075866 175 PRVIFADEPTGALD--TRSARQVLLLlqEAARVHGRTVVMVTHDpvaasyADSVVFLAD---------GRLAGRMDAP 241
Cdd:COG4525 153 PRFLLMDEPFGALDalTREQMQELLL--DVWQRTGKGVFLITHS------VEEALFLATrlvvmspgpGRIVERLELD 222
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
48-237 |
2.76e-54 |
|
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: 174.41 E-value: 2.76e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 48 GTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFRRGRVGFVFQQYNLLETLTVAQNTVLPLKL 127
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPHLNVRENLAFGLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 128 AGRRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHG 207
Cdd:cd03297 103 KRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLN 182
|
170 180 190
....*....|....*....|....*....|.
gi 490075866 208 RTVVMVTHDPVAASY-ADSVVFLADGRLAGR 237
Cdd:cd03297 183 IPVIFVTHDLSEAEYlADRIVVMEDGRLQYI 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
33-234 |
2.72e-53 |
|
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: 173.60 E-value: 2.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 33 NAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFRRGRVGFVFQQYNLL 112
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 113 ETLTVAQNTVLPLKLAG--RRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDT- 189
Cdd:cd03294 115 PHRTVLENVAFGLEVQGvpRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPl 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490075866 190 --RSARQVLLLLQeaaRVHGRTVVMVTHDPVAA-SYADSVVFLADGRL 234
Cdd:cd03294 195 irREMQDELLRLQ---AELQKTIVFITHDLDEAlRLGDRIAIMKDGRL 239
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
19-254 |
2.98e-53 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 172.25 E-value: 2.98e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYG----SADnavtaldgvtLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAEl 94
Cdd:COG3840 2 LRLDDLTYRYGdfplRFD----------LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 95 tkfrrgR-VGFVFQQYNLLETLTVAQNTVL---P-LKLagRRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIAR 169
Cdd:COG3840 71 ------RpVSMLFQENNLFPHLTVAQNIGLglrPgLKL--TAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALAR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 170 ALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDPV-AASYADSVVFLADGRLA--GR----MDAPT 242
Cdd:COG3840 143 CLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEdAARIADRVLLVADGRIAadGPtaalLDGEP 222
|
250
....*....|..
gi 490075866 243 PDAVAerlAHLG 254
Cdd:COG3840 223 PPALA---AYLG 231
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
14-234 |
5.62e-53 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 171.50 E-value: 5.62e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 14 PASEALRLVKVTRTYGSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAE 93
Cdd:PRK10584 2 PAENIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 94 LTKFRRGRVGFVFQQYNLLETLTVAQNTVLPLKLAGR--RVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARAL 171
Cdd:PRK10584 82 RAKLRAKHVGFVFQSFMLIPTLNALENVELPALLRGEssRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490075866 172 VTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDPVAASYADSVVFLADGRL 234
Cdd:PRK10584 162 NGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
27-251 |
2.59e-52 |
|
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: 177.40 E-value: 2.59e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 27 TYGSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPD---SGIVCVDGKELTGGGEAEltkfRRGRVG 103
Cdd:COG1123 11 SVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL----RGRRIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 104 FVFQQY-NLLETLTVAQNTVLPLKLAG--RRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFA 180
Cdd:COG1123 87 MVFQDPmTQLNPVTVGDQIAEALENLGlsRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490075866 181 DEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDP-VAASYADSVVFLADGRLAGRMDAPTPDAVAERLA 251
Cdd:COG1123 167 DEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLgVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALA 238
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
38-234 |
3.91e-52 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 169.61 E-value: 3.91e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFRRGRVGFVFQQYNLLETLTV 117
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 118 AQNTVLPLKLAGRRVD--RKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQV 195
Cdd:PRK11629 105 LENVAMPLLIGKKKPAeiNSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSI 184
|
170 180 190
....*....|....*....|....*....|....*....
gi 490075866 196 LLLLQEAARVHGRTVVMVTHDPVAASYADSVVFLADGRL 234
Cdd:PRK11629 185 FQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-227 |
1.36e-51 |
|
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: 170.62 E-value: 1.36e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRP---DSGIVCVDGKELTGGGEAELT 95
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 96 KFRRGRVGFVFQQ-YNLLE-TLTVAQNTVLPLKL---AGRRVDRKRAREVLTSVGLGD---RLGHRPDQLSGGQRQRVAI 167
Cdd:COG0444 82 KIRGREIQMIFQDpMTSLNpVMTVGDQIAEPLRIhggLSKAEARERAIELLERVGLPDperRLDRYPHELSGGMRQRVMI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490075866 168 ARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHD-PVAASYADSVV 227
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDlGVVAEIADRVA 222
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
19-234 |
3.30e-51 |
|
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: 166.28 E-value: 3.30e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSadnaVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAEltkfr 98
Cdd:cd03301 1 VELENVTKRFGN----VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RGrVGFVFQQYNLLETLTVAQNTVLPLKLAGRRVD--RKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPR 176
Cdd:cd03301 72 RD-IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDeiDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490075866 177 VIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDPVAA-SYADSVVFLADGRL 234
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAmTMADRIAVMNDGQI 209
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
23-235 |
3.90e-51 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 167.19 E-value: 3.90e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 23 KVTRTYGsadnAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAEltKFRRGRV 102
Cdd:PRK09493 6 NVSKHFG----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDE--RLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 103 GFVFQQYNLLETLTVAQNTVL-PLKL--AGRRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIF 179
Cdd:PRK09493 80 GMVFQQFYLFPHLTALENVMFgPLRVrgASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490075866 180 ADEPTGALDTRSARQVLLLLQEAARvHGRTVVMVTHD-PVAASYADSVVFLADGRLA 235
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLAE-EGMTMVIVTHEiGFAEKVASRLIFIDKGRIA 215
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
23-234 |
4.01e-51 |
|
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: 166.43 E-value: 4.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 23 KVTRTYGsadNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFRRgRV 102
Cdd:cd03292 5 NVTKTYP---NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRR-KI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 103 GFVFQQYNLLETLTVAQNTVLPLKL--AGRRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFA 180
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVtgVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490075866 181 DEPTGALDTRSARQVLLLLQEAARVhGRTVVMVTHDP-VAASYADSVVFLADGRL 234
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKeLVDTTRHRVIALERGKL 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
36-234 |
8.07e-51 |
|
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: 164.15 E-value: 8.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 36 TALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKfrrgRVGFVFQqynlletl 115
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELAR----KIAYVPQ-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 116 tvaqntvlplklagrrvdrkrareVLTSVGLGDrLGHRP-DQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQ 194
Cdd:cd03214 81 ------------------------ALELLGLAH-LADRPfNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIE 135
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490075866 195 VLLLLQEAARVHGRTVVMVTHDP-VAASYADSVVFLADGRL 234
Cdd:cd03214 136 LLELLRRLARERGKTVVMVLHDLnLAARYADRVILLKDGRI 176
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
19-234 |
1.04e-49 |
|
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: 161.03 E-value: 1.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSadnaVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTgggeaELTKFR 98
Cdd:cd03230 1 IEVRNLSKRYGK----KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK-----KEPEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RGRVGFVFQQYNLLETLTVAQNtvlpLKLagrrvdrkrarevltsvglgdrlghrpdqlSGGQRQRVAIARALVTEPRVI 178
Cdd:cd03230 72 KRRIGYLPEEPSLYENLTVREN----LKL------------------------------SGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490075866 179 FADEPTGALDTRSARQVLLLLQEAARvHGRTVVMVTHD-PVAASYADSVVFLADGRL 234
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKK-EGKTILLSSHIlEEAERLCDRVAILNNGRI 173
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
19-248 |
1.27e-49 |
|
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: 163.24 E-value: 1.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSADNAVtalDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTgggEAELTKFR 98
Cdd:cd03295 1 IEFENVTKRYGGGKKAV---NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIR---EQDPVELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RgRVGFVFQQYNLLETLTVAQNTVLPLKLAG--RRVDRKRAREVLTSVGLGDR-LGHR-PDQLSGGQRQRVAIARALVTE 174
Cdd:cd03295 75 R-KIGYVIQQIGLFPHMTVEENIALVPKLLKwpKEKIRERADELLALVGLDPAeFADRyPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 175 PRVIFADEPTGALD--TRSARQvllllQEAARVH---GRTVVMVTHD-PVAASYADSVVFLADGRLAGR------MDAPT 242
Cdd:cd03295 154 PPLLLMDEPFGALDpiTRDQLQ-----EEFKRLQqelGKTIVFVTHDiDEAFRLADRIAIMKNGEIVQVgtpdeiLRSPA 228
|
....*.
gi 490075866 243 PDAVAE 248
Cdd:cd03295 229 NDFVAE 234
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
24-230 |
1.14e-48 |
|
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: 160.01 E-value: 1.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 24 VTRTYGSadnaVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGgeaeltkfrRGRVG 103
Cdd:cd03235 5 LTVSYGG----HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE---------RKRIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 104 FVFQQYNLLETLTVaqnTVLPLKLAGR-----------RVDRKRAREVLTSVGLGDrLGHRP-DQLSGGQRQRVAIARAL 171
Cdd:cd03235 72 YVPQRRSIDRDFPI---SVRDVVLMGLyghkglfrrlsKADKAKVDEALERVGLSE-LADRQiGELSGGQQQRVLLARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 172 VTEPRVIFADEPTGALDTRSARQVLLLLQEAARvHGRTVVMVTHDPVAAS-YADSVVFLA 230
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDLGLVLeYFDRVLLLN 206
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-235 |
1.15e-48 |
|
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: 170.79 E-value: 1.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 3 RSGARGNHDPGPASEALRLVKVTRTYGSADNAVtaLDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVD 82
Cdd:COG2274 458 REEGRSKLSLPRLKGDIELENVSFRYPGDSPPV--LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILID 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 83 GKELTgggEAELTKFRRgRVGFVFQQYNLLETlTVAQNtvlpLKLAGRRVDRKRAREVLTSVGLGD-----------RLG 151
Cdd:COG2274 536 GIDLR---QIDPASLRR-QIGVVLQDVFLFSG-TIREN----ITLGDPDATDEEIIEAARLAGLHDfiealpmgydtVVG 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 152 HRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARvhGRTVVMVTHDPVAASYADSVVFLAD 231
Cdd:COG2274 607 EGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLADRIIVLDK 684
|
....
gi 490075866 232 GRLA 235
Cdd:COG2274 685 GRIV 688
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
14-233 |
1.90e-48 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 160.74 E-value: 1.90e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 14 PASEALRLVKVTRTYGsaDNAVtaLDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKEL----TGG 89
Cdd:COG4598 4 TAPPALEVRDLHKSFG--DLEV--LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpDRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 90 GEAELTKFR-----RGRVGFVFQQYNLLETLTVAQNTVL-PLKLAGRRVD--RKRAREVLTSVGLGDRLGHRPDQLSGGQ 161
Cdd:COG4598 80 GELVPADRRqlqriRTRLGMVFQSFNLWSHMTVLENVIEaPVHVLGRPKAeaIERAEALLAKVGLADKRDAYPAHLSGGQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490075866 162 RQRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARvHGRTVVMVTHD-PVAASYADSVVFLADGR 233
Cdd:COG4598 160 QQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAE-EGRTMLVVTHEmGFARDVSSHVVFLHQGR 231
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
20-256 |
2.03e-48 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 162.18 E-value: 2.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 20 RLVKVTRTYGsadNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELtkfRR 99
Cdd:COG1125 3 EFENVTKRYP---DGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVEL---RR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 100 gRVGFVFQQYNLLETLTVAQNTVLPLKLAG--RRVDRKRAREVLTSVGL-GDRLGHR-PDQLSGGQRQRVAIARALVTEP 175
Cdd:COG1125 77 -RIGYVIQQIGLFPHMTVAENIATVPRLLGwdKERIRARVDELLELVGLdPEEYRDRyPHELSGGQQQRVGVARALAADP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 176 RVIFADEPTGALD--TRSARQVLLL-LQEAArvhGRTVVMVTHDpV--AASYADSVVFLADGRLAgRMDAPtpdavAERL 250
Cdd:COG1125 156 PILLMDEPFGALDpiTREQLQDELLrLQREL---GKTIVFVTHD-IdeALKLGDRIAVMREGRIV-QYDTP-----EEIL 225
|
....*.
gi 490075866 251 AHLGDD 256
Cdd:COG1125 226 ANPAND 231
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
18-234 |
2.13e-48 |
|
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: 160.20 E-value: 2.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 18 ALRLVKVTRTYGSAdnavTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGggeaelTKF 97
Cdd:cd03296 2 SIEVRNVSKRFGDF----VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATD------VPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 98 RRGRVGFVFQQYNLLETLTVAQNTVLPLKLAGRRVD------RKRAREVLTSVGLgDRLGHR-PDQLSGGQRQRVAIARA 170
Cdd:cd03296 72 QERNVGFVFQHYALFRHMTVFDNVAFGLRVKPRSERppeaeiRAKVHELLKLVQL-DWLADRyPAQLSGGQRQRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490075866 171 LVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDPVAA-SYADSVVFLADGRL 234
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEAlEVADRVVVMNKGRI 215
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
38-250 |
3.76e-48 |
|
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: 159.42 E-value: 3.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTgggeaELTKFRRGrVGFVFQQYNLLETLTV 117
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT-----NLPPEKRD-ISYVPQNYALFPHMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 118 AQNTVLPLKLagRRVDR----KRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSAR 193
Cdd:cd03299 89 YKNIAYGLKK--RKVDKkeieRKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490075866 194 QVLLLLQEAARVHGRTVVMVTHDPV-AASYADSVVFLADGRL--AGRMDA----PTPDAVAERL 250
Cdd:cd03299 167 KLREELKKIRKEFGVTVLHVTHDFEeAWALADKVAIMLNGKLiqVGKPEEvfkkPKNEFVAEFL 230
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
19-250 |
1.82e-47 |
|
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: 157.71 E-value: 1.82e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSadnaVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELtgggeAELTKFR 98
Cdd:COG4555 2 IEVENLSKKYGK----VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDV-----RKEPREA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RGRVGFVFQQYNLLETLTVAQNTVLPLKLAG--RRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPR 176
Cdd:COG4555 73 RRQIGVLPDERGLYDRLTVRENIRYFAELYGlfDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490075866 177 VIFADEPTGALDTRSARQVLLLLQEAARvHGRTVVMVTHDP-VAASYADSVVFLADGRLAgrmDAPTPDAVAERL 250
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKK-EGKTVLFSSHIMqEVEALCDRVVILHKGKVV---AQGSLDELREEI 223
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
12-237 |
2.96e-47 |
|
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: 164.94 E-value: 2.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 12 PGPASEALRLVKVTRTYgsADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGE 91
Cdd:COG4987 327 PAPGGPSLELEDVSFRY--PGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 92 AELtkfrRGRVGFVFQQYNLLETlTVAQNtvlpLKLAGRRVDRKRAREVLTSVGLGDRLGHRPD-----------QLSGG 160
Cdd:COG4987 405 DDL----RRRIAVVPQRPHLFDT-TLREN----LRLARPDATDEELWAALERVGLGDWLAALPDgldtwlgeggrRLSGG 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490075866 161 QRQRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARvhGRTVVMVTHDPVAASYADSVVFLADGRLAGR 237
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERMDRILVLEDGRIVEQ 550
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
19-233 |
4.62e-47 |
|
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: 154.46 E-value: 4.62e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSADNAVtaLDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELtkfr 98
Cdd:cd03228 1 IEFKNVSFSYPGRPKPV--LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RGRVGFVFQQYNLLETlTVAQNTvlplklagrrvdrkrarevltsvglgdrlghrpdqLSGGQRQRVAIARALVTEPRVI 178
Cdd:cd03228 75 RKNIAYVPQDPFLFSG-TIRENI-----------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490075866 179 FADEPTGALDTRSARQVLLLLQEAARvhGRTVVMVTHDPVAASYADSVVFLADGR 233
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
12-237 |
9.16e-47 |
|
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: 163.39 E-value: 9.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 12 PGPASEALRLVKVTRTYgsaDNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGE 91
Cdd:COG4988 330 PAAGPPSIELEDVSFSY---PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDP 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 92 AELtkfrRGRVGFVFQQYNLLETlTVAQNtvlpLKLAGRRVDRKRAREVLTSVGLGD-----------RLGHRPDQLSGG 160
Cdd:COG4988 407 ASW----RRQIAWVPQNPYLFAG-TIREN----LRLGRPDASDEELEAALEAAGLDEfvaalpdgldtPLGEGGRGLSGG 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490075866 161 QRQRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARvhGRTVVMVTHDPVAASYADSVVFLADGRLAGR 237
Cdd:COG4988 478 QAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQADRILVLDDGRIVEQ 552
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
19-234 |
1.50e-46 |
|
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: 155.29 E-value: 1.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSadnaVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTkfR 98
Cdd:cd03219 1 LEVRGLTKRFGG----LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA--R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RGrVGFVFQQYNLLETLTVAQNTVLPLKLAGR------------RVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVA 166
Cdd:cd03219 75 LG-IGRTFQIPRLFPELTVLENVMVAAQARTGsglllararreeREARERAEELLERVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490075866 167 IARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARvHGRTVVMVTHD-PVAASYADSVVFLADGRL 234
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDmDVVMSLADRVTVLDQGRV 221
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
18-252 |
1.73e-46 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 155.17 E-value: 1.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 18 ALRLVKVTRTYGSADnavtALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKEL---TGGGEAEL 94
Cdd:COG4161 2 SIQLKNINCFYGSHQ----ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 95 TKFRRgRVGFVFQQYNLLETLTVAQNTV-LPLKLAG--RRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARAL 171
Cdd:COG4161 78 RLLRQ-KVGMVFQQYNLWPHLTVMENLIeAPCKVLGlsKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 172 VTEPRVIFADEPTGALDTRSARQVLLLLQEAARVhGRTVVMVTHD-PVAASYADSVVFLADGRLAGRMDA-----PTPDA 245
Cdd:COG4161 157 MMEPQVLLFDEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEvEFARKVASQVVYMEKGRIIEQGDAshftqPQTEA 235
|
....*..
gi 490075866 246 VAERLAH 252
Cdd:COG4161 236 FAHYLSH 242
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
15-259 |
1.76e-46 |
|
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: 155.58 E-value: 1.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 15 ASEALRLVKVTRTYGsadnAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGggeaeL 94
Cdd:COG0411 1 SDPLLEVRGLTKRFG----GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITG-----L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 95 TKFRRGRVGFV--FQQYNLLETLTVAQN-----------------TVLPLKLAGRRVDRKRAREVLTSVGLGDRLGHRPD 155
Cdd:COG0411 72 PPHRIARLGIArtFQNPRLFPELTVLENvlvaaharlgrgllaalLRLPRARREEREARERAEELLERVGLADRADEPAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 156 QLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHD-PVAASYADSVVFLADGRL 234
Cdd:COG0411 152 NLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDmDLVMGLADRIVVLDFGRV 231
|
250 260 270
....*....|....*....|....*....|.
gi 490075866 235 --AGrmdapTPDAVAE----RLAHLGDDVPA 259
Cdd:COG0411 232 iaEG-----TPAEVRAdprvIEAYLGEEAAA 257
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
37-235 |
3.80e-46 |
|
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: 157.57 E-value: 3.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 37 ALDgVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFRRGRVGFVFQQYNLLETLT 116
Cdd:COG4148 15 TLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPPHRRRIGYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 117 VAQNtvlpLKLAGRRVDRKRAR----EVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSA 192
Cdd:COG4148 94 VRGN----LLYGRKRAPRAERRisfdEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490075866 193 RQVLLLLQeaaRVHGRT---VVMVTHDPV-AASYADSVVFLADGRLA 235
Cdd:COG4148 170 AEILPYLE---RLRDELdipILYVSHSLDeVARLADHVVLLEQGRVV 213
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
38-184 |
6.30e-46 |
|
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: 150.88 E-value: 6.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEaeltKFRRGRVGFVFQQYNLLETLTV 117
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDER----KSLRKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490075866 118 AQNTVLPLKLAG--RRVDRKRAREVLTSVGLGD----RLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPT 184
Cdd:pfam00005 77 RENLRLGLLLKGlsKREKDARAEEALEKLGLGDladrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
19-258 |
8.69e-46 |
|
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: 154.13 E-value: 8.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYgsADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTggGEAELTKFR 98
Cdd:TIGR04520 1 IEVENVSFSY--PESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTL--DEENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RgRVGFVFQ----QYnlletltVAqNTV------------LPLKLAGRRVDrkrarEVLTSVGLGDRLGHRPDQLSGGQR 162
Cdd:TIGR04520 77 K-KVGMVFQnpdnQF-------VG-ATVeddvafglenlgVPREEMRKRVD-----EALKLVGMEDFRDREPHLLSGGQK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 163 QRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDPVAASYADSVVFLADGRLAgrMDApT 242
Cdd:TIGR04520 143 QRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIV--AEG-T 219
|
250
....*....|....*....
gi 490075866 243 PDAV---AERLAHLGDDVP 258
Cdd:TIGR04520 220 PREIfsqVELLKEIGLDVP 238
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
20-233 |
1.08e-45 |
|
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: 150.47 E-value: 1.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 20 RLVKVTRTYGSadnaVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTgggeAELTKFRR 99
Cdd:cd00267 1 EIENLSFRYGG----RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA----KLPLEELR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 100 GRVGFVFQqynlletltvaqntvlplklagrrvdrkrarevltsvglgdrlghrpdqLSGGQRQRVAIARALVTEPRVIF 179
Cdd:cd00267 73 RRIGYVPQ-------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490075866 180 ADEPTGALDTRSARQVLLLLQEAARvHGRTVVMVTHDP-VAASYADSVVFLADGR 233
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAE-EGRTVIIVTHDPeLAELAADRVIVLKDGK 157
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
53-235 |
2.06e-45 |
|
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: 154.96 E-value: 2.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 53 VMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTgggeaELTKFRRGrVGFVFQQYNLLETLTVAQNTVLPLKLagRRV 132
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT-----NVPPHLRH-INMVFQSYALFPHMTVEENVAFGLKM--RKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 133 DRK----RAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGR 208
Cdd:TIGR01187 73 PRAeikpRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGI 152
|
170 180
....*....|....*....|....*...
gi 490075866 209 TVVMVTHDPVAA-SYADSVVFLADGRLA 235
Cdd:TIGR01187 153 TFVFVTHDQEEAmTMSDRIAIMRKGKIA 180
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
18-252 |
4.05e-45 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 151.71 E-value: 4.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 18 ALRLVKVTRTYGSADnavtALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKEL---TGGGEAEL 94
Cdd:PRK11124 2 SIQLNGINCFYGAHQ----ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 95 TKFRRgRVGFVFQQYNLLETLTVAQNTV-LPLKLAG--RRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARAL 171
Cdd:PRK11124 78 RELRR-NVGMVFQQYNLWPHLTVQQNLIeAPCRVLGlsKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 172 VTEPRVIFADEPTGALDTRSARQVLLLLQEAARVhGRTVVMVTHD-PVAASYADSVVFLADGRLAGRMDA-----PTPDA 245
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIRELAET-GITQVIVTHEvEVARKTASRVVYMENGHIVEQGDAscftqPQTEA 235
|
....*..
gi 490075866 246 VAERLAH 252
Cdd:PRK11124 236 FKNYLSH 242
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
19-235 |
1.82e-44 |
|
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: 149.18 E-value: 1.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSadnavTALDgVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTkfr 98
Cdd:cd03298 1 VRLDKIRFSYGE-----QPMH-FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 rgrVGFVFQQYNLLETLTVAQNTVLPL--KLAGRRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPR 176
Cdd:cd03298 72 ---VSMLFQENNLFAHLTVEQNVGLGLspGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 177 VIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDPV-AASYADSVVFLADGRLA 235
Cdd:cd03298 149 VLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEdAKRLAQRVVFLDNGRIA 208
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
19-226 |
1.46e-43 |
|
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: 146.47 E-value: 1.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSadnaVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAeltkfR 98
Cdd:COG4133 3 LEAENLSCRRGE----RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED-----Y 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RGRVGFVFQQYNLLETLTVAQNTVLPLKLAGRRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVI 178
Cdd:COG4133 74 RRRLAYLGHADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490075866 179 FADEPTGALDTRSARQVLLLLQEAARvHGRTVVMVTHDPVAASYADSV 226
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAHLA-RGGAVLLTTHQPLELAAARVL 200
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
38-243 |
6.59e-43 |
|
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: 145.69 E-value: 6.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTkfrrgrvgfVFQQYNLLETLTV 117
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV---------VFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 118 AQNTVLPLKLAGRRVDRKRAREV----LTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALD--TRS 191
Cdd:TIGR01184 72 RENIALAVDRVLPDLSKSERRAIveehIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDalTRG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490075866 192 ARQVLLLlqEAARVHGRTVVMVTHDPVAASY-ADSVVFLADG---RLAGRMDAPTP 243
Cdd:TIGR01184 152 NLQEELM--QIWEEHRVTVLMVTHDVDEALLlSDRVVMLTNGpaaNIGQILEVPFP 205
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
29-216 |
1.32e-41 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 144.87 E-value: 1.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 29 GSADNAVTALDGVTLSLGRG-TFtAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFRRgRVGFVFQ 107
Cdd:COG4608 25 GRTVGVVKAVDGVSFDIRRGeTL-GLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRR-RMQMVFQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 108 Q-YNLLET-LTVAQNTVLPLK---LAGRRVDRKRAREVLTSVGLGDRLGHR-PDQLSGGQRQRVAIARALVTEPRVIFAD 181
Cdd:COG4608 103 DpYASLNPrMTVGDIIAEPLRihgLASKAERRERVAELLELVGLRPEHADRyPHEFSGGQRQRIGIARALALNPKLIVCD 182
|
170 180 190
....*....|....*....|....*....|....*.
