|
Name |
Accession |
Description |
Interval |
E-value |
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-258 |
0e+00 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 525.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 1 MAKRIDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTPGGRVEGKVLLDDEDLYGAGIDP 80
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGARVEGEILLDGEDIYDPDVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 81 VSVRREIGMVFQRPNPFPtMSIFDNVAAGLRLNGSYKKSELADIVEKSLKGANLWNEVKDRLNKPGSGLSGGQQQRLCIA 160
Cdd:COG1117 88 VELRRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDEVKDRLKKSALGLSGGQQQRLCIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 161 RAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERFTIVIVTHNMQQAARVSDRTAFFNLaavgqpGKLIEIDDTERI 240
Cdd:COG1117 167 RALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYL------GELVEFGPTEQI 240
|
250
....*....|....*...
gi 512057730 241 FSNPSVQATEDYISGRFG 258
Cdd:COG1117 241 FTNPKDKRTEDYITGRFG 258
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
5-257 |
1.04e-149 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 417.47 E-value: 1.04e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTPGGRVEGKVLLDDEDLYGAGIDPVSVR 84
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPGVRIEGKVLFDGQDIYDKKIDVVELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIGMVFQRPNPFPtMSIFDNVAAGLRLNGSYKKSELADIVEKSLKGANLWNEVKDRLNKPGSGLSGGQQQRLCIARAIA 164
Cdd:TIGR00972 82 RRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALWDEVKDRLHDSALGLSGGQQQRLCIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 165 VEPKVLLMDEPCSALDPISTLAIEDLIGELKERFTIVIVTHNMQQAARVSDRTAFFNLaavgqpGKLIEIDDTERIFSNP 244
Cdd:TIGR00972 161 VEPEVLLLDEPTSALDPIATGKIEELIQELKKKYTIVIVTHNMQQAARISDRTAFFYD------GELVEYGPTEQIFTNP 234
|
250
....*....|...
gi 512057730 245 SVQATEDYISGRF 257
Cdd:TIGR00972 235 KEKRTEDYISGRF 247
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
10-258 |
8.53e-136 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 382.98 E-value: 8.53e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 10 LTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTPGGRVEGKVLLDDEDLYGAGIDPVSVRREIGM 89
Cdd:PRK14243 16 LNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFHGKNLYAPDVDPVEVRRRIGM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 90 VFQRPNPFPTmSIFDNVAAGLRLNGSykKSELADIVEKSLKGANLWNEVKDRLNKPGSGLSGGQQQRLCIARAIAVEPKV 169
Cdd:PRK14243 96 VFQKPNPFPK-SIYDNIAYGARINGY--KGDMDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 170 LLMDEPCSALDPISTLAIEDLIGELKERFTIVIVTHNMQQAARVSDRTAFFNLAAV---GQPGKLIEIDDTERIFSNPSV 246
Cdd:PRK14243 173 ILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTeggGRYGYLVEFDRTEKIFNSPQQ 252
|
250
....*....|..
gi 512057730 247 QATEDYISGRFG 258
Cdd:PRK14243 253 QATRDYVSGRFG 264
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-240 |
2.28e-135 |
|
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: 380.37 E-value: 2.28e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTPGGRVEGKVLLDDEDLYGAGIDPVSVR 84
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIGMVFQRPNPFPtMSIFDNVAAGLRLNGSYKKSELADIVEKSLKGANLWNEVKDRLNkpGSGLSGGQQQRLCIARAIA 164
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRLH--ALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512057730 165 VEPKVLLMDEPCSALDPISTLAIEDLIGELKERFTIVIVTHNMQQAARVSDRTAFFNlaavgqPGKLIEIDDTERI 240
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLL------NGRLVEFGPTEQI 227
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
5-258 |
9.99e-118 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 336.75 E-value: 9.99e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTPGGRVEGKVLLDDEDLYGAGIDPVSVR 84
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSPRTDTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIGMVFQRPNPFPtMSIFDNVAAGLRLNGSYKKSELADIVEKSLKGANLWNEVKDRLNKPGSGLSGGQQQRLCIARAIA 164
Cdd:PRK14239 86 KEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIARVLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 165 VEPKVLLMDEPCSALDPISTLAIEDLIGELKERFTIVIVTHNMQQAARVSDRTAFFnlaavgQPGKLIEIDDTERIFSNP 244
Cdd:PRK14239 165 TSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFF------LDGDLIEYNDTKQMFMNP 238
|
250
....*....|....
gi 512057730 245 SVQATEDYISGRFG 258
Cdd:PRK14239 239 KHKETEDYISGKFG 252
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-258 |
2.93e-101 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 295.21 E-value: 2.93e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 1 MAKRIDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTPGGRVEGKVLLDDEDLYGAGIDP 80
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 81 VSVRREIGMVFQRPNPFPTMSIFDNVAAGLRLNGSYK-KSELADIVEKSLKGANLWNEVKDRLNKPGSGLSGGQQQRLCI 159
Cdd:PRK14267 81 IEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKsKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 160 ARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERFTIVIVTHNMQQAARVSDRTAFFNLaavgqpGKLIEIDDTER 239
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYL------GKLIEVGPTRK 234
|
250
....*....|....*....
gi 512057730 240 IFSNPSVQATEDYISGRFG 258
Cdd:PRK14267 235 VFENPEHELTEKYVTGALG 253
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-258 |
5.56e-94 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 276.92 E-value: 5.56e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTPGGRVEGKVLLDDEDLYGAGIDPVSVR 84
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIGMVFQRPNPFPtMSIFDNVAAGLRLNGSYKKSELADIVEKSLKGANLWNEVKDRLNKPGSGLSGGQQQRLCIARAIA 164
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 165 VEPKVLLMDEPCSALDPISTLAIEDLI--GELKERFTIVIVTHNMQQAARVSDRTAFF--NLAAVGQpgkLIEIDDTERI 240
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgNENRIGQ---LVEFGLTKKI 243
|
250
....*....|....*...
gi 512057730 241 FSNPSVQATEDYISGRFG 258
Cdd:PRK14258 244 FNSPHDSRTREYVLSRLG 261
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-256 |
4.12e-92 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 271.79 E-value: 4.12e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 4 RIDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTPGGRVEGKVLLDDEDLYGagIDPVSV 83
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIFK--MDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 84 RREIGMVFQRPNPFPTMSIFDNVAAGLRLNGSYK-KSELADIVEKSLKGANLWNEVKDRLNKPGSGLSGGQQQRLCIARA 162
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNLSIFENVALGLKLNRLVKsKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 163 IAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERFTIVIVTHNMQQAARVSDRTAFFnlaavgQPGKLIEIDDTERIFS 242
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFL------YKGQIVEWGPTREVFT 234
|
250
....*....|....
gi 512057730 243 NPSVQATEDYISGR 256
Cdd:PRK14247 235 NPRHELTEKYVTGR 248
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-256 |
9.52e-77 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 233.02 E-value: 9.52e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 6 DVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTPGG-RVEGKVLLDDEDLYGagIDPVSVR 84
Cdd:PRK14246 12 NISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKiKVDGKVLYFGKDIFQ--IDAIKLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIGMVFQRPNPFPTMSIFDNVAAGLRLNGSYKKSELADIVEKSLKGANLWNEVKDRLNKPGSGLSGGQQQRLCIARAIA 164
Cdd:PRK14246 90 KEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 165 VEPKVLLMDEPCSALDPISTLAIEDLIGELKERFTIVIVTHNMQQAARVSDRTAFFnlaavgQPGKLIEIDDTERIFSNP 244
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFL------YNGELVEWGSSNEIFTSP 243
|
250
....*....|..
gi 512057730 245 SVQATEDYISGR 256
Cdd:PRK14246 244 KNELTEKYVIGR 255
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-258 |
3.36e-73 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 224.59 E-value: 3.36e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 10 LTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTPGGRVEGKVLLDDEDLYGAGiDPVSVRREIGM 89
Cdd:PRK14271 27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYR-DVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 90 VFQRPNPFPtMSIFDNVAAGLRLNGSYKKSELADIVEKSLKGANLWNEVKDRLNKPGSGLSGGQQQRLCIARAIAVEPKV 169
Cdd:PRK14271 106 LFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 170 LLMDEPCSALDPISTLAIEDLIGELKERFTIVIVTHNMQQAARVSDRTAFFNlaavgqPGKLIEIDDTERIFSNPSVQAT 249
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFF------DGRLVEEGPTEQLFSSPKHAET 258
|
....*....
gi 512057730 250 EDYISGRFG 258
Cdd:PRK14271 259 ARYVAGLSG 267
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-254 |
2.03e-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: 221.41 E-value: 2.03e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAGIDPVSVR 84
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPD-----SGTITVDGEDLTDSKKDINKLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIGMVFQRPNPFPTMSIFDNVAAGLRLNGSYKKSELADIVEKSLK--GanlwneVKDRLNK-PGSgLSGGQQQRLCIAR 161
Cdd:COG1126 77 RKVGMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLErvG------LADKADAyPAQ-LSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 162 AIAVEPKVLLMDEPCSALDPISTLAIEDLIGEL-KERFTIVIVTHNMQQAARVSDRTAFFNlaavgqPGKLIEIDDTERI 240
Cdd:COG1126 150 ALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLaKEGMTMVVVTHEMGFAREVADRVVFMD------GGRIVEEGPPEEF 223
|
250
....*....|....
gi 512057730 241 FSNPSVQATEDYIS 254
Cdd:COG1126 224 FENPQHERTRAFLS 237
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
13-244 |
2.33e-63 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 200.32 E-value: 2.33e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 13 YYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVSVRREIGMVFQ 92
Cdd:COG1125 11 YPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPT-----SGRILIDGEDI--RDLDPVELRRRIGYVIQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 93 RPNPFPTMSIFDNVAAGLRLNGsYKKSELADIVEKSLKGANLW-NEVKDRlnKPgSGLSGGQQQRLCIARAIAVEPKVLL 171
Cdd:COG1125 84 QIGLFPHMTVAENIATVPRLLG-WDKERIRARVDELLELVGLDpEEYRDR--YP-HELSGGQQQRVGVARALAADPPILL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 512057730 172 MDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDRTAFFNlaavgqPGKLIEIDDTERIFSNP 244
Cdd:COG1125 160 MDEPFGALDPITREQLQDELLRLQRELgkTIVFVTHDIDEALKLGDRIAVMR------EGRIVQYDTPEEILANP 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-244 |
5.96e-63 |
|
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: 205.14 E-value: 5.96e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSH-----KAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGA-GI 78
Cdd:COG1123 261 LEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPT-----SGSILFDGKDLTKLsRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 79 DPVSVRREIGMVFQrpNPF----PTMSIFDNVAAGLRLNGSYKKSELADIVEKSLKGANLWNEVKDRLnkPGSgLSGGQQ 154
Cdd:COG1123 336 SLRELRRRVQMVFQ--DPYsslnPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRY--PHE-LSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 155 QRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDRTAFFNLaavgqpGKLI 232
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYLFISHDLAVVRYIADRVAVMYD------GRIV 484
|
250
....*....|..
gi 512057730 233 EIDDTERIFSNP 244
Cdd:COG1123 485 EDGPTEEVFANP 496
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-221 |
2.10e-60 |
|
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: 189.65 E-value: 2.10e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVsvR 84
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPD-----SGEILIDGRDV--TGVPPE--R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIGMVFQRPNPFPTMSIFDNVAAGLRLNGSyKKSELADIVEKSLKGANLwnevKDRLNKPGSGLSGGQQQRLCIARAIA 164
Cdd:cd03259 72 RNIGMVFQDYALFPHLTVAENIAFGLKLRGV-PKAEIRARVRELLELVGL----EGLLNRYPHELSGGQQQRVALARALA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 512057730 165 VEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDRTAFFN 221
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEEALALADRIAVMN 205
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-244 |
6.02e-60 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 193.01 E-value: 6.02e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 1 MAK-RIDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDlygagID 79
Cdd:COG3842 1 MAMpALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPD-----SGRILLDGRD-----VT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 80 PVSV-RREIGMVFQRPNPFPTMSIFDNVAAGLRLNGsYKKSELADIVEKSLKGANLwNEVKDRlnKPGSgLSGGQQQRLC 158
Cdd:COG3842 71 GLPPeKRNVGMVFQDYALFPHLTVAENVAFGLRMRG-VPKAEIRARVAELLELVGL-EGLADR--YPHQ-LSGGQQQRVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 159 IARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDRTAFFNLaavgqpGKLIEIDD 236
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELgiTFIYVTHDQEEALALADRIAVMND------GRIEQVGT 219
|
....*...