gi 490075866 182 EPTGALDTrSAR-QVLLLLQEAARVHGRTVVMVTHD 216
Cdd:COG4608 183 EPVSALDV-SIQaQVLNLLEDLQDELGLTYLFISHD 217
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
36-240 |
1.36e-41 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 142.97 E-value: 1.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 36 TALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTG----GGEAELTKFRRGRVGFVFQQYNL 111
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTarslSQQKGLIRQLRQHVGFVFQNFNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 112 LETLTVAQNTV---LPLKLAGRRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALD 188
Cdd:PRK11264 97 FPHRTVLENIIegpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490075866 189 TRSARQVLLLLQEAARvHGRTVVMVTHD-PVAASYADSVVFLADGRLAGRMDA 240
Cdd:PRK11264 177 PELVGEVLNTIRQLAQ-EKRTMVIVTHEmSFARDVADRAIFMDQGRIVEQGPA 228
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
19-235 |
1.94e-41 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 145.86 E-value: 1.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSAdnavTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGgEAEltkfR 98
Cdd:PRK09452 15 VELRGISKSFDGK----EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHV-PAE----N 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RgRVGFVFQQYNLLETLTVAQNTVLPLKLAGRRVD--RKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPR 176
Cdd:PRK09452 86 R-HVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAeiTPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 177 VIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDPVAA-SYADSVVFLADGRLA 235
Cdd:PRK09452 165 VLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEAlTMSDRIVVMRDGRIE 224
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
43-235 |
3.34e-41 |
|
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: 140.77 E-value: 3.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 43 LSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGggeaeLTKFRRgRVGFVFQQYNLLETLTVAQNTV 122
Cdd:TIGR01277 19 LNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTG-----LAPYQR-PVSMLFQENNLFAHLTVRQNIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 123 LPLK--LAGRRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQ 200
Cdd:TIGR01277 93 LGLHpgLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVK 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 490075866 201 EAARVHGRTVVMVTHDPV-AASYADSVVFLADGRLA 235
Cdd:TIGR01277 173 QLCSERQRTLLMVTHHLSdARAIASQIAVVSQGKIK 208
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
37-234 |
9.33e-41 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 140.94 E-value: 9.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 37 ALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCaagLDR-----PD---SGIVCVDGKELTGGGeAELTKFRRgRVGFVFQQ 108
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRC---LNRmndliPGarvEGEILLDGEDIYDPD-VDVVELRR-RVGMVFQK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 109 YNLLeTLTVAQNTVLPLKLAGRRvDRK----RAREVLTSVGL----GDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFA 180
Cdd:COG1117 101 PNPF-PKSIYDNVAYGLRLHGIK-SKSeldeIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLM 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490075866 181 DEPTGALDTRSARQVLLLLQEAARVHgrTVVMVTHDPV-AASYADSVVFLADGRL 234
Cdd:COG1117 179 DEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQqAARVSDYTAFFYLGEL 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-240 |
1.42e-40 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 145.93 E-value: 1.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 18 ALRLVKVTRTYGsadnAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGG--EAElt 95
Cdd:COG1129 4 LLEMRGISKSFG----GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSprDAQ-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 96 kfRRGrVGFVFQQYNLLETLTVAQNTVLP-LKLAGRRVDRK----RAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARA 170
Cdd:COG1129 78 --AAG-IAIIHQELNLVPNLSVAENIFLGrEPRRGGLIDWRamrrRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490075866 171 LVTEPRVIFADEPTGALdTRSARQVLLLLQEAARVHGRTVVMVTH--DPVAAsYADSVVFLADGRLAGRMDA 240
Cdd:COG1129 155 LSRDARVLILDEPTASL-TEREVERLFRIIRRLKAQGVAIIYISHrlDEVFE-IADRVTVLRDGRLVGTGPV 224
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
20-235 |
1.47e-40 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 140.22 E-value: 1.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 20 RLVKVTRTYGSAdnavTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKfrr 99
Cdd:COG4604 3 EIKNVSKRYGGK----VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 100 gRVGFVFQQYNLLETLTVAQntvlpLKLAGR---------RVDRKRAREVLTSVGLGDrLGHRP-DQLSGGQRQRVAIAR 169
Cdd:COG4604 76 -RLAILRQENHINSRLTVRE-----LVAFGRfpyskgrltAEDREIIDEAIAYLDLED-LADRYlDELSGGQRQRAFIAM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490075866 170 ALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHD-PVAASYADSVVFLADGRLA 235
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDiNFASCYADHIVAMKDGRVV 215
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
37-258 |
2.75e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 140.54 E-value: 2.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 37 ALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFRRGRVGFVFQ--QYNLLET 114
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLRKKVGIVFQfpEHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 115 lTVAQNTVL-PLKLAGRRVD-RKRAREVLTSVGLGDRLGHR-PDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRS 191
Cdd:PRK13634 102 -TVEKDICFgPMNFGVSEEDaKQKAREMIELVGLPEELLARsPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490075866 192 ARQVLLLLQEAARVHGRTVVMVTH---DpvAASYADSVVFLADGRLAGRmdaPTPDAV---AERLAHLGDDVP 258
Cdd:PRK13634 181 RKEMMEMFYKLHKEKGLTTVLVTHsmeD--AARYADQIVVMHKGTVFLQ---GTPREIfadPDELEAIGLDLP 248
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
27-234 |
5.65e-40 |
|
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: 144.83 E-value: 5.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 27 TYGSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKS----TLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFRRGRV 102
Cdd:COG4172 15 AFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRIRGNRI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 103 GFVFQQ----YNLLetLTVAQNTVLPLKL---AGRRVDRKRAREVLTSVGLGD---RLGHRPDQLSGGQRQRVAIARALV 172
Cdd:COG4172 95 AMIFQEpmtsLNPL--HTIGKQIAEVLRLhrgLSGAAARARALELLERVGIPDperRLDAYPHQLSGGQRQRVMIAMALA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490075866 173 TEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHD-PVAASYADSVVFLADGRL 234
Cdd:COG4172 173 NEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDlGVVRRFADRVAVMRQGEI 235
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
38-234 |
5.70e-40 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 141.37 E-value: 5.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGggeaeLTKFRRGrVGFVFQQYNLLETLTV 117
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITN-----LPPEKRG-IAYVYQNYMLFPHKTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 118 AQNTVLPLKLagRRVDR----KRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALD--TRS 191
Cdd:NF040840 90 FENIAFGLKL--RKVPKeeieRKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDvqTRD 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490075866 192 ArqvllLLQEAARVH---GRTVVMVTHD-PVAASYADSVVFLADGRL 234
Cdd:NF040840 168 E-----LIREMKRWHrefGFTAIHVTHNfEEALSLADRVGIMLNGRL 209
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
37-236 |
8.95e-40 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 137.31 E-value: 8.95e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 37 ALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFRRgRVGFVFQQYNLLETLT 116
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRR-QIGMIFQDHHLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 117 VAQNTVLPLKLAGRRVD--RKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQ 194
Cdd:PRK10908 96 VYDNVAIPLIIAGASGDdiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490075866 195 VLLLLQEAARVhGRTVVMVTHD-PVAASYADSVVFLADGRLAG 236
Cdd:PRK10908 176 ILRLFEEFNRV-GVTVLMATHDiGLISRRSYRMLTLSDGHLHG 217
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
15-235 |
1.02e-39 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 141.32 E-value: 1.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 15 ASEALRlvKVTRTYGsaDNAVTalDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTgggeaEL 94
Cdd:PRK11000 2 ASVTLR--NVTKAYG--DVVIS--KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN-----DV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 95 TKFRRGrVGFVFQQYNLLETLTVAQNTVLPLKLAG--RRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALV 172
Cdd:PRK11000 71 PPAERG-VGMVFQSYALYPHLSVAENMSFGLKLAGakKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490075866 173 TEPRVIFADEPTGALDtrSARQVLLLLqEAARVH---GRTVVMVTHDPVAA-SYADSVVFLADGRLA 235
Cdd:PRK11000 150 AEPSVFLLDEPLSNLD--AALRVQMRI-EISRLHkrlGRTMIYVTHDQVEAmTLADKIVVLDAGRVA 213
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
37-251 |
1.47e-39 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 137.91 E-value: 1.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 37 ALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGeAELtkfrrgrvGFVFQQYNLLETLT 116
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-AER--------GVVFQNEGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 117 VAQNTVLPLKLAG--RRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALD--TRSA 192
Cdd:PRK11248 87 VQDNVAFGLQLAGveKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDafTREQ 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490075866 193 RQVLLLlqEAARVHGRTVVMVTHDPVAAsyadsvVFLADGRLagrMDAPTPDAVAERLA 251
Cdd:PRK11248 167 MQTLLL--KLWQETGKQVLLITHDIEEA------VFMATELV---LLSPGPGRVVERLP 214
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
14-235 |
1.84e-39 |
|
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: 135.76 E-value: 1.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 14 PASEALRLVKVTRTYGSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAG-LDRP-DSGIVCVDGKELtggge 91
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrRTGLgVSGEVLINGRPL----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 92 aELTKFRRgRVGFVFQQYNLLETLTVAQNTVLPLKLAGrrvdrkrarevltsvglgdrlghrpdqLSGGQRQRVAIARAL 171
Cdd:cd03213 76 -DKRSFRK-IIGYVPQDDILHPTLTVRETLMFAAKLRG---------------------------LSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490075866 172 VTEPRVIFADEPTGALDTRSARQVLLLLQEAARvHGRTVVMVTHDPVAASYA--DSVVFLADGRLA 235
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAD-TGRTIICSIHQPSSEIFElfDKLLLLSQGRVI 191
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
8-237 |
2.39e-39 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 143.77 E-value: 2.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 8 GNHDPGPASEALRLVKVTRTYgsaDNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELT 87
Cdd:COG1132 329 GAVPLPPVRGEIEFENVSFSY---PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 88 GGGEAELtkfrRGRVGFVFQQYNLLETlTVAQNtvlpLKLAGRRVDRKRAREVLTSVGLGD-----------RLGHRPDQ 156
Cdd:COG1132 406 DLTLESL----RRQIGVVPQDTFLFSG-TIREN----IRYGRPDATDEEVEEAAKAAQAHEfiealpdgydtVVGERGVN 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 157 LSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARvhGRTVVMVTHDPVAASYADSVVFLADGRLAG 236
Cdd:COG1132 477 LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRNADRILVLDDGRIVE 554
|
.
gi 490075866 237 R 237
Cdd:COG1132 555 Q 555
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
35-233 |
3.01e-39 |
|
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: 142.90 E-value: 3.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 35 VTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDrPDSGIVCVDGKELTGGGEAELTKFRRgRVGFVFQQ-YNLLE 113
Cdd:COG4172 299 VKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRPLRR-RMQVVFQDpFGSLS 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 114 T-LTVAQNTVLPLKLAGRRVD----RKRAREVLTSVGLGDRLGHR-PDQLSGGQRQRVAIARALVTEPRVIFADEPTGAL 187
Cdd:COG4172 377 PrMTVGQIIAEGLRVHGPGLSaaerRARVAEALEEVGLDPAARHRyPHEFSGGQRQRIAIARALILEPKLLVLDEPTSAL 456
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490075866 188 DtRSAR-QVLLLLQEAARVHGRTVVMVTHD-PVAASYADSVVFLADGR 233
Cdd:COG4172 457 D-VSVQaQILDLLRDLQREHGLAYLFISHDlAVVRALAHRVMVMKDGK 503
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-261 |
4.74e-39 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 141.70 E-value: 4.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 18 ALRLVKVTRTYGSadnaVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGG--EAelt 95
Cdd:COG3845 5 ALELRGITKRFGG----VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSprDA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 96 kfRRGRVGFVFQQYNLLETLTVAQNTVLPL-KLAGRRVDRKRAREVLTSvgLGDRLG-----HRP-DQLSGGQRQRVAIA 168
Cdd:COG3845 78 --IALGIGMVHQHFMLVPNLTVAENIVLGLePTKGGRLDRKAARARIRE--LSERYGldvdpDAKvEDLSVGEQQRVEIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 169 RALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARvHGRTVVMVTH--DPVAAsYADSVVFLADGRLAGRMDapTPDAV 246
Cdd:COG3845 154 KALYRGARILILDEPTAVLTPQEADELFEILRRLAA-EGKSIIFITHklREVMA-IADRVTVLRRGKVVGTVD--TAETS 229
|
250
....*....|....*..
gi 490075866 247 AERLAHL--GDDVPAGV 261
Cdd:COG3845 230 EEELAELmvGREVLLRV 246
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
36-251 |
9.68e-39 |
|
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: 138.32 E-value: 9.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 36 TALDGVTLSLGRGTfTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFRRGRVGFVFQQYNLLETL 115
Cdd:TIGR02142 12 FSLDADFTLPGQGV-TAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 116 TVAQNTVLPLKLAGRRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQV 195
Cdd:TIGR02142 91 SVRGNLRYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490075866 196 LLLLQEAARVHGRTVVMVTHDPV-AASYADSVVFLADGRLAGrmdAPTPDAVAERLA 251
Cdd:TIGR02142 171 LPYLERLHAEFGIPILYVSHSLQeVLRLADRVVVLEDGRVAA---AGPIAEVWASPD 224
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-216 |
1.05e-38 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 135.60 E-value: 1.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTY--GSAdNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGggeaeLTK 96
Cdd:COG1101 2 LELKNLSKTFnpGTV-NEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTK-----LPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 97 FRRGR-VGFVFQqyNLL----ETLTVAQNTVL--------PLKLAGRRVDRKRAREVLTSVGLG--DRLGHRPDQLSGGQ 161
Cdd:COG1101 76 YKRAKyIGRVFQ--DPMmgtaPSMTIEENLALayrrgkrrGLRRGLTKKRRELFRELLATLGLGleNRLDTKVGLLSGGQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490075866 162 RQRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHD 216
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHN 208
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
19-234 |
2.18e-38 |
|
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: 133.78 E-value: 2.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSADNavTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTgggeAELTKFR 98
Cdd:cd03263 1 LQIRNLTKTYKKGTK--PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR----TDRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RgRVGFVFQQYNLLETLTVAQNTVLPLKLAGRRVDRKRAR--EVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPR 176
Cdd:cd03263 75 Q-SLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEveLLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490075866 177 VIFADEPTGALDTRSARQVLLLLQEAarVHGRTVVMVTHDP-VAASYADSVVFLADGRL 234
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMdEAEALCDRIAIMSDGKL 210
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
15-234 |
2.71e-38 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 134.71 E-value: 2.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 15 ASEALRLVKVTRTYGSADnavtALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKE--LTGGGEA 92
Cdd:PRK10619 2 SENKLNVIDLHKRYGEHE----VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinLVRDKDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 93 ELTKFR-------RGRVGFVFQQYNLLETLTVAQNTV-LPLKLAG--RRVDRKRAREVLTSVGLGDRL-GHRPDQLSGGQ 161
Cdd:PRK10619 78 QLKVADknqlrllRTRLTMVFQHFNLWSHMTVLENVMeAPIQVLGlsKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490075866 162 RQRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARvHGRTVVMVTHDPVAASYADS-VVFLADGRL 234
Cdd:PRK10619 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFARHVSShVIFLHQGKI 230
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
38-246 |
2.80e-38 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 137.14 E-value: 2.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGggeaelTKFRRGRVGFVFQQYNLLETLTV 117
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR------LHARDRKVGFVFQHYALFRHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 118 AQNTVLPLKLAGRR------VDRKRAREVLTSVGLGdRLGHR-PDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDT- 189
Cdd:PRK10851 92 FDNIAFGLTVLPRRerpnaaAIKAKVTQLLEMVQLA-HLADRyPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAq 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 190 --RSARQVLLLLQEAARVhgrTVVMVTHD-PVAASYADSVVFLADGRLAgrmDAPTPDAV 246
Cdd:PRK10851 171 vrKELRRWLRQLHEELKF---TSVFVTHDqEEAMEVADRVVVMSQGNIE---QAGTPDQV 224
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
19-257 |
6.10e-38 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 133.65 E-value: 6.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSAdnavTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGivcvdgkELTGGgEAELTKFR 98
Cdd:PRK11247 13 LLLNAVSKRYGER----TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG-------ELLAG-TAPLAEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RgRVGFVFQQYNLLETLTVAQNTVLPLKlaGRRvdRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVI 178
Cdd:PRK11247 81 E-DTRLMFQDARLLPWKKVIDNVGLGLK--GQW--RDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 179 FADEPTGALD--TRSARQVLL--LLQEaarvHGRTVVMVTHD-PVAASYADSVVFLADGR--LAGRMDAPTPDAV-AERL 250
Cdd:PRK11247 156 LLDEPLGALDalTRIEMQDLIesLWQQ----HGFTVLLVTHDvSEAVAMADRVLLIEEGKigLDLTVDLPRPRRRgSARL 231
|
....*..
gi 490075866 251 AHLGDDV 257
Cdd:PRK11247 232 AELEAEV 238
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-258 |
8.04e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 133.99 E-value: 8.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 15 ASEALRLVKVTRTYgsADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTgggEAEL 94
Cdd:PRK13635 2 KEEIIRVEHISFRY--PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS---EETV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 95 TKFRRgRVGFVFQQY-NLLETLTVAQNTVLPLKLAGrrVDR----KRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIAR 169
Cdd:PRK13635 77 WDVRR-QVGMVFQNPdNQFVGATVQDDVAFGLENIG--VPReemvERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 170 ALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDPVAASYADSVVFLADGRLagrMDAPTPDAV--- 246
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEI---LEEGTPEEIfks 230
|
250
....*....|..
gi 490075866 247 AERLAHLGDDVP 258
Cdd:PRK13635 231 GHMLQEIGLDVP 242
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
36-232 |
1.15e-37 |
|
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: 131.23 E-value: 1.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 36 TALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTgggeaelTKFRRGRVGFVFQ--QYNLLE 113
Cdd:cd03226 14 EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK-------AKERRKSIGYVMQdvDYQLFT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 114 TlTVAQNTVLPLKLAGRrvDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSAR 193
Cdd:cd03226 87 D-SVREELLLGLKELDA--GNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNME 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490075866 194 QVLLLLQEAARVhGRTVVMVTHDP-VAASYADSVVFLADG 232
Cdd:cd03226 164 RVGELIRELAAQ-GKAVIVITHDYeFLAKVCDRVLLLANG 202
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
36-252 |
1.87e-37 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 132.16 E-value: 1.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 36 TALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKfRRGrvgfVFQQYNLLE-T 114
Cdd:COG4559 15 TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELAR-RRA----VLPQHSSLAfP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 115 LTVAQntVLPLKLA----GRRVDRKRAREVLTSVGLGDrLGHRP-DQLSGGQRQRVAIARALV-------TEPRVIFADE 182
Cdd:COG4559 90 FTVEE--VVALGRAphgsSAAQDRQIVREALALVGLAH-LAGRSyQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490075866 183 PTGALDTRSARQVLLLLQEAARvHGRTVVMVTHD-PVAASYADSVVFLADGRLAGrmdAPTPDAV--AERLAH 252
Cdd:COG4559 167 PTSALDLAHQHAVLRLARQLAR-RGGGVVAVLHDlNLAAQYADRILLLHQGRLVA---QGTPEEVltDELLER 235
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
19-235 |
2.17e-37 |
|
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: 130.78 E-value: 2.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSADnavtALDGVTLSLGRGtFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEaeltKFR 98
Cdd:cd03264 1 LQLENLTKRYGKKR----ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ----KLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RgRVGFVFQQYNLLETLTV--AQNTVLPLK-LAGRRVDrKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEP 175
Cdd:cd03264 72 R-RIGYLPQEFGVYPNFTVreFLDYIAWLKgIPSKEVK-ARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490075866 176 RVIFADEPTGALDTRSARQVLLLLQEAARvhGRTVVMVTH--DPVAASyADSVVFLADGRLA 235
Cdd:cd03264 150 SILIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHivEDVESL-CNQVAVLNKGKLV 208
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
38-231 |
3.16e-36 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 127.60 E-value: 3.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPD---SGIVCVDGKELTGGgEAEltkfRRgRVGFVFQQYNLLET 114
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTAL-PAE----QR-RIGILFQDDLLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 115 LTVAQNtvLPLKLA---GRRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRS 191
Cdd:COG4136 91 LSVGEN--LAFALPptiGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAAL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490075866 192 ARQVLLLLQEAARVHGRTVVMVTHDPVAASYADSVVFLAD 231
Cdd:COG4136 169 RAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-235 |
3.67e-36 |
|
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: 128.16 E-value: 3.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPD---SGIVCVDGKELtgggEAELT 95
Cdd:cd03234 4 LPWWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPR----KPDQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 96 KFRrgrVGFVFQQYNLLETLTVAQNTVLPLKLAGRRVDRKRAREVLTSVGLGDRLGHRP------DQLSGGQRQRVAIAR 169
Cdd:cd03234 80 QKC---VAYVRQDDILLPGLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRiggnlvKGISGGERRRVSIAV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490075866 170 ALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARvHGRTVVMVTHDPVAASYA--DSVVFLADGRLA 235
Cdd:cd03234 157 QLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLAR-RNRIVILTIHQPRSDLFRlfDRILLLSSGEIV 223
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
24-258 |
6.49e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 129.15 E-value: 6.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 24 VTRTYgsADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDS---GIVCVDGKELTGGGEAELtkfrRG 100
Cdd:PRK13640 11 VSFTY--PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDI----RE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 101 RVGFVFQQY-NLLETLTVAQNTVLPLKlaGRRVDR----KRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEP 175
Cdd:PRK13640 85 KVGIVFQNPdNQFVGATVGDDVAFGLE--NRAVPRpemiKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 176 RVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDPVAASYADSVVFLADGRLagrMDAPTPDAV---AERLAH 252
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKL---LAQGSPVEIfskVEMLKE 239
|
....*.
gi 490075866 253 LGDDVP 258
Cdd:PRK13640 240 IGLDIP 245
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
19-234 |
8.84e-36 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 130.22 E-value: 8.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSAdnavTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGggeaelTKFR 98
Cdd:PRK11432 7 VVLKNITKRFGSN----TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH------RSIQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RGRVGFVFQQYNLLETLTVAQNTVLPLKLAGRRVD--RKRAREVLTSV---GLGDRLghrPDQLSGGQRQRVAIARALVT 173
Cdd:PRK11432 77 QRDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEerKQRVKEALELVdlaGFEDRY---VDQISGGQQQRVALARALIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490075866 174 EPRVIFADEPTGALDT---RSARQVLLLLQEAARVhgrTVVMVTHDPVAA-SYADSVVFLADGRL 234
Cdd:PRK11432 154 KPKVLLFDEPLSNLDAnlrRSMREKIRELQQQFNI---TSLYVTHDQSEAfAVSDTVIVMNKGKI 215
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
19-240 |
1.01e-35 |
|
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: 126.78 E-value: 1.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGsadnAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTkfR 98
Cdd:cd03224 1 LEVENLNAGYG----KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERA--R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RGrVGFVFQQYNLLETLTVAQNtvlpLKLAGRRVDRKRAREVLTSV-----GLGDRLGHRPDQLSGGQRQRVAIARALVT 173
Cdd:cd03224 75 AG-IGYVPEGRRIFPELTVEEN----LLLGAYARRRAKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 174 EPRVIFADEPTGALDTRSARQVLLLLQEAARvHGRTVVMVTHD-PVAASYADSVVFLADGR--LAGRMDA 240
Cdd:cd03224 150 RPKLLLLDEPSEGLAPKIVEEIFEAIRELRD-EGVTILLVEQNaRFALEIADRAYVLERGRvvLEGTAAE 218
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
37-234 |
1.64e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 127.94 E-value: 1.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 37 ALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFRRGRVGFVFQ--QYNLLET 114
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQfpESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 115 lTVAQNTVL-PLKLAGRRVD-RKRAREVLTSVGLGDRLGHR-PDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRS 191
Cdd:PRK13649 102 -TVLKDVAFgPQNFGVSQEEaEALAREKLALVGISESLFEKnPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490075866 192 ARQVLLLLQEAARvHGRTVVMVTH--DPVaASYADSVVFLADGRL 234
Cdd:PRK13649 181 RKELMTLFKKLHQ-SGMTIVLVTHlmDDV-ANYADFVYVLEKGKL 223
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
16-215 |
2.21e-35 |
|
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: 126.74 E-value: 2.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 16 SEALRLVKVTRTYGSadnaVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGI-VCVDGKELtgGGE--A 92
Cdd:COG1119 1 DPLLELRNVTVRRGG----KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERR--GGEdvW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 93 ELtkfrRGRVGFV--FQQYNLLETLTVAqNTVLPLKLA--GR-----RVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQ 163
Cdd:COG1119 75 EL----RKRIGLVspALQLRFPRDETVL-DVVLSGFFDsiGLyreptDEQRERARELLELLGLAHLADRPFGTLSQGEQR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490075866 164 RVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTH 215
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH 201
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
19-234 |
2.78e-35 |
|
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: 124.25 E-value: 2.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSADNAVtaLDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELtkfr 98
Cdd:cd03246 1 LEVENVSFRYPGAEPPV--LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RGRVGFVFQQYNLLETlTVAQNTvlplklagrrvdrkrarevltsvglgdrlghrpdqLSGGQRQRVAIARALVTEPRVI 178
Cdd:cd03246 75 GDHVGYLPQDDELFSG-SIAENI-----------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490075866 179 FADEPTGALDTRSARQVLLLLQeAARVHGRTVVMVTHDPVAASYADSVVFLADGRL 234
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIA-ALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
33-229 |
7.36e-35 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 123.50 E-value: 7.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 33 NAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKEltgggeaeltkfrrgRVGFVFQQYNLL 112
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA---------------RVAYVPQRSEVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 113 ETL------TVAQNTVLPLKLAGR--RVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPT 184
Cdd:NF040873 68 DSLpltvrdLVAMGRWARRGLWRRltRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490075866 185 GALDTRSARQVLLLLQEAARvHGRTVVMVTHDPVAASYADSVVFL 229
Cdd:NF040873 148 TGLDAESRERIIALLAEEHA-RGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
19-253 |
9.07e-35 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 125.51 E-value: 9.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYgsadNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCvdGKELTG------GGEA 92
Cdd:PRK09984 5 IRVEKLAKTF----NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGS--HIELLGrtvqreGRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 93 ELTKFRRGRVGFVFQQYNLLETLTVAQNTVL------PL-KLAGR---RVDRKRAREVLTSVGLGDRLGHRPDQLSGGQR 162
Cdd:PRK09984 79 RDIRKSRANTGYIFQQFNLVNRLSVLENVLIgalgstPFwRTCFSwftREQKQRALQALTRVGMVHFAHQRVSTLSGGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 163 QRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHD-PVAASYADSVVFLADGRLAgrMDAP 241
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQvDYALRYCERIVALRQGHVF--YDGS 236
|
250
....*....|..
gi 490075866 242 TPDAVAERLAHL 253
Cdd:PRK09984 237 SQQFDNERFDHL 248
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
17-235 |
9.11e-35 |
|
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: 124.40 E-value: 9.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 17 EALRLVKVtrtYGSadnaVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTgggeAELTK 96
Cdd:cd03265 2 EVENLVKK---YGD----FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPRE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 97 FRRgRVGFVFQQYNLLETLTVAQNTVLPLKLAG--RRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTE 174
Cdd:cd03265 71 VRR-RIGIVFQDLSVDDELTGWENLYIHARLYGvpGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490075866 175 PRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHD-PVAASYADSVVFLADGRLA 235
Cdd:cd03265 150 PEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYmEEAEQLCDRVAIIDHGRII 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
37-234 |
1.03e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 125.58 E-value: 1.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 37 ALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAeLTKFRRgRVGFVFQQY-NLLETL 115
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKS-LLEVRK-TVGIVFQNPdDQLFAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 116 TVAQNTV---LPLKLAGRRVDrKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSA 192
Cdd:PRK13639 95 TVEEDVAfgpLNLGLSKEEVE-KRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490075866 193 RQVLLLLQEAARvHGRTVVMVTHD-PVAASYADSVVFLADGRL 234
Cdd:PRK13639 174 SQIMKLLYDLNK-EGITIIISTHDvDLVPVYADKVYVMSDGKI 215
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
42-242 |
1.80e-34 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 123.92 E-value: 1.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 42 TLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTgggeaeLTKFRRGRVGFVFQQYNLLETLTVAQNT 121
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHT------TTPPSRRPVSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 122 VL---P-LKLAGRRvdRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQVLL 197
Cdd:PRK10771 93 GLglnPgLKLNAAQ--REKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490075866 198 LLQEAARVHGRTVVMVTH---DpvAASYADSVVFLADGRLAgrMDAPT 242
Cdd:PRK10771 171 LVSQVCQERQLTLLMVSHsleD--AARIAPRSLVVADGRIA--WDGPT 214
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
37-216 |
1.82e-34 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 127.26 E-value: 1.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 37 ALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELtgggeAELTKFRRgRVGFVFQQYNLLETLT 116
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-----SHVPPYQR-PINMMFQSYALFPHMT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 117 VAQNTVLPLK---LAGRRVdRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTR-SA 192
Cdd:PRK11607 108 VEQNIAFGLKqdkLPKAEI-ASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlRD 186
|
170 180
....*....|....*....|....
gi 490075866 193 RQVLLLLQEAARVhGRTVVMVTHD 216
Cdd:PRK11607 187 RMQLEVVDILERV-GVTCVMVTHD 209
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
12-229 |
2.52e-34 |
|
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: 129.33 E-value: 2.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 12 PGPASEALRLVKVTRTYGSADNAvtaLDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGE 91
Cdd:TIGR02857 315 TAAPASSLEFSGVSVAYPGRRPA---LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 92 AeltkFRRGRVGFVFQQYNLLETlTVAQNtvlpLKLAGRRVDRKRAREVLTSVGLGD-----------RLGHRPDQLSGG 160
Cdd:TIGR02857 392 D----SWRDQIAWVPQHPFLFAG-TIAEN----IRLARPDASDAEIREALERAGLDEfvaalpqgldtPIGEGGAGLSGG 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490075866 161 QRQRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARvhGRTVVMVTHDPVAASYADSVVFL 229
Cdd:TIGR02857 463 QAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRIVVL 529
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
37-258 |
2.71e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 124.77 E-value: 2.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 37 ALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGeAELTKFRRgRVGFVFQ--QYNLLET 114
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKK-VKLSDIRK-KVGLVFQypEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 115 lTVAQNTVLPLKLAGRRVD--RKRAREVLTSVGLG--DRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTR 190
Cdd:PRK13637 100 -TIEKDIAFGPINLGLSEEeiENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490075866 191 SARQVLLLLQEAARVHGRTVVMVTH--DPVaASYADSVVFLADGR--LAGrmdapTPDAV---AERLAHLGDDVP 258
Cdd:PRK13637 179 GRDEILNKIKELHKEYNMTIILVSHsmEDV-AKLADRIIVMNKGKceLQG-----TPREVfkeVETLESIGLAVP 247
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
18-233 |
2.86e-34 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 126.50 E-value: 2.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 18 ALRLVKVTRTYgsaDNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAEltkf 97
Cdd:PRK11650 3 GLKLQAVRKSY---DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 98 rRGrVGFVFQQYNLLETLTVAQNTVLPLKLAG--RRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEP 175
Cdd:PRK11650 76 -RD-IAMVFQNYALYPHMSVRENMAYGLKIRGmpKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490075866 176 RVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDPVAA-SYADSVVFLADGR 233
Cdd:PRK11650 154 AVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAmTLADRVVVMNGGV 212
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
18-234 |
4.47e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 123.95 E-value: 4.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 18 ALRLVKVTRTYGSADNavTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTgggeAELTKF 97
Cdd:PRK13632 7 MIKVENVSFSYPNSEN--NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS----KENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 98 RRGRVGFVFQQY-NLLETLTVAQNtvLPLKLAGRRVDRKRAREVLTS----VGLGDRLGHRPDQLSGGQRQRVAIARALV 172
Cdd:PRK13632 81 IRKKIGIIFQNPdNQFIGATVEDD--IAFGLENKKVPPKKMKDIIDDlakkVGMEDYLDKEPQNLSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490075866 173 TEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDPVAASYADSVVFLADGRL 234
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKL 220
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
38-241 |
4.80e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 124.17 E-value: 4.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGG-GEAELTKFRRgRVGFVFQ--QYNLLEt 114
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPEtGNKNLKKLRK-KVSLVFQfpEAQLFE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 115 ltvaqNTVL------PLKL-AGRRVDRKRAREVLTSVGLGDRL-GHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGA 186
Cdd:PRK13641 101 -----NTVLkdvefgPKNFgFSEDEAKEKALKWLKKVGLSEDLiSKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490075866 187 LDTRSARQVLLLLQEAARVhGRTVVMVTH--DPVaASYADSVVFLADGRLAgRMDAP 241
Cdd:PRK13641 176 LDPEGRKEMMQLFKDYQKA-GHTVILVTHnmDDV-AEYADDVLVLEHGKLI-KHASP 229
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
34-234 |
5.53e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 124.43 E-value: 5.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 34 AVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSG---IVCVDGKELTGGGEAE---------LTKFR--- 98
Cdd:PRK13651 19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtieWIFKDEKNKKKTKEKEkvleklviqKTRFKkik 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 -----RGRVGFVFQ--QYNLLETlTVAQNTVL-PLKLAGRRVD-RKRAREVLTSVGLG-DRLGHRPDQLSGGQRQRVAIA 168
Cdd:PRK13651 99 kikeiRRRVGVVFQfaEYQLFEQ-TIEKDIIFgPVSMGVSKEEaKKRAAKYIELVGLDeSYLQRSPFELSGGQKRRVALA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490075866 169 RALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARvHGRTVVMVTHD-PVAASYADSVVFLADGRL 234
Cdd:PRK13651 178 GILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNK-QGKTIILVTHDlDNVLEWTKRTIFFKDGKI 243
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-234 |
7.77e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 122.71 E-value: 7.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 35 VTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCaagLDR-----PD---SGIVCVDGKELTgggEAELTKFRRgRVGFVF 106
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRV---FNRlielyPEarvSGEVYLDGQDIF---KMDVIELRR-RVQMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 107 QQYNLLETLTVAQNTVLPLKL----AGRRVDRKRAREVLTSVGL----GDRLGHRPDQLSGGQRQRVAIARALVTEPRVI 178
Cdd:PRK14247 89 QIPNPIPNLSIFENVALGLKLnrlvKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490075866 179 FADEPTGALDTRSARQVLLLLQEAARvhGRTVVMVTHDPV-AASYADSVVFLADGRL 234
Cdd:PRK14247 169 LADEPTANLDPENTAKIESLFLELKK--DMTIVLVTHFPQqAARISDYVAFLYKGQI 223
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
18-250 |
8.56e-34 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 128.83 E-value: 8.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 18 ALRLVKVTRTYGSADNAvtALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELtkf 97
Cdd:TIGR03375 463 EIEFRNVSFAYPGQETP--ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADL--- 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 98 rRGRVGFVfQQYNLLETLTVAQNtvlpLKLAGRRVDRKRAREVLTSVGLGD-----------RLGHRPDQLSGGQRQRVA 166
Cdd:TIGR03375 538 -RRNIGYV-PQDPRLFYGTLRDN----IALGAPYADDEEILRAAELAGVTEfvrrhpdgldmQIGERGRSLSGGQRQAVA 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 167 IARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAarVHGRTVVMVTHDPVAASYADSVVFLADGRLagRMDAPtPDAV 246
Cdd:TIGR03375 612 LARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRW--LAGKTLVLVTHRTSLLDLVDRIIVMDNGRI--VADGP-KDQV 686
|
....
gi 490075866 247 AERL 250
Cdd:TIGR03375 687 LEAL 690
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-236 |
1.27e-33 |
|
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: 119.46 E-value: 1.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGsadnAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELtkfR 98
Cdd:cd03216 1 LELRGITKRFG----GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDA---R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RGRVGFVFQqynlletltvaqntvlplklagrrvdrkrarevltsvglgdrlghrpdqLSGGQRQRVAIARALVTEPRVI 178
Cdd:cd03216 74 RAGIAMVYQ-------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 179 FADEPTGALDTRSARQVLLLLQEAARvHGRTVVMVTH--DPVAAsYADSVVFLADGRLAG 236
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRA-QGVAVIFISHrlDEVFE-IADRVTVLRDGRVVG 162
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
37-233 |
1.33e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 122.92 E-value: 1.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 37 ALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELtkfrRGRVGFVFQQYN-LLETL 115
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV----RSKVGLVFQDPDdQVFSS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 116 TVAQNTV---LPLKLAGRRVDRkRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSA 192
Cdd:PRK13647 96 TVWDDVAfgpVNMGLDKDEVER-RVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490075866 193 RQVLLLLQEAARvHGRTVVMVTHD-PVAASYADSVVFLADGR 233
Cdd:PRK13647 175 ETLMEILDRLHN-QGKTVIVATHDvDLAAEWADQVIVLKEGR 215
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
37-234 |
2.69e-33 |
|
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: 120.39 E-value: 2.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 37 ALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELtkfrRGRVGFVFQQYNLLETlT 116
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL----RRNIGYVPQDVTLFYG-T 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 117 VAQNtvlpLKLAGRRVDRKRAREVLTSVGLGD-----------RLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTG 185
Cdd:cd03245 94 LRDN----ITLGAPLADDERILRAAELAGVTDfvnkhpngldlQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490075866 186 ALDTRSARQVLLLLQEAARvhGRTVVMVTHDPVAASYADSVVFLADGRL 234
Cdd:cd03245 170 AMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
19-234 |
3.95e-33 |
|
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: 118.95 E-value: 3.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGsaDNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELtgggeAELTKFR 98
Cdd:cd03247 1 LSINNVSFSYP--EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV-----SDLEKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RGRVGFVFQQYNLLETlTVAQNTvlplklaGRRvdrkrarevltsvglgdrlghrpdqLSGGQRQRVAIARALVTEPRVI 178
Cdd:cd03247 74 SSLISVLNQRPYLFDT-TLRNNL-------GRR-------------------------FSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490075866 179 FADEPTGALDTRSARQVLLLLQEAARvhGRTVVMVTHDPVAASYADSVVFLADGRL 234
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHMDKILFLENGKI 174
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
24-238 |
4.30e-33 |
|
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: 119.63 E-value: 4.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 24 VTRTYGSadnaVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAeltkfrRGRVG 103
Cdd:cd03268 6 LTKTYGK----KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA------LRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 104 FVFQQYNLLETLTVAQNtvLPLKLAGRRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEP 183
Cdd:cd03268 76 ALIEAPGFYPNLTAREN--LRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490075866 184 TGALD---TRSARQVLLLLQEaarvHGRTVVMVTH-----DPVaasyADSVVFLADGRLAGRM 238
Cdd:cd03268 154 TNGLDpdgIKELRELILSLRD----QGITVLISSHllseiQKV----ADRIGIINKGKLIEEG 208
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-234 |
1.13e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 119.77 E-value: 1.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 24 VTRTYGSADNAVTaLDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEA---ELTKFRRg 100
Cdd:PRK14246 13 ISRLYLYINDKAI-LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIfqiDAIKLRK- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 101 RVGFVFQQYNLLETLTVAQNTVLPLKLAG---RRVDRKRAREVLTSVGLG----DRLGHRPDQLSGGQRQRVAIARALVT 173
Cdd:PRK14246 91 EVGMVFQQPNPFPHLSIYDNIAYPLKSHGikeKREIKKIVEECLRKVGLWkevyDRLNSPASQLSGGQQQRLTIARALAL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490075866 174 EPRVIFADEPTGALDTRSARQVLLLLQEAARvhGRTVVMVTHDP-VAASYADSVVFLADGRL 234
Cdd:PRK14246 171 KPKVLLMDEPTSMIDIVNSQAIEKLITELKN--EIAIVIVSHNPqQVARVADYVAFLYNGEL 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
17-216 |
2.76e-32 |
|
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: 123.76 E-value: 2.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 17 EALRLVKVTRTYGSADNAVT-ALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVdgkeLTGGGEAELT 95
Cdd:TIGR03269 278 PIIKVRNVSKRYISVDRGVVkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV----RVGDEWVDMT 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 96 KFR---RGRV----GFVFQQYNL------LETLTVAQNTVLPLKLAgrrvdRKRAREVLTSVGLGDR-----LGHRPDQL 157
Cdd:TIGR03269 354 KPGpdgRGRAkryiGILHQEYDLyphrtvLDNLTEAIGLELPDELA-----RMKAVITLKMVGFDEEkaeeiLDKYPDEL 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490075866 158 SGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHD 216
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHD 487
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
38-259 |
7.48e-32 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 123.23 E-value: 7.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDsgiVCVDGKELTGGGEAELTKFRRgRVGFVFQQYNLLETLTV 117
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKG---VKGSGSVLLNGMPIDAKEMRA-ISAYVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 118 AQNTVLP--LKLaGRRV--DRKRAR--EVLTSVGLGD----RLG--HRPDQLSGGQRQRVAIARALVTEPRVIFADEPTG 185
Cdd:TIGR00955 117 REHLMFQahLRM-PRRVtkKEKRERvdEVLQALGLRKcantRIGvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490075866 186 ALDTRSARQVLLLLQEAARvHGRTVVMVTHDPVAASYA--DSVVFLADGRLAGRmdaPTPDAVAERLAHLGDDVPA 259
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQ-KGKTIICTIHQPSSELFElfDKIILMAEGRVAYL---GSPDQAVPFFSDLGHPCPE 267
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
19-237 |
7.73e-32 |
|
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: 116.70 E-value: 7.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKE-LTGGGEAeltkf 97
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDvVKEPAEA----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 98 rRGRVGFVFQQYNLLETLTVAQNTVLPLKLAGRRVDRKRAR--EVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEP 175
Cdd:cd03266 77 -RRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARleELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490075866 176 RVIFADEPTGALDTRSARQVLLLLQEaARVHGRTVVMVTHD-PVAASYADSVVFLADGRLAGR 237
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQ-LRALGKCILFSTHImQEVERLCDRVVVLHRGRVVYE 217
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
35-233 |
1.08e-31 |
|
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: 116.38 E-value: 1.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 35 VTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSG--IVCVDGK--ELTGGGEAELTKFRRGRVGFVFQqyn 110
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGsiLVRHDGGwvDLAQASPREILALRRRTIGYVSQ--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 111 LLETL-------TVAQntvlPLKLAG--RRVDRKRAREVLTSVGLGDRLGH-RPDQLSGGQRQRVAIARALVTEPRVIFA 180
Cdd:COG4778 101 FLRVIprvsaldVVAE----PLLERGvdREEARARARELLARLNLPERLWDlPPATFSGGEQQRVNIARGFIADPPLLLL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490075866 181 DEPTGALDTRSARQVLLLLQEaARVHGRTVVMVTHDP-VAASYADSVVFLADGR 233
Cdd:COG4778 177 DEPTASLDAANRAVVVELIEE-AKARGTAIIGIFHDEeVREAVADRVVDVTPFS 229
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
36-235 |
1.52e-31 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 116.79 E-value: 1.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 36 TALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKfRRGrvgfVFQQYNLLE-T 114
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELAR-RRA----VLPQHSSLSfP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 115 LTVAQntVLPLKLAGRRVDRKRAR----EVLTSVGLGDrLGHRP-DQLSGGQRQRVAIARALV------TEPRVIFADEP 183
Cdd:PRK13548 91 FTVEE--VVAMGRAPHGLSRAEDDalvaAALAQVDLAH-LAGRDyPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490075866 184 TGALDTRSARQVLLLLQEAARVHGRTVVMVTHD-PVAASYADSVVFLADGRLA 235
Cdd:PRK13548 168 TSALDLAHQHHVLRLARQLAHERGLAVIVVLHDlNLAARYADRIVLLHQGRLV 220
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
28-235 |
1.77e-31 |
|
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: 116.23 E-value: 1.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 28 YGsadnAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTkfRRGrVGFVFQ 107
Cdd:COG0410 13 YG----GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIA--RLG-IGYVPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 108 QYNLLETLTVAQNtvlpLKLAGR-RVDRKRAREVLTSVG-----LGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFAD 181
Cdd:COG0410 86 GRRIFPSLTVEEN----LLLGAYaRRDRAEVRADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490075866 182 EPTGALDTRSARQVLLLLQEAARvHGRTVVMVTHD-PVAASYADSVVFLADGRLA 235
Cdd:COG0410 162 EPSLGLAPLIVEEIFEIIRRLNR-EGVTILLVEQNaRFALEIADRAYVLERGRIV 215
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
37-234 |
2.12e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 117.19 E-value: 2.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 37 ALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFRRGRVGFVFQ--QYNLLET 114
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQfpESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 115 lTVAQNTVLPLKLAGRRVD--RKRAREVLTSVGLG-DRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRS 191
Cdd:PRK13646 102 -TVEREIIFGPKNFKMNLDevKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQS 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490075866 192 ARQVLLLLQEAARVHGRTVVMVTHD-PVAASYADSVVFLADGRL 234
Cdd:PRK13646 181 KRQVMRLLKSLQTDENKTIILVSHDmNEVARYADEVIVMKEGSI 224
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
23-258 |
2.91e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 116.73 E-value: 2.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 23 KVTRTYGSADNAV--TALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGkeLTGGGEAELTKFRRg 100
Cdd:PRK13633 9 NVSYKYESNEESTekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLWDIRN- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 101 RVGFVFQQY-NLLETLTVAQNT--------VLPLKLagrrvdRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARAL 171
Cdd:PRK13633 86 KAGMVFQNPdNQIVATIVEEDVafgpenlgIPPEEI------RERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 172 VTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDPVAASYADSVVFLADGRLAgrMDApTPDAV---AE 248
Cdd:PRK13633 160 AMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVV--MEG-TPKEIfkeVE 236
|
250
....*....|
gi 490075866 249 RLAHLGDDVP 258
Cdd:PRK13633 237 MMKKIGLDVP 246
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
15-239 |
3.67e-31 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 115.20 E-value: 3.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 15 ASEALRLVKVtrtyGSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTgggeaEL 94
Cdd:PRK10247 4 NSPLLQLQNV----GYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIS-----TL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 95 TKFR-RGRVGFVFQQYNLLETlTVAQNTVLPLKLAGRRVDRKRAREVLTSVGLGDR-LGHRPDQLSGGQRQRVAIARALV 172
Cdd:PRK10247 75 KPEIyRQQVSYCAQTPTLFGD-TVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTiLTKNIAELSGGEKQRISLIRNLQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490075866 173 TEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDPVAASYADSVVFLADGrlAGRMD 239
Cdd:PRK10247 154 FMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQPH--AGEMQ 218
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
19-233 |
4.09e-31 |
|
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: 115.02 E-value: 4.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSADNAVtaLDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTgggEAELTKFR 98
Cdd:cd03251 1 VEFKNVTFRYPGDGPPV--LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVR---DYTLASLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RgRVGFVFQQYNLLETlTVAQNtvlpLKLAGRRVDRKRAREVLTSV-----------GLGDRLGHRPDQLSGGQRQRVAI 167
Cdd:cd03251 76 R-QIGLVSQDVFLFND-TVAEN----IAYGRPGATREEVEEAARAAnahefimelpeGYDTVIGERGVKLSGGQRQRIAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490075866 168 ARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARvhGRTVVMVTHDPVAASYADSVVFLADGR 233
Cdd:cd03251 150 ARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIENADRIVVLEDGK 213
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
24-233 |
4.55e-31 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 117.37 E-value: 4.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 24 VTRTYGSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELtKFRRGRVG 103
Cdd:PRK11308 17 VKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQ-KLLRQKIQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 104 FVFQqyNLLETL----TVAQNTVLPLKL-----AGRRvdRKRAREVLTSVGLGDRLGHR-PDQLSGGQRQRVAIARALVT 173
Cdd:PRK11308 96 IVFQ--NPYGSLnprkKVGQILEEPLLIntslsAAER--REKALAMMAKVGLRPEHYDRyPHMFSGGQRQRIAIARALML 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490075866 174 EPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHD-PVAASYADSVVFLADGR 233
Cdd:PRK11308 172 DPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDlSVVEHIADEVMVMYLGR 232
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
35-233 |
5.17e-31 |
|
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: 114.94 E-value: 5.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 35 VTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCaagLDR---PDSGIVCVDGKELTgggeaELT-KFRRGRVGFVFQQYN 110
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSL---LERfydPTSGEILLDGVDIR-----DLNlRWLRSQIGLVSQEPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 111 LLETlTVAQNTVLPLKLAGRRVDRKRAR-----EVLTSV--GLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEP 183
Cdd:cd03249 88 LFDG-TIAENIRYGKPDATDEEVEEAAKkanihDFIMSLpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490075866 184 TGALDTRSARQVLLLLQEAARvhGRTVVMVTHDPVAASYADSVVFLADGR 233
Cdd:cd03249 167 TSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRNADLIAVLQNGQ 214
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
8-234 |
9.66e-31 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 119.54 E-value: 9.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 8 GNHDPGPASEALRLVKVTRTYgsADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCaagLDR---PDSGIVCVDGK 84
Cdd:PRK11160 328 TTSTAAADQVSLTLNNVSFTY--PDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQL---LTRawdPQQGEILLNGQ 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 85 ELTGGGEAELtkfrRGRVGFVFQQYNLLETlTVAQNtvlpLKLAGRRVDRKRAREVLTSVGLGDRL------------GH 152
Cdd:PRK11160 403 PIADYSEAAL----RQAISVVSQRVHLFSA-TLRDN----LLLAAPNASDEALIEVLQQVGLEKLLeddkglnawlgeGG 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 153 RpdQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARvhGRTVVMVTHDPVAASYADSVVFLADG 232
Cdd:PRK11160 474 R--QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQFDRICVMDNG 549
|
..
gi 490075866 233 RL 234
Cdd:PRK11160 550 QI 551
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
37-233 |
2.62e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 114.17 E-value: 2.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 37 ALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKEL--TGGGEAELtkfrRGRVGFVFQQY-NLLE 113
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKL----RESVGMVFQDPdNQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 114 TLTVAQNT---VLPLKLAGRRVdRKRAREVLTSVGLgDRLGHRPDQ-LSGGQRQRVAIARALVTEPRVIFADEPTGALDT 189
Cdd:PRK13636 97 SASVYQDVsfgAVNLKLPEDEV-RKRVDNALKRTGI-EHLKDKPTHcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490075866 190 RSARQVLLLLQEAARVHGRTVVMVTHD-PVAASYADSVVFLADGR 233
Cdd:PRK13636 175 MGVSEIMKLLVEMQKELGLTIIIATHDiDIVPLYCDNVFVMKEGR 219
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
35-216 |
3.89e-30 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 113.39 E-value: 3.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 35 VTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGeaelTKFRRGRVGFVFQQYN--LL 112
Cdd:COG4167 26 FEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD----YKYRCKHIRMIFQDPNtsLN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 113 ETLTVAQNTVLPLKLAGRRVDRKRAREV---LTSVGL-GDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALD 188
Cdd:COG4167 102 PRLNIGQILEEPLRLNTDLTAEEREERIfatLRLVGLlPEHANFYPHMLSSGQKQRVALARALILQPKIIIADEALAALD 181
|
170 180 190
....*....|....*....|....*....|
gi 490075866 189 --TRSarQVLLLLQEAARVHGRTVVMVTHD 216
Cdd:COG4167 182 msVRS--QIINLMLELQEKLGISYIYVSQH 209
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
19-246 |
3.98e-30 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 113.19 E-value: 3.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGsadnAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKfr 98
Cdd:PRK11231 3 LRTENLTVGYG----TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLAR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 rgRVGFVFQQYNLLETLTVAQ------NTVLPL--KLAGRrvDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARA 170
Cdd:PRK11231 77 --RLALLPQHHLTPEGITVRElvaygrSPWLSLwgRLSAE--DNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490075866 171 LVTEPRVIFADEPTGALDTrsARQVLL--LLQEaARVHGRTVVMVTHDPVAAS-YADSVVFLADGRLagrMDAPTPDAV 246
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLDI--NHQVELmrLMRE-LNTQGKTVVTVLHDLNQASrYCDHLVVLANGHV---MAQGTPEEV 225
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
21-216 |
5.26e-30 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 113.24 E-value: 5.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 21 LVKVTRTYG--SADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFR 98
Cdd:PRK10419 9 LSHHYAHGGlsGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RGrVGFVFQ--------QYNLLETLTVAQNTVLPLKLAGRRVdrkRAREVLTSVGLGDRLGHR-PDQLSGGQRQRVAIAR 169
Cdd:PRK10419 89 RD-IQMVFQdsisavnpRKTVREIIREPLRHLLSLDKAERLA---RASEMLRAVDLDDSVLDKrPPQLSGGQLQRVCLAR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490075866 170 ALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHD 216
Cdd:PRK10419 165 ALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHD 211
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
19-233 |
8.67e-30 |
|
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: 110.83 E-value: 8.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSadnaVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGeaeltkfr 98
Cdd:cd03269 1 LEVENVTKRFGR----VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RGRVGFVFQQYNLLETLTVAQNTVLPLKLAG--RRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPR 176
Cdd:cd03269 69 RNRIGYLPEERGLYPKMKVIDQLVYLAQLKGlkKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490075866 177 VIFADEPTGALDTRSARQVLLLLQEAARvHGRTVVMVTH--DPVAAsYADSVVFLADGR 233
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELAR-AGKTVILSTHqmELVEE-LCDRVLLLNKGR 205
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-234 |
1.29e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 111.86 E-value: 1.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 18 ALRLVKVTRTYGSadNAVtaLDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGL-----DRPDSGIVCVDGKELTGGgEA 92
Cdd:PRK14267 4 AIETVNLRVYYGS--NHV--IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSP-DV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 93 ELTKFRRgRVGFVFQQYNLLETLTVAQNTVLPLKLAGRRVDRK----RAREVLTSVGL----GDRLGHRPDQLSGGQRQR 164
Cdd:PRK14267 79 DPIEVRR-EVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKeldeRVEWALKKAALwdevKDRLNDYPSNLSGGQRQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490075866 165 VAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHgrTVVMVTHDPV-AASYADSVVFLADGRL 234
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAqAARVSDYVAFLYLGKL 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-253 |
1.31e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 112.52 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYG-SADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKF 97
Cdd:PRK13643 2 IKFEKVNYTYQpNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 98 RRGRVGFVFQ--QYNLLETLTVAQNTVLPLKLA-GRRVDRKRAREVLTSVGLGDRLGHR-PDQLSGGQRQRVAIARALVT 173
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGPQNFGiPKEKAEKIAAEKLEMVGLADEFWEKsPFELSGGQMRRVAIAGILAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 174 EPRVIFADEPTGALDTRsARQVLLLLQEAARVHGRTVVMVTH--DPVaASYADSVVFLADGRLagrMDAPTPDAVAERLA 251
Cdd:PRK13643 162 EPEVLVLDEPTAGLDPK-ARIEMMQLFESIHQSGQTVVLVTHlmDDV-ADYADYVYLLEKGHI---ISCGTPSDVFQEVD 236
|
..