gi 512057730 237 TERIFSNP 244
Cdd:COG3842 220 PEEIYERP 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-221 |
7.64e-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: 187.01 E-value: 7.64e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAGIDPVSVR 84
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPD-----SGSILIDGEDLTDLEDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIGMVFQRPNPFPTMSIFDNVAAGLrlngsykkseladivekslkganlwnevkdrlnkpgsglSGGQQQRLCIARAIA 164
Cdd:cd03229 76 RRIGMVFQDFALFPHLTVLENIALGL---------------------------------------SGGQQQRVALARALA 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 512057730 165 VEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDRTAFFN 221
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKSLQAQLgiTVVLVTHDLDEAARLADRVVVLR 175
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-220 |
1.67e-59 |
|
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: 187.35 E-value: 1.67e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAGIDPVSVR 84
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPD-----SGTIIIDGLKLTDDKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIGMVFQRPNPFPTMSIFDNVAAGLRLNGSYKKSELADIVEKSLKGANLwnevKDRLNKPGSGLSGGQQQRLCIARAIA 164
Cdd:cd03262 76 QKVGMVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGL----ADKADAYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 512057730 165 VEPKVLLMDEPCSALDPISTLAIEDLIGEL-KERFTIVIVTHNMQQAARVSDRTAFF 220
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMKDLaEEGMTMVVVTHEMGFAREVADRVIFM 208
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-234 |
2.41e-59 |
|
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: 187.29 E-value: 2.41e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGS----HKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAGidp 80
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPT-----SGEVLVDGEPVTGPG--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 81 vsvrREIGMVFQRPNPFPTMSIFDNVAAGLRLNGSyKKSELADIVEKSLKGANLwnevKDRLNKPGSGLSGGQQQRLCIA 160
Cdd:cd03293 73 ----PDRGYVFQQDALLPWLTVLDNVALGLELQGV-PKAEARERAEELLELVGL----SGFENAYPHQLSGGMRQRVALA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512057730 161 RAIAVEPKVLLMDEPCSALDPISTLAIEDLIGEL--KERFTIVIVTHNMQQAARVSDRTAFFNlaavGQPGKLIEI 234
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDIwrETGKTVLLVTHDIDEAVFLADRVVVLS----ARPGRIVAE 215
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
5-248 |
2.81e-59 |
|
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: 187.88 E-value: 2.81e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAGIDP-VSV 83
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPD-----SGEILVDGQDITGLSEKElYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 84 RREIGMVFQRPNPFPTMSIFDNVAAGLRLNGSYKKSELADIVEKSLKGANLwNEVKDRLnkPgSGLSGGQQQRLCIARAI 163
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGL-PGAADKM--P-SELSGGMRKRVALARAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 164 AVEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDRTAFfnLAAvgqpGKLIEIDDTERIF 241
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAIADRVAV--LAD----GKIIAEGTPEELL 230
|
....*....
gi 512057730 242 --SNPSVQA 248
Cdd:COG1127 231 asDDPWVRQ 239
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-258 |
3.91e-59 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 187.99 E-value: 3.91e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 1 MAKRIDVSGLTAYY----GSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGA 76
Cdd:COG1116 4 AAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPT-----SGEVLVDGKPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 77 GidpvsvrREIGMVFQRPNPFPTMSIFDNVAAGLRLNGsYKKSELADIVEKSLKGANLwnevKDRLNK-PGSgLSGGQQQ 155
Cdd:COG1116 79 G-------PDRGVVFQEPALLPWLTVLDNVALGLELRG-VPKAERRERARELLELVGL----AGFEDAyPHQ-LSGGMRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 156 RLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGEL--KERFTIVIVTHNMQQAARVSDRTAFFNlaavGQPGKLIE 233
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHDVDEAVFLADRVVVLS----ARPGRIVE 221
|
250 260 270
....*....|....*....|....*....|..
gi 512057730 234 IDD-------TERIFSNPSVQATEDYISGRFG 258
Cdd:COG1116 222 EIDvdlprprDRELRTSPEFAALRAEILDLLR 253
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-236 |
1.82e-58 |
|
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: 185.78 E-value: 1.82e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMheVTPggrVEGKVLLDDEDLYGAG-IDPVSV 83
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGL--LRP---DSGEVLIDGEDISGLSeAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 84 RREIGMVFQRPNPFPTMSIFDNVAAGLRLNGSYKKSELADIVEKSLKGANLwnevKDRLNKPGSGLSGGQQQRLCIARAI 163
Cdd:cd03261 76 RRRMGMLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGL----RGAEDLYPAELSGGMKKRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 512057730 164 AVEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDRTAFF---NLAAVGQPGKLIEIDD 236
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELglTSIMVTHDLDTAFAIADRIAVLydgKIVAEGTPEELRASDD 229
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-244 |
1.20e-56 |
|
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: 180.61 E-value: 1.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLT-AYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAgiDPVSV 83
Cdd:COG1122 1 IELENLSfSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPT-----SGEVLVDGKDITKK--NLREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 84 RREIGMVFQrpNP-----FPTmsIFDNVAAGLRLNGsYKKSELADIVEKSLKGANLWnevkDRLNKPGSGLSGGQQQRLC 158
Cdd:COG1122 74 RRKVGLVFQ--NPddqlfAPT--VEEDVAFGPENLG-LPREEIRERVEEALELVGLE----HLADRPPHELSGGQKQRVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 159 IARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERF-TIVIVTHNMQQAARVSDRTAFFNlaavgqPGKLIEIDDT 237
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGkTVIIVTHDLDLVAELADRVIVLD------DGRIVADGTP 218
|
....*..
gi 512057730 238 ERIFSNP 244
Cdd:COG1122 219 REVFSDY 225
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
13-253 |
3.16e-56 |
|
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: 180.19 E-value: 3.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 13 YYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVSVRREIGMVFQ 92
Cdd:cd03295 10 YGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPT-----SGEIFIDGEDI--REQDPVELRRKIGYVIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 93 RPNPFPTMSIFDNVAAGLRLNGsYKKSELADIVEKSLKGANLwnEVKDRLNKPGSGLSGGQQQRLCIARAIAVEPKVLLM 172
Cdd:cd03295 83 QIGLFPHMTVEENIALVPKLLK-WPKEKIRERADELLALVGL--DPAEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 173 DEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDRTAFFNlaavgqPGKLIEIDDTERIFSNPSVQATE 250
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQELgkTIVFVTHDIDEAFRLADRIAIMK------NGEIVQVGTPDEILRSPANDFVA 233
|
...
gi 512057730 251 DYI 253
Cdd:cd03295 234 EFV 236
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-244 |
4.46e-56 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 183.04 E-value: 4.46e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRT---LnrmheVTPGgrvEGKVLLDDEDLYgagIDpV 81
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIiagL-----ETPD---SGRIVLNGRDLF---TN-L 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 82 SVR-REIGMVFQRPNPFPTMSIFDNVAAGLRlNGSYKKSELADIVEKSLKGANLwNEVKDRlnKPgSGLSGGQQQRLCIA 160
Cdd:COG1118 71 PPReRRVGFVFQHYALFPHMTVAENIAFGLR-VRPPSKAEIRARVEELLELVQL-EGLADR--YP-SQLSGGQRQRVALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 161 RAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDRtaffnLAAVGQpGKLIEIDDTE 238
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELggTTVFVTHDQEEALELADR-----VVVMNQ-GRIEQVGTPD 219
|
....*.
gi 512057730 239 RIFSNP 244
Cdd:COG1118 220 EVYDRP 225
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-233 |
8.51e-56 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 178.72 E-value: 8.51e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGagiDPVSVR 84
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPT-----SGEVRVLGEDVAR---DPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIGMVFQRPNPFPTMSIFDNVAAGLRLNGsYKKSELADIVEKSLKGANLWnevkDRLNKPGSGLSGGQQQRLCIARAIA 164
Cdd:COG1131 73 RRIGYVPQEPALYPDLTVRENLRFFARLYG-LPRKEARERIDELLELFGLT----DAADRKVGTLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 512057730 165 VEPKVLLMDEPCSALDPISTLAIEDLIGELKERF-TIVIVTHNMQQAARVSDRTAFFN---LAAVGQPGKLIE 233
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRELAAEGkTVLLSTHYLEEAERLCDRVAIIDkgrIVADGTPDELKA 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-234 |
1.34e-55 |
|
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: 178.08 E-value: 1.34e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYY----GSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAGIDP 80
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPT-----SGSIIFDGKDLLKLSRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 81 VSVRR-EIGMVFQrpNPF----PTMSIFDNVAAGLRLNG-SYKKSELADIVEKSLKGANLwneVKDRLNKPGSGLSGGQQ 154
Cdd:cd03257 77 RKIRRkEIQMVFQ--DPMsslnPRMTIGEQIAEPLRIHGkLSKKEARKEAVLLLLVGVGL---PEEVLNRYPHELSGGQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 155 QRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDRTAFFNLaavgqpGKLI 232
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKIADRVAVMYA------GKIV 225
|
..
gi 512057730 233 EI 234
Cdd:cd03257 226 EE 227
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-254 |
1.93e-55 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 181.04 E-value: 1.93e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYY----GSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDP 80
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPT-----SGSVLVDGVDL--TALSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 81 ---VSVRREIGMVFQRPNPFPTMSIFDNVAAGLRLNGsYKKSELADIVEKSLKGANLwnevKDRLNKPGSGLSGGQQQRL 157
Cdd:COG1135 75 relRAARRKIGMIFQHFNLLSSRTVAENVALPLEIAG-VPKAEIRKRVAELLELVGL----SDKADAYPSQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 158 CIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDRtaffnlAAVGQPGKLIEID 235
Cdd:COG1135 150 GIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELglTIVLITHEMDVVRRICDR------VAVLENGRIVEQG 223
|
250
....*....|....*....
gi 512057730 236 DTERIFSNPSVQATEDYIS 254
Cdd:COG1135 224 PVLDVFANPQSELTRRFLP 242
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-217 |
4.89e-55 |
|
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: 176.14 E-value: 4.89e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGS----HKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAG-ID 79
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPT-----SGEVRVDGTDISKLSeKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 80 PVSVRRE-IGMVFQRPNPFPTMSIFDNVAAGLRLNGSyKKSELADIVEKSLKGANLwnevKDRLNKPGSGLSGGQQQRLC 158
Cdd:cd03255 76 LAAFRRRhIGFVFQSFNLLPDLTALENVELPLLLAGV-PKKERRERAEELLERVGL----GDRLNHYPSELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 512057730 159 IARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMqQAARVSDRT 217
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDP-ELAEYADRI 210
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-244 |
4.22e-53 |
|
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: 174.47 E-value: 4.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYY----GSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEvtPGGRVEGKVLLDDEDLygAGIDP 80
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLP--PPGITSGEILFDGEDL--LKLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 81 VSVR----REIGMVFQrpNPF----PTMSIFDNVAAGLRLNGSYKKSELADIVEKSLKGANLwNEVKDRLNK-PGSgLSG 151
Cdd:COG0444 78 KELRkirgREIQMIFQ--DPMtslnPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGL-PDPERRLDRyPHE-LSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 152 GQQQRLCIARAIAVEPKVLLMDEPCSALDpISTLA-IEDLIGELKERF--TIVIVTHNMQQAARVSDRTAFFNLaavgqp 228
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALD-VTIQAqILNLLKDLQRELglAILFITHDLGVVAEIADRVAVMYA------ 226
|
250
....*....|....*.
gi 512057730 229 GKLIEIDDTERIFSNP 244
Cdd:COG0444 227 GRIVEEGPVEELFENP 242
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-244 |
7.39e-53 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 174.88 E-value: 7.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 1 MAkRIDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDP 80
Cdd:COG3839 1 MA-SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPT-----SGEILIGGRDV--TDLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 81 VsvRREIGMVFQRPNPFPTMSIFDNVAAGLRLNGsYKKSELADIVEKSLKGANLwNEVKDRlnKPgSGLSGGQQQRLCIA 160
Cdd:COG3839 73 K--DRNIAMVFQSYALYPHMTVYENIAFPLKLRK-VPKAEIDRRVREAAELLGL-EDLLDR--KP-KQLSGGQRQRVALG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 161 RAIAVEPKVLLMDEPCSALDPisTLAIEdLIGELKE-----RFTIVIVTHNMQQAARVSDRTAFFNLaavgqpGKLIEID 235
Cdd:COG3839 146 RALVREPKVFLLDEPLSNLDA--KLRVE-MRAEIKRlhrrlGTTTIYVTHDQVEAMTLADRIAVMND------GRIQQVG 216
|
....*....
gi 512057730 236 DTERIFSNP 244
Cdd:COG3839 217 TPEELYDRP 225
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-217 |
1.44e-52 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 170.22 E-value: 1.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 1 MAKRIDVSGLTAYYGS----HKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLnrmhevtpGG--RV-EGKVLLDDEDL 73
Cdd:COG1136 1 MSPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIL--------GGldRPtSGEVLIDGQDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 74 YGAGIDPVSV--RREIGMVFQRPNPFPTMSIFDNVAAGLRLNGsYKKSELADIVEKSLKGANLwnevKDRLNKPGSGLSG 151
Cdd:COG1136 73 SSLSERELARlrRRHIGFVFQFFNLLPELTALENVALPLLLAG-VSRKERRERARELLERVGL----GDRLDHRPSQLSG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 512057730 152 GQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARvSDRT 217
Cdd:COG1136 148 GQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgtTIVMVTHDPELAAR-ADRV 214
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-217 |
4.68e-52 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 168.46 E-value: 4.68e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVSVR 84
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPT-----SGEIYLDGKPL--SAMPPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIGMVFQRPNPFPtmsifDNVAAGLRLNGSYKKSEL-ADIVEKSLKGANLWNEVkdrLNKPGSGLSGGQQQRLCIARAI 163
Cdd:COG4619 74 RQVAYVPQEPALWG-----GTVRDNLPFPFQLRERKFdRERALELLERLGLPPDI---LDKPVERLSGGERQRLALIRAL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 512057730 164 AVEPKVLLMDEPCSALDPISTLAIEDLIGEL--KERFTIVIVTHNMQQAARVSDRT 217
Cdd:COG4619 146 LLQPDVLLLDEPTSALDPENTRRVEELLREYlaEEGRAVLWVSHDPEQIERVADRV 201
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-249 |
8.42e-52 |
|
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: 168.83 E-value: 8.42e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGS----HKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAgiDP 80
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPW-----SGEVTFDGRPVTRR--RR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 81 VSVRREIGMVFQRP----NPFptMSIFDNVAAGLRLNGsykKSELADIVEKSLKGANLWNEVKDRlnKPGSgLSGGQQQR 156
Cdd:COG1124 75 KAFRRRVQMVFQDPyaslHPR--HTVDRILAEPLRIHG---LPDREERIAELLEQVGLPPSFLDR--YPHQ-LSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 157 LCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKER--FTIVIVTHNMQQAARVSDRTAFFnlaavgQPGKLIEI 234
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErgLTYLFVSHDLAVVAHLCDRVAVM------QNGRIVEE 220
|
250
....*....|....*
gi 512057730 235 DDTERIFSNPSVQAT 249
Cdd:COG1124 221 LTVADLLAGPKHPYT 235
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-245 |
1.02e-51 |
|
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: 168.14 E-value: 1.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSH----KAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYG-AGID 79
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPT-----SGSVLVDGTDLTLlSGKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 80 PVSVRREIGMVFQRPNPFPTMSIFDNVAAGLRLNGsYKKSELADIVEKSLKGANLwnevKDRLNKPGSGLSGGQQQRLCI 159
Cdd:cd03258 77 LRKARRRIGMIFQHFNLLSSRTVFENVALPLEIAG-VPKAEIEERVLELLELVGL----EDKADAYPAQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 160 ARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDRtaffnlAAVGQPGKLIEIDDT 237
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRICDR------VAVMEKGEVVEEGTV 225
|
....*...
gi 512057730 238 ERIFSNPS 245
Cdd:cd03258 226 EEVFANPQ 233
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-256 |
5.23e-51 |
|
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: 167.14 E-value: 5.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 4 RIDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVSV 83
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPS-----SGEVLLDGRDL--ASLSRREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 84 RREIGMVFQRPNPFPTMSIFDNVAAG----LRLNGSYKKSELAdIVEKSLKGANLWnEVKDRlnkPGSGLSGGQQQRLCI 159
Cdd:COG1120 74 ARRIAYVPQEPPAPFGLTVRELVALGryphLGLFGRPSAEDRE-AVEEALERTGLE-HLADR---PVDELSGGERQRVLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 160 ARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDRTAFFN---LAAVGQPGKLIEI 234
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERgrTVVMVLHDLNLAARYADRLVLLKdgrIVAQGPPEEVLTP 228
|
250 260
....*....|....*....|..
gi 512057730 235 DDTERIFSNPsVQATEDYISGR 256
Cdd:COG1120 229 ELLEEVYGVE-ARVIEDPVTGR 249
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-221 |
1.17e-50 |
|
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: 164.95 E-value: 1.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 7 VSGLTAYYGSH--KAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMhevtpGGRVEGKVLLDDEDLYGAGIdpVSVR 84
Cdd:cd03225 2 LKNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGL-----LGPTSGEVLVDGKDLTKLSL--KELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIGMVFQrpNP---FPTMSIFDNVAAGLRLNGsYKKSELADIVEKSLKGANLWnevkDRLNKPGSGLSGGQQQRLCIAR 161
Cdd:cd03225 75 RKVGLVFQ--NPddqFFGPTVEEEVAFGLENLG-LPEEEIEERVEEALELVGLE----GLRDRSPFTLSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 512057730 162 AIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSDRTAFFN 221
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDLLLELADRVIVLE 208
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-244 |
1.42e-50 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 165.65 E-value: 1.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 1 MAKRIDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLnrMHEVTPggrVEGKVLLDdedlygaGIDP 80
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAI--LGLLPP---TSGTVRLF-------GKPP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 81 VSVRREIGMVFQRPN---PFPtMSIFDNVAAGL----RLNGSYKKSElADIVEKSLKGANLWnevkDRLNKPGSGLSGGQ 153
Cdd:COG1121 71 RRARRRIGYVPQRAEvdwDFP-ITVRDVVLMGRygrrGLFRRPSRAD-REAVDEALERVGLE----DLADRPIGELSGGQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 154 QQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSDRTAFFN--LAAVGQPGK 230
Cdd:COG1121 145 QQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHDLGAVREYFDRVLLLNrgLVAHGPPEE 224
|
250
....*....|....
gi 512057730 231 LIEIDDTERIFSNP 244
Cdd:COG1121 225 VLTPENLSRAYGGP 238
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-245 |
1.69e-50 |
|
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: 165.10 E-value: 1.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVsvR 84
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPT-----SGEILLDGKDI--TNLPPH--K 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIGMVFQRPNPFPTMSIFDNVAAGLRLNGSyKKSELADIVEKSLKGANLwnevKDRLNKPGSGLSGGQQQRLCIARAIA 164
Cdd:cd03300 72 RPVNTVFQNYALFPHLTVFENIAFGLRLKKL-PKAEIKERVAEALDLVQL----EGYANRKPSQLSGGQQQRVAIARALV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 165 VEPKVLLMDEPCSALDpiSTLAiEDLIGELKE-----RFTIVIVTHNMQQAARVSDRTAFFNlaavgqPGKLIEIDDTER 239
Cdd:cd03300 147 NEPKVLLLDEPLGALD--LKLR-KDMQLELKRlqkelGITFVFVTHDQEEALTMSDRIAVMN------KGKIQQIGTPEE 217
|
....*.
gi 512057730 240 IFSNPS 245
Cdd:cd03300 218 IYEEPA 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-244 |
2.02e-50 |
|
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: 172.40 E-value: 2.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 1 MAKRIDVSGLTAYY--GSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMheVTPGGRVEGKVLLDDEDLYGAgi 78
Cdd:COG1123 1 MTPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGL--LPHGGRISGEVLLDGRDLLEL-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 79 dPVSVR-REIGMVFQRP-NPFPTMSIFDNVAAGLRlNGSYKKSELADIVEKSLKGANLwnevKDRLNKPGSGLSGGQQQR 156
Cdd:COG1123 77 -SEALRgRRIGMVFQDPmTQLNPVTVGDQIAEALE-NLGLSRAEARARVLELLEAVGL----ERRLDRYPHQLSGGQRQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 157 LCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDRTaffnlaAVGQPGKLIEI 234
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIADRV------VVMDDGRIVED 224
|
250
....*....|
gi 512057730 235 DDTERIFSNP 244
Cdd:COG1123 225 GPPEEILAAP 234
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-240 |
7.36e-50 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 163.73 E-value: 7.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAGIDPVSVR 84
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEIT-----SGDLIVDGLKVNDPKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIGMVFQRPNPFPTMSIFDNVAAG-LRLNGSyKKSELADIVEKSLKGANLwnevKDRLNKPGSGLSGGQQQRLCIARAI 163
Cdd:PRK09493 77 QEAGMVFQQFYLFPHLTALENVMFGpLRVRGA-SKEEAEKQARELLAKVGL----AERAHHYPSELSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 164 AVEPKVLLMDEPCSALDP---------ISTLAiedligelKERFTIVIVTHNMQQAARVSDRTAFFN---LAAVGQPGKL 231
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDPelrhevlkvMQDLA--------EEGMTMVIVTHEIGFAEKVASRLIFIDkgrIAEDGDPQVL 223
|
....*....
gi 512057730 232 IEIDDTERI 240
Cdd:PRK09493 224 IKNPPSQRL 232
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-216 |
1.10e-48 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 160.99 E-value: 1.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLT-AYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAGIDPV-S 82
Cdd:COG3638 3 LELRNLSkRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPT-----SGEILVDGQDVTALRGRALrR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 83 VRREIGMVFQRPNPFPTMSIFDNVAAGlRLN---------GSYKKSELAdIVEKSLKGANLwnevKDRLNKPGSGLSGGQ 153
Cdd:COG3638 78 LRRRIGMIFQQFNLVPRLSVLTNVLAG-RLGrtstwrsllGLFPPEDRE-RALEALERVGL----ADKAYQRADQLSGGQ 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 512057730 154 QQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDR 216
Cdd:COG3638 152 QQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgiTVVVNLHQVDLARRYADR 216
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-246 |
6.53e-48 |
|
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: 158.75 E-value: 6.53e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDP-VSV 83
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPT-----SGSVLFDGEDI--TGLPPhEIA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 84 RREIGMVFQRPNPFPTMSIFDNVAAGLRLNGSY---------KKSELADIVEKSLKGANLWnevkDRLNKPGSGLSGGQQ 154
Cdd:cd03219 74 RLGIGRTFQIPRLFPELTVLENVMVAAQARTGSglllararrEEREARERAEELLERVGLA----DLADRPAGELSYGQQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 155 QRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSDRTAFFNLaavgqpGKLIE 233
Cdd:cd03219 150 RRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERgITVLLVEHDMDVVMSLADRVTVLDQ------GRVIA 223
|
250
....*....|...
gi 512057730 234 IDDTERIFSNPSV 246
Cdd:cd03219 224 EGTPDEVRNNPRV 236
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-221 |
1.33e-46 |
|
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: 152.94 E-value: 1.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygaGIDPVSVR 84
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPD-----SGEIKVLGKDI---KKEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIGMVFQRPNPFPTMSIFDNVAaglrlngsykkseladivekslkganlwnevkdrlnkpgsgLSGGQQQRLCIARAIA 164
Cdd:cd03230 73 RRIGYLPEEPSLYENLTVRENLK-----------------------------------------LSGGMKQRLALAQALL 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 512057730 165 VEPKVLLMDEPCSALDPISTLAIEDLIGELKERF-TIVIVTHNMQQAARVSDRTAFFN 221
Cdd:cd03230 112 HDPELLILDEPTSGLDPESRREFWELLRELKKEGkTILLSSHILEEAERLCDRVAILN 169
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-254 |
1.80e-46 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 158.04 E-value: 1.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLT-AYYGSHKAIE---DISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAGIDP 80
Cdd:PRK11153 2 IELKNISkVFPQGGRTIHalnNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPT-----SGRVLVDGQDLTALSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 81 -VSVRREIGMVFQRPNPFPTMSIFDNVAAGLRLNGSYKK------SELADIVEKSlkganlwnevkDRLNKPGSGLSGGQ 153
Cdd:PRK11153 77 lRKARRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAeikarvTELLELVGLS-----------DKADRYPAQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 154 QQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDRTaffnlaAVGQPGKL 231
Cdd:PRK11153 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELglTIVLITHEMDVVKRICDRV------AVIDAGRL 219
|
250 260
....*....|....*....|...