gi 490075866 252 HL 253
Cdd:PRK13643 237 FL 238
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
37-216 |
1.62e-29 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 113.26 E-value: 1.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 37 ALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFRRgRVGFVFQQ--YNLLET 114
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRS-DIQMIFQDplASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 115 LTVAQNTVLPL-----KLAGRRVdRKRAREVLTSVGLGDRLGHR-PDQLSGGQRQRVAIARALVTEPRVIFADEPTGALD 188
Cdd:PRK15079 115 MTIGEIIAEPLrtyhpKLSRQEV-KDRVKAMMLKVGLLPNLINRyPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180
....*....|....*....|....*...
gi 490075866 189 TRSARQVLLLLQEAARVHGRTVVMVTHD 216
Cdd:PRK15079 194 VSIQAQVVNLLQQLQREMGLSLIFIAHD 221
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
37-240 |
1.82e-29 |
|
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: 110.92 E-value: 1.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 37 ALDGVTLSLGRGTFTAVMGPSGSGKStlLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFRRGRVGFVFQQ----YNLL 112
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKS--LTCLAILGLLPPGLTQTSGEILLDGRPLLPLSIRGRHIATIMQNprtaFNPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 113 etLTVAQNTVLPLKLAGR--RVDRKRAREVLTSVGLGDR---LGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGAL 187
Cdd:TIGR02770 79 --FTMGNHAIETLRSLGKlsKQARALILEALEAVGLPDPeevLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490075866 188 DTRSARQVLLLLQEAARVHGRTVVMVTHD-PVAASYADSVVFLADGRLAGRMDA 240
Cdd:TIGR02770 157 DVVNQARVLKLLRELRQLFGTGILLITHDlGVVARIADEVAVMDDGRIVERGTV 210
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
30-234 |
1.83e-29 |
|
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: 110.78 E-value: 1.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 30 SADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELtkfrRGRVGFVFQQY 109
Cdd:cd03254 11 SYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL----RSMIGVVLQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 110 NLLETlTVAQNtvlpLKLAGRRVDRKRAREVLTSVGLGD-----------RLGHRPDQLSGGQRQRVAIARALVTEPRVI 178
Cdd:cd03254 87 FLFSG-TIMEN----IRLGRPNATDEEVIEAAKEAGAHDfimklpngydtVLGENGGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490075866 179 FADEPTGALDTRSARqvllLLQEAARV--HGRTVVMVTHDPVAASYADSVVFLADGRL 234
Cdd:cd03254 162 ILDEATSNIDTETEK----LIQEALEKlmKGRTSIIIAHRLSTIKNADKILVLDDGKI 215
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
37-234 |
4.21e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 110.25 E-value: 4.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 37 ALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCaagLDR-----PD---SGIVCVDGKELTGGgEAELTKFRRgRVGFVFQQ 108
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRS---INRmndlnPEvtiTGSIVYNGHNIYSP-RTDTVDLRK-EIGMVFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 109 YNLLeTLTVAQNTVLPLKLAGRRvDRKRAREVLTSVGLG--------DRLGHRPDQLSGGQRQRVAIARALVTEPRVIFA 180
Cdd:PRK14239 95 PNPF-PMSIYENVVYGLRLKGIK-DKQVLDEAVEKSLKGasiwdevkDRLHDSALGLSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490075866 181 DEPTGALDTRSARQV---LLLLQeaarvHGRTVVMVTHDPVAAS-YADSVVFLADGRL 234
Cdd:PRK14239 173 DEPTSALDPISAGKIeetLLGLK-----DDYTMLLVTRSMQQASrISDRTGFFLDGDL 225
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
37-235 |
7.41e-29 |
|
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: 109.50 E-value: 7.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 37 ALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELtggGEAELTKFRRgRVGFVFQQyNLLETLT 116
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDL---ALADPAWLRR-QVGVVLQE-NVLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 117 VAQNtvlpLKLAGRRVDRKRAREVLT-----------SVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTG 185
Cdd:cd03252 92 IRDN----IALADPGMSMERVIEAAKlagahdfiselPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490075866 186 ALDTRSARQVLLLLQEAARvhGRTVVMVTHDPVAASYADSVVFLADGRLA 235
Cdd:cd03252 168 ALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKNADRIIVMEKGRIV 215
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
42-246 |
1.35e-28 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 112.05 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 42 TLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFRRGRVGFVFQQYNLLETLTVAQNT 121
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 122 VLPLKLAGRRVD--RKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALD--TRSARQVLL 197
Cdd:PRK10070 128 AFGMELAGINAEerREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDplIRTEMQDEL 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490075866 198 LLQEAArvHGRTVVMVTHD-PVAASYADSVVFLADGRLagrMDAPTPDAV 246
Cdd:PRK10070 208 VKLQAK--HQRTIVFISHDlDEAMRIGDRIAIMQNGEV---VQVGTPDEI 252
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
8-234 |
2.19e-28 |
|
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: 112.89 E-value: 2.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 8 GNHDPGPASEALRLVKVTRTYGSADnaVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELT 87
Cdd:TIGR02203 320 GTRAIERARGDVEFRNVTFRYPGRD--RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLA 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 88 gggEAELTKFRRgRVGFVFQQYNLLETlTVAQNTVLPlklAGRRVDRKRAREVLTSVGLGDRLGHRPD-----------Q 156
Cdd:TIGR02203 398 ---DYTLASLRR-QVALVSQDVVLFND-TIANNIAYG---RTEQADRAEIERALAAAYAQDFVDKLPLgldtpigengvL 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490075866 157 LSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARvhGRTVVMVTHDPVAASYADSVVFLADGRL 234
Cdd:TIGR02203 470 LSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEKADRIVVMDDGRI 545
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
27-235 |
2.79e-28 |
|
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: 112.53 E-value: 2.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 27 TYGSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELtkfrrGR-VGFV 105
Cdd:COG4618 337 TVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREEL-----GRhIGYL 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 106 FQQYNLLETlTVAQN-----------TVLPLKLAGrrvdrkrAREVLTSVGLG-D-RLGHRPDQLSGGQRQRVAIARALV 172
Cdd:COG4618 412 PQDVELFDG-TIAENiarfgdadpekVVAAAKLAG-------VHEMILRLPDGyDtRIGEGGARLSGGQRQRIGLARALY 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490075866 173 TEPRVIFADEPTGALDTRSARQVLLLLQeAARVHGRTVVMVTHDPVAASYADSVVFLADGRLA 235
Cdd:COG4618 484 GDPRLVVLDEPNSNLDDEGEAALAAAIR-ALKARGATVVVITHRPSLLAAVDKLLVLRDGRVQ 545
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
38-243 |
2.80e-28 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 112.59 E-value: 2.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSG-IVCVDGKELTgggeaeltkfrrgrvgFVFQQ-YNLLETL 115
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGrIARPAGARVL----------------FLPQRpYLPLGTL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 116 tvAQNTVLPLklAGRRVDRKRAREVLTSVGLGDrLGHRPDQ-------LSGGQRQRVAIARALVTEPRVIFADEPTGALD 188
Cdd:COG4178 443 --REALLYPA--TAEAFSDAELREALEAVGLGH-LAERLDEeadwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALD 517
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490075866 189 TRSARQVLLLLQEaaRVHGRTVVMVTHDPVAASYADSVVFLADGRLAGRMDAPTP 243
Cdd:COG4178 518 EENEAALYQLLRE--ELPGTTVISVGHRSTLAAFHDRVLELTGDGSWQLLPAEAP 570
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
38-258 |
4.24e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 108.28 E-value: 4.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTgggEAELTKFRRgRVGFVFQQY-NLLETLT 116
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT---EENVWDIRH-KIGMVFQNPdNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 117 VA-------QNTVLPLKLAGRRVDrkrarEVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDT 189
Cdd:PRK13650 99 VEddvafglENKGIPHEEMKERVN-----EALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490075866 190 RSARQVLLLLQEAARVHGRTVVMVTHDPVAASYADSVVFLADGRLAgrmDAPTPDAV---AERLAHLGDDVP 258
Cdd:PRK13650 174 EGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVE---STSTPRELfsrGNDLLQLGLDIP 242
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-239 |
4.45e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 108.66 E-value: 4.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 18 ALRLVKVTRTYGSadnaVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGeaeltkf 97
Cdd:COG4152 1 MLELKGLTKRFGD----KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 98 rRGRVGFV------FQQYNLLETLT-VAQntvlpLKLAGRRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARA 170
Cdd:COG4152 70 -RRRIGYLpeerglYPKMKVGEQLVyLAR-----LKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490075866 171 LVTEPRVIFADEPTGALDTRSARQVL-LLLQEAARvhGRTVVMVTHD-PVAASYADSVVFLADGR--LAGRMD 239
Cdd:COG4152 144 LLHDPELLILDEPFSGLDPVNVELLKdVIRELAAK--GTTVIFSSHQmELVEELCDRIVIINKGRkvLSGSVD 214
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
35-236 |
6.67e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 107.97 E-value: 6.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 35 VTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFrrgrVGFVFQQYN-LLE 113
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKF----VGLVFQNPDdQIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 114 TLTVAQNTVL-PLKLA-GRRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRS 191
Cdd:PRK13652 93 SPTVEQDIAFgPINLGlDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490075866 192 ARQVLLLLQEAARVHGRTVVMVTHD-PVAASYADSVVFLADGRLAG 236
Cdd:PRK13652 173 VKELIDFLNDLPETYGMTVIFSTHQlDLVPEMADYIYVMDKGRIVA 218
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
32-258 |
1.00e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 107.49 E-value: 1.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 32 DNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTgggeAELTKFRRGRVGFVFQQY-N 110
Cdd:PRK13642 17 ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLT----AENVWNLRRKIGMVFQNPdN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 111 LLETLTVAQNTVLPLKLAG--RRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALD 188
Cdd:PRK13642 93 QFVGATVEDDVAFGMENQGipREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLD 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 189 TRSARQVLLLLQEAARVHGRTVVMVTHDPVAASYADSVVFLADGRLAGRMDAPTPDAVAERLAHLGDDVP 258
Cdd:PRK13642 173 PTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDMVEIGLDVP 242
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
19-233 |
1.03e-27 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 106.93 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGsadnAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGK-----ELTGGGEAE 93
Cdd:PRK11701 7 LSVRGLTKLYG----PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 94 LTKFRRGRVGFVFQ--QYNLLETLTVAQNTVLPLKLAGRR---VDRKRAREVLTSVGLG-DRLGHRPDQLSGGQRQRVAI 167
Cdd:PRK11701 83 RRRLLRTEWGFVHQhpRDGLRMQVSAGGNIGERLMAVGARhygDIRATAGDWLERVEIDaARIDDLPTTFSGGMQQRLQI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490075866 168 ARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHD-PVAASYADSVVFLADGR 233
Cdd:PRK11701 163 ARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDlAVARLLAHRLLVMKQGR 229
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
33-234 |
1.53e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 107.63 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 33 NAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCV------DGKELTGGGEAELTK----FRRGR- 101
Cdd:PRK13631 37 NELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigDKKNNHELITNPYSKkiknFKELRr 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 102 -VGFVFQ--QYNLLETlTVAQNTVL-PLKLAGRRVD-RKRAREVLTSVGLGDR-LGHRPDQLSGGQRQRVAIARALVTEP 175
Cdd:PRK13631 117 rVSMVFQfpEYQLFKD-TIEKDIMFgPVALGVKKSEaKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAIQP 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490075866 176 RVIFADEPTGALDTRSARQVLLLLQEaARVHGRTVVMVTH--DPVaASYADSVVFLADGRL 234
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHtmEHV-LEVADEVIVMDKGKI 254
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
38-237 |
1.61e-27 |
|
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: 105.78 E-value: 1.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTgggEAELTKFRRgRVGFVFQQynlletlTV 117
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIR---EVTLDSLRR-AIGVVPQD-------TV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 118 AQNTVLPLKLAGRRVD---------RKRAR--EVLTSV--GLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPT 184
Cdd:cd03253 86 LFNDTIGYNIRYGRPDatdeevieaAKAAQihDKIMRFpdGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEAT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490075866 185 GALDTRSARQVLLLLQEAARvhGRTVVMVTHDPVAASYADSVVFLADGRLAGR 237
Cdd:cd03253 166 SALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVNADKIIVLKDGRIVER 216
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
31-258 |
1.82e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 106.37 E-value: 1.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 31 ADNAVTaLDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELtkfrRGRVGFVFQ--- 107
Cdd:PRK13648 19 SDASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL----RKHIGIVFQnpd 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 108 --------QYNLLETLtvaQNTVLPLKLAGRRVdrkraREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIF 179
Cdd:PRK13648 94 nqfvgsivKYDVAFGL---ENHAVPYDEMHRRV-----SEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVII 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 180 ADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDPVAASYADSVVFLADGRLagrMDAPTPDAV---AERLAHLGDD 256
Cdd:PRK13648 166 LDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTV---YKEGTPTEIfdhAEELTRIGLD 242
|
..
gi 490075866 257 VP 258
Cdd:PRK13648 243 LP 244
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
37-233 |
2.57e-27 |
|
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: 104.47 E-value: 2.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 37 ALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVdgkeltgggeaeltkfrRGRVGFVFQQYNLLETlT 116
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV-----------------PGSIAYVSQEPWIQNG-T 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 117 VAQNTvlplkLAGRRVDRKRAREVLTSVGL---------GDR--LGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTG 185
Cdd:cd03250 82 IRENI-----LFGKPFDEERYEKVIKACALepdleilpdGDLteIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490075866 186 ALDTRSARQVL--LLLQEAArvHGRTVVMVTHDPVAASYADSVVFLADGR 233
Cdd:cd03250 157 AVDAHVGRHIFenCILGLLL--NNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
37-217 |
3.32e-27 |
|
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: 109.37 E-value: 3.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 37 ALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELtkfrRGRVGFVFQQYNLLETlT 116
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV----RRRVSVCAQDAHLFDT-T 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 117 VAQNtvlpLKLAGRRVDRKRAREVLTSVGLGDRLGHRPD-----------QLSGGQRQRVAIARALVTEPRVIFADEPTG 185
Cdd:TIGR02868 425 VREN----LRLARPDATDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTE 500
|
170 180 190
....*....|....*....|....*....|..
gi 490075866 186 ALDTRSARQVLLLLQEAARvhGRTVVMVTHDP 217
Cdd:TIGR02868 501 HLDAETADELLEDLLAALS--GRTVVLITHHL 530
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
19-188 |
3.45e-27 |
|
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: 104.93 E-value: 3.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSAdnavTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGggeaeLTKFR 98
Cdd:cd03218 1 LRAENLSKRYGKR----KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITK-----LPMHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RGRVGFVF--QQYNLLETLTVAQNTVLPLKLAG--RRVDRKRAREVLTSVGLgDRLGHRP-DQLSGGQRQRVAIARALVT 173
Cdd:cd03218 72 RARLGIGYlpQEASIFRKLTVEENILAVLEIRGlsKKEREEKLEELLEEFHI-THLRKSKaSSLSGGERRRVEIARALAT 150
|
170
....*....|....*
gi 490075866 174 EPRVIFADEPTGALD 188
Cdd:cd03218 151 NPKFLLLDEPFAGVD 165
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
19-251 |
3.74e-27 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 104.53 E-value: 3.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSAdnavTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGggeaeLTKFR 98
Cdd:TIGR03410 1 LEVSNLNVYYGQS----HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITK-----LPPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RGR--VGFVFQQYNLLETLTVAQNTVLPLKLAGRRvDRKRAREVLT--SVgLGDRLGHRPDQLSGGQRQRVAIARALVTE 174
Cdd:TIGR03410 72 RARagIAYVPQGREIFPRLTVEENLLTGLAALPRR-SRKIPDEIYElfPV-LKEMLGRRGGDLSGGQQQQLAIARALVTR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 175 PRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMV-THDPVAASYADSVVFLADGR--LAGRMDAPTPDAVAERLA 251
Cdd:TIGR03410 150 PKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVeQYLDFARELADRYYVMERGRvvASGAGDELDEDKVRRYLA 229
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
11-235 |
4.76e-27 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 109.66 E-value: 4.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 11 DPGPASEALRLVKVTRTYGSADNAVtaLDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGG 90
Cdd:TIGR03797 444 DPGKLSGAIEVDRVTFRYRPDGPLI--LDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLD 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 91 EAELtkfrRGRVGFVFQQYNLLeTLTVAQNTVlplklAGRRVDRKRAREVLTSVGLGDRLGHRP-----------DQLSG 159
Cdd:TIGR03797 522 VQAV----RRQLGVVLQNGRLM-SGSIFENIA-----GGAPLTLDEAWEAARMAGLAEDIRAMPmgmhtviseggGTLSG 591
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490075866 160 GQRQRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLqEAARVhgrTVVMVTHDPVAASYADSVVFLADGRLA 235
Cdd:TIGR03797 592 GQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESL-ERLKV---TRIVIAHRLSTIRNADRIYVLDAGRVV 663
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
30-234 |
5.55e-27 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 104.78 E-value: 5.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 30 SADNAVTALDGVTLSLGRGTFTAVMGPSGSGKStlLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFRRGRVGFVFQQ- 108
Cdd:PRK10418 11 ALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRVLLDGKPVAPCALRGRKIATIMQNp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 109 ---YNLLETLtvAQNTVLPLKLAGRRVDRKRAREVLTSVGLGDR---LGHRPDQLSGGQRQRVAIARALVTEPRVIFADE 182
Cdd:PRK10418 89 rsaFNPLHTM--HTHARETCLALGKPADDATLTAALEAVGLENAarvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490075866 183 PTGALDTRSARQVLLLLQEAARVHGRTVVMVTHD-PVAASYADSVVFLADGRL 234
Cdd:PRK10418 167 PTTDLDVVAQARILDLLESIVQKRALGMLLVTHDmGVVARLADDVAVMSHGRI 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
35-257 |
8.44e-27 |
|
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: 108.35 E-value: 8.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 35 VTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLD--RPDSGIV------C-----VDGKELTG------GGEAELT 95
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalCekcgyVERPSKVGepcpvcGGTLEPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 96 K-------------FRRgRVGFVFQQ-YNLLETLTVAQNTVLPLKLAGRRVDR--KRAREVLTSVGLGDRLGHRPDQLSG 159
Cdd:TIGR03269 93 EvdfwnlsdklrrrIRK-RIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEavGRAVDLIEMVQLSHRITHIARDLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 160 GQRQRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDP-VAASYADSVVFLADGRLagrM 238
Cdd:TIGR03269 172 GEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPeVIEDLSDKAIWLENGEI---K 248
|
250
....*....|....*....
gi 490075866 239 DAPTPDAVAERLAHLGDDV 257
Cdd:TIGR03269 249 EEGTPDEVVAVFMEGVSEV 267
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
15-233 |
1.06e-26 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 105.58 E-value: 1.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 15 ASEALRLVKVTR-TYGSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPD---SGIVCVDGKELTGGG 90
Cdd:PRK09473 8 QADALLDVKDLRvTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 91 EAELTKFRRGRVGFVFQQ--YNLLETLTVAQNTVLPLKLAgRRVDRKRAREvlTSVGLGD---------RLGHRPDQLSG 159
Cdd:PRK09473 88 EKELNKLRAEQISMIFQDpmTSLNPYMRVGEQLMEVLMLH-KGMSKAEAFE--ESVRMLDavkmpearkRMKMYPHEFSG 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490075866 160 GQRQRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHD-PVAASYADSVVFLADGR 233
Cdd:PRK09473 165 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDlGVVAGICDKVLVMYAGR 239
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
36-234 |
1.74e-26 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 103.73 E-value: 1.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 36 TALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFRRgRVGFVFQ-------- 107
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFRR-DVQLVFQdspsavnp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 108 QYNLLETLTVAQNTVLPLKLAGRrvdRKRAREVLTSVGL-GDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGA 186
Cdd:TIGR02769 104 RMTVRQIIGEPLRHLTSLDESEQ---KARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSN 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490075866 187 LDTRSARQVLLLLQEAARVHGRTVVMVTHD-PVAASYADSVVFLADGRL 234
Cdd:TIGR02769 181 LDMVLQAVILELLRKLQQAFGTAYLFITHDlRLVQSFCQRVAVMDKGQI 229
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
19-234 |
1.01e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 101.99 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYgsaDNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGkeLTGGGEAELTKFR 98
Cdd:PRK13644 2 IRLENVSYSY---PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKLQGIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RgRVGFVFQ----QY---NLLETLTVA-QNTVLPLKLAGRRVDRkrareVLTSVGLGDRLGHRPDQLSGGQRQRVAIARA 170
Cdd:PRK13644 77 K-LVGIVFQnpetQFvgrTVEEDLAFGpENLCLPPIEIRKRVDR-----ALAEIGLEKYRHRSPKTLSGGQGQCVALAGI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490075866 171 LVTEPRVIFADEPTGALDTRSARQVlllLQEAARVH--GRTVVMVTHDPVAASYADSVVFLADGRL 234
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAV---LERIKKLHekGKTIVYITHNLEELHDADRIIVMDRGKI 213
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
38-235 |
1.05e-25 |
|
type I secretion system ABC transporter, HlyB 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: 273831 [Multi-domain] Cd Length: 694 Bit Score: 105.59 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELtggGEAELTKFRRgRVGFVFQQyNLLETLTV 117
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDL---AIADPAWLRR-QMGVVLQE-NVLFSRSI 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 118 AQNTVL------------PLKLAGRRVDRKRAREvltsvGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTG 185
Cdd:TIGR01846 548 RDNIALcnpgapfehvihAAKLAGAHDFISELPQ-----GYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATS 622
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490075866 186 ALDTRSARQVLLLLQEAARvhGRTVVMVTHDPVAASYADSVVFLADGRLA 235
Cdd:TIGR01846 623 ALDYESEALIMRNMREICR--GRTVIIIAHRLSTVRACDRIIVLEKGQIA 670
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
35-234 |
1.13e-25 |
|
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: 100.87 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 35 VTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGkeLTGGGEAEltKFRRgRVGFVFQQYN-LLE 113
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG--LVPWKRRK--KFLR-RIGVVFGQKTqLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 114 TLTVAQNtvLPLKLAGRRVD----RKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDT 189
Cdd:cd03267 109 DLPVIDS--FYLLAAIYDLPparfKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490075866 190 RSARQVLLLLQEAARVHGRTVVMVTHD--PVAAsYADSVVFLADGRL 234
Cdd:cd03267 187 VAQENIRNFLKEYNRERGTTVLLTSHYmkDIEA-LARRVLVIDKGRL 232
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
38-234 |
3.66e-25 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 104.03 E-value: 3.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTllqCAAGLDR---PDSGIVCVDGKELTgggEAElTKFRRGRVGFVfQQYNLLET 114
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKST---VAALLQNlyqPTGGQVLLDGVPLV---QYD-HHYLHRQVALV-GQEPVLFS 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 115 LTVAQNTVLPLKLAGRRVDRKRAREVLT-------SVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGAL 187
Cdd:TIGR00958 569 GSVRENIAYGLTDTPDEEIMAAAKAANAhdfimefPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490075866 188 DTRSARqvllLLQEAARVHGRTVVMVTHDPVAASYADSVVFLADGRL 234
Cdd:TIGR00958 649 DAECEQ----LLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSV 691
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
17-183 |
3.79e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 99.72 E-value: 3.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 17 EALRLVKvtrTYGSAdnavTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGggeaeLTK 96
Cdd:COG1137 5 EAENLVK---SYGKR----TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITH-----LPM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 97 FRRGR--VGFVFQQYNLLETLTVAQNTVLPLKLAG--RRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALV 172
Cdd:COG1137 73 HKRARlgIGYLPQEASIFRKLTVEDNILAVLELRKlsKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALA 152
|
170
....*....|.
gi 490075866 173 TEPRVIFADEP 183
Cdd:COG1137 153 TNPKFILLDEP 163
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
38-234 |
4.65e-25 |
|
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: 99.08 E-value: 4.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTgggeAELTKFRRGRVGFVFQQYNLLETlTV 117
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS----QYEHKYLHSKVSLVGQEPVLFAR-SL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 118 AQN-----TVLPLKLAGRRVDRKRAREVLTSVGLG--DRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTR 190
Cdd:cd03248 105 QDNiayglQSCSFECVKEAAQKAHAHSFISELASGydTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490075866 191 SARQVLLLLQEAARvhGRTVVMVTHDPVAASYADSVVFLADGRL 234
Cdd:cd03248 185 SEQQVQQALYDWPE--RRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
27-235 |
6.10e-25 |
|
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: 103.20 E-value: 6.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 27 TYGSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFrrgrVGFVF 106
Cdd:TIGR01842 323 TIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKH----IGYLP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 107 QQYNLLETlTVAQN------------TVLPLKLAGrrvdrkrAREVLTSV--GLGDRLGHRPDQLSGGQRQRVAIARALV 172
Cdd:TIGR01842 399 QDVELFPG-TVAENiarfgenadpekIIEAAKLAG-------VHELILRLpdGYDTVIGPGGATLSGGQRQRIALARALY 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490075866 173 TEPRVIFADEPTGALDTrSARQVLLLLQEAARVHGRTVVMVTHDPVAASYADSVVFLADGRLA 235
Cdd:TIGR01842 471 GDPKLVVLDEPNSNLDE-EGEQALANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRIA 532
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
38-232 |
7.63e-25 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 97.70 E-value: 7.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGldRPDSGIVcvdGKELTGGGEAELTKFRRgRVGFVFQQYNLLETLTV 117
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVI---TGEILINGRPLDKNFQR-STGYVEQQDVHSPNLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 118 aqntvlplklagrrvdrkraREVLT-SVGLGDrlghrpdqLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQVL 196
Cdd:cd03232 97 --------------------REALRfSALLRG--------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIV 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 490075866 197 LLLQEAARvHGRTVVMVTHDPVAA--SYADSVVFLADG 232
Cdd:cd03232 149 RFLKKLAD-SGQAILCTIHQPSASifEKFDRLLLLKRG 185
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
19-234 |
8.87e-25 |
|
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: 99.13 E-value: 8.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSAdnavTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGK-----ELTGGGEAE 93
Cdd:TIGR02323 4 LQVSGLSKSYGGG----KGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRsgaelELYQLSEAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 94 LTKFRRGRVGFVFQQY--NLLETLTVAQNTVLPLKLAGRR---VDRKRAREVLTSVGLG-DRLGHRPDQLSGGQRQRVAI 167
Cdd:TIGR02323 80 RRRLMRTEWGFVHQNPrdGLRMRVSAGANIGERLMAIGARhygNIRATAQDWLEEVEIDpTRIDDLPRAFSGGMQQRLQI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490075866 168 ARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHD-PVAASYADSVVFLADGRL 234
Cdd:TIGR02323 160 ARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDlGVARLLAQRLLVMQQGRV 227
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
19-234 |
8.99e-25 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 99.29 E-value: 8.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSAdnavTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKfr 98
Cdd:PRK10253 8 LRGEQLTLGYGKY----TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVAR-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 rgRVGFVFQQYNLLETLTVaQNTVL-------PLKLAGRRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARAL 171
Cdd:PRK10253 82 --RIGLLAQNATTPGDITV-QELVArgryphqPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490075866 172 VTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHD-PVAASYADSVVFLADGRL 234
Cdd:PRK10253 159 AQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDlNQACRYASHLIALREGKI 222
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
37-216 |
1.76e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 98.14 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 37 ALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGggeaeLTKFRRGRVGFV--------FQQ 108
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEG-----LPGHQIARMGVVrtfqhvrlFRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 109 YNLLETLTVAQNTVLP-------LKLAG-RRVDRK---RAREVLTSVGLGDrLGHRP-DQLSGGQRQRVAIARALVTEPR 176
Cdd:PRK11300 95 MTVIENLLVAQHQQLKtglfsglLKTPAfRRAESEaldRAATWLERVGLLE-HANRQaGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490075866 177 VIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHD 216
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHD 213
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-257 |
2.29e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 98.24 E-value: 2.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 5 GARGNHDPGPASEALRLVKVTRTYGSAdnavTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVcVDGK 84
Cdd:PRK14271 8 GQSGAADVDAAAPAMAAVNLTLGFAGK----TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYR-YSGD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 85 ELTGGGEA----ELTKFRRgRVGFVFQQYNLLeTLTVAQNTVLPL---KLAGRRVDRKRAREVLTSVGL----GDRLGHR 153
Cdd:PRK14271 83 VLLGGRSIfnyrDVLEFRR-RVGMLFQRPNPF-PMSIMDNVLAGVrahKLVPRKEFRGVAQARLTEVGLwdavKDRLSDS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 154 PDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAArvHGRTVVMVTHD-PVAASYADSVVFLADG 232
Cdd:PRK14271 161 PFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA--DRLTVIIVTHNlAQAARISDRAALFFDG 238
|
250 260 270
....*....|....*....|....*....|.
gi 490075866 233 RLAGR------MDAPTPDAVAERLAHLGDDV 257
Cdd:PRK14271 239 RLVEEgpteqlFSSPKHAETARYVAGLSGDV 269
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
35-235 |
3.09e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 100.76 E-value: 3.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 35 VTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELtgggeaeltKFRRGR------VGFVFQQ 108
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM---------RFASTTaalaagVAIIYQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 109 YNLLETLTVAQNTVL---PLKLA--GRRVDRKRAREVLTsvGLGDRLGhrPDQ----LSGGQRQRVAIARALVTEPRVIF 179
Cdd:PRK11288 88 LHLVPEMTVAENLYLgqlPHKGGivNRRLLNYEAREQLE--HLGVDID--PDTplkyLSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490075866 180 ADEPTGALDTRSARQvLLLLQEAARVHGRTVVMVTH--DPVAAsYADSVVFLADGRLA 235
Cdd:PRK11288 164 FDEPTSSLSAREIEQ-LFRVIRELRAEGRVILYVSHrmEEIFA-LCDAITVFKDGRYV 219
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
43-234 |
3.25e-24 |
|
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: 96.84 E-value: 3.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 43 LSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGgeaeltkfrRGRVGFVFQQYNLLETLTVAQNTV 122
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKG---------WRHIGYVPQRHEFAWDFPISVAHT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 123 LPLKLAG--------RRVDRKRAREVLTSVGLGDrLGHRP-DQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSAR 193
Cdd:TIGR03771 72 VMSGRTGhigwlrrpCVADFAAVRDALRRVGLTE-LADRPvGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQE 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490075866 194 QVLLLLQEAARvHGRTVVMVTHDPVAASYADSVVFLADGRL 234
Cdd:TIGR03771 151 LLTELFIELAG-AGTAILMTTHDLAQAMATCDRVVLLNGRV 190
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
39-241 |
5.13e-24 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 97.14 E-value: 5.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 39 DGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFRRgRVGFVFQQYNLLETLTVA 118
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRK-RMSMLFQSGALFTDMNVF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 119 QNTVLPLKLAGRRVD---RKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQV 195
Cdd:PRK11831 103 DNVAYPLREHTQLPApllHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490075866 196 LLLLQEAARVHGRTVVMVTHD-PVAASYADSVVFLADGRLAGRMDAP 241
Cdd:PRK11831 183 VKLISELNSALGVTCVVVSHDvPEVLSIADHAYIVADKKIVAHGSAQ 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
36-233 |
1.17e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 99.39 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 36 TALDGVTLSLGRGTFTAVMGPSGSGKS-TLLQCAAGLDRPD----SGIVCVDGKELTGGGEAELTKFRRGRVGFVFQQ-- 108
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRGVRGNKIAMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 109 --YNLLETLTVAQNTVLPLKlagRRVDRKRAR-EVLT---SVGL---GDRLGHRPDQLSGGQRQRVAIARALVTEPRVIF 179
Cdd:PRK15134 103 vsLNPLHTLEKQLYEVLSLH---RGMRREAARgEILNcldRVGIrqaAKRLTDYPHQLSGGERQRVMIAMALLTRPELLI 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490075866 180 ADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHD-PVAASYADSVVFLADGR 233
Cdd:PRK15134 180 ADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNlSIVRKLADRVAVMQNGR 234
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
37-228 |
1.38e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 96.00 E-value: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 37 ALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLD------RPDsGIVCVDGKELTGGgEAELTKFRRgRVGFVFQQYN 110
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNdlipgfRVE-GKVTFHGKNLYAP-DVDPVEVRR-RIGMVFQKPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 111 LLETlTVAQNTVLPLKLAGRRVD-----RKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTG 185
Cdd:PRK14243 102 PFPK-SIYDNIAYGARINGYKGDmdelvERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCS 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490075866 186 ALDTRSARQVLLLLQEAARVHgrTVVMVTHD-PVAASYADSVVF 228
Cdd:PRK14243 181 ALDPISTLRIEELMHELKEQY--TIIIVTHNmQQAARVSDMTAF 222
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
35-246 |
1.52e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 97.99 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 35 VTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKfrrgRVGFVFQQYNLLET 114
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASR----RVASVPQDTSLSFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 115 LTVAQ-----NTVLPLKLAGRRVDRKRAREVLTSVGLGDRLGHRP-DQLSGGQRQRVAIARALVTEPRVIFADEPTGALD 188
Cdd:PRK09536 92 FDVRQvvemgRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPvTSLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490075866 189 TRSARQVLLLLQEAARvHGRTVVMVTHD-PVAASYADSVVFLADGRLagrMDAPTPDAV 246
Cdd:PRK09536 172 INHQVRTLELVRRLVD-DGKTAVAAIHDlDLAARYCDELVLLADGRV---RAAGPPADV 226
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
20-217 |
2.83e-23 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 94.25 E-value: 2.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 20 RLVKVTRTYGSADNAV--TALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAG--LDRPDSGIVCVDGKELTgggeaelt 95
Cdd:COG2401 26 RVAIVLEAFGVELRVVerYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQFG-------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 96 kfrrgrvgfvfQQYNLLETLtvaqntvlplklaGRRVDRKRAREVLTSVGLGDR--LGHRPDQLSGGQRQRVAIARALVT 173
Cdd:COG2401 98 -----------REASLIDAI-------------GRKGDFKDAVELLNAVGLSDAvlWLRRFKELSTGQKFRFRLALLLAE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490075866 174 EPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDP 217
Cdd:COG2401 154 RPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHY 197
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
36-233 |
4.11e-23 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 98.03 E-value: 4.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 36 TALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGldRPDSGivCVDGKELTGGGEaeLTKFRRGRVGFVFQQYNLLETL 115
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAG--RIQGN--NFTGTILANNRK--PTKQILKRTGFVTQDDILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 116 TVAQNTV------LPLKLAgRRVDRKRAREVLTSVGL----GDRLGHRPDQ-LSGGQRQRVAIARALVTEPRVIFADEPT 184
Cdd:PLN03211 156 TVRETLVfcsllrLPKSLT-KQEKILVAESVISELGLtkceNTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490075866 185 GALDTRSARQVLLLLQEAARvHGRTVVMVTHDPVAASYA--DSVVFLADGR 233
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSLAQ-KGKTIVTSMHQPSSRVYQmfDSVLVLSEGR 284
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
37-234 |
4.35e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 95.07 E-value: 4.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 37 ALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEA--ELTKFRRgRVGFVFQ--QYNLL 112
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKikEVKRLRK-EIGLVFQfpEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 113 ETlTVAQNTVL-PLKLAGRRVD-RKRAREVLTSVGLGDRLGHR-PDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDT 189
Cdd:PRK13645 105 QE-TIEKDIAFgPVNLGENKQEaYKKVPELLKLVQLPEDYVKRsPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDP 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490075866 190 RSARQVLLLLQEAARVHGRTVVMVTH--DPVaASYADSVVFLADGRL 234
Cdd:PRK13645 184 KGEEDFINLFERLNKEYKKRIIMVTHnmDQV-LRIADEVIVMHEGKV 229
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
36-234 |
5.65e-23 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 94.47 E-value: 5.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 36 TALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELtggGEAELTKFRRgRVGFVFQQYNLLETL 115
Cdd:PRK10575 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPL---ESWSSKAFAR-KVAYLPQQLPAAEGM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 116 TVAQNTVL---PLKLA-GR--RVDRKRAREVLTSVGLgDRLGHR-PDQLSGGQRQRVAIARALVTEPRVIFADEPTGALD 188
Cdd:PRK10575 101 TVRELVAIgryPWHGAlGRfgAADREKVEEAISLVGL-KPLAHRlVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490075866 189 TRSARQVLLLLQEAARVHGRTVVMVTHD-PVAASYADSVVFLADGRL 234
Cdd:PRK10575 180 IAHQVDVLALVHRLSQERGLTVIAVLHDiNMAARYCDYLVALRGGEM 226
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
35-235 |
6.18e-23 |
|
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: 93.37 E-value: 6.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 35 VTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGK-----ELTGGGEAELTkfrrGRvgfvfqqy 109
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvssllGLGGGFNPELT----GR-------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 110 nlletltvaQNTVLPLKLAGRRVDRKRAR--EVLTSVGLGDRLgHRP-DQLSGGQRQRVAIARALVTEPRVIFADEPTGA 186
Cdd:cd03220 103 ---------ENIYLNGRLLGLSRKEIDEKidEIIEFSELGDFI-DLPvKTYSSGMKARLAFAIATALEPDILLIDEVLAV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490075866 187 LDTRSARQVLLLLQEAARvHGRTVVMVTHDPVA-ASYADSVVFLADGRLA 235
Cdd:cd03220 173 GDAAFQEKCQRRLRELLK-QGKTVILVSHDPSSiKRLCDRALVLEKGKIR 221
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
35-248 |
7.74e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 93.61 E-value: 7.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 35 VTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGK-----ELTGGGEAELTkfrrGRvgfvfqqy 109
Cdd:COG1134 39 FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsallELGAGFHPELT----GR-------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 110 nlletltvaQNTVLPLKLAGrrVDRKRAREVLTSV----GLGDRLghrpDQ----LSGGQRQRVAIARALVTEPRVIFAD 181
Cdd:COG1134 107 ---------ENIYLNGRLLG--LSRKEIDEKFDEIvefaELGDFI----DQpvktYSSGMRARLAFAVATAVDPDILLVD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490075866 182 EPTGALDTRSARQVLLLLQEAARvHGRTVVMVTHDP-VAASYADSVVFLADGRLagRMDAPTPDAVAE 248
Cdd:COG1134 172 EVLAVGDAAFQKKCLARIRELRE-SGRTVIFVSHSMgAVRRLCDRAIWLEKGRL--VMDGDPEEVIAA 236
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
22-232 |
1.08e-22 |
|
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: 92.78 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 22 VKVTRTYGSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFRRGR 101
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 102 VGFVFQQYNLLETlTVAQNTVLplklaGRRVDRKRAREVLTSVGL---------GDR--LGHRPDQLSGGQRQRVAIARA 170
Cdd:cd03290 81 VAYAAQKPWLLNA-TVEENITF-----GSPFNKQRYKAVTDACSLqpdidllpfGDQteIGERGINLSGGQRQRICVARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490075866 171 LVTEPRVIFADEPTGALDTRSARQ-----VLLLLQEAArvhgRTVVMVTHDPVAASYADSVVFLADG 232
Cdd:cd03290 155 LYQNTNIVFLDDPFSALDIHLSDHlmqegILKFLQDDK----RTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
35-237 |
1.39e-22 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 93.32 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 35 VTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAeltkFRRGRVGFVFQ--QYNLL 112
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS----YRSQRIRMIFQdpSTSLN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 113 ETLTVAQNTVLPLKL-----AGRRvdRKRAREVLTSVGL-GDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGA 186
Cdd:PRK15112 102 PRQRISQILDFPLRLntdlePEQR--EKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALAS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490075866 187 LDTRSARQVLLLLQEAARVHGRTVVMVT-HDPVAASYADSVVFLADGRLAGR 237
Cdd:PRK15112 180 LDMSMRSQLINLMLELQEKQGISYIYVTqHLGMMKHISDQVLVMHQGEVVER 231
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
41-233 |
1.74e-22 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 94.56 E-value: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 41 VTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTgggEAE----LTKFRRgRVGFVFQQYNLLETLT 116
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLF---DAEkgicLPPEKR-RIGYVFQDARLFPHYK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 117 VAQNtvlpLKLAGRRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQVL 196
Cdd:PRK11144 93 VRGN----LRYGMAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELL 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 490075866 197 LLLQEAARVHGRTVVMVTH--DPVaASYADSVVFLADGR 233
Cdd:PRK11144 169 PYLERLAREINIPILYVSHslDEI-LRLADRVVVLEQGK 206
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
36-216 |
4.57e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 94.77 E-value: 4.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 36 TALDGVTLSLGRGTFTAVMGPSGSGKSTllqCAAGLDR--PDSGIVCVDGKELTGGGEAELTKFRRgRVGFVFQQYN--L 111
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKST---TGLALLRliNSQGEIWFDGQPLHNLNRRQLLPVRH-RIQVVFQDPNssL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 112 LETLTVAQntvlpLKLAGRRVDRK---------RAREVLTSVGLGDRLGHR-PDQLSGGQRQRVAIARALVTEPRVIFAD 181
Cdd:PRK15134 376 NPRLNVLQ-----IIEEGLRVHQPtlsaaqreqQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190
....*....|....*....|....*....|....*
gi 490075866 182 EPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHD 216
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHD 485
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
38-234 |
5.82e-22 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 91.44 E-value: 5.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLdRPDSGIVCVDGKELTGGGEAELTKFRrgrvGFVFQQYNLLETLTV 117
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHR----AYLSQQQSPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 118 AQNTVLPLKLAGRRVDRKRAREVLTS-VGLGDRLGHRPDQLSGGQRQRVAIARALVT-------EPRVIFADEPTGALDT 189
Cdd:COG4138 87 FQYLALHQPAGASSEAVEQLLAQLAEaLGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDV 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490075866 190 rsARQVLL--LLQEAARvHGRTVVMVTHD-PVAASYADSVVFLADGRL 234
Cdd:COG4138 167 --AQQAALdrLLRELCQ-QGITVVMSSHDlNHTLRHADRVWLLKQGKL 211
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
24-216 |
6.11e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 94.36 E-value: 6.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 24 VTRTYGsadnAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGivcvdgkeltgggeaELTKFRRGRVG 103
Cdd:COG0488 4 LSKSFG----GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSG---------------EVSIPKGLRIG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 104 FVFQQYNLLETLTVAQnTVL----PLKLAGRRVDRK-------------------------------RAREVLTSVGLGD 148
Cdd:COG0488 65 YLPQEPPLDDDLTVLD-TVLdgdaELRALEAELEELeaklaepdedlerlaelqeefealggweaeaRAEEILSGLGFPE 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490075866 149 RLGHRP-DQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSarqVLLLLQEAARVHGrTVVMVTHD 216
Cdd:COG0488 144 EDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEWLEEFLKNYPG-TVLVVSHD 208
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
37-240 |
6.41e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 94.31 E-value: 6.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 37 ALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGG--GEAeltkfRRGRVGFV---FQQYNL 111
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRspRDA-----IRAGIAYVpedRKGEGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 112 LETLTVAQNTVLPL--KLA-GRRVDRKRAREVLTSvgLGDRLG---HRPDQ----LSGGQRQRVAIARALVTEPRVIFAD 181
Cdd:COG1129 342 VLDLSIRENITLASldRLSrGGLLDRRRERALAEE--YIKRLRiktPSPEQpvgnLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 182 EPTGALDTRSARQVLLLLQEAARvHGRTVVMVTHD-PVAASYADSVVFLADGRLAGRMDA 240
Cdd:COG1129 420 EPTRGIDVGAKAEIYRLIRELAA-EGKAVIVISSElPELLGLSDRILVMREGRIVGELDR 478
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
35-234 |
6.70e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 94.53 E-value: 6.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 35 VTALDGVTL------SLGRGTFTAVMGPSGSGKSTLLQCAAGLdRPDSGIVCVDGKELTgggEAELTKFRRgRVGFVFQQ 108
Cdd:PRK11174 357 ILSPDGKTLagplnfTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELR---ELDPESWRK-HLSWVGQN 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 109 YNLLETlTVAQNtvlpLKLAGRRVDRKRAREVLTSVGLGDRLGHRP--------DQ---LSGGQRQRVAIARALVTEPRV 177
Cdd:PRK11174 432 PQLPHG-TLRDN----VLLGNPDASDEQLQQALENAWVSEFLPLLPqgldtpigDQaagLSVGQAQRLALARALLQPCQL 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490075866 178 IFADEPTGALDTRSARQVLLLLQEAARvhGRTVVMVTH--DPVAAsyADSVVFLADGRL 234
Cdd:PRK11174 507 LLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHqlEDLAQ--WDQIWVMQDGQI 561
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
37-234 |
7.16e-22 |
|
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: 89.41 E-value: 7.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 37 ALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAEltkFRRGRVGFV---FQQYNLLE 113
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRD---AIRAGIAYVpedRKREGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 114 TLTVAQNTVLPlklagrrvdrkrarevltsvglgdrlghrpDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSAR 193
Cdd:cd03215 92 DLSVAENIALS------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490075866 194 QVLLLLQEAARvHGRTVVMVTHD-PVAASYADSVVFLADGRL 234
Cdd:cd03215 142 EIYRLIRELAD-AGKAVLLISSElDELLGLCDRILVMYEGRI 182
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
21-234 |
8.36e-22 |
|
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: 94.70 E-value: 8.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 21 LVKVTRTYGSAdnavtALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELtgggEAELTKFRRG 100
Cdd:TIGR01257 934 LVKIFEPSGRP-----AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVRQS 1004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 101 rVGFVFQQYNLLETLTVAQNTVLPLKLAGRRVDRKR--AREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVI 178
Cdd:TIGR01257 1005 -LGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQleMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVV 1083
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490075866 179 FADEPTGALDTRSARQVL-LLLQEAArvhGRTVVMVTHDPVAAS-YADSVVFLADGRL 234
Cdd:TIGR01257 1084 VLDEPTSGVDPYSRRSIWdLLLKYRS---GRTIIMSTHHMDEADlLGDRIAIISQGRL 1138
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
19-216 |
2.32e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 90.96 E-value: 2.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGL-DRPdsGIVCVD-----GKELTGGGEA 92
Cdd:PRK11022 4 LNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLiDYP--GRVMAEklefnGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 93 ELTKFRRGRVGFVFQQ------------YNLLETLTVAQNtvlplklAGRRVDRKRAREVLTSVGLGD---RLGHRPDQL 157
Cdd:PRK11022 82 ERRNLVGAEVAMIFQDpmtslnpcytvgFQIMEAIKVHQG-------GNKKTRRQRAIDLLNQVGIPDpasRLDVYPHQL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490075866 158 SGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHD 216
Cdd:PRK11022 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHD 213
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
8-237 |
3.43e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 92.39 E-value: 3.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 8 GNHDPGPASEALRLVKVTRTYGSADNAvtALDGVTLSLGRGTFTAVMGPSGSGKSTLlqcAAGLDR---PDSGIVCVDGK 84
Cdd:PRK11176 331 GKRVIERAKGDIEFRNVTFTYPGKEVP--ALRNINFKIPAGKTVALVGRSGSGKSTI---ANLLTRfydIDEGEILLDGH 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 85 ELTgggEAELTKFRRgRVGFVFQQYNLLETlTVAQNTVLPLKLAGRRVDRKRAREVLTSVGLGDRLGHRPDQ-------- 156
Cdd:PRK11176 406 DLR---DYTLASLRN-QVALVSQNVHLFND-TIANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTvigengvl 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 157 LSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARvhGRTVVMVTHDPVAASYADSVVFLADGRLAG 236
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEKADEILVVEDGEIVE 558
|
.
gi 490075866 237 R 237
Cdd:PRK11176 559 R 559
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
39-220 |
3.85e-21 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 87.94 E-value: 3.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 39 DGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELtgggeaeltkfRRGRVGFvfqQYNLL------ 112
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI-----------RRQRDEY---HQDLLylghqp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 113 ---ETLTVAQNTVLPLKLAGrRVDRKRAREVLTSVGLGDRLgHRP-DQLSGGQRQRVAIARALVTEPRVIFADEPTGALD 188
Cdd:PRK13538 84 gikTELTALENLRFYQRLHG-PGDDEALWEALAQVGLAGFE-DVPvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170 180 190
....*....|....*....|....*....|..