gi 512057730 232 IEIDDTERIFSNPSVQATEDYIS 254
Cdd:PRK11153 220 VEQGTVSEVFSHPKHPLTREFIQ 242
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
5-254 |
3.28e-46 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 154.40 E-value: 3.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMhEVTPGGRVEgkvLLDDEDLYGAGIDPVSV- 83
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLL-EMPRSGTLN---IAGNHFDFSKTPSDKAIr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 84 --RREIGMVFQRPNPFPTMSIFDN-VAAGLRLNGSYKKSELADiVEKSLKGANLwNEVKDRLnkPGSgLSGGQQQRLCIA 160
Cdd:PRK11124 79 elRRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALAR-AEKLLERLRL-KPYADRF--PLH-LSGGQQQRVAIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 161 RAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSDRTAFFnlaavgQPGKLIEIDDTER 239
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETgITQVIVTHEVEVARKTASRVVYM------ENGHIVEQGDASC 227
|
250
....*....|....*
gi 512057730 240 iFSNPSVQATEDYIS 254
Cdd:PRK11124 228 -FTQPQTEAFKNYLS 241
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-216 |
4.04e-46 |
|
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: 151.77 E-value: 4.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGS--HKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVS 82
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPT-----SGEILIDGVDL--RDLDLES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 83 VRREIGMVFQRPNPFpTMSIFDNVaaglrlngsykkseladivekslkganlwnevkdrlnkpgsgLSGGQQQRLCIARA 162
Cdd:cd03228 74 LRKNIAYVPQDPFLF-SGTIRENI------------------------------------------LSGGQRQRIAIARA 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 512057730 163 IAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERFTIVIVTHNMQQAARVsDR 216
Cdd:cd03228 111 LLRDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDA-DR 163
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-177 |
4.99e-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: 4.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 20 IEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAGIDpvSVRREIGMVFQRPNPFPT 99
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPT-----EGTILLDGQDLTDDERK--SLRKEIGYVFQDPQLFPR 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 512057730 100 MSIFDNVAAGLRLnGSYKKSELADIVEKSLKGANLWNEVKDRLNKPGSGLSGGQQQRLCIARAIAVEPKVLLMDEPCS 177
Cdd:pfam00005 74 LTVRENLRLGLLL-KGLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
6-248 |
9.58e-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: 153.66 E-value: 9.58e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 6 DVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVSV-R 84
Cdd:COG0411 6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPT-----SGRILFDGRDI--TGLPPHRIaR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIGMVFQRPNPFPTMSIFDNVAAGL--RLNGSYKKS------------ELADIVEKSLKGANLwnevKDRLNKPGSGLS 150
Cdd:COG0411 79 LGIARTFQNPRLFPELTVLENVLVAAhaRLGRGLLAAllrlprarreerEARERAEELLERVGL----ADRADEPAGNLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 151 GGQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDRTAFFNLaavgqp 228
Cdd:COG0411 155 YGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERgiTILLIEHDMDLVMGLADRIVVLDF------ 228
|
250 260
....*....|....*....|
gi 512057730 229 GKLIEIDDTERIFSNPSVQA 248
Cdd:COG0411 229 GRVIAEGTPAEVRADPRVIE 248
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-216 |
1.74e-45 |
|
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: 151.82 E-value: 1.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLnrMHEVTPggrVEGKVLLDDEDLygAGIDPVS-V 83
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTI--MGLLPP---RSGSIRFDGRDI--TGLPPHErA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 84 RREIGMVFQRPNPFPTMSIFDNVAAGLRLNgsyKKSELADIVEKSLkgaNLWNEVKDRLNKPGSGLSGGQQQRLCIARAI 163
Cdd:cd03224 74 RAGIGYVPEGRRIFPELTVEENLLLGAYAR---RRAKRKARLERVY---ELFPRLKERRKQLAGTLSGGEQQMLAIARAL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 512057730 164 AVEPKVLLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSDR 216
Cdd:cd03224 148 MSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEgVTILLVEQNARFALEIADR 201
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-251 |
1.90e-45 |
|
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: 152.34 E-value: 1.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGS-HKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAGIDPV-S 82
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPT-----SGSVLIDGTDINKLKGKALrQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 83 VRREIGMVFQRPNPFPTMSIFDNVAAGlRLN---------GSYKKSELADIVEkSLKGANLwnevKDRLNKPGSGLSGGQ 153
Cdd:cd03256 76 LRRQIGMIFQQFNLIERLSVLENVLSG-RLGrrstwrslfGLFPKEEKQRALA-ALERVGL----LDKAYQRADQLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 154 QQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDRtaffnlaavgqpgkL 231
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLAREYADR--------------I 215
|
250 260
....*....|....*....|
gi 512057730 232 IEIDDTERIFSNPSVQATED 251
Cdd:cd03256 216 VGLKDGRIVFDGPPAELTDE 235
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-254 |
3.86e-45 |
|
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: 152.41 E-value: 3.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 19 AIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVSV----RREIGMVFQRP 94
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPT-----SGKVLIDGQDI--AAMSRKELrelrRKKISMVFQSF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 95 NPFPTMSIFDNVAAGLRLNGSYKKSELADIVEkSLKGANLwnevKDRLNKPGSGLSGGQQQRLCIARAIAVEPKVLLMDE 174
Cdd:cd03294 112 ALLPHRTVLENVAFGLEVQGVPRAEREERAAE-ALELVGL----EGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 175 PCSALDPISTLAIEDLIGEL--KERFTIVIVTHNMQQAARVSDRTAFFnlaavgQPGKLIEIDDTERIFSNPSvqatEDY 252
Cdd:cd03294 187 AFSALDPLIRREMQDELLRLqaELQKTIVFITHDLDEALRLGDRIAIM------KDGRLVQVGTPEEILTNPA----NDY 256
|
..
gi 512057730 253 IS 254
Cdd:cd03294 257 VR 258
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
15-255 |
2.38e-44 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 153.08 E-value: 2.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 15 GSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVSV----RREIGMV 90
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPT-----AGQIFIDGENI--MKQSPVELrevrRKKIGMV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 91 FQRPNPFPTMSIFDNVAAGLRLNGsYKKSELADIVEKSLKGANLWNEVKDRLNKpgsgLSGGQQQRLCIARAIAVEPKVL 170
Cdd:TIGR01186 77 FQQFALFPHMTILQNTSLGPELLG-WPEQERKEKALELLKLVGLEEYEHRYPDE----LSGGMQQRVGLARALAAEPDIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 171 LMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDRTAFFnlaavgQPGKLIEIDDTERIFSNPSVQA 248
Cdd:TIGR01186 152 LMDEAFSALDPLIRDSMQDELKKLQATLqkTIVFITHDLDEAIRIGDRIVIM------KAGEIVQVGTPDEILRNPANEY 225
|
....*..
gi 512057730 249 TEDYISG 255
Cdd:TIGR01186 226 VEEFIGK 232
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-205 |
5.82e-44 |
|
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: 157.69 E-value: 5.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 4 RIDVSGLTAYYGSHK--AIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPV 81
Cdd:COG2274 473 DIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT-----SGRILIDGIDL--RQIDPA 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 82 SVRREIGMVFQRPNPFPTmSIFDNVAAGlrlngsYKKSELADIVEkSLKGANLWNEVK---DRLNKP----GSGLSGGQQ 154
Cdd:COG2274 546 SLRRQIGVVLQDVFLFSG-TIRENITLG------DPDATDEEIIE-AARLAGLHDFIEalpMGYDTVvgegGSNLSGGQR 617
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 512057730 155 QRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERFTIVIVTH 205
Cdd:COG2274 618 QRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAH 668
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-231 |
7.48e-44 |
|
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: 147.52 E-value: 7.48e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTPG-GRVEGkvllddedlYGAGIDPVSV 83
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGrATVAG---------HDVVREPREV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 84 RREIGMVFQRPNPFPTMSIFDNVAAGLRLNGsYKKSELADIVEKSLKGANLWnEVKDRLNKPgsgLSGGQQQRLCIARAI 163
Cdd:cd03265 72 RRRIGIVFQDLSVDDELTGWENLYIHARLYG-VPGAERRERIDELLDFVGLL-EAADRLVKT---YSGGMRRRLEIARSL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 512057730 164 AVEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDRTAFFN---LAAVGQPGKL 231
Cdd:cd03265 147 VHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAEQLCDRVAIIDhgrIIAEGTPEEL 219
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-229 |
9.27e-44 |
|
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: 147.02 E-value: 9.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVsvR 84
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPT-----SGRIYIGGRDV--TDLPPK--D 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIGMVFQRPNPFPTMSIFDNVAAGLRLNGSYKkselADIVEKSLKGANLWnEVKDRLNKPGSGLSGGQQQRLCIARAIA 164
Cdd:cd03301 72 RDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPK----DEIDERVREVAELL-QIEHLLDRKPKQLSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 512057730 165 VEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDRTAFFNLAAVGQPG 229
Cdd:cd03301 147 REPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLgtTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-237 |
1.17e-43 |
|
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: 147.87 E-value: 1.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGagidpVSVR 84
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPD-----SGTILFGGEDATD-----VPVQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 -REIGMVFQRPNPFPTMSIFDNVAAGLRLNgsyKKSELADIVEKSLKGANLWNEVK-DRL-NKPGSGLSGGQQQRLCIAR 161
Cdd:cd03296 73 eRNVGFVFQHYALFRHMTVFDNVAFGLRVK---PRSERPPEAEIRAKVHELLKLVQlDWLaDRYPAQLSGGQRQRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 512057730 162 AIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDRTAFFNLAAVGQPGKLIEIDDT 237
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELhvTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
5-254 |
2.20e-43 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 147.08 E-value: 2.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMhEVTPGGRVEgkvLLDDEDLYGAGIDP---V 81
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLL-ETPDSGQLN---IAGHQFDFSQKPSEkaiR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 82 SVRREIGMVFQRPNPFPTMSIFDN-VAAGLRLNGSYKKS--ELADIVEKSLKganlwneVKDRLNKPGSGLSGGQQQRLC 158
Cdd:COG4161 79 LLRQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQarEKAMKLLARLR-------LTDKADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 159 IARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSDRTAFFnlaavgQPGKLIEIDDT 237
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTgITQVIVTHEVEFARKVASQVVYM------EKGRIIEQGDA 225
|
250
....*....|....*..
gi 512057730 238 ErIFSNPSVQATEDYIS 254
Cdd:COG4161 226 S-HFTQPQTEAFAHYLS 241
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-221 |
6.51e-43 |
|
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: 143.15 E-value: 6.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 7 VSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVSVRRE 86
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT-----SGEILIDGKDI--AKLPLEELRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 87 IGMVFQrpnpfptmsifdnvaaglrlngsykkseladivekslkganlwnevkdrlnkpgsgLSGGQQQRLCIARAIAVE 166
Cdd:cd00267 75 IGYVPQ--------------------------------------------------------LSGGQRQRVALARALLLN 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 512057730 167 PKVLLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSDRTAFFN 221
Cdd:cd00267 99 PDLLLLDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAADRVIVLK 154
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-253 |
8.58e-43 |
|
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: 145.52 E-value: 8.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGS-HKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGA-GIDPVS 82
Cdd:TIGR02315 2 LEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPS-----SGSILLEGTDITKLrGKKLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 83 VRREIGMVFQRPNPFPTMSIFDNVAAGlRLN---------GSYKKSELADIVEkSLKGANLwnevKDRLNKPGSGLSGGQ 153
Cdd:TIGR02315 77 LRRRIGMIFQHYNLIERLTVLENVLHG-RLGykptwrsllGRFSEEDKERALS-ALERVGL----ADKAYQRADQLSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 154 QQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDRtaffnlaavgqpgkL 231
Cdd:TIGR02315 151 QQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDgiTVIINLHQVDLAKKYADR--------------I 216
|
250 260
....*....|....*....|..
gi 512057730 232 IEIDDTERIFSNPSVQATEDYI 253
Cdd:TIGR02315 217 VGLKAGEIVFDGAPSELDDEVL 238
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
5-244 |
3.19e-42 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 146.42 E-value: 3.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYY-----------GSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDL 73
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPT-----SGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 74 YGA-GIDPVSVRREIGMVFQrpNPF----PTMSIFDNVAAGLRLNGSYKKSELADIVEKSLKGANLWNEVKDRLnkPGSg 148
Cdd:COG4608 83 TGLsGRELRPLRRRMQMVFQ--DPYaslnPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRY--PHE- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 149 LSGGQQQRLCIARAIAVEPKVLLMDEPCSALDpISTLA-IEDLIGELKERF--TIVIVTHNMQQAARVSDRTAFFNLaav 225
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALD-VSIQAqVLNLLEDLQDELglTYLFISHDLSVVRHISDRVAVMYL--- 233
|
250
....*....|....*....
gi 512057730 226 gqpGKLIEIDDTERIFSNP 244
Cdd:COG4608 234 ---GKIVEIAPRDELYARP 249
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-221 |
3.52e-42 |
|
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: 143.06 E-value: 3.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 7 VSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLnrMHEVTPggrVEGKVLLDdedlygaGIDPVSVRRE 86
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAI--LGLLKP---TSGSIRVF-------GKPLEKERKR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 87 IGMVFQRPN---PFPtMSIFDNVAAGL----RLNGSYKKSElADIVEKSLKGANLwNEVKDRlnkPGSGLSGGQQQRLCI 159
Cdd:cd03235 70 IGYVPQRRSidrDFP-ISVRDVVLMGLyghkGLFRRLSKAD-KAKVDEALERVGL-SELADR---QIGELSGGQQQRVLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 512057730 160 ARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSDRTAFFN 221
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEYFDRVLLLN 206
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-205 |
8.17e-42 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 150.32 E-value: 8.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 12 AYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVSVRREIGMVF 91
Cdd:COG1132 348 SYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPT-----SGRILIDGVDI--RDLTLESLRRQIGVVP 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 92 QRPNPFpTMSIFDNVAAGlRLNGSykkseLADIVEkSLKGANLWNEVKD-------RLNKPGSGLSGGQQQRLCIARAIA 164
Cdd:COG1132 421 QDTFLF-SGTIRENIRYG-RPDAT-----DEEVEE-AAKAAQAHEFIEAlpdgydtVVGERGVNLSGGQRQRIAIARALL 492
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 512057730 165 VEPKVLLMDEPCSALDPISTLAIEDLIGELKERFTIVIVTH 205
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAH 533
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
6-216 |
3.51e-41 |
|
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: 141.27 E-value: 3.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 6 DVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVS-VR 84
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPR-----SGSIRFDGEDI--TGLPPHRiAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIGMVFQRPNPFPTMSIFDNVAAGLRLNGSykKSELADIVEKSLkgaNLWNEVKDRLNKPGSGLSGGQQQRLCIARAIA 164
Cdd:COG0410 78 LGIGYVPEGRRIFPSLTVEENLLLGAYARRD--RAEVRADLERVY---ELFPRLKERRRQRAGTLSGGEQQMLAIGRALM 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 512057730 165 VEPKVLLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSDR 216
Cdd:COG0410 153 SRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREgVTILLVEQNARFALEIADR 205
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
13-213 |
5.41e-41 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 140.19 E-value: 5.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 13 YYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVSV---RREIGM 89
Cdd:COG2884 11 YPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPT-----SGQVLVNGQDL--SRLKRREIpylRRRIGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 90 VFQRPNPFPTMSIFDNVAAGLRLNGsYKKSELADIVEKSLKGANLwnevKDRLNKPGSGLSGGQQQRLCIARAIAVEPKV 169
Cdd:COG2884 84 VFQDFRLLPDRTVYENVALPLRVTG-KSRKEIRRRVREVLDLVGL----SDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 512057730 170 LLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNM----QQAARV 213
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEINRRgTTVLIATHDLelvdRMPKRV 207
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
17-244 |
5.42e-41 |
|
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: 141.82 E-value: 5.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 17 HKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLY-GAGIDPVSVRREIGMVFQrpn 95
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPT-----SGTVTIDGRDITaKKKKKLKDLRKKVGLVFQ--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 96 pFPTMSIF-----DNVAAGLRlNGSYKKSELADIVEKSLKGANLWNEVKDRlnkpgS--GLSGGQQQRLCIARAIAVEPK 168
Cdd:TIGR04521 90 -FPEHQLFeetvyKDIAFGPK-NLGLSEEEAEERVKEALELVGLDEEYLER-----SpfELSGGQMRRVAIAGVLAMEPE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 512057730 169 VLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDRtaffnlAAVGQPGKLIEIDDTERIFSNP 244
Cdd:TIGR04521 163 VLILDEPTAGLDPKGRKEILDLFKRLHKEKglTVILVTHSMEDVAEYADR------VIVMHKGKIVLDGTPREVFSDV 234
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
19-253 |
6.24e-41 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 144.48 E-value: 6.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 19 AIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVS---VRRE-IGMVFQRP 94
Cdd:COG4175 42 GVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPT-----AGEVLIDGEDI--TKLSKKElreLRRKkMSMVFQHF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 95 NPFPTMSIFDNVAAGLRLNGsYKKSELADIVEKSLKGANLwnevKDRLNKPGSGLSGGQQQRLCIARAIAVEPKVLLMDE 174
Cdd:COG4175 115 ALLPHRTVLENVAFGLEIQG-VPKAERRERAREALELVGL----AGWEDSYPDELSGGMQQRVGLARALATDPDILLMDE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 175 PCSALDPIstlaI-----EDLIgELKERF--TIVIVTHNMQQAARVSDRTAFFnlaavgQPGKLIEIDDTERIFSNPsvq 247
Cdd:COG4175 190 AFSALDPL----IrremqDELL-ELQAKLkkTIVFITHDLDEALRLGDRIAIM------KDGRIVQIGTPEEILTNP--- 255
|
....*.
gi 512057730 248 ATeDYI 253
Cdd:COG4175 256 AN-DYV 260
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-234 |
3.08e-40 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 142.39 E-value: 3.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVsvR 84
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPD-----SGRIMLDGQDI--THVPAE--N 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIGMVFQRPNPFPTMSIFDNVAAGLRLNGSyKKSELADIVEKSLKGANLwNEVKDRlnKPgSGLSGGQQQRLCIARAIA 164
Cdd:PRK09452 86 RHVNTVFQSYALFPHMTVFENVAFGLRMQKT-PAAEITPRVMEALRMVQL-EEFAQR--KP-HQLSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 512057730 165 VEPKVLLMDEPCSALDPISTLAIEDligELK--ER---FTIVIVTHNMQQAARVSDRTAFFNLAAVGQPGKLIEI 234
Cdd:PRK09452 161 NKPKVLLLDESLSALDYKLRKQMQN---ELKalQRklgITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
36-245 |
4.47e-40 |
|
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: 141.09 E-value: 4.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 36 IGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygagIDPVSVRREIGMVFQRPNPFPTMSIFDNVAAGLRLNGS 115
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPD-----SGSIMLDGEDV----TNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 116 yKKSELADIVEKSLKGANLwNEVKDRlnKPgSGLSGGQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELK 195
Cdd:TIGR01187 73 -PRAEIKPRVLEALRLVQL-EEFADR--KP-HQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 512057730 196 ERF--TIVIVTHNMQQAARVSDRTAFFNlaavgqPGKLIEIDDTERIFSNPS 245
Cdd:TIGR01187 148 EQLgiTFVFVTHDQEEAMTMSDRIAIMR------KGKIAQIGTPEEIYEEPA 193
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
5-254 |
6.97e-40 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 138.34 E-value: 6.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMhEVTPGGRVE-GKVLLDDEDLYGAGIDPV-S 82
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLL-EQPEAGTIRvGDITIDTARSLSQQKGLIrQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 83 VRREIGMVFQRPNPFPTMSIFDNVAAGlrlngsykkselADIVEKSLKGANLwNEVKDRLNKPG-SG--------LSGGQ 153
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIEG------------PVIVKGEPKEEAT-ARARELLAKVGlAGketsyprrLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 154 QQRLCIARAIAVEPKVLLMDEPCSALDPistlaieDLIGEL--------KERFTIVIVTHNMQQAARVSDRTAFFNlaav 225
Cdd:PRK11264 150 QQRVAIARALAMRPEVILFDEPTSALDP-------ELVGEVlntirqlaQEKRTMVIVTHEMSFARDVADRAIFMD---- 218
|
250 260
....*....|....*....|....*....
gi 512057730 226 gqPGKLIEIDDTERIFSNPSVQATEDYIS 254
Cdd:PRK11264 219 --QGRIVEQGPAKALFADPQQPRTRQFLE 245
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-245 |
1.18e-39 |
|
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: 137.47 E-value: 1.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKaIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLnrMHEVTPGGrveGKVLLDDEDLygAGIDPVsvR 84
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETI--AGFIKPDS---GKILLNGKDI--TNLPPE--K 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIGMVFQRPNPFPTMSIFDNVAAGLRLngsyKKSELADIVEKSLKGANLWN--EVKDRlnKPGSgLSGGQQQRLCIARA 162
Cdd:cd03299 71 RDISYVPQNYALFPHMTVYKNIAYGLKK----RKVDKKEIERKVLEIAEMLGidHLLNR--KPET-LSGGEQQRVAIARA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 163 IAVEPKVLLMDEPCSALDPistLAIEDLIGELKE-----RFTIVIVTHNMQQAARVSDRTAFFNlaavgqPGKLIEIDDT 237
Cdd:cd03299 144 LVVNPKILLLDEPFSALDV---RTKEKLREELKKirkefGVTVLHVTHDFEEAWALADKVAIML------NGKLIQVGKP 214
|
....*...
gi 512057730 238 ERIFSNPS 245
Cdd:cd03299 215 EEVFKKPK 222
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
10-245 |
4.00e-39 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 139.08 E-value: 4.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 10 LTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAGIDpvsvRREIGM 89
Cdd:PRK11432 12 ITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPT-----EGQIFIDGEDVTHRSIQ----QRDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 90 VFQRPNPFPTMSIFDNVAAGLRLNGsYKKSELADIVEKSLKGANLwNEVKDRLNKPgsgLSGGQQQRLCIARAIAVEPKV 169
Cdd:PRK11432 83 VFQSYALFPHMSLGENVGYGLKMLG-VPKEERKQRVKEALELVDL-AGFEDRYVDQ---ISGGQQQRVALARALILKPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 512057730 170 LLMDEPCSALDPISTLAIEDLIGELKERFTI--VIVTHNMQQAARVSDRTAFFNlaavgqPGKLIEIDDTERIFSNPS 245
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIRELQQQFNItsLYVTHDQSEAFAVSDTVIVMN------KGKIMQIGSPQELYRQPA 229
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
5-245 |
5.93e-39 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 136.08 E-value: 5.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNrMHEvTPGgrvEGKVLLDDE----------DLY 74
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCIN-LLE-TPD---SGEIRVGGEeirlkpdrdgELV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 75 GAGIDPV-SVRREIGMVFQRPNPFPTMSIFDNVAAG----LRLNgsykKSELADIVEKSLKGANLWnevkDRLNKPGSGL 149
Cdd:COG4598 84 PADRRQLqRIRTRLGMVFQSFNLWSHMTVLENVIEApvhvLGRP----KAEAIERAEALLAKVGLA----DKRDAYPAHL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 150 SGGQQQRLCIARAIAVEPKVLLMDEPCSALDPistlaieDLIGE-LK-------ERFTIVIVTHNMQQAARVSDRTAFFN 221
Cdd:COG4598 156 SGGQQQRAAIARALAMEPEVMLFDEPTSALDP-------ELVGEvLKvmrdlaeEGRTMLVVTHEMGFARDVSSHVVFLH 228
|
250 260
....*....|....*....|....
gi 512057730 222 LaavgqpGKLIEIDDTERIFSNPS 245
Cdd:COG4598 229 Q------GRIEEQGPPAEVFGNPK 246
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-219 |
6.15e-39 |
|
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: 133.71 E-value: 6.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 6 DVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVSVRR 85
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPS-----SGEILLDGKDL--ASLSPKELAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 86 EIGMVFQrpnpfpTMSIFDnvaaglrlngsykkseLADIVEKSlkganlWNEvkdrlnkpgsgLSGGQQQRLCIARAIAV 165
Cdd:cd03214 74 KIAYVPQ------ALELLG----------------LAHLADRP------FNE-----------LSGGERQRVLLARALAQ 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 512057730 166 EPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDRTAF 219
Cdd:cd03214 115 EPPILLLDEPTSHLDIAHQIELLELLRRLARERgkTVVMVLHDLNLAARYADRVIL 170
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-213 |
2.45e-38 |
|
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: 140.66 E-value: 2.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLT-AYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVSV 83
Cdd:COG4988 337 IELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPY-----SGSILINGVDL--SDLDPASW 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 84 RREIGMVFQRPNPFPTmSIFDNVAAGlRLNGSykKSELADIVEKslkgANLWNEVK---DRLNKP----GSGLSGGQQQR 156
Cdd:COG4988 410 RRQIAWVPQNPYLFAG-TIRENLRLG-RPDAS--DEELEAALEA----AGLDEFVAalpDGLDTPlgegGRGLSGGQAQR 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 157 LCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERFTIVIVTH---NMQQAARV 213
Cdd:COG4988 482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHrlaLLAQADRI 541
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
23-253 |
4.36e-38 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 132.96 E-value: 4.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 23 ISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMheVTPGGrveGKVLLDDEDLYGAGID--PVSvrreigMVFQRPNPFPTM 100
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGF--LPPDS---GRILWNGQDLTALPPAerPVS------MLFQENNLFPHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 101 SIFDNVA----AGLRLNGSyKKSELADIVEK-SLKGanlwneVKDRlnKPGSgLSGGQQQRLCIARAIAVEPKVLLMDEP 175
Cdd:COG3840 87 TVAQNIGlglrPGLKLTAE-QRAQVEQALERvGLAG------LLDR--LPGQ-LSGGQRQRVALARCLVRKRPILLLDEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 176 CSALDPIstLAIE--DLIGEL-KER-FTIVIVTHNMQQAARVSDRTAFfnlaaVGQpGKLIEIDDTERIFSNPSVQATED 251
Cdd:COG3840 157 FSALDPA--LRQEmlDLVDELcRERgLTVLMVTHDPEDAARIADRVLL-----VAD-GRIAADGPTAALLDGEPPPALAA 228
|
..
gi 512057730 252 YI 253
Cdd:COG3840 229 YL 230
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-231 |
2.64e-37 |
|
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: 130.70 E-value: 2.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGS--HKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygaGIDPVS 82
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPT-----SGTAYINGYSI---RTDRKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 83 VRREIGMVFQRPNPFPTMSIFDNVAAGLRLNGsYKKSELADIVEKSLKGANLwnevKDRLNKPGSGLSGGQQQRLCIARA 162
Cdd:cd03263 73 ARQSLGYCPQFDALFDELTVREHLRFYARLKG-LPKSEIKEEVELLLRVLGL----TDKANKRARTLSGGMKRKLSLAIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512057730 163 IAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERFTIVIVTHNMQQAARVSDRTAFFN---LAAVGQPGKL 231
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSdgkLRCIGSPQEL 219
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-253 |
3.55e-37 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 134.58 E-value: 3.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVsvR 84
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPT-----AGQIMLDGVDL--SHVPPY--Q 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIGMVFQRPNPFPTMSIFDNVAAGLRLNgSYKKSELADIVEKSLKGANLwNEVKDRlnKPGSgLSGGQQQRLCIARAIA 164
Cdd:PRK11607 91 RPINMMFQSYALFPHMTVEQNIAFGLKQD-KLPKAEIASRVNEMLGLVHM-QEFAKR--KPHQ-LSGGQRQRVALARSLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 165 VEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDRTAFFNlaavgqPGKLIEIDDTERIFS 242
Cdd:PRK11607 166 KRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVgvTCVMVTHDQEEAMTMAGRIAIMN------RGKFVQIGEPEEIYE 239
|
250
....*....|.