gi 490075866 189 TRSARQVLLLLQEAARvHGRTVVMVTHDPVAA 220
Cdd:PRK13538 162 KQGVARLEALLAQHAE-QGGMVILTTHQDLPV 192
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
38-229 |
6.62e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 88.94 E-value: 6.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCaagLDRPDS--GIVCVDGK-ELTGGGEAE----LTKFRRgRVGFVFQQYN 110
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKC---LNRMNEleSEVRVEGRvEFFNQNIYErrvnLNRLRR-QVSMVHPKPN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 111 LLeTLTVAQNTVLPLKLAGRRVDRKR---AREVLTSVGLGDRLGHRPDQ----LSGGQRQRVAIARALVTEPRVIFADEP 183
Cdd:PRK14258 99 LF-PMSVYDNVAYGVKIVGWRPKLEIddiVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARALAVKPKVLLMDEP 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490075866 184 TGALDTRSARQVLLLLQEAARVHGRTVVMVTHD-PVAASYADSVVFL 229
Cdd:PRK14258 178 CFGLDPIASMKVESLIQSLRLRSELTMVIVSHNlHQVSRLSDFTAFF 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-215 |
1.01e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.00 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGsadnAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKE---LTGGGEAELT 95
Cdd:PRK09700 6 ISMAGIGKSFG----PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 96 kfrrgrVGFVFQQYNLLETLTVAQNTV---LPLK--LAGRRVD----RKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVA 166
Cdd:PRK09700 82 ------IGIIYQELSVIDELTVLENLYigrHLTKkvCGVNIIDwremRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490075866 167 IARALVTEPRVIFADEPTGALdTRSARQVLLLLQEAARVHGRTVVMVTH 215
Cdd:PRK09700 156 IAKTLMLDAKVIIMDEPTSSL-TNKEVDYLFLIMNQLRKEGTAIVYISH 203
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
38-232 |
1.05e-20 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 91.32 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGldRPDSGIVcVDGKELTGGGEAELTkFRRgRVGFVFQQYNLLETLTV 117
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVI-TGGDRLVNGRPLDSS-FQR-SIGYVQQQDLHLPTSTV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 118 A----------QNTVLPLKLAGRRVD--------RKRAREVLTSVGLGdrlghrpdqLSGGQRQRVAIARALVTEPR-VI 178
Cdd:TIGR00956 854 ReslrfsaylrQPKSVSKSEKMEYVEevikllemESYADAVVGVPGEG---------LNVEQRKRLTIGVELVAKPKlLL 924
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490075866 179 FADEPTGALDTRSARQVLLLLQEAARvHGRTVVMVTHDPVAASYA--DSVVFLADG 232
Cdd:TIGR00956 925 FLDEPTSGLDSQTAWSICKLMRKLAD-HGQAILCTIHQPSAILFEefDRLLLLQKG 979
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
38-234 |
1.84e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 87.76 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTkfRRGRVGFVFQQYNL------ 111
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLA--LRQQVATVFQDPEQqifytd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 112 --------LETLTVAQNTVlplklaGRRVDrkrarEVLTSVGlGDRLGHRPDQ-LSGGQRQRVAIARALVTEPRVIFADE 182
Cdd:PRK13638 95 idsdiafsLRNLGVPEAEI------TRRVD-----EALTLVD-AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490075866 183 PTGALDTRSARQVLLLLQEAARvHGRTVVMVTHD-PVAASYADSVVFLADGRL 234
Cdd:PRK13638 163 PTAGLDPAGRTQMIAIIRRIVA-QGNHVIISSHDiDLIYEISDAVYVLRQGQI 214
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
30-239 |
2.18e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 90.02 E-value: 2.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 30 SADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLqcaAGLDR---PDSGIVCVDGKELTGGGEAELtkfrRGRVGFVF 106
Cdd:PRK13657 343 SYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLI---NLLQRvfdPQSGRILIDGTDIRTVTRASL----RRNIAVVF 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 107 QQYNLLETlTVAQN--------TVLPLKLAGRR------VDRKrarevltSVGLGDRLGHRPDQLSGGQRQRVAIARALV 172
Cdd:PRK13657 416 QDAGLFNR-SIEDNirvgrpdaTDEEMRAAAERaqahdfIERK-------PDGYDTVVGERGRQLSGGERQRLAIARALL 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490075866 173 TEPRVIFADEPTGALDTRSARQVLLLLQEAarVHGRTVVMVTHDPVAASYADSVVFLADGRL--AGRMD 239
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDEL--MKGRTTFIIAHRLSTVRNADRILVFDNGRVveSGSFD 554
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
53-234 |
2.53e-20 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 86.91 E-value: 2.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 53 VMGPSGSGKSTLLQCAAGLdRPDSGIVCVDGKELTGGGEAELTKFRrgrvGFVFQQYNLLETLTVAQntVLPLKL-AGRR 131
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHR----AYLSQQQTPPFAMPVFQ--YLTLHQpDKTR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 132 VD--RKRAREVLTSVGLGDRLgHRP-DQLSGGQRQRVAIA-------RALVTEPRVIFADEPTGALDTrsARQVLL--LL 199
Cdd:PRK03695 100 TEavASALNEVAEALGLDDKL-GRSvNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLDV--AQQAALdrLL 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 490075866 200 QEAARvHGRTVVMVTHD-PVAASYADSVVFLADGRL 234
Cdd:PRK03695 177 SELCQ-QGIAVVMSSHDlNHTLRHADRVWLLKQGKL 211
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
30-239 |
3.72e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 87.65 E-value: 3.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 30 SADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLdRPDSGIVCVD-----GKELTGGGEAELTKFRRGRVGF 104
Cdd:COG4170 15 TPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVTADrfrwnGIDLLKLSPRERRKIIGREIAM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 105 VFQ--QYNLLETLTVAQ-------NTVLPLKLAGRRVDRK-RAREVLTSVGLGDrlgHR------PDQLSGGQRQRVAIA 168
Cdd:COG4170 94 IFQepSSCLDPSAKIGDqlieaipSWTFKGKWWQRFKWRKkRAIELLHRVGIKD---HKdimnsyPHELTEGECQKVMIA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490075866 169 RALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDPVA-ASYADSVVFLADGRL--AGRMD 239
Cdd:COG4170 171 MAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESiSQWADTITVLYCGQTveSGPTE 244
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
18-215 |
5.08e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 87.58 E-value: 5.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 18 ALRLVKVTRTYGsaDNAVtaLDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAEltkf 97
Cdd:PRK13536 41 AIDLAGVSKSYG--DKAV--VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA---- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 98 rRGRVGFVFQQYNLLETLTVAQNtvlpLKLAGR--RVDRKRAREVLTSVGLGDRLGHRPD----QLSGGQRQRVAIARAL 171
Cdd:PRK13536 113 -RARIGVVPQFDNLDLEFTVREN----LLVFGRyfGMSTREIEAVIPSLLEFARLESKADarvsDLSGGMKRRLTLARAL 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490075866 172 VTEPRVIFADEPTGALDTRsARQVLLLLQEAARVHGRTVVMVTH 215
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPH-ARHLIWERLRSLLARGKTILLTTH 230
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
35-216 |
5.43e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 87.06 E-value: 5.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 35 VTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTgggeAELTKFRRgRVGFVFQQYN-LLE 113
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPF----KRRKEFAR-RIGVVFGQRSqLWW 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 114 TLTVAQNtvlpLKLAGR--RVDRKRAREVLTSV----GLGDRLgHRP-DQLSGGQRQRVAIARALVTEPRVIFADEPTGA 186
Cdd:COG4586 110 DLPAIDS----FRLLKAiyRIPDAEYKKRLDELvellDLGELL-DTPvRQLSLGQRMRCELAAALLHRPKILFLDEPTIG 184
|
170 180 190
....*....|....*....|....*....|
gi 490075866 187 LDTRSARQVLLLLQEAARVHGRTVVMVTHD 216
Cdd:COG4586 185 LDVVSKEAIREFLKEYNRERGTTILLTSHD 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
19-234 |
5.98e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.58 E-value: 5.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGsaDNAVtaLDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGivcvdgkeltgggeaeltKFR 98
Cdd:COG0488 316 LELEGLSKSYG--DKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSG------------------TVK 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RG---RVGFVFQQYNLL-ETLTVAQNtvlpLKLAGRRVDRKRAREVLTSVGL-GDRLGHRPDQLSGGQRQRVAIARALVT 173
Cdd:COG0488 374 LGetvKIGYFDQHQEELdPDKTVLDE----LRDGAPGGTEQEVRGYLGRFLFsGDDAFKPVGVLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490075866 174 EPRVIFADEPTGALDTRSaRQVLL-LLQEAArvhGrTVVMVTHDPvaasY-----ADSVVFLADGRL 234
Cdd:COG0488 450 PPNVLLLDEPTNHLDIET-LEALEeALDDFP---G-TVLLVSHDR----YfldrvATRILEFEDGGV 507
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
33-217 |
6.63e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.93 E-value: 6.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 33 NAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGkeltggGEAELTKFRrGRVGFVFQQYNLL 112
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG------GDIDDPDVA-EACHYLGHRNAMK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 113 ETLTVAQNTVLPLKLAGRRvdRKRAREVLTSVGLGDrLGHRPDQ-LSGGQRQRVAIARALVTEPRVIFADEPTGALDTRS 191
Cdd:PRK13539 86 PALTVAENLEFWAAFLGGE--ELDIAAALEAVGLAP-LAHLPFGyLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA 162
|
170 180
....*....|....*....|....*....
gi 490075866 192 ARqvllLLQEAARVH---GRTVVMVTHDP 217
Cdd:PRK13539 163 VA----LFAELIRAHlaqGGIVIAATHIP 187
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
38-215 |
7.47e-20 |
|
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: 88.46 E-value: 7.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELtgggeAELTKFR-RGRVGFVFQQYNLLETlT 116
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPR-----EEIPREVlANSVAMVDQDIFLFEG-T 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 117 VAQNtvlpLKLAGRRVDRKRAREVLTSVGLGDRLGHRPDQ-----------LSGGQRQRVAIARALVTEPRVIFADEPTG 185
Cdd:TIGR03796 569 VRDN----LTLWDPTIPDADLVRACKDAAIHDVITSRPGGydaelaegganLSGGQRQRLEIARALVRNPSILILDEATS 644
|
170 180 190
....*....|....*....|....*....|
gi 490075866 186 ALDTRSARQVLlllqEAARVHGRTVVMVTH 215
Cdd:TIGR03796 645 ALDPETEKIID----DNLRRRGCTCIIVAH 670
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
36-217 |
9.92e-20 |
|
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: 84.08 E-value: 9.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 36 TALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVcvdgkELTGGGEAELTKFRRGRVGFVFQQYNLLETL 115
Cdd:cd03231 14 ALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRV-----LLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 116 TVAQNtvlpLKLAGRRVDRKRAREVLTSVGLGDrLGHRP-DQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRS-AR 193
Cdd:cd03231 89 SVLEN----LRFWHADHSDEQVEEALARVGLNG-FEDRPvAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGvAR 163
|
170 180
....*....|....*....|....
gi 490075866 194 QVLLLLQEAARvhGRTVVMVTHDP 217
Cdd:cd03231 164 FAEAMAGHCAR--GGMVVLTTHQD 185
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-233 |
1.12e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 87.68 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGsadnAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLdRPD---SGIVCVDGKELTGGG--EAE 93
Cdd:PRK13549 6 LEMKNITKTFG----GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQASNirDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 94 ltkfRRGrVGFVFQQYNLLETLTVAQNTVLPLKL-AGRRVD----RKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIA 168
Cdd:PRK13549 81 ----RAG-IAIIHQELALVKELSVLENIFLGNEItPGGIMDydamYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490075866 169 RALVTEPRVIFADEPTGALdTRSARQVLLLLQEAARVHGRTVVMVTH--DPVAAsYADSVVFLADGR 233
Cdd:PRK13549 156 KALNKQARLLILDEPTASL-TESETAVLLDIIRDLKAHGIACIYISHklNEVKA-ISDTICVIRDGR 220
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
33-218 |
1.23e-19 |
|
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: 83.95 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 33 NAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELtgggeAELTKFRRGRVGFVFQQYNLL 112
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL-----AEQRDEPHENILYLGHLPGLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 113 ETLTVAQNtvLPLKLAGRRVDRKRAREVLTSVGLGDrLGHRP-DQLSGGQRQRVAIARALVTEPRVIFADEPTGALDtrs 191
Cdd:TIGR01189 86 PELSALEN--LHFWAAIHGGAQRTIEDALAAVGLTG-FEDLPaAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD--- 159
|
170 180 190
....*....|....*....|....*....|
gi 490075866 192 aRQVLLLLQEAARVH---GRTVVMVTHDPV 218
Cdd:TIGR01189 160 -KAGVALLAGLLRAHlarGGIVLLTTHQDL 188
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-242 |
1.61e-19 |
|
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: 87.19 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSadnaVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLdRPD---SGIVCVDGKELTGGGEAELt 95
Cdd:TIGR02633 2 LEMKGIVKTFGG----VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIYWSGSPLKASNIRDT- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 96 kfRRGRVGFVFQQYNLLETLTVAQNTVL--PLKLAGRRVDR----KRAREVLTSVGLGDRLGHRP-DQLSGGQRQRVAIA 168
Cdd:TIGR02633 76 --ERAGIVIIHQELTLVPELSVAENIFLgnEITLPGGRMAYnamyLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490075866 169 RALVTEPRVIFADEPTGALdTRSARQVLLLLQEAARVHGRTVVMVTH--DPVAAsYADSVVFLADGRLAGRMDAPT 242
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSL-TEKETEILLDIIRDLKAHGVACVYISHklNEVKA-VCDTICVIRDGQHVATKDMST 227
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
35-215 |
1.12e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.06 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 35 VTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGG-----EAEltkfrrgrVGFVFQQY 109
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGpkssqEAG--------IGIIHQEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 110 NLLETLTVAQNTVLPLKLAGR--RVDRKRAREvlTSVGLGDRLG--HRPDQLSG----GQRQRVAIARALVTEPRVIFAD 181
Cdd:PRK10762 89 NLIPQLTIAENIFLGREFVNRfgRIDWKKMYA--EADKLLARLNlrFSSDKLVGelsiGEQQMVEIAKVLSFESKVIIMD 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 490075866 182 EPTGAL---DTRSARQVLLLLQEaarvHGRTVVMVTH 215
Cdd:PRK10762 167 EPTDALtdtETESLFRVIRELKS----QGRGIVYISH 199
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
38-237 |
1.31e-18 |
|
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: 84.87 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELtkfrRGRVGFVFQqynllETL-- 115
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL----RAAIGIVPQ-----DTVlf 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 116 --TVAQNtvlplkLAGRRVDRKRA--REVLTSVGLGD-----------RLGHRPDQLSGGQRQRVAIARALVTEPRVIFA 180
Cdd:COG5265 445 ndTIAYN------IAYGRPDASEEevEAAARAAQIHDfieslpdgydtRVGERGLKLSGGEKQRVAIARTLLKNPPILIF 518
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490075866 181 DEPTGALDTRSARQVLLLLQEAARvhGRTVVMVTHDPVAASYADSVVFLADGRLAGR 237
Cdd:COG5265 519 DEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVDADEILVLEAGRIVER 573
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
13-215 |
1.58e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 82.93 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 13 GPASEA-LRLVKVTRTYGSAdnavTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGe 91
Cdd:PRK13537 1 GPMSVApIDFRNVEKRYGDK----LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 92 aeltKFRRGRVGFVFQQYNLLETLTVAQNtvlpLKLAGRRVD------RKRAREVLTSVGLGDRLGHRPDQLSGGQRQRV 165
Cdd:PRK13537 76 ----RHARQRVGVVPQFDNLDPDFTVREN----LLVFGRYFGlsaaaaRALVPPLLEFAKLENKADAKVGELSGGMKRRL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490075866 166 AIARALVTEPRVIFADEPTGALDTRsARQVLLLLQEAARVHGRTVVMVTH 215
Cdd:PRK13537 148 TLARALVNDPDVLVLDEPTTGLDPQ-ARHLMWERLRSLLARGKTILLTTH 196
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
32-235 |
4.25e-18 |
|
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: 80.23 E-value: 4.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 32 DNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELtkfrRGRVGFVFQQyNL 111
Cdd:cd03244 14 PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL----RSRISIIPQD-PV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 112 LETLTVAQNtVLPLKLAG-----RRVDRKRAREVLTSV--GLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPT 184
Cdd:cd03244 89 LFSGTIRSN-LDPFGEYSdeelwQALERVGLKEFVESLpgGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEAT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490075866 185 GALDTRSARQVLLLLQEAarVHGRTVVMVTH--DPVAASyaDSVVFLADGRLA 235
Cdd:cd03244 168 ASVDPETDALIQKTIREA--FKDCTVLTIAHrlDTIIDS--DRILVLDKGRVV 216
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
38-235 |
5.07e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 80.50 E-value: 5.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLD--RPDSGIVCVDGKELTgggeaELTKFRRGRVG-FV-FQQ----- 108
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDIL-----ELSPDERARAGiFLaFQYpveip 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 109 ----YNLLETltvAQNTVLPLKLAGRRvDRKRAREVLTSVGLGDRLGHRP--DQLSGGQRQRVAIARALVTEPRVIFADE 182
Cdd:COG0396 91 gvsvSNFLRT---ALNARRGEELSARE-FLKLLKEKMKELGLDEDFLDRYvnEGFSGGEKKRNEILQMLLLEPKLAILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490075866 183 PTGALDTRSARQVLLLLqEAARVHGRTVVMVTHDPVAASY--ADSVVFLADGRLA 235
Cdd:COG0396 167 TDSGLDIDALRIVAEGV-NKLRSPDRGILIITHYQRILDYikPDFVHVLVDGRIV 220
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
19-216 |
5.96e-18 |
|
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: 77.87 E-value: 5.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGsaDNAVtaLDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKEltgggeaeltkfr 98
Cdd:cd03221 1 IELENLSKTYG--GKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 rgRVGFVfqqynlletltvaqntvlplklagrrvdrkrarevltsvglgdrlghrpDQLSGGQRQRVAIARALVTEPRVI 178
Cdd:cd03221 64 --KIGYF-------------------------------------------------EQLSGGEKMRLALAKLLLENPNLL 92
|
170 180 190
....*....|....*....|....*....|....*...
gi 490075866 179 FADEPTGALDTRSarqvLLLLQEAARVHGRTVVMVTHD 216
Cdd:cd03221 93 LLDEPTNHLDLES----IEALEEALKEYPGTVILVSHD 126
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
14-253 |
7.68e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.38 E-value: 7.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 14 PASEALRLVKVTRTygsADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAE 93
Cdd:COG3845 253 PGEVVLEVENLSVR---DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 94 ltkFRRGRVGFV---FQQYNLLETLTVAQNTVL-----PLKLAGRRVDRKRARE----------VLTSvGLGDRLGhrpd 155
Cdd:COG3845 330 ---RRRLGVAYIpedRLGRGLVPDMSVAENLILgryrrPPFSRGGFLDRKAIRAfaeelieefdVRTP-GPDTPAR---- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 156 QLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQVL-LLLQEAARvhGRTVVMVTHD-PVAASYADSVVFLADGR 233
Cdd:COG3845 402 SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHqRLLELRDA--GAAVLLISEDlDEILALSDRIAVMYEGR 479
|
250 260
....*....|....*....|
gi 490075866 234 LAGRMDAPTPDavAERLAHL 253
Cdd:COG3845 480 IVGEVPAAEAT--REEIGLL 497
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
35-233 |
8.62e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 82.60 E-value: 8.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 35 VTALDGVTLSLGRGTFTAVMGPSGSGKST-------LLQCAAGLDRPDSGIVCVDGKELTGGGE---AELTKFRRGRVGF 104
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGGLVQCDKMLLRRRSRQVIELSEqsaAQMRHVRGADMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 105 VFQQ--YNLLETLTVAQNTVLPLKL---AGRRVDRKRAREVLTSVGLGDR---LGHRPDQLSGGQRQRVAIARALVTEPR 176
Cdd:PRK10261 109 IFQEpmTSLNPVFTVGEQIAESIRLhqgASREEAMVEAKRMLDQVRIPEAqtiLSRYPHQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490075866 177 VIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHD-PVAASYADSVVFLADGR 233
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDmGVVAEIADRVLVMYQGE 246
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
35-216 |
2.07e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.44 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 35 VTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFRRGrVGFVFQQ-YNLLE 113
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRD-IQFIFQDpYASLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 114 T-LTVAQNTVLPLKLAGR---RVDRKRAREVLTSVGLGDRLGHR-PDQLSGGQRQRVAIARALVTEPRVIFADEPTGALD 188
Cdd:PRK10261 416 PrQTVGDSIMEPLRVHGLlpgKAAAARVAWLLERVGLLPEHAWRyPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180
....*....|....*....|....*...
gi 490075866 189 TRSARQVLLLLQEAARVHGRTVVMVTHD 216
Cdd:PRK10261 496 VSIRGQIINLLLDLQRDFGIAYLFISHD 523
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
24-233 |
3.55e-17 |
|
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: 77.30 E-value: 3.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 24 VTRTYGSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDrpdSGIVCVDGKELTGGGEA-ELTKFRRGRV 102
Cdd:cd03233 9 ISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRT---EGNVSVEGDIHYNGIPYkEFAEKYPGEI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 103 GFVFQQYNLLETLTVAQNTVLPLKLAGRRVDRKrarevltsvglgdrlghrpdqLSGGQRQRVAIARALVTEPRVIFADE 182
Cdd:cd03233 86 IYVSEEDVHFPTLTVRETLDFALRCKGNEFVRG---------------------ISGGERKRVSIAEALVSRASVLCWDN 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490075866 183 PTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDPVAASYA--DSVVFLADGR 233
Cdd:cd03233 145 STRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIYDlfDKVLVLYEGR 197
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
16-216 |
4.07e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 78.23 E-value: 4.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 16 SEALRLVKVTRTYGSAdnavTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKEltgggeaelt 95
Cdd:PRK09544 2 TSLVSLENVSVSFGQR----RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 96 kfrrgRVGFVFQQYNLLETLTVAQNTVLPLKLAGRRVDRKRArevLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEP 175
Cdd:PRK09544 68 -----RIGYVPQKLYLDTTLPLTVNRFLRLRPGTKKEDILPA---LKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRP 139
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490075866 176 RVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHD 216
Cdd:PRK09544 140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHD 180
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
42-227 |
5.11e-17 |
|
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: 76.04 E-value: 5.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 42 TLSLGRGTFTAVMGPSGSGKSTLLQCAAGLdrpdsgivcvdgkeltgggeaelTKFRRGRVGFVFQQynllETLTVAQNT 121
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRALAGL-----------------------WPWGSGRIGMPEGE----DLLFLPQRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 122 VLPlklagrrvdRKRAREVLTsvglgdrlghRP--DQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLL 199
Cdd:cd03223 74 YLP---------LGTLREQLI----------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL 134
|
170 180
....*....|....*....|....*...
gi 490075866 200 QEaarvHGRTVVMVTHDPVAASYADSVV 227
Cdd:cd03223 135 KE----LGITVISVGHRPSLWKFHDRVL 158
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
19-234 |
1.48e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 76.46 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSadnaVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTkfr 98
Cdd:PRK11614 6 LSFDKVSAHYGK----IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIM--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RGRVGFVFQQYNLLETLTVAQNtvlpLKLAGRRVDRKRAREVLTSV-GLGDRLGHRPDQ----LSGGQRQRVAIARALVT 173
Cdd:PRK11614 79 REAVAIVPEGRRVFSRMTVEEN----LAMGGFFAERDQFQERIKWVyELFPRLHERRIQragtMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490075866 174 EPRVIFADEPTGALDTRSARQVLLLLQEaARVHGRTVVMVTHDP-VAASYADSVVFLADGRL 234
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQ-LREQGMTIFLVEQNAnQALKLADRGYVLENGHV 215
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
38-235 |
2.99e-16 |
|
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: 74.87 E-value: 2.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLD--RPDSGIVCVDGKELTgggeaELTKFRRGRVG-FVFQQYnllet 114
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDIT-----DLPPEERARLGiFLAFQY----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 115 ltvaqntvlPLKLAGRRVdrkraREVLTSVGLGdrlghrpdqLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQ 194
Cdd:cd03217 86 ---------PPEIPGVKN-----ADFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490075866 195 VLLLLQEAARVhGRTVVMVTHDPVAASY--ADSVVFLADGRLA 235
Cdd:cd03217 143 VAEVINKLREE-GKSVLIITHYQRLLDYikPDRVHVLYDGRIV 184
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
27-235 |
4.19e-16 |
|
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: 77.68 E-value: 4.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 27 TYGSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAG-LDRpdsgivcVDGKELTgggeaeltkfrRGRVGFV 105
Cdd:TIGR00957 643 TFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAeMDK-------VEGHVHM-----------KGSVAYV 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 106 FQQyNLLETLTVAQNTvlplkLAGRRVDRKRAREVLTSVGL---------GDR--LGHRPDQLSGGQRQRVAIARALVTE 174
Cdd:TIGR00957 705 PQQ-AWIQNDSLRENI-----LFGKALNEKYYQQVLEACALlpdleilpsGDRteIGEKGVNLSGGQKQRVSLARAVYSN 778
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490075866 175 PRVIFADEPTGALDTRSARQVL-LLLQEAARVHGRTVVMVTHDPVAASYADSVVFLADGRLA 235
Cdd:TIGR00957 779 ADIYLFDDPLSAVDAHVGKHIFeHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKIS 840
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
47-216 |
1.09e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.39 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 47 RGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVcvdgkELTGGGEAELTKFRrgrvGFVFQQY--NLLE-TLTVAQNT-- 121
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDY-----EEEPSWDEVLKRFR----GTELQNYfkKLYNgEIKVVHKPqy 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 122 --VLPLKLAG------RRVD-RKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSA 192
Cdd:PRK13409 169 vdLIPKVFKGkvrellKKVDeRGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQR 248
|
170 180
....*....|....*....|....
gi 490075866 193 RQVLLLLQEAARvhGRTVVMVTHD 216
Cdd:PRK13409 249 LNVARLIRELAE--GKYVLVVEHD 270
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
24-216 |
2.28e-15 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 74.45 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 24 VTRTYGSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRpDSGIVCVDGKELTGGGEAELTKFRRGR-- 101
Cdd:PRK15093 9 LTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK-DNWRVTADRMRFDDIDLLRLSPRERRKlv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 102 ---VGFVFQQynlletltvAQNTVLPLKLAGRRV-------------------DRKRAREVLTSVGLGDR---LGHRPDQ 156
Cdd:PRK15093 88 ghnVSMIFQE---------PQSCLDPSERVGRQLmqnipgwtykgrwwqrfgwRKRRAIELLHRVGIKDHkdaMRSFPYE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 157 LSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHD 216
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHD 218
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
26-237 |
3.51e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 74.75 E-value: 3.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 26 RTYGSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTgggEAELTKFRrGRVGFV 105
Cdd:PRK10789 319 RQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT---KLQLDSWR-SRLAVV 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 106 fQQYNLLETLTVAQNTVLPLKLAGRRVDRKRARevLTSV---------GLGDRLGHRPDQLSGGQRQRVAIARALVTEPR 176
Cdd:PRK10789 395 -SQTPFLFSDTVANNIALGRPDATQQEIEHVAR--LASVhddilrlpqGYDTEVGERGVMLSGGQKQRISIARALLLNAE 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490075866 177 VIFADEPTGALDTRSARQVLLLLQEAARvhGRTVVMVTHDPVAASYADSVVFLADGRLAGR 237
Cdd:PRK10789 472 ILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTEASEILVMQHGHIAQR 530
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
15-216 |
6.59e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.61 E-value: 6.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 15 ASEALRLVKVTRTYgsaDNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTgggeael 94
Cdd:PRK15056 3 QQAGIVVNDVTVTW---RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 95 TKFRRGRVGFVFQQYNLLETLTVAQNTVLPLKLAG-----RRV---DRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVA 166
Cdd:PRK15056 73 QALQKNLVAYVPQSEEVDWSFPVLVEDVVMMGRYGhmgwlRRAkkrDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490075866 167 IARALVTEPRVIFADEPTGALDTRSARQVLLLLQEaARVHGRTVVMVTHD 216
Cdd:PRK15056 153 LARAIAQQGQVILLDEPFTGVDVKTEARIISLLRE-LRDEGKTMLVSTHN 201
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
19-247 |
6.91e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 73.85 E-value: 6.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSADNAVTALDgvtLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELtkfr 98
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPIN---LTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDY---- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 RGRVGFVFQQYNLLETLtvaqntvlpLKLAGRRVDRKRAREVLTSVGLGDRLGHRPD-----QLSGGQRQRVAIARALVT 173
Cdd:PRK10522 396 RKLFSAVFTDFHLFDQL---------LGPEGKPANPALVEKWLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLALAE 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 174 EPRVIFADEPTGALDTRSAR---QVLL-LLQEAarvhGRTVVMVTHDPVAASYADSVVFLADGRLA----GRMDAPTPDA 245
Cdd:PRK10522 467 ERDILLLDEWAADQDPHFRRefyQVLLpLLQEM----GKTIFAISHDDHYFIHADRLLEMRNGQLSeltgEERDAASRDA 542
|
..
gi 490075866 246 VA 247
Cdd:PRK10522 543 VA 544
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
38-216 |
9.98e-15 |
|
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: 73.43 E-value: 9.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDrpdsgivcvdgKELTGggEAELTKFRRgrVGFVFQQYNLLETLTV 117
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVD-----------KDFNG--EARPQPGIK--VGYLPQEPQLDPTKTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 118 AQNT---VLPLKLAGRRVDRKRAR-------------------EVLTSVGLGDrLGHRPDQ----------------LSG 159
Cdd:TIGR03719 86 RENVeegVAEIKDALDRFNEISAKyaepdadfdklaaeqaelqEIIDAADAWD-LDSQLEIamdalrcppwdadvtkLSG 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490075866 160 GQRQRVAIARALVTEPRVIFADEPTGALDtrsARQVLLLLQEAARVHGrTVVMVTHD 216
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLD---AESVAWLERHLQEYPG-TVVAVTHD 217
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
21-216 |
1.14e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 73.23 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 21 LVKVTRTYGSaDNAVtaLDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGivcvdgkeltgggEAELTKfrrG 100
Cdd:PRK11819 9 MNRVSKVVPP-KKQI--LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG-------------EARPAP---G 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 101 -RVGFVFQQYNLLETLTVAQNT---VLPLKLAGRRVDRKRAR-------------------EVLTSVGLGDrLGHRPDQ- 156
Cdd:PRK11819 70 iKVGYLPQEPQLDPEKTVRENVeegVAEVKAALDRFNEIYAAyaepdadfdalaaeqgelqEIIDAADAWD-LDSQLEIa 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490075866 157 ---------------LSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSarqVLLLLQEAARVHGrTVVMVTHD 216
Cdd:PRK11819 149 mdalrcppwdakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES---VAWLEQFLHDYPG-TVVAVTHD 219
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
14-233 |
1.29e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 73.22 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 14 PASEALRLVKVTRTygsaDNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAA----GLDRPDSGIVCVDGKeltgg 89
Cdd:TIGR00956 57 ILTRGFRKLKKFRD----TKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGI----- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 90 GEAELTKFRRGRVGFVFQQYNLLETLTVAQ--NTVLPLKLAGRR---VDRKRAREVLTSVGL---GdrLGHRPDQ----- 156
Cdd:TIGR00956 128 TPEEIKKHYRGDVVYNAETDVHFPHLTVGEtlDFAARCKTPQNRpdgVSREEYAKHIADVYMatyG--LSHTRNTkvgnd 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 157 ----LSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDPVAASYA--DSVVFLA 230
Cdd:TIGR00956 206 fvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQDAYElfDKVIVLY 285
|
...