gi 512057730 243 NPSVQATEDYI 253
Cdd:PRK11607 240 HPTTRYSAEFI 250
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-234 |
6.83e-37 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 133.24 E-value: 6.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 1 MAKRIDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAgidP 80
Cdd:TIGR03265 1 SSPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQT-----AGTIYQGGRDITRL---P 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 81 VSvRREIGMVFQRPNPFPTMSIFDNVAAGLRlNGSYKKSELADIVekslkganlwNEVKDRLNKPGSG------LSGGQQ 154
Cdd:TIGR03265 73 PQ-KRDYGIVFQSYALFPNLTVADNIAYGLK-NRGMGRAEVAERV----------AELLDLVGLPGSErkypgqLSGGQQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 155 QRLCIARAIAVEPKVLLMDEPCSALDpisTLAIEDLIGELKE-----RFTIVIVTHNMQQAARVSDRTAFFNLAAVGQPG 229
Cdd:TIGR03265 141 QRVALARALATSPGLLLLDEPLSALD---ARVREHLRTEIRQlqrrlGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVG 217
|
....*
gi 512057730 230 KLIEI 234
Cdd:TIGR03265 218 TPQEI 222
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-233 |
8.26e-37 |
|
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: 136.43 E-value: 8.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 4 RIDVSGLTAYY--GSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPV 81
Cdd:COG4987 333 SLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQ-----SGSITLGGVDL--RDLDED 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 82 SVRREIGMVFQRPNPFPTmSIFDNvaagLRL---NGS-------YKKSELADIVEKSLKGANLWneVKDRlnkpGSGLSG 151
Cdd:COG4987 406 DLRRRIAVVPQRPHLFDT-TLREN----LRLarpDATdeelwaaLERVGLGDWLAALPDGLDTW--LGEG----GRRLSG 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 152 GQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAI-EDLIGELKERfTIVIVTHNMQQAARVsDRTAFFN---LAAVGQ 227
Cdd:COG4987 475 GERRRLALARALLRDAPILLLDEPTEGLDAATEQALlADLLEALAGR-TVLLITHRLAGLERM-DRILVLEdgrIVEQGT 552
|
....*.
gi 512057730 228 PGKLIE 233
Cdd:COG4987 553 HEELLA 558
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-233 |
1.14e-36 |
|
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: 129.58 E-value: 1.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 17 HKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVSVRREIGMVFQRPNP 96
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPT-----SGEILLDGVDI--RDLNLRWLRSQIGLVSQEPVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 97 FPTmSIFDNVAAGlrlngsyKKSELADIVEKSLKGANLWN-----------EVKDRlnkpGSGLSGGQQQRLCIARAIAV 165
Cdd:cd03249 89 FDG-TIAENIRYG-------KPDATDEEVEEAAKKANIHDfimslpdgydtLVGER----GSQLSGGQKQRIAIARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 512057730 166 EPKVLLMDEPCSALDPISTLAIEDLIGELKERFTIVIVTHNMqQAARVSDRTAFFnlaavgQPGKLIE 233
Cdd:cd03249 157 NPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRL-STIRNADLIAVL------QNGQVVE 217
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-220 |
2.77e-36 |
|
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: 127.80 E-value: 2.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 22 DISMTVePRTVTAFIGPSGCGKSTFLRTLNRMhEVTPGGRVE--GKVLLDDEDlygaGIDPVSVRREIGMVFQRPNPFPT 99
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGL-EKPDGGTIVlnGTVLFDSRK----KINLPPQQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 100 MSIFDNVAAGLRLNGSykkSELADIVEKSLKGANLwNEVKDRlnkPGSGLSGGQQQRLCIARAIAVEPKVLLMDEPCSAL 179
Cdd:cd03297 90 LNVRENLAFGLKRKRN---REDRISVDELLDLLGL-DHLLNR---YPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 512057730 180 DPISTLAIEDLIGELKERFTI--VIVTHNMQQAARVSDRTAFF 220
Cdd:cd03297 163 DRALRLQLLPELKQIKKNLNIpvIFVTHDLSEAEYLADRIVVM 205
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-244 |
3.53e-36 |
|
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: 131.38 E-value: 3.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 22 DISMTVEPRTVTAFIGPSGCGKSTFLRT---LNRmhevTPGGRVE--GKVLLDDEdlygAGID-PVSvRREIGMVFQRPN 95
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLER----PDSGRIRlgGEVLQDSA----RGIFlPPH-RRRIGYVFQEAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 96 PFPTMSIFDNVAAGL-RLNGSYKKSELADIVEksLKG-ANLwnevkdrLNKPGSGLSGGQQQRLCIARAIAVEPKVLLMD 173
Cdd:COG4148 88 LFPHLSVRGNLLYGRkRAPRAERRISFDEVVE--LLGiGHL-------LDRRPATLSGGERQRVAIGRALLSSPRLLLMD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 512057730 174 EPCSALDPISTLAIEDLIGELKERFTI--VIVTHNMQQAARVSDRTAFfnLAAvgqpGKLIEIDDTERIFSNP 244
Cdd:COG4148 159 EPLAALDLARKAEILPYLERLRDELDIpiLYVSHSLDEVARLADHVVL--LEQ----GRVVASGPLAEVLSRP 225
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
13-231 |
7.80e-36 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 129.05 E-value: 7.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 13 YYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTPG-GRVEGkvllddedlYGAGIDPVSVRREIGMVF 91
Cdd:TIGR01188 2 VYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGtARVAG---------YDVVREPRKVRRSIGIVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 92 QRPNPFPTMSIFDNVAAGLRLNGsYKKSELADIVEKSLKGANLWnevkDRLNKPGSGLSGGQQQRLCIARAIAVEPKVLL 171
Cdd:TIGR01188 73 QYASVDEDLTGRENLEMMGRLYG-LPKDEAEERAEELLELFELG----EAADRPVGTYSGGMRRRLDIAASLIHQPDVLF 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 512057730 172 MDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSDRTAFFN---LAAVGQPGKL 231
Cdd:TIGR01188 148 LDEPTTGLDPRTRRAIWDYIRALKEEgVTILLTTHYMEEADKLCDRIAIIDhgrIIAEGTPEEL 211
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
5-245 |
9.83e-36 |
|
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: 127.93 E-value: 9.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLT-AYYGSHK-AIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMheVTPggrVEGKVLLDdedlygaGIDPVS 82
Cdd:TIGR04520 1 IEVENVSfSYPESEKpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGL--LLP---TSGKVTVD-------GLDTLD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 83 ------VRREIGMVFQRP-NPFPTMSIFDNVAAGLRlNGSYKKSELADIVEKSLKGANLWnevkDRLNKPGSGLSGGQQQ 155
Cdd:TIGR04520 69 eenlweIRKKVGMVFQNPdNQFVGATVEDDVAFGLE-NLGVPREEMRKRVDEALKLVGME----DFRDREPHLLSGGQKQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 156 RLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARvSDRTAFFNlaavgqPGKLIE 233
Cdd:TIGR04520 144 RVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEAVL-ADRVIVMN------KGKIVA 216
|
250
....*....|..
gi 512057730 234 IDDTERIFSNPS 245
Cdd:TIGR04520 217 EGTPREIFSQVE 228
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-217 |
1.42e-35 |
|
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: 132.80 E-value: 1.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 2 AKRIDVSGLT-AYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDP 80
Cdd:TIGR02857 319 ASSLEFSGVSvAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT-----EGSIAVNGVPL--ADADA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 81 VSVRREIGMVFQRPNPFPTmSIFDNVAAGlRLNGSykkselADIVEKSLKGANLWNEVKDR---LNKP----GSGLSGGQ 153
Cdd:TIGR02857 392 DSWRDQIAWVPQHPFLFAG-TIAENIRLA-RPDAS------DAEIREALERAGLDEFVAALpqgLDTPigegGAGLSGGQ 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 512057730 154 QQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERFTIVIVTHNMQQAARVsDRT 217
Cdd:TIGR02857 464 AQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALA-DRI 526
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-228 |
9.71e-35 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 127.51 E-value: 9.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDlygagIDPVSVR 84
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQT-----SGHIRFHGTD-----VSRLHAR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 -REIGMVFQRPNPFPTMSIFDNVAAGLRLNGSYKKSELADIVEKSLKganLWNEVK-DRL-NKPGSGLSGGQQQRLCIAR 161
Cdd:PRK10851 73 dRKVGFVFQHYALFRHMTVFDNIAFGLTVLPRRERPNAAAIKAKVTQ---LLEMVQlAHLaDRYPAQLSGGQKQRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512057730 162 AIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKE--RFTIVIVTHNMQQAARVSDRTAFF---NLAAVGQP 228
Cdd:PRK10851 150 ALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEelKFTSVFVTHDQEEAMEVADRVVVMsqgNIEQAGTP 221
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
12-217 |
1.27e-34 |
|
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: 123.51 E-value: 1.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 12 AYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTPGG-RVEGKVL--LDDEDLygagidpVSVRREIG 88
Cdd:TIGR02673 10 AYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQvRIAGEDVnrLRGRQL-------PLLRRRIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 89 MVFQRPNPFPTMSIFDNVAAGLRLNGSyKKSELADIVEKSLKGANLwnevKDRLNKPGSGLSGGQQQRLCIARAIAVEPK 168
Cdd:TIGR02673 83 VVFQDFRLLPDRTVYENVALPLEVRGK-KEREIQRRVGAALRQVGL----EHKADAFPEQLSGGEQQRVAIARAIVNSPP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 512057730 169 VLLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSDRT 217
Cdd:TIGR02673 158 LLLADEPTGNLDPDLSERILDLLKRLNKRgTTVIVATHDLSLVDRVAHRV 207
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-255 |
3.37e-34 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 123.93 E-value: 3.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 3 KRIDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTPGG-RVEGKV--LLDDEDLYGAGID 79
Cdd:PRK10619 4 NKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSiVVNGQTinLVRDKDGQLKVAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 80 P---VSVRREIGMVFQRPNPFPTMSIFDNV-AAGLRLNGsYKKSELADIVEKSLKGANLWNEVKDrlnKPGSGLSGGQQQ 155
Cdd:PRK10619 84 KnqlRLLRTRLTMVFQHFNLWSHMTVLENVmEAPIQVLG-LSKQEARERAVKYLAKVGIDERAQG---KYPVHLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 156 RLCIARAIAVEPKVLLMDEPCSALDPistlaieDLIGEL--------KERFTIVIVTHNMQQAARVSDRTAFFNlaavgq 227
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDP-------ELVGEVlrimqqlaEEGKTMVVVTHEMGFARHVSSHVIFLH------ 226
|
250 260
....*....|....*....|....*...