gi 490075866 231 DGR 233
Cdd:TIGR00956 286 EGY 288
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
34-246 |
1.40e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.78 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 34 AVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGggeaeLTKFRRGRVG--FVFQQYNL 111
Cdd:PRK15439 23 GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCAR-----LTPAKAHQLGiyLVPQEPLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 112 LETLTVAQNTVlpLKLAGRRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALD--- 188
Cdd:PRK15439 98 FPNLSVKENIL--FGLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTpae 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490075866 189 -TRSARQVLLLLQEaarvhGRTVVMVTHD-PVAASYADSVVFLADGR--LAGRMDAPTPDAV 246
Cdd:PRK15439 176 tERLFSRIRELLAQ-----GVGIVFISHKlPEIRQLADRISVMRDGTiaLSGKTADLSTDDI 232
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-184 |
1.93e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 72.85 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 7 RGNHDPGPASEALRLvkvTRTYGSadnaVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKEL 86
Cdd:NF033858 258 PADDDDEPAIEARGL---TMRFGD----FTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 87 TGGGEAEltkfrRGRVGFVFQQYNLLETLTVAQNTVL-------PLKLAGRRVDrkrarEVLTSVGLGDRLGHRPDQLSG 159
Cdd:NF033858 331 DAGDIAT-----RRRVGYMSQAFSLYGELTVRQNLELharlfhlPAAEIAARVA-----EMLERFDLADVADALPDSLPL 400
|
170 180
....*....|....*....|....*
gi 490075866 160 GQRQRVAIARALVTEPRVIFADEPT 184
Cdd:NF033858 401 GIRQRLSLAVAVIHKPELLILDEPT 425
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
38-235 |
2.00e-14 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 70.75 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGldRPD----SGIVCVDGKELTgggeaELTKFRRGRVG-FVFQQY--- 109
Cdd:TIGR01978 16 LKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG--HPSyevtSGTILFKGQDLL-----ELEPDERARAGlFLAFQYpee 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 110 ----NLLETLTVAQNTVL------PLKLAGRrvdRKRAREVLTSVGLGDRLGHRP--DQLSGGQRQRVAIARALVTEPRV 177
Cdd:TIGR01978 89 ipgvSNLEFLRSALNARRsargeePLDLLDF---EKLLKEKLALLDMDEEFLNRSvnEGFSGGEKKRNEILQMALLEPKL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 178 IFADEPTGALDTRSARQVLLLLQEaARVHGRTVVMVTHDPVAASY--ADSVVFLADGRLA 235
Cdd:TIGR01978 166 AILDEIDSGLDIDALKIVAEGINR-LREPDRSFLIITHYQRLLNYikPDYVHVLLDGRIV 224
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
38-235 |
4.42e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 71.73 E-value: 4.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQcaagldrpdsgivcvdgkelTGGGEAELTKfrrGRV------GFVFQQYNL 111
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQ--------------------SLLSQFEISE---GRVwaersiAYVPQQAWI 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 112 LETlTVAQNTVL-----PLKLAGR-RVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTG 185
Cdd:PTZ00243 733 MNA-TVRGNILFfdeedAARLADAvRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLS 811
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490075866 186 ALDT----RSARQVLLllqeaARVHGRTVVMVTHDPVAASYADSVVFLADGRLA 235
Cdd:PTZ00243 812 ALDAhvgeRVVEECFL-----GALAGKTRVLATHQVHVVPRADYVVALGDGRVE 860
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
38-233 |
4.67e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 71.29 E-value: 4.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELtkfRRGrVGFVfQQYNLLETLTV 117
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL---RQG-VAMV-QQDPVVLADTF 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 118 AQNTVLplklaGRRVDRKRAREVLTSV-----------GLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGA 186
Cdd:PRK10790 432 LANVTL-----GRDISEEQVWQALETVqlaelarslpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATAN 506
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490075866 187 LDTRSARQVLLLLQeAARVHgRTVVMVTHDPVAASYADSVVFLADGR 233
Cdd:PRK10790 507 IDSGTEQAIQQALA-AVREH-TTLVVIAHRLSTIVEADTILVLHRGQ 551
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
35-249 |
5.29e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 70.97 E-value: 5.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 35 VTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGldrpdsgivcV------DGKELTGGGEAELTKFRRG-RVGFVF- 106
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG----------VyphgsyEGEILFDGEVCRFKDIRDSeALGIVIi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 107 -QQYNLLETLTVAQNTVLPLKLAGRRV-----DRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFA 180
Cdd:NF040905 84 hQELALIPYLSIAENIFLGNERAKRGVidwneTNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLIL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490075866 181 DEPTGALDTRSARQVLLLLQEaARVHGRTVVMVTH--DPVAAsYADSVVFLADGRLAGRMDAPTPDAVAER 249
Cdd:NF040905 164 DEPTAALNEEDSAALLDLLLE-LKAQGITSIIISHklNEIRR-VADSITVLRDGRTIETLDCRADEVTEDR 232
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
47-216 |
6.22e-14 |
|
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: 70.97 E-value: 6.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 47 RGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVcvdgkELTGGGEAELTKFRrgrvGFVFQQY--NLLE-TLTVAQNT-- 121
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDY-----DEEPSWDEVLKRFR----GTELQDYfkKLANgEIKVAHKPqy 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 122 --VLPLKLAGR------RVD-RKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSA 192
Cdd:COG1245 169 vdLIPKVFKGTvrelleKVDeRGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQR 248
|
170 180
....*....|....*....|....
gi 490075866 193 RQVLLLLQEAARVhGRTVVMVTHD 216
Cdd:COG1245 249 LNVARLIRELAEE-GKYVLVVEHD 271
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
26-217 |
1.28e-13 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 70.26 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 26 RTYGSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGldRPDSGIVcvDGKELTGGGEAELTKFRRGRvGFV 105
Cdd:PLN03140 884 KEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYI--EGDIRISGFPKKQETFARIS-GYC 958
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 106 FQ------QYNLLETLTVAQNTVLPLKLAG----RRVDRkrAREVLTSVGLGDRLGHRP--DQLSGGQRQRVAIARALVT 173
Cdd:PLN03140 959 EQndihspQVTVRESLIYSAFLRLPKEVSKeekmMFVDE--VMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVA 1036
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490075866 174 EPRVIFADEPTGALDTRSARQVLLLLQEAARVhGRTVVMVTHDP 217
Cdd:PLN03140 1037 NPSIIFMDEPTSGLDARAAAIVMRTVRNTVDT-GRTVVCTIHQP 1079
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
37-235 |
1.41e-13 |
|
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: 67.44 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 37 ALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGeaeLTKFRRgRVGFVFQQYNLLETlT 116
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP---LEDLRS-SLTIIPQDPTLFSG-T 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 117 VAQNtvlpLKLAGRRVDRKrAREVLTSVGLGDrlghrpdQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARqvl 196
Cdd:cd03369 98 IRSN----LDPFDEYSDEE-IYGALRVSEGGL-------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDA--- 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490075866 197 lLLQEAAR--VHGRTVVMVTHDPVAASYADSVVFLADGRLA 235
Cdd:cd03369 163 -LIQKTIReeFTNSTILTIAHRLRTIIDYDKILVMDAGEVK 202
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
35-187 |
1.92e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 69.37 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 35 VTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKEL--TGGGEAeltkFRRGrVGFVFQQYNLL 112
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfKSSKEA----LENG-ISMVHQELNLV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 113 ETLTVAQNTVL---PLKlaGRRVDRKRAREvlTSVGLGDRLGHRPD------QLSGGQRQRVAIARALVTEPRVIFADEP 183
Cdd:PRK10982 86 LQRSVMDNMWLgryPTK--GMFVDQDKMYR--DTKAIFDELDIDIDprakvaTLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
....
gi 490075866 184 TGAL 187
Cdd:PRK10982 162 TSSL 165
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
38-224 |
2.21e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 66.90 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELtgggEAELTKFRRgRVGFVFQQYNLLETLTV 117
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQK-QLCFVGHRSGINPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 118 AQNTVLPLKLAGRRVDrkrAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQVLL 197
Cdd:PRK13540 92 RENCLYDIHFSPGAVG---ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIIT 168
|
170 180
....*....|....*....|....*..
gi 490075866 198 LLQEaARVHGRTVVMVTHDPVAASYAD 224
Cdd:PRK13540 169 KIQE-HRAKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
36-216 |
4.06e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.84 E-value: 4.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 36 TALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAEltKFRRGrVGFVFQQYNLLETL 115
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RARRG-IGYLPQEASIFRRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 116 TVAQN--TVLPLKLAGRRVDRK-RAREVLTSVG---LGDRLGHrpdQLSGGQRQRVAIARALVTEPRVIFADEPTGALDT 189
Cdd:PRK10895 94 SVYDNlmAVLQIRDDLSAEQREdRANELMEEFHiehLRDSMGQ---SLSGGERRRVEIARALAANPKFILLDEPFAGVDP 170
|
170 180
....*....|....*....|....*..
gi 490075866 190 RSARQVLLLLQEaARVHGRTVVMVTHD 216
Cdd:PRK10895 171 ISVIDIKRIIEH-LRDSGLGVLITDHN 196
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
18-194 |
4.56e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 68.61 E-value: 4.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 18 ALRLVKVTRTYGsadnAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVcvdgkELTGGGEAElTKF 97
Cdd:NF033858 1 VARLEGVSHRYG----KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRV-----EVLGGDMAD-ARH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 98 RR---GRVGFVFQQY--NLLETLTVAQNTVLPLKLAGRRVDRKRAR--EVLTSVGLgDRLGHRP-DQLSGGQRQRVAIAR 169
Cdd:NF033858 71 RRavcPRIAYMPQGLgkNLYPTLSVFENLDFFGRLFGQDAAERRRRidELLRATGL-APFADRPaGKLSGGMKQKLGLCC 149
|
170 180
....*....|....*....|....*
gi 490075866 170 ALVTEPRVIFADEPTGALDTRSARQ 194
Cdd:NF033858 150 ALIHDPDLLILDEPTTGVDPLSRRQ 174
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
48-216 |
7.79e-13 |
|
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: 66.24 E-value: 7.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 48 GTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVD-----------GKELtgggEAELTKFRRGRVGFVFQ-QYNLLETL 115
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPpdwdeildefrGSEL----QNYFTKLLEGDVKVIVKpQYVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 116 TVAQNTVLPLKlagrRVDRKRAREVLTsvglgDRLGHRP------DQLSGGQRQRVAIARALVTEPRVIFADEPTGALDT 189
Cdd:cd03236 102 AVKGKVGELLK----KKDERGKLDELV-----DQLELRHvldrniDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180
....*....|....*....|....*..
gi 490075866 190 RSARQVLLLLQEAARvHGRTVVMVTHD 216
Cdd:cd03236 173 KQRLNAARLIRELAE-DDNYVLVVEHD 198
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
41-240 |
1.05e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.12 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 41 VTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELT--------GGGEAELTKFRRgRVGFvFQQYNLL 112
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprspldavKKGMAYITESRR-DNGF-FPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 113 ETLTVAQNtvlpLKLAG---------RRVDRKRAREVLTSVGLG-DRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADE 182
Cdd:PRK09700 360 QNMAISRS----LKDGGykgamglfhEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDE 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490075866 183 PTGALDTRSARQVLLLLQEAARvHGRTVVMVTHD-PVAASYADSVVFLADGRLAGRMDA 240
Cdd:PRK09700 436 PTRGIDVGAKAEIYKVMRQLAD-DGKVILMVSSElPEIITVCDRIAVFCEGRLTQILTN 493
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
38-258 |
1.31e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 66.00 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGlDRPDS---------GIVCVDGKELTGGGEAELTKFR-----RGRVG 103
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGGgaprgarvtGDVTLNGEPLAAIDAPRLARLRavlpqAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 104 FVFqqyNLLETLTVAQNTVLPLKLAGRRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARAL---------VTE 174
Cdd:PRK13547 96 FAF---SAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 175 PRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDP-VAASYADSVVFLADGRLAGR---MDAPTPDAVAE-- 248
Cdd:PRK13547 173 PRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPnLAARHADRIAMLADGAIVAHgapADVLTPAHIARcy 252
|
250
....*....|....
gi 490075866 249 ----RLAHLGDDVP 258
Cdd:PRK13547 253 gfavRLVDAGDGVP 266
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
38-254 |
1.67e-12 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 65.12 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFT-----AVMGPSGSGKSTLLQCAAGLDRPDsgivcvdgkeltgGGEAELTkfrRGRVGFVFQQYNLL 112
Cdd:cd03237 10 LGEFTLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPD-------------EGDIEIE---LDTVSYKPQYIKAD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 113 ETLTVAQntVLPLKLAGRRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSA 192
Cdd:cd03237 74 YEGTVRD--LLSSITKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490075866 193 RQVLLLLQEAARVHGRTVVMVTHDPVAASY-ADSV-VFlaDGRLAGRMDAPTPDAVAER----LAHLG 254
Cdd:cd03237 152 LMASKVIRRFAENNEKTAFVVEHDIIMIDYlADRLiVF--EGEPSVNGVANPPQSLRSGmnrfLKNLD 217
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
52-235 |
1.99e-12 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 66.81 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 52 AVMGPSGSGKSTLLQCAAGLDRPDSGIVcvdgkeltgggeaeltkFRRGRVGF-VFQQYNLlETLTVAQNTVLPLKLAGR 130
Cdd:PLN03073 539 AMVGPNGIGKSTILKLISGELQPSSGTV-----------------FRSAKVRMaVFSQHHV-DGLDLSSNPLLYMMRCFP 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 131 RVDRKRAREVLTSVGLGDRLGHRPD-QLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSarqVLLLLQEAARVHGrT 209
Cdd:PLN03073 601 GVPEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA---VEALIQGLVLFQG-G 676
|
170 180
....*....|....*....|....*..
gi 490075866 210 VVMVTHDP-VAASYADSVVFLADGRLA 235
Cdd:PLN03073 677 VLMVSHDEhLISGSVDELWVVSEGKVT 703
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
38-232 |
4.83e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.53 E-value: 4.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVdgkeltgggeaeltkfRRGRVGFVfQQYNLLETLTV 117
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV----------------IRGTVAYV-PQVSWIFNATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 118 AQNTvlplkLAGRRVDRKRAREVLTSVGL---------GD--RLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGA 186
Cdd:PLN03130 696 RDNI-----LFGSPFDPERYERAIDVTALqhdldllpgGDltEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490075866 187 LDTRSARQVL-LLLQEAARvhGRTVVMVTHDPVAASYADSVVFLADG 232
Cdd:PLN03130 771 LDAHVGRQVFdKCIKDELR--GKTRVLVTNQLHFLSQVDRIILVHEG 815
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
38-216 |
2.20e-11 |
|
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: 63.42 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVdgkeltggGEAEltkfrrgRVGFVFQQYNLLEtltv 117
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI--------GETV-------KLAYVDQSRDALD---- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 118 AQNTVLP--------LKLAGRRVDrkrAREVLTSVGL-GDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALD 188
Cdd:TIGR03719 399 PNKTVWEeisggldiIKLGKREIP---SRAYVGRFNFkGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
170 180
....*....|....*....|....*...
gi 490075866 189 TRSARQvlllLQEAARVHGRTVVMVTHD 216
Cdd:TIGR03719 476 VETLRA----LEEALLNFAGCAVVISHD 499
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-261 |
2.40e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.46 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 22 VKVTRTYGSADNAVT--ALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGlDRPDSGIVCVDgkeltgggeaeltkfRR 99
Cdd:PLN03232 615 ISIKNGYFSWDSKTSkpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG-ELSHAETSSVV---------------IR 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 100 GRVGFVfQQYNLLETLTVAQNTVLPLKLA----GRRVDRKRAREVLTSVGLGDR--LGHRPDQLSGGQRQRVAIARALVT 173
Cdd:PLN03232 679 GSVAYV-PQVSWIFNATVRENILFGSDFEseryWRAIDVTALQHDLDLLPGRDLteIGERGVNISGGQKQRVSMARAVYS 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 174 EPRVIFADEPTGALDTRSARQVL-LLLQEAARvhGRTVVMVTHDPVAASYADSVVFLADGRL------------------ 234
Cdd:PLN03232 758 NSDIYIFDDPLSALDAHVAHQVFdSCMKDELK--GKTRVLVTNQLHFLPLMDRIILVSEGMIkeegtfaelsksgslfkk 835
|
250 260 270
....*....|....*....|....*....|..
gi 490075866 235 ----AGRMDAPTP-DAVAERLAHLGDDVPAGV 261
Cdd:PLN03232 836 lmenAGKMDATQEvNTNDENILKLGPTVTIDV 867
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
53-220 |
7.62e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 60.25 E-value: 7.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 53 VMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTgggEAELTKFrrgrVGFVFQQYNLLETLTVAQNTVLPLKLAGRRV 132
Cdd:PRK13543 42 VQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT---RGDRSRF----MAYLGHLPGLKADLSTLENLHFLCGLHGRRA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 133 dRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVm 212
Cdd:PRK13543 115 -KQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGGGAALV- 192
|
....*...
gi 490075866 213 VTHDPVAA 220
Cdd:PRK13543 193 TTHGAYAA 200
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
35-232 |
2.15e-10 |
|
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: 58.10 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 35 VTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQcaagldrpdSGIVCVDGKELTGGgeaeLTKFRRGRVGFVFQqynllet 114
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN---------EGLYASGKARLISF----LPKFSRNKLIFIDQ------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 115 ltvaqntvlpLKLagrrvdrkrarevLTSVGLGD-RLGHRPDQLSGGQRQRVAIARALV--TEPRVIFADEPTGALDTRS 191
Cdd:cd03238 68 ----------LQF-------------LIDVGLGYlTLGQKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQD 124
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490075866 192 ARQVLLLLQEAaRVHGRTVVMVTHDPVAASYADSVVFLADG 232
Cdd:cd03238 125 INQLLEVIKGL-IDLGNTVILIEHNLDVLSSADWIIDFGPG 164
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
157-227 |
4.37e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.66 E-value: 4.37e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490075866 157 LSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDPVAASYADSVV 227
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIV 1429
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
35-215 |
4.45e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 58.98 E-value: 4.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 35 VTALDGVTLSLGRGTFTAVMGPSGSGKSTlLQCAAGLDRPDSG-------IVCVDGKEL--TGGGEAELTKFRRgrvgfv 105
Cdd:NF000106 26 VKAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGrrpwrf*TWCANRRALrrTIG*HRPVR*GRR------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 106 fqqynllETLTVAQNtvlpLKLAGRRVD------RKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIF 179
Cdd:NF000106 99 -------ESFSGREN----LYMIGR*LDlsrkdaRARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLY 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 490075866 180 ADEPTGALDTRSARQVLLLLQEAARvHGRTVVMVTH 215
Cdd:NF000106 168 LDEPTTGLDPRTRNEVWDEVRSMVR-DGATVLLTTQ 202
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
47-217 |
6.91e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 56.23 E-value: 6.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 47 RGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVdgkeltgggeaeltkfrrgrvgfvfqqynlletltvaqntvlplk 126
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------------------------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 127 lagrrVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQVLLL-----LQE 201
Cdd:smart00382 36 -----IDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLL 110
|
170
....*....|....*.
gi 490075866 202 AARVHGRTVVMVTHDP 217
Cdd:smart00382 111 LKSEKNLTVILTTNDE 126
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
150-256 |
2.16e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.73 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 150 LGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDPVAASYADSVVFL 229
Cdd:PTZ00265 573 VGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIFVL 652
|
90 100 110
....*....|....*....|....*....|...
gi 490075866 230 ADGRLAGRMDA------PTPDAVAERLAHLGDD 256
Cdd:PTZ00265 653 SNRERGSTVDVdiigedPTKDNKENNNKNNKDD 685
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
38-236 |
2.33e-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: 57.14 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGL-DRPDSGIVCVDGKELTGGGEAELTKFRRGRVGFVFQQYNLLETLT 116
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 117 VAQNTVLPL--KLAGR-RVDrkrAREVLTSVGLG-DRLGHR---PD----QLSGGQRQRVAIARALVTEPRVIFADEPTG 185
Cdd:TIGR02633 356 VGKNITLSVlkSFCFKmRID---AAAELQIIGSAiQRLKVKtasPFlpigRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490075866 186 ALDTRSARQVLLLLQEAARvHGRTVVMVTHD-PVAASYADSVVFLADGRLAG 236
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQ-EGVAIIVVSSElAEVLGLSDRVLVIGEGKLKG 483
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
38-195 |
4.64e-09 |
|
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: 55.63 E-value: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVcvdgkeltgggeaeltkFRRGRVGFVfQQYNLLETLTV 117
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-----------------KHSGRISFS-SQFSWIMPGTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 118 AQNTVlplklAGRRVDRKRAREVLTSVGLGDRLGHRPDQ-----------LSGGQRQRVAIARALVTEPRVIFADEPTGA 186
Cdd:cd03291 115 KENII-----FGVSYDEYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
....*....
gi 490075866 187 LDTRSARQV 195
Cdd:cd03291 190 LDVFTEKEI 198
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
38-250 |
7.33e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.78 E-value: 7.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELT--------GGGEAELTKFRRGRvGFVFQqy 109
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtrspqdglANGIVYISEDRKRD-GLVLG-- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 110 nlletLTVAQNTVLP----LKLAGRRVDRKRAREVLTS-VGLGDRLGHRPDQ----LSGGQRQRVAIARALVTEPRVIFA 180
Cdd:PRK10762 345 -----MSVKENMSLTalryFSRAGGSLKHADEQQAVSDfIRLFNIKTPSMEQaiglLSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490075866 181 DEPTGALDTRSARQVLLLLQEaARVHGRTVVMVTHD-PVAASYADSVVFLADGRLAGRMDAptPDAVAERL 250
Cdd:PRK10762 420 DEPTRGVDVGAKKEIYQLINQ-FKAEGLSIILVSSEmPEVLGMSDRILVMHEGRISGEFTR--EQATQEKL 487
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
13-215 |
1.40e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 55.40 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 13 GPASEALRLVKVTRTY-GSADNAVtalDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKE-LTGGG 90
Cdd:TIGR01257 1932 GNKTDILRLNELTKVYsGTSSPAV---DRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNIS 2008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 91 EAELTkfrrgrVGFVFQQYNLLETLTVAQNTVLPLKLAGRRVDR--KRAREVLTSVGL---GDRLGhrpDQLSGGQRQRV 165
Cdd:TIGR01257 2009 DVHQN------MGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEieKVANWSIQSLGLslyADRLA---GTYSGGNKRKL 2079
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490075866 166 AIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARvHGRTVVMVTH 215
Cdd:TIGR01257 2080 STAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIR-EGRAVVLTSH 2128
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-216 |
2.26e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.41 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 19 LRLVKVTRTYGSAdnavTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSgivcvdgkeltggGEAELTKfr 98
Cdd:PRK10636 313 LKMEKVSAGYGDR----IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVS-------------GEIGLAK-- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 99 rG-RVGFvFQQYNlLETLTVAQNTVLPLKLAGRRVDRKRAREVLTSVGL-GDRLGHRPDQLSGGQRQRVAIARALVTEPR 176
Cdd:PRK10636 374 -GiKLGY-FAQHQ-LEFLRADESPLQHLARLAPQELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPN 450
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490075866 177 VIFADEPTGALDTrSARQVlllLQEAARVHGRTVVMVTHD 216
Cdd:PRK10636 451 LLLLDEPTNHLDL-DMRQA---LTEALIDFEGALVVVSHD 486
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
41-253 |
2.81e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.90 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 41 VTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAEltkfrRGRVGFVF-----QQYNLLETL 115
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-----RLARGLVYlpedrQSSGLYLDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 116 TVAQNTV-LPLKLAGRRVDRKRAREVLTSV--GLGDRLGHrPDQ----LSGGQRQRVAIARALVTEPRVIFADEPTGALD 188
Cdd:PRK15439 357 PLAWNVCaLTHNRRGFWIKPARENAVLERYrrALNIKFNH-AEQaartLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490075866 189 TrSARQVLLLLQEAARVHGRTVVMVTHD-PVAASYADSVVFLADGRLAGrmdAPTPDAVA-ERLAHL 253
Cdd:PRK15439 436 V-SARNDIYQLIRSIAAQNVAVLFISSDlEEIEQMADRVLVMHQGEISG---ALTGAAINvDTIMRL 498
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
38-227 |
3.66e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 51.59 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLqCAAGLdrpdsgivcvdgkeltgggeAELTKFRRGRVGFVFQQynlleTLTV 117
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTIL-DAIGL--------------------ALGGAQSATRRRSGVKA-----GCIV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 118 AQNTVlplklagrrvdrkrarEVLTSVglgdrlghrpDQLSGGQRQRVAIARALV---TEPRVIFA-DEPTGALDTRSAR 193
Cdd:cd03227 65 AAVSA----------------ELIFTR----------LQLSGGEKELSALALILAlasLKPRPLYIlDEIDRGLDPRDGQ 118
|
170 180 190
....*....|....*....|....*....|....