gi 512057730 228 PGKLIEIDDTERIFSNPSVQATEDYISG 255
Cdd:PRK10619 227 QGKIEEEGAPEQLFGNPQSPRLQQFLKG 254
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
7-211 |
4.32e-34 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 122.21 E-value: 4.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 7 VSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEvtPGGRVEGKVLLDDEDLYGAGIDpvsvRRE 86
Cdd:COG4136 4 LENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLS--PAFSASGEVLLNGRRLTALPAE----QRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 87 IGMVFQRPNPFPTMSIFDNVAAGLRlnGSYKKSELADIVEKSLKGANLwnevKDRLNKPGSGLSGGQQQRLCIARAIAVE 166
Cdd:COG4136 78 IGILFQDDLLFPHLSVGENLAFALP--PTIGRAQRRARVEQALEEAGL----AGFADRDPATLSGGQRARVALLRALLAE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 512057730 167 PKVLLMDEPCSALDPISTLAIEDLI-GELKERFTIVI-VTHNMQQAA 211
Cdd:COG4136 152 PRALLLDEPFSKLDAALRAQFREFVfEQIRQRGIPALlVTHDEEDAP 198
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-204 |
1.88e-33 |
|
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: 120.28 E-value: 1.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 4 RIDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLnrMHEVTPggrVEGKVLLDDEDLygaGIDPVSV 83
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRIL--AGLLPP---SAGEVLWNGEPI---RDAREDY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 84 RREIGMVFQRPNPFPTMSIFDNVAAGLRLNGSYKKSELadiVEKSLKGANLwnevKDRLNKPGSGLSGGQQQRLCIARAI 163
Cdd:COG4133 74 RRRLAYLGHADGLKPELTVRENLRFWAALYGLRADREA---IDEALEAVGL----AGLADLPVRQLSAGQKRRVALARLL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 512057730 164 AVEPKVLLMDEPCSALDPISTLAIEDLIGELKERFTIVIVT 204
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLT 187
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-219 |
4.39e-33 |
|
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: 119.78 E-value: 4.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYY----GSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMheVTPGGrveGKVLLDDEDlygAGIDP 80
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGL--LEPDA---GFATVDGFD---VVKEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 81 VSVRREIGMVFQRPNPFPTMSIFDNVAAGLRLNGsYKKSELADIVEKSLKGAnlwnEVKDRLNKPGSGLSGGQQQRLCIA 160
Cdd:cd03266 74 AEARRRLGFVSDSTGLYDRLTARENLEYFAGLYG-LKGDELTARLEELADRL----GMEELLDRRVGGFSTGMRQKVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 161 RAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSDRTAF 219
Cdd:cd03266 149 RALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERLCDRVVV 208
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-221 |
4.50e-33 |
|
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: 119.31 E-value: 4.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDdedlyGAGIDPvSVR 84
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPD-----SGEVLFD-----GKPLDI-AAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIGMVFQRPNPFPTMSIFDNVAAGLRLNGsYKKSELADIVEKSLKGAnlwnEVKDRLNKPGSGLSGGQQQRLCIARAIA 164
Cdd:cd03269 70 NRIGYLPEERGLYPKMKVIDQLVYLAQLKG-LKKEEARRRIDEWLERL----ELSEYANKRVEELSKGNQQKVQFIAAVI 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 512057730 165 VEPKVLLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSDRTAFFN 221
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEELCDRVLLLN 202
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-210 |
6.58e-33 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 120.35 E-value: 6.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 4 RIDVSGLTAYYGSHK----AIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAGID 79
Cdd:COG4525 3 MLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPS-----SGEITLDGVPVTGPGAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 80 pvsvrReiGMVFQRPNPFPTMSIFDNVAAGLRLNGsYKKSELADIVEKSLKGANLwnevKDRLNKPGSGLSGGQQQRLCI 159
Cdd:COG4525 78 -----R--GVVFQKDALLPWLNVLDNVAFGLRLRG-VPKAERRARAEELLALVGL----ADFARRRIWQLSGGMRQRVGI 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 512057730 160 ARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGEL--KERFTIVIVTHNMQQA 210
Cdd:COG4525 146 ARALAADPRFLLMDEPFGALDALTREQMQELLLDVwqRTGKGVFLITHSVEEA 198
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
12-207 |
1.30e-32 |
|
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: 118.87 E-value: 1.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 12 AYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVSVRREIGMVF 91
Cdd:cd03253 9 AYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVS-----SGSILIDGQDI--REVTLDSLRRAIGVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 92 QRPNPFPTmSIFDNVAAGlRLNGS-------YKKSELADIVEKSLKGANlwNEVKDRlnkpGSGLSGGQQQRLCIARAIA 164
Cdd:cd03253 82 QDTVLFND-TIGYNIRYG-RPDATdeevieaAKAAQIHDKIMRFPDGYD--TIVGER----GLKLSGGEKQRVAIARAIL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 512057730 165 VEPKVLLMDEPCSALDPISTLAIEDLIGELKERFTIVIVTHNM 207
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRL 196
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
5-240 |
1.97e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 119.77 E-value: 1.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYY--GS---HKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAGID 79
Cdd:PRK13637 3 IKIENLTHIYmeGTpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPT-----SGKIIIDGVDITDKKVK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 80 PVSVRREIGMVFQRP--NPFPTmSIFDNVAAGLRlNGSYKKSELADIVEKSLKGANL-WNEVKDRlnKPGSgLSGGQQQR 156
Cdd:PRK13637 78 LSDIRKKVGLVFQYPeyQLFEE-TIEKDIAFGPI-NLGLSEEEIENRVKRAMNIVGLdYEDYKDK--SPFE-LSGGQKRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 157 LCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDRTAFFNLAAV---GQPGKL 231
Cdd:PRK13637 153 VAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKLADRIIVMNKGKCelqGTPREV 232
|
250
....*....|
gi 512057730 232 I-EIDDTERI 240
Cdd:PRK13637 233 FkEVETLESI 242
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
7-216 |
3.39e-32 |
|
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: 117.63 E-value: 3.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 7 VSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVS-VRR 85
Cdd:TIGR03410 3 VSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVK-----SGSIRLDGEDI--TKLPPHErARA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 86 EIGMVFQRPNPFPTMSIFDNVAAGLRLNGSYKKSELADIVEkslkganLWNEVKDRLNKPGSGLSGGQQQRLCIARAIAV 165
Cdd:TIGR03410 76 GIAYVPQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYE-------LFPVLKEMLGRRGGDLSGGQQQQLAIARALVT 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 512057730 166 EPKVLLMDEPCSALDPISTLAIEDLIGELKER--FTIVIVTHNMQQAARVSDR 216
Cdd:TIGR03410 149 RPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEggMAILLVEQYLDFARELADR 201
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-216 |
5.26e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 119.06 E-value: 5.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygagidPVSVR 84
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPD-----SGEVLWDGEPL------DPEDR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIG-MvfqrpnP-----FPTMSIFDNVAAGLRLNGsYKKSEladiVEKSLKGanlWNE---VKDRLNKPGSGLSGGQQQ 155
Cdd:COG4152 71 RRIGyL------PeerglYPKMKVGEQLVYLARLKG-LSKAE----AKRRADE---WLErlgLGDRANKKVEELSKGNQQ 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512057730 156 RLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERFTIVIV-THNMQQAARVSDR 216
Cdd:COG4152 137 KVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFsSHQMELVEELCDR 198
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-205 |
5.62e-32 |
|
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: 116.52 E-value: 5.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPrTVTAFIGPSGCGKSTFLRTLnrMHEVTPggrVEGKVLLDDEDlygAGIDPVSVR 84
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGP-GMYGLLGPNGAGKTTLMRIL--ATLTPP---SSGTIRIDGQD---VLKQPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIGMVFQRPNPFPTMSIFDNVAAGLRLNGSYKKSELAdIVEKSLKGANLWnevkDRLNKPGSGLSGGQQQRLCIARAIA 164
Cdd:cd03264 72 RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKA-RVDEVLELVNLG----DRAKKKIGSLSGGMRRRVGIAQALV 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 512057730 165 VEPKVLLMDEPCSALDPISTLAIEDLIGELKERFTIVIVTH 205
Cdd:cd03264 147 GDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTH 187
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
14-234 |
6.82e-32 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 120.13 E-value: 6.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 14 YGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTPGGRVEGKVLLDDedlygagIDPVsvRREIGMVFQR 93
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMND-------VPPA--ERGVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 94 PNPFPTMSIFDNVAAGLRLNGSyKKSELADIVEKS---LKGANLWnevkDRlnKPGSgLSGGQQQRLCIARAIAVEPKVL 170
Cdd:PRK11000 84 YALYPHLSVAENMSFGLKLAGA-KKEEINQRVNQVaevLQLAHLL----DR--KPKA-LSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512057730 171 LMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDRTAFFNLAAVGQPGKLIEI 234
Cdd:PRK11000 156 LLDEPLSNLDAALRVQMRIEISRLHKRLgrTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-244 |
7.05e-32 |
|
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: 122.49 E-value: 7.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHK----AIEDISMTVEPRTVTAFIGPSGCGKS-TFLRTLNRMHEvtPGGRVEGKVLLDDEDLYGAGID 79
Cdd:COG4172 7 LSVEDLSVAFGQGGgtveAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPD--PAAHPSGSILFDGQDLLGLSER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 80 PV-SVR-REIGMVFQRP----NPFptMSIFDNVAAGLRLNGSYKKSEL-ADIVEkslkganLWNEV-----KDRLNKPGS 147
Cdd:COG4172 85 ELrRIRgNRIAMIFQEPmtslNPL--HTIGKQIAEVLRLHRGLSGAAArARALE-------LLERVgipdpERRLDAYPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 148 GLSGGQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDRTaffnlaAV 225
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELgmALLLITHDLGVVRRFADRV------AV 229
|
250
....*....|....*....
gi 512057730 226 GQPGKLIEIDDTERIFSNP 244
Cdd:COG4172 230 MRQGEIVEQGPTAELFAAP 248
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-244 |
1.17e-31 |
|
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: 121.72 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 15 GSHKAIEDISMTVEP-RTVtAFIGPSGCGKSTFLRTLNRMHevtpggRVEGKVLLDDEDLYGAGIDPV-SVRREIGMVFQ 92
Cdd:COG4172 297 GHVKAVDGVSLTLRRgETL-GLVGESGSGKSTLGLALLRLI------PSEGEIRFDGQDLDGLSRRALrPLRRRMQVVFQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 93 rpNPF----PTMSIFDNVAAGLRLNG-SYKKSELADIVEKSLKGANLWNEVKDRLnkPGSgLSGGQQQRLCIARAIAVEP 167
Cdd:COG4172 370 --DPFgslsPRMTVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGLDPAARHRY--PHE-FSGGQRQRIAIARALILEP 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 168 KVLLMDEPCSALDpISTLA-IEDLIGELKERF--TIVIVTHNMQQAARVSDRTaffnlaAVGQPGKLIEIDDTERIFSNP 244
Cdd:COG4172 445 KLLVLDEPTSALD-VSVQAqILDLLRDLQREHglAYLFISHDLAVVRALAHRV------MVMKDGKVVEQGPTEQVFDAP 517
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
13-226 |
1.52e-31 |
|
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: 115.43 E-value: 1.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 13 YYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEvtpggRVEGKVLLDDEDlygagIDPVSVRREIGMVFQ 92
Cdd:cd03226 9 YKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIK-----ESSGSILLNGKP-----IKAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 93 RPNpfpTMSIFDNVAAGLRLnGSYKKSELADIVEKSLKGANLWnEVKDRLnkPGSgLSGGQQQRLCIARAIAVEPKVLLM 172
Cdd:cd03226 79 DVD---YQLFTDSVREELLL-GLKELDAGNEQAETVLKDLDLY-ALKERH--PLS-LSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 512057730 173 DEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSDRTAFFNLAAVG 226
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAAQgKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
13-217 |
3.02e-31 |
|
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: 114.81 E-value: 3.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 13 YYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTPGG-RVEGKvllDDEDLYGAGIdPVsVRREIGMVF 91
Cdd:cd03292 10 YPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTiRVNGQ---DVSDLRGRAI-PY-LRRKIGVVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 92 QRPNPFPTMSIFDNVAAGLRLNGSyKKSELADIVEKSLKGANLwnevKDRLNKPGSGLSGGQQQRLCIARAIAVEPKVLL 171
Cdd:cd03292 85 QDFRLLPDRNVYENVAFALEVTGV-PPREIRKRVPAALELVGL----SHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 512057730 172 MDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSDRT 217
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKAgTTVVVATHAKELVDTTRHRV 206
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
13-205 |
4.87e-31 |
|
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: 114.63 E-value: 4.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 13 YYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDlyGAGIDPVSVRREIGMVFQ 92
Cdd:cd03254 12 YDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQ-----KGQILIDGID--IRDISRKSLRSMIGVVLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 93 RPNPFPTmSIFDNvaagLRLNGSYKKSELadiVEKSLKGANLWNEVKDR-------LNKPGSGLSGGQQQRLCIARAIAV 165
Cdd:cd03254 85 DTFLFSG-TIMEN----IRLGRPNATDEE---VIEAAKEAGAHDFIMKLpngydtvLGENGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 512057730 166 EPKVLLMDEPCSALDPISTLAIEDLIGELKERFTIVIVTH 205
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAH 196
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
7-217 |
7.04e-31 |
|
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: 113.48 E-value: 7.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 7 VSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLnrmhevtpgGRVE----GKVLLDDEDLYG-AGIDPV 81
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNII---------GLLEkfdsGQVYLNGQETPPlNSKKAS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 82 SVRRE-IGMVFQRPNPFPTMSIFDNVAAGLRLNGSYKKSELADIVEkSLKGANLWNevkdRLNKPGSGLSGGQQQRLCIA 160
Cdd:TIGR03608 72 KFRREkLGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKE-ALEKVGLNL----KLKQKIYELSGGEQQRVALA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 512057730 161 RAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARvSDRT 217
Cdd:TIGR03608 147 RAILKPPPLILADEPTGSLDPKNRDEVLDLLLELNDEgKTIIIVTHDPEVAKQ-ADRV 203
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
4-180 |
1.06e-30 |
|
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: 120.06 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 4 RIDVSGLTAYYG--SHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLnrMHEVTPGgrvEGKVLLDDEDLygAGIDPV 81
Cdd:TIGR03797 451 AIEVDRVTFRYRpdGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLL--LGFETPE---SGSVFYDGQDL--AGLDVQ 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 82 SVRREIGMVFQRPNPFPTmSIFDNVAAGLRLNgsykkselADIVEKSLKGANLWNEVKDR-------LNKPGSGLSGGQQ 154
Cdd:TIGR03797 524 AVRRQLGVVLQNGRLMSG-SIFENIAGGAPLT--------LDEAWEAARMAGLAEDIRAMpmgmhtvISEGGGTLSGGQR 594
|
170 180
....*....|....*....|....*.
gi 512057730 155 QRLCIARAIAVEPKVLLMDEPCSALD 180
Cdd:TIGR03797 595 QRLLIARALVRKPRILLFDEATSALD 620
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-242 |
1.07e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 115.11 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 1 MAKR-IDVSGLTAYY--GSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRM-----HEVTPGGRVegkvlLDDED 72
Cdd:PRK13635 1 MKEEiIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLllpeaGTITVGGMV-----LSEET 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 73 LYgagidpvSVRREIGMVFQRP-NPFPTMSIFDNVAAGLRLNGsYKKSELADIVEKSLKGANLwnevKDRLNKPGSGLSG 151
Cdd:PRK13635 76 VW-------DVRRQVGMVFQNPdNQFVGATVQDDVAFGLENIG-VPREEMVERVDQALRQVGM----EDFLNREPHRLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 152 GQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKE--RFTIVIVTHNMQQAARvSDRTAFFNlaavgqPG 229
Cdd:PRK13635 144 GQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEqkGITVLSITHDLDEAAQ-ADRVIVMN------KG 216
|
250
....*....|...