gi 490075866 194 QVLLLLQEaARVHGRTVVMVTHDPVAASYADSVV 227
Cdd:cd03227 119 ALAEAILE-HLVKGAQVIVITHLPELAELADKLI 151
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
38-215 |
5.08e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.09 E-value: 5.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGlDRPDsgivcvdgkeltgGGEAELTKF--RRG----------RVGFV 105
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQ-------------GYSNDLTLFgrRRGsgetiwdikkHIGYV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 106 FQQYNLLETLTVAQNTVLplkLAG--------RRV-DRKR--AREVLTSVGLGDRLGHRPDQ-LSGGQRQRVAIARALVT 173
Cdd:PRK10938 342 SSSLHLDYRVSTSVRNVI---LSGffdsigiyQAVsDRQQklAQQWLDILGIDKRTADAPFHsLSWGQQRLALIVRALVK 418
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490075866 174 EPRVIFADEPTGALDTRSaRQVLLLLQEAARVHGRT-VVMVTH 215
Cdd:PRK10938 419 HPTLLILDEPLQGLDPLN-RQLVRRFVDVLISEGETqLLFVSH 460
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
12-234 |
5.24e-08 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 53.26 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 12 PGPASEALRLVKVTRTY-GSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTggg 90
Cdd:COG4615 321 APADFQTLELRGVTYRYpGEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT--- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 91 EAELTKFRRgRVGFVFQQYNLLETLTVAQNTVLPlklagrrvdrKRAREVLTSVGLGDRLGHRPD-----QLSGGQRQRV 165
Cdd:COG4615 398 ADNREAYRQ-LFSAVFSDFHLFDRLLGLDGEADP----------ARARELLERLELDHKVSVEDGrfsttDLSQGQRKRL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 166 AIARALVtEPRVIFadeptgALDTRSA-----------RQVLLLLQEAarvhGRTVVMVTHDPVAASYADSVVFLADGRL 234
Cdd:COG4615 467 ALLVALL-EDRPIL------VFDEWAAdqdpefrrvfyTELLPELKAR----GKTVIAISHDDRYFDLADRVLKMDYGKL 535
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-246 |
5.36e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.99 E-value: 5.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 26 RTYGSADNAVTALDG------VTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTkfrr 99
Cdd:PRK11288 251 RPLGEVRLRLDGLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAI---- 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 100 gRVGFVF-----QQYNLLETLTVAQNtvlpLKLAGRR--------VDRKR----AREVLTSVGLGDRLGHRP-DQLSGGQ 161
Cdd:PRK11288 327 -RAGIMLcpedrKAEGIIPVHSVADN----INISARRhhlragclINNRWeaenADRFIRSLNIKTPSREQLiMNLSGGN 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 162 RQRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVhGRTVVMVTHD-PVAASYADSVVFLADGRLAG---R 237
Cdd:PRK11288 402 QQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDlPEVLGVADRIVVMREGRIAGelaR 480
|
....*....
gi 490075866 238 MDApTPDAV 246
Cdd:PRK11288 481 EQA-TERQA 488
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
38-196 |
7.65e-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: 52.99 E-value: 7.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGivcvdgkeltgggeaeltKFRR-GRVGFVfQQYNLLETLT 116
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEG------------------KIKHsGRISFS-PQTSWIMPGT 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 117 VAQNTVLplklaGRRVDRKRAREVLTSVGLGDRLGHRPDQ-----------LSGGQRQRVAIARALVTEPRVIFADEPTG 185
Cdd:TIGR01271 503 IKDNIIF-----GLSYDEYRYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170
....*....|.
gi 490075866 186 ALDTRSARQVL 196
Cdd:TIGR01271 578 HLDVVTEKEIF 588
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
38-237 |
8.66e-08 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 51.49 E-value: 8.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLL---------------------QCAAGLDRPD-------SGIVCVDGKelTGG 89
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDvdsieglSPAIAIDQK--TTS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 90 GEAeltkfrRGRVGFVFQQYNLLETLTVaqntvlplklagrRVDRKRAREVLTSVGLGD-RLGHRPDQLSGGQRQRVAIA 168
Cdd:cd03270 89 RNP------RSTVGTVTEIYDYLRLLFA-------------RVGIRERLGFLVDVGLGYlTLSRSAPTLSGGEAQRIRLA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490075866 169 RALVTE-PRVIFA-DEPTGALDTRSARQVLLLLQEAaRVHGRTVVMVTHDPVAASYADSVVFLADGrlAGR 237
Cdd:cd03270 150 TQIGSGlTGVLYVlDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIRAADHVIDIGPG--AGV 217
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
136-188 |
9.34e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.65 E-value: 9.34e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 490075866 136 RAREVLTSVGLGdrlghrPDQ----LSGGQRQRVAIARALVTEPRVIFADEPTGALD 188
Cdd:PRK11147 138 RINEVLAQLGLD------PDAalssLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
50-230 |
1.09e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 51.07 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 50 FTAVMGPSGSGKSTLLQC----AAGLDRPDSGIVCVDGKeLTGGGEaeltkfRRGRVGFVFQQYNlletltvaqntvlpl 125
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEAlkyaLTGELPPNSKGGAHDPK-LIREGE------VRAQVKLAFENAN--------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 126 klaGRRVDRKRAREVLTSV-----GLGDRLGHRP-DQLSGGQRQ------RVAIARALVTEPRVIFADEPTGALDTRSAR 193
Cdd:cd03240 82 ---GKKYTITRSLAILENVifchqGESNWPLLDMrGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIE 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 490075866 194 QVLL-LLQEAARVHGRTVVMVTHDPVAASYADSVVFLA 230
Cdd:cd03240 159 ESLAeIIEERKSQKNFQLIVITHDEELVDAADHIYRVE 196
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
7-236 |
1.40e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.85 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 7 RGNHDPGpaSEALRLVKVTrTYGSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDS-GIVCVDGKE 85
Cdd:PRK13549 250 REPHTIG--EVILEVRNLT-AWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKP 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 86 LT--------GGGEAELTKFRRgrvgfvfqQYNLLETLTVAQNTVLPL--KLAGRRV--DRKRAREVLTSVglgDRLGHR 153
Cdd:PRK13549 327 VKirnpqqaiAQGIAMVPEDRK--------RDGIVPVMGVGKNITLAAldRFTGGSRidDAAELKTILESI---QRLKVK 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 154 ---PDQ----LSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARvHGRTVVMVTHD-PVAASYADS 225
Cdd:PRK13549 396 tasPELaiarLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQ-QGVAIIVISSElPEVLGLSDR 474
|
250
....*....|.
gi 490075866 226 VVFLADGRLAG 236
Cdd:PRK13549 475 VLVMHEGKLKG 485
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
33-195 |
1.62e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.80 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 33 NAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGldRPD----SGIVCVDGKELTgggeaELTKFRRGRVG-FVFQ 107
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESIL-----DLEPEERAHLGiFLAF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 108 QYNlLETLTVAQNTVLPLKLAGRRVDRKRA-----------REVLTSVGLGDRLGHR--PDQLSGGQRQRVAIARALVTE 174
Cdd:CHL00131 91 QYP-IEIPGVSNADFLRLAYNSKRKFQGLPeldplefleiiNEKLKLVGMDPSFLSRnvNEGFSGGEKKRNEILQMALLD 169
|
170 180
....*....|....*....|.
gi 490075866 175 PRVIFADEPTGALDTRSARQV 195
Cdd:CHL00131 170 SELAILDETDSGLDIDALKII 190
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
18-216 |
2.03e-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: 51.32 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 18 ALRLVKVTRTYGSADNAVTALDGVTLSLGRGTF-----TAVMGPSGSGKSTLLQCAAGLDRPDSGIVcvdgkeltgggEA 92
Cdd:COG1245 331 APRREKEEETLVEYPDLTKSYGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEV-----------DE 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 93 ELT---KfrrgrvgfvfQQYnlLET---LTVAQNtvlpL-KLAGRRVDRKRAR-EVLTSVGLgDRLGHRP-DQLSGGQRQ 163
Cdd:COG1245 400 DLKisyK----------PQY--ISPdydGTVEEF----LrSANTDDFGSSYYKtEIIKPLGL-EKLLDKNvKDLSGGELQ 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490075866 164 RVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHD 216
Cdd:COG1245 463 RVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHD 515
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
39-216 |
2.45e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.27 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 39 DGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVdgkeltggGEAEltkfrrgRVGFVFQQYNLLEtltvA 118
Cdd:PRK11819 341 DDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI--------GETV-------KLAYVDQSRDALD----P 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 119 QNTVLP--------LKLAGRRVDrKRArevltSVGlgdRLGHR-PDQ------LSGGQRQRVAIARALVTEPRVIFADEP 183
Cdd:PRK11819 402 NKTVWEeisggldiIKVGNREIP-SRA-----YVG---RFNFKgGDQqkkvgvLSGGERNRLHLAKTLKQGGNVLLLDEP 472
|
170 180 190
....*....|....*....|....*....|...
gi 490075866 184 TGALDTRSARQvlllLQEAARVHGRTVVMVTHD 216
Cdd:PRK11819 473 TNDLDVETLRA----LEEALLEFPGCAVVISHD 501
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
157-236 |
3.41e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.88 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 157 LSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARvHGRTVVMVTHD-PVAASYADSVVFLADGRLA 235
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAK-KDKGIIIISSEmPELLGITDRILVMSNGLVA 470
|
.
gi 490075866 236 G 236
Cdd:PRK10982 471 G 471
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
9-227 |
5.59e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.24 E-value: 5.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 9 NHDP---GPASEALRLVKVTRTYGSADNAVTAldGVTLSLGRgtFTAVMGPSGSGKSTLLQCAA-----GLDRpDSGIVC 80
Cdd:PLN03073 165 NHDGnggGPAIKDIHMENFSISVGGRDLIVDA--SVTLAFGR--HYGLVGRNGTGKTTFLRYMAmhaidGIPK-NCQILH 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 81 VDgKELTG----------GGEAELTKFRRGRVGFVFQQYNL-LETLT----VAQNTVLPLKLAGRRVDR----------- 134
Cdd:PLN03073 240 VE-QEVVGddttalqcvlNTDIERTQLLEEEAQLVAQQRELeFETETgkgkGANKDGVDKDAVSQRLEEiykrleliday 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 135 ---KRAREVLTSVGLGDRLGHR-PDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSarqvLLLLQEAARVHGRTV 210
Cdd:PLN03073 319 taeARAASILAGLSFTPEMQVKaTKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA----VLWLETYLLKWPKTF 394
|
250
....*....|....*..
gi 490075866 211 VMVTHdpvAASYADSVV 227
Cdd:PLN03073 395 IVVSH---AREFLNTVV 408
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
38-249 |
6.35e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.36 E-value: 6.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGeaeLTKFRRgrVGFVFQQYNLLETLTV 117
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG---LTDLRR--VLSIIPQSPVLFSGTV 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 118 AQNtVLPLKLAG-----RRVDRKRAREVL--TSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALDTR 190
Cdd:PLN03232 1327 RFN-IDPFSEHNdadlwEALERAHIKDVIdrNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVR 1405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490075866 191 SARqvllLLQEAARVHGR--TVVMVTHDPVAASYADSVVFLADGRLagrMDAPTPDAVAER 249
Cdd:PLN03232 1406 TDS----LIQRTIREEFKscTMLVIAHRLNTIIDCDKILVLSSGQV---LEYDSPQELLSR 1459
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
31-252 |
8.76e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.63 E-value: 8.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 31 ADNAVTALDGVTLSlgRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDgkeltgggeaeltkFRRG-RVGFVfQQY 109
Cdd:PRK10938 14 SDTKTLQLPSLTLN--AGDSWAFVGANGSGKSALARALAGELPLLSGERQSQ--------------FSHItRLSFE-QLQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 110 NLLETLTVAQNTVLpLKLA----GRRV---------DRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPR 176
Cdd:PRK10938 77 KLVSDEWQRNNTDM-LSPGeddtGRTTaeiiqdevkDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 177 VIFADEPTGALDTRSARQVLLLLQEAARvHGRTVVMVT---HD-PvaaSYADSVVFLADGRLA--GRMDAPTPDAVAERL 250
Cdd:PRK10938 156 LLILDEPFDGLDVASRQQLAELLASLHQ-SGITLVLVLnrfDEiP---DFVQFAGVLADCTLAetGEREEILQQALVAQL 231
|
..
gi 490075866 251 AH 252
Cdd:PRK10938 232 AH 233
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
53-216 |
1.52e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.65 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 53 VMGPSGSGKSTLLQCAAGLDRPDSGIVcvdgkeltgggEAELT---KfrrgrvgfvfQQYnlLET---LTVAQNtvlpLK 126
Cdd:PRK13409 370 IVGPNGIGKTTFAKLLAGVLKPDEGEV-----------DPELKisyK----------PQY--IKPdydGTVEDL----LR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 127 LAGRRVDRKRAR-EVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGALD-------TRSARQVlll 198
Cdd:PRK13409 423 SITDDLGSSYYKsEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavAKAIRRI--- 499
|
170
....*....|....*...
gi 490075866 199 lqeaARVHGRTVVMVTHD 216
Cdd:PRK13409 500 ----AEEREATALVVDHD 513
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
47-216 |
3.75e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.64 E-value: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 47 RGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDgkeltgggeaelTKFRrgrVGFvFQQY--NLLETLTVAQNtvlp 124
Cdd:PRK11147 344 RGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG------------TKLE---VAY-FDQHraELDPEKTVMDN---- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 125 lkLAgrrvDRK-------RAREVLTSvgLGDRLGHrPDQ-------LSGGQRQRVAIARALVTEPRVIFADEPTGALDTr 190
Cdd:PRK11147 404 --LA----EGKqevmvngRPRHVLGY--LQDFLFH-PKRamtpvkaLSGGERNRLLLARLFLKPSNLLILDEPTNDLDV- 473
|
170 180
....*....|....*....|....*.
gi 490075866 191 sarQVLLLLQEAARVHGRTVVMVTHD 216
Cdd:PRK11147 474 ---ETLELLEELLDSYQGTVLLVSHD 496
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
136-215 |
5.88e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 47.32 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 136 RAREVLTSVGLGD-RLGHRPDQLSGGQRQRVAIARAL---VTEPRVIFADEPTGALDTRSARQVLLLLQEAarVH-GRTV 210
Cdd:TIGR00630 808 RKLQTLCDVGLGYiRLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRL--VDkGNTV 885
|
....*
gi 490075866 211 VMVTH 215
Cdd:TIGR00630 886 VVIEH 890
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
157-232 |
6.53e-06 |
|
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: 45.26 E-value: 6.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 157 LSGGQRQRVAIARALVTEPRVIFADEPTGALDTR----SARQVLLLLQEAArvhgRTVVMVTHDPVAASYADSVVFLADG 232
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAARAIRRLSEEGK----KTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
32-215 |
8.85e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.55 E-value: 8.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 32 DNAVtaLDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLD--RPDSGIVCVDGKELTGGGEAEltkfRRGRVGFVFQQY 109
Cdd:PRK09580 13 DKAI--LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPED----RAGEGIFMAFQY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 110 NlLETLTVAQNtvLPLKLAGRRVDRKRAREVLTSVGLGD------RLGHRPDQL---------SGGQRQRVAIARALVTE 174
Cdd:PRK09580 87 P-VEIPGVSNQ--FFLQTALNAVRSYRGQEPLDRFDFQDlmeekiALLKMPEDLltrsvnvgfSGGEKKRNDILQMAVLE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490075866 175 PRVIFADEPTGALDTrSARQVLLLLQEAARVHGRTVVMVTH 215
Cdd:PRK09580 164 PELCILDESDSGLDI-DALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
157-234 |
2.38e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.22 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 157 LSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDPVAASYA--DSVVFLADGRL 234
Cdd:PLN03140 337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQPAPETFDlfDDIILLSEGQI 416
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
38-191 |
2.63e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.11 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTK----------FRRGRVGF--- 104
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKvlgiipqapvLFSGTVRFnld 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 105 VFQQYN---LLETLTVAQntvlpLKLAGRRvdrkrarevlTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFAD 181
Cdd:PLN03130 1335 PFNEHNdadLWESLERAH-----LKDVIRR----------NSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLD 1399
|
170
....*....|
gi 490075866 182 EPTGALDTRS 191
Cdd:PLN03130 1400 EATAAVDVRT 1409
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
39-216 |
4.88e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.08 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 39 DGVTLSLGRGTFtAVMGPSGSGKSTLLQC--------AAGLDRPDSGIVCVDGKEL-------TGGGEAELTKF------ 97
Cdd:COG0419 15 DTETIDFDDGLN-LIVGPNGAGKSTILEAiryalygkARSRSKLRSDLINVGSEEAsvelefeHGGKRYRIERRqgefae 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 98 --------RRGRVGFVFQ--QYNLLETLTVAQNTVLPLKLAGRRVDRKRAREVLTSV-GLGDrlghrPDQLSGGQRQRVA 166
Cdd:COG0419 94 fleakpseRKEALKRLLGleIYEELKERLKELEEALESALEELAELQKLKQEILAQLsGLDP-----IETLSGGERLRLA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490075866 167 IARALvteprVIFADepTGALDTRSARQVLLLLQEAArvhgrtvvMVTHD 216
Cdd:COG0419 169 LADLL-----SLILD--FGSLDEERLERLLDALEELA--------IITHV 203
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
106-227 |
5.60e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 5.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 106 FQQYNLLEtLTVAQNTVLPLKLAGRRV-DRKRAR-EVLTSVGLGDRLGHRP-DQLSGGQRQRVAIARALVTEPRVI--FA 180
Cdd:PRK00635 424 FQQMSLQE-LFIFLSQLPSKSLSIEEVlQGLKSRlSILIDLGLPYLTPERAlATLSGGEQERTALAKHLGAELIGItyIL 502
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 490075866 181 DEPTGALDTRSARQVLLLLQEaARVHGRTVVMVTHDPVAASYADSVV 227
Cdd:PRK00635 503 DEPSIGLHPQDTHKLINVIKK-LRDQGNTVLLVEHDEQMISLADRII 548
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
48-217 |
1.77e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 42.43 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 48 GTFTAVMGPSGSGKSTLLQCAAGLdRPdsgivcvdgkeLTGGgeaELTKFRRGRVGFVFQQ-YNLLETL---TVAQNTVL 123
Cdd:TIGR00954 478 GNNLLICGPNGCGKSSLFRILGEL-WP-----------VYGG---RLTKPAKGKLFYVPQRpYMTLGTLrdqIIYPDSSE 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 124 PLKLAGrrVDRKRAREVLTSVGLGDRLGHR---------PDQLSGGQRQRVAIARALVTEPRVIFADEPTGALdtrsARQ 194
Cdd:TIGR00954 543 DMKRRG--LSDKDLEQILDNVQLTHILEREggwsavqdwMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAV----SVD 616
|
170 180
....*....|....*....|...
gi 490075866 195 VLLLLQEAARVHGRTVVMVTHDP 217
Cdd:TIGR00954 617 VEGYMYRLCREFGITLFSVSHRK 639
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
38-65 |
2.89e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.98 E-value: 2.89e-04
10 20
....*....|....*....|....*...
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLL 65
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLI 652
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
38-215 |
4.08e-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: 41.47 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELtgggeaeltkfrrGRVGFvfqqYNLLETLTV 117
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNI-------------AKIGL----HDLRFKITI 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 118 -AQNTVL---PLKLAGRRVDRKRAREVLTSVGLG----------DRLGHR----PDQLSGGQRQRVAIARALVTEPRVIF 179
Cdd:TIGR00957 1365 iPQDPVLfsgSLRMNLDPFSQYSDEEVWWALELAhlktfvsalpDKLDHEcaegGENLSVGQRQLVCLARALLRKTKILV 1444
|
170 180 190
....*....|....*....|....*....|....*...
gi 490075866 180 ADEPTGALDTRSARqvllLLQEAARVHGR--TVVMVTH 215
Cdd:TIGR00957 1445 LDEATAAVDLETDN----LIQSTIRTQFEdcTVLTIAH 1478
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
154-227 |
4.22e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 154 PDQLSGGQRQ------RVAIARaLVTE--------PRVIFaDEPTGALDTRSARQVLLLLQEAARVHGRTVVMVTHDPVA 219
Cdd:PRK02224 779 PEQLSGGERAlfnlslRCAIYR-LLAEgiegdaplPPLIL-DEPTVFLDSGHVSQLVDLVESMRRLGVEQIVVVSHDDEL 856
|
....*...
gi 490075866 220 ASYADSVV 227
Cdd:PRK02224 857 VGAADDLV 864
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
18-79 |
5.06e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.03 E-value: 5.06e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490075866 18 ALRLVKVTRTYGSAdnavTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIV 79
Cdd:PRK15064 319 ALEVENLTKGFDNG----PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
141-237 |
5.87e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.15 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 141 LTSVGLGD-RLGHRPDQLSGGQRQRVAIARALVTE-PRVIFA-DEPTGAL---DTRSARQVLLLLQEAarvhGRTVVMVT 214
Cdd:TIGR00630 472 LIDVGLDYlSLSRAAGTLSGGEAQRIRLATQIGSGlTGVLYVlDEPSIGLhqrDNRRLINTLKRLRDL----GNTLIVVE 547
|
90 100
....*....|....*....|...
gi 490075866 215 HDPVAASYADSVVFLADGrlAGR 237
Cdd:TIGR00630 548 HDEDTIRAADYVIDIGPG--AGE 568
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
139-253 |
7.06e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 7.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 139 EVLTSVGLGD-RLGHRPDQLSGGQRQRVAIARAL---VTEPRVIFADEPTGALDTRSARQVLLLLQEAARvHGRTVVMVT 214
Cdd:PRK00635 791 HALCSLGLDYlPLGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTH-QGHTVVIIE 869
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 490075866 215 HDPVAASYADSVVFLA--DGRLAGRMDAP-TPdavaERLAHL 253
Cdd:PRK00635 870 HNMHVVKVADYVLELGpeGGNLGGYLLAScSP----EELIHL 907
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
39-65 |
7.42e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 36.81 E-value: 7.42e-04
10 20
....*....|....*....|....*..
gi 490075866 39 DGVTLSLGRGTFTAVMGPSGSGKSTLL 65
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLL 39
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
38-66 |
8.40e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.39 E-value: 8.40e-04
10 20
....*....|....*....|....*....
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQ 66
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTLVN 649
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
139-216 |
8.95e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 39.91 E-value: 8.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 139 EVLTSVGLGD-RLGHRPDQLSGGQRQRVAIARAL---VTEPRVIFADEPTGALDTRSARQVLLLLQEAARvHGRTVVMVT 214
Cdd:cd03271 151 QTLCDVGLGYiKLGQPATTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVD-KGNTVVVIE 229
|
..
gi 490075866 215 HD 216
Cdd:cd03271 230 HN 231
|
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
46-79 |
1.71e-03 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 38.25 E-value: 1.71e-03
10 20 30
....*....|....*....|....*....|....
gi 490075866 46 GRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIV 79
Cdd:COG3709 3 GPGRLIYVVGPSGAGKDSLLAAARARLAADPRLV 36
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
29-216 |
1.79e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.03 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 29 GSADNAVTALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGivcvdgkELTGGGEAELTKFRRGRVGfvfqq 108
Cdd:PRK13546 31 KHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVG-------KVDRNGEVSVIAISAGLSG----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 109 ynlleTLTVAQNTVLPLKLAG--RRVDRKRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEPTGA 186
Cdd:PRK13546 99 -----QLTGIENIEFKMLCMGfkRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSV 173
|
170 180 190
....*....|....*....|....*....|
gi 490075866 187 LDTRSARQVLLLLQEaARVHGRTVVMVTHD 216
Cdd:PRK13546 174 GDQTFAQKCLDKIYE-FKEQNKTIFFVSHN 202
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
108-228 |
1.94e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 108 QYNLLETLTVAQNTVLP--LKLAG---RRVDRKRAREVLTS------VGLGDRLGHRPDQLSGGQR-Q-----RVAIARA 170
Cdd:COG4717 499 LELLEEAREEYREERLPpvLERASeyfSRLTDGRYRLIRIDedlslkVDTEDGRTRPVEELSRGTReQlylalRLALAEL 578
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 490075866 171 LVTEPRVIFADEPTGALDTRSARQVLLLLQEAARvhGRTVVMVTHDPVAASYADSVVF 228
Cdd:COG4717 579 LAGEPLPLILDDAFVNFDDERLRAALELLAELAK--GRQVIYFTCHEELVELFQEEGA 634
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
38-216 |
2.53e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.00 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELTKFRRGRVGFVF---QQYNLLET 114
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPALEYVIdgdREYRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 115 -LTVA--QNTVLPLKLAGRRVD-------RKRAREVLTSVGLG-DRLGHRPDQLSGGQRQRVAIARALVTEPRVIFADEP 183
Cdd:PRK10636 97 qLHDAneRNDGHAIATIHGKLDaidawtiRSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEP 176
|
170 180 190
....*....|....*....|....*....|...
gi 490075866 184 TGALDTrsarQVLLLLQEAARVHGRTVVMVTHD 216
Cdd:PRK10636 177 TNHLDL----DAVIWLEKWLKSYQGTLILISHD 205
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
47-78 |
2.74e-03 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 37.97 E-value: 2.74e-03
10 20 30
....*....|....*....|....*....|....
gi 490075866 47 RGTFTAVMGPSGSGKSTL-LQ-CAAGLDRPDSGI 78
Cdd:COG0467 19 RGSSTLLSGPPGTGKTTLaLQfLAEGLRRGEKGL 52
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
155-234 |
4.71e-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: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 155 DQLSGGQRQRVAIARALVTEPRVIFADEPTGALD--TRSARQVLLLLQEAarvhGRTVVMVTHDPVAASYADSVVFLADG 232
Cdd:cd03288 155 ENFSVGQRQLFCLARAFVRKSSILIMDEATASIDmaTENILQKVVMTAFA----DRTVVTIAHRVSTILDADLVLVLSRG 230
|
..
gi 490075866 233 RL 234
Cdd:cd03288 231 IL 232
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
157-253 |
7.20e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 37.46 E-value: 7.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 157 LSGGQRQRVAIARALVTEPRVIFADEPTGALDTRSARQVLLLLQEAARvHGRTVVMVTHD-PVAASYADSVVFLADGRLA 235
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAA-EGKGVIVISSElPELLGMCDRIYVMNEGRIT 483
|
90
....*....|....*...
gi 490075866 236 GRMdaPTPDAVAERLAHL 253
Cdd:NF040905 484 GEL--PREEASQERIMRL 499
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
38-241 |
7.59e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 37.45 E-value: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 38 LDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDGKELTGGGEAELtkfrRGRVGFVFQQYNLLETlTV 117
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLREL----RRQFSMIPQDPVLFDG-TV 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490075866 118 AQNtVLP------------LKLAGRrvdrkRAREVLTSVGLGDRLGHRPDQLSGGQRQRVAIARALVTEPR-VIFADEPT 184
Cdd:PTZ00243 1401 RQN-VDPfleassaevwaaLELVGL-----RERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSgFILMDEAT 1474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490075866 185 GALDTRSARQVLLLLQEAARVHgrTVVMVTHDPVAASYADSVVFLADGRLAgRMDAP 241
Cdd:PTZ00243 1475 ANIDPALDRQIQATVMSAFSAY--TVITIAHRLHTVAQYDKIIVMDHGAVA-EMGSP 1528
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
37-83 |
8.40e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 37.18 E-value: 8.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 490075866 37 ALDGVTLSLGRGTFTAVMGPSGSGKSTLLQCAAGLDRPDSGIVCVDG 83
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG 85
|
|
| |