gi 512057730 230 KLIEIDDTERIFS 242
Cdd:PRK13635 217 EILEEGTPEEIFK 229
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
7-216 |
1.14e-30 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 114.39 E-value: 1.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 7 VSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTPGGRVEGKVLLDDedlygagidpvsVRRE 86
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE------------ARED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 87 IGMVFQRPNPFPTMSIFDNVAAGLRlnGSYKKSELadiveKSLKGANLwnevKDRLNKPGSGLSGGQQQRLCIARAIAVE 166
Cdd:PRK11247 83 TRLMFQDARLLPWKKVIDNVGLGLK--GQWRDAAL-----QALAAVGL----ADRANEWPAALSGGQKQRVALARALIHR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 512057730 167 PKVLLMDEPCSALDPISTLAIEDLIGEL--KERFTIVIVTHNMQQAARVSDR 216
Cdd:PRK11247 152 PGLLLLDEPLGALDALTRIEMQDLIESLwqQHGFTVLLVTHDVSEAVAMADR 203
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
5-242 |
1.59e-30 |
|
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: 114.52 E-value: 1.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSH---------KAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYG 75
Cdd:TIGR02769 3 LEVRDVTHTYRTGglfgakqraPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPA-----QGTVSFRGQDLYQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 76 agIDPVS---VRREIGMVFQ-RPNPF-PTMSIFDNVAAGLRLNGSYKKSELADIVEKSLKGANLWNEVKDRLNKPgsgLS 150
Cdd:TIGR02769 78 --LDRKQrraFRRDVQLVFQdSPSAVnPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQ---LS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 151 GGQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERFTI--VIVTHNMQQAARVSDRTaffnlaAVGQP 228
Cdd:TIGR02769 153 GGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSFCQRV------AVMDK 226
|
250
....*....|....
gi 512057730 229 GKLIEIDDTERIFS 242
Cdd:TIGR02769 227 GQIVEECDVAQLLS 240
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
10-241 |
3.22e-30 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 113.06 E-value: 3.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 10 LTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTflrTLNRMHEVTPggRVEGKVLLDDEDLygaGIDPV--SVRREI 87
Cdd:PRK10895 9 LAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTT---TFYMVVGIVP--RDAGNIIIDDEDI---SLLPLhaRARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 88 GMVFQRPNPFPTMSIFDNVAAGLRLNGSYKKSELADIVEKSLKGANLwNEVKDRLnkpGSGLSGGQQQRLCIARAIAVEP 167
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHI-EHLRDSM---GQSLSGGERRRVEIARALAANP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 512057730 168 KVLLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSDRTAFF---NLAAVGQPGKLIEIDDTERIF 241
Cdd:PRK10895 157 KFILLDEPFAGVDPISVIDIKRIIEHLRDSgLGVLITDHNVRETLAVCERAYIVsqgHLIAHGTPTEILQDEHVKRVY 234
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-233 |
3.56e-30 |
|
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: 111.93 E-value: 3.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygagIDPVSVR 84
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPD-----SGEITFDGKSY----QKNIEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIGMVFQRPNPFPTMSIFDNVAAGLRLNGSYKKseladIVEKSLKGANLWNEVKDRLnkpgSGLSGGQQQRLCIARAIA 164
Cdd:cd03268 72 RRIGALIEAPGFYPNLTARENLRLLARLLGIRKK-----RIDEVLDVVGLKDSAKKKV----KGFSLGMKQRLGIALALL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 165 VEPKVLLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSDRTAFFNlaavgqPGKLIE 233
Cdd:cd03268 143 GNPDLLILDEPTNGLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKVADRIGIIN------KGKLIE 206
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-253 |
5.04e-30 |
|
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: 112.17 E-value: 5.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 20 IEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTPGGrvegkVLLDDEDLYGAGIDPVsvrreigMVFQRPNPFPT 99
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGG-----VILEGKQITEPGPDRM-------VVFQNYSLLPW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 100 MSIFDNVAAGL-RLNGSYKKSELADIVEKSLKGANLwNEVKDRlnKPGSgLSGGQQQRLCIARAIAVEPKVLLMDEPCSA 178
Cdd:TIGR01184 69 LTVRENIALAVdRVLPDLSKSERRAIVEEHIALVGL-TEAADK--RPGQ-LSGGMKQRVAIARALSIRPKVLLLDEPFGA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 179 LDPISTLAIEDLIGELKE--RFTIVIVTHNMQQAARVSDRTAFFNLAAVGQPGKLIEID-----DTERIFSNPSVQATED 251
Cdd:TIGR01184 145 LDALTRGNLQEELMQIWEehRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVPfprprDRLEVVEDPSYYDLRN 224
|
..
gi 512057730 252 YI 253
Cdd:TIGR01184 225 EA 226
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-246 |
6.27e-30 |
|
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: 111.87 E-value: 6.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTflrTLNRMHEVTPGGrvEGKVLLDDEDLYGagiDPVSVR 84
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTT---TFYMIVGLVKPD--SGKILLDGQDITK---LPMHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIGMVF--QRPNPFPTMSIFDNVAAGLRLNGsYKKSELADIVEKSLKGANLwnevKDRLNKPGSGLSGGQQQRLCIARA 162
Cdd:cd03218 73 ARLGIGYlpQEASIFRKLTVEENILAVLEIRG-LSKKEREEKLEELLEEFHI----THLRKSKASSLSGGERRRVEIARA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 163 IAVEPKVLLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSDRtaffnlAAVGQPGKLIEIDDTERIF 241
Cdd:cd03218 148 LATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRgIGVLITDHNVRETLSITDR------AYIIYEGKVLAEGTPEEIA 221
|
....*
gi 512057730 242 SNPSV 246
Cdd:cd03218 222 ANELV 226
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
22-219 |
8.78e-30 |
|
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: 111.05 E-value: 8.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 22 DISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHevTPGgrvEGKVLLDDEDLYGAgidPVSvRREIGMVFQRPNPFPTMS 101
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFE--TPQ---SGRVLINGVDVTAA---PPA-DRPVSMLFQENNLFAHLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 102 IFDNVAAG----LRLNGSYKKSeladiVEKSLKGANLWNEVKdrlNKPGSgLSGGQQQRLCIARAIAVEPKVLLMDEPCS 177
Cdd:cd03298 87 VEQNVGLGlspgLKLTAEDRQA-----IEVALARVGLAGLEK---RLPGE-LSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 512057730 178 ALDPISTLAIEDLIGEL--KERFTIVIVTHNMQQAARVSDRTAF 219
Cdd:cd03298 158 ALDPALRAEMLDLVLDLhaETKMTVLMVTHQPEDAKRLAQRVVF 201
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-205 |
1.40e-29 |
|
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: 111.17 E-value: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHK--AIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVS 82
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVD-----SGRILIDGHDV--RDYTLAS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 83 VRREIGMVFQRPNPFPTmSIFDNVAAGlrlngsyKKSELADIVEKSLKGANLwNEVKDRLNKP--------GSGLSGGQQ 154
Cdd:cd03251 74 LRRQIGLVSQDVFLFND-TVAENIAYG-------RPGATREEVEEAARAANA-HEFIMELPEGydtvigerGVKLSGGQR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 512057730 155 QRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERFTIVIVTH 205
Cdd:cd03251 145 QRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAH 195
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
7-246 |
2.50e-29 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 110.44 E-value: 2.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 7 VSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMheVTPGgrvEGKVLLDDEDLYGAGIDPVSvRRE 86
Cdd:TIGR04406 4 AENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGL--VRPD---AGKILIDGQDITHLPMHERA-RLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 87 IGMVFQRPNPFPTMSIFDNVAAGLRLNGSYKKSELADIVEKSLKGANLwnevKDRLNKPGSGLSGGQQQRLCIARAIAVE 166
Cdd:TIGR04406 78 IGYLPQEASIFRKLTVEENIMAVLEIRKDLDRAEREERLEALLEEFQI----SHLRDNKAMSLSGGERRRVEIARALATN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 167 PKVLLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSDRtaffnlAAVGQPGKLIEIDDTERIFSNPS 245
Cdd:TIGR04406 154 PKFILLDEPFAGVDPIAVGDIKKIIKHLKERgIGVLITDHNVRETLDICDR------AYIISDGKVLAEGTPAEIVANEK 227
|
.
gi 512057730 246 V 246
Cdd:TIGR04406 228 V 228
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-257 |
3.01e-29 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 113.59 E-value: 3.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 19 AIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVSVR----REIGMVFQRP 94
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPT-----RGQVLIDGVDI--AKISDAELRevrrKKIAMVFQSF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 95 NPFPTMSIFDNVAAGLRLNGsYKKSELADIVEKSLKGANLWNEVKDRLNKpgsgLSGGQQQRLCIARAIAVEPKVLLMDE 174
Cdd:PRK10070 116 ALMPHMTVLDNTAFGMELAG-INAEERREKALDALRQVGLENYAHSYPDE----LSGGMRQRVGLARALAINPDILLMDE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 175 PCSALDPISTLAIEDLIGEL--KERFTIVIVTHNMQQAARVSDRTaffnlaAVGQPGKLIEIDDTERIFSNPSvqatEDY 252
Cdd:PRK10070 191 AFSALDPLIRTEMQDELVKLqaKHQRTIVFISHDLDEAMRIGDRI------AIMQNGEVVQVGTPDEILNNPA----NDY 260
|
....*
gi 512057730 253 ISGRF 257
Cdd:PRK10070 261 VRTFF 265
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-216 |
4.99e-29 |
|
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: 107.51 E-value: 4.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAgiDPV-SV 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPD-----SGEILVDGKEVSFA--SPRdAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 84 RREIGMVFQrpnpfptmsifdnvaaglrlngsykkseladivekslkganlwnevkdrlnkpgsgLSGGQQQRLCIARAI 163
Cdd:cd03216 74 RAGIAMVYQ--------------------------------------------------------LSVGERQMVEIARAL 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 512057730 164 AVEPKVLLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSDR 216
Cdd:cd03216 98 ARNARLLILDEPTAALTPAEVERLFKVIRRLRAQgVAVIFISHRLDEVFEIADR 151
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
5-217 |
5.00e-29 |
|
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: 109.45 E-value: 5.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKA----IEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAGIDP 80
Cdd:COG4181 9 IELRGLTKTVGTGAGeltiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPT-----SGTVRLAGQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 81 VS-VRRE-IGMVFQRpnpF---PTMSIFDNVAAGLRLNGsykKSELADIVEKSLKGANLwnevKDRLNKPGSGLSGGQQQ 155
Cdd:COG4181 84 RArLRARhVGFVFQS---FqllPTLTALENVMLPLELAG---RRDARARARALLERVGL----GHRLDHYPAQLSGGEQQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 512057730 156 RLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARvSDRT 217
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgtTLVLVTHDPALAAR-CDRV 216
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
18-216 |
1.01e-28 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 108.27 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 18 KAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNrMHEVTPggrvEGKVLLDDEDLYGAGI-DPVSVRRE-IGMVFQRPN 95
Cdd:NF038007 19 KVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIG-MFDSLD----SGSLTLAGKEVTNLSYsQKIILRRElIGYIFQSFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 96 PFPTMSIFDNVAAGLRLNGSYKKselaDIVEKSLKGANLWNEVKDRLNKPgSGLSGGQQQRLCIARAIAVEPKVLLMDEP 175
Cdd:NF038007 94 LIPHLSIFDNVALPLKYRGVAKK----ERIERVNQVLNLFGIDNRRNHKP-MQLSGGQQQRVAIARAMVSNPALLLADEP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 512057730 176 CSALDPISTLAIEDLIGELKER-FTIVIVTHNmQQAARVSDR 216
Cdd:NF038007 169 TGNLDSKNARAVLQQLKYINQKgTTIIMVTHS-DEASTYGNR 209
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
7-216 |
2.08e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 112.42 E-value: 2.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 7 VSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHevTPGgrvEGKVLLDDEDLygAGIDPVSVRRE 86
Cdd:COG1129 7 MRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVY--QPD---SGEILLDGEPV--RFRSPRDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 87 -IGMVFQRPNPFPTMSIFDNVAAG--LRLNGSYKKSELADIVEKSLK--GANLwnevkdRLNKPGSGLSGGQQQRLCIAR 161
Cdd:COG1129 80 gIAIIHQELNLVPNLSVAENIFLGrePRRGGLIDWRAMRRRARELLArlGLDI------DPDTPVGDLSVAQQQLVEIAR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 512057730 162 AIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSDR 216
Cdd:COG1129 154 ALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQgVAIIYISHRLDEVFEIADR 209
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
19-246 |
2.22e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 109.12 E-value: 2.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 19 AIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNrmhevtpggrveGKVLLDDEDLYGAGIDPVS--------VRREIGMV 90
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLIN------------GLLLPDDNPNSKITVDGITltaktvwdIREKVGIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 91 FQRP-NPFPTMSIFDNVAAGLRlNGSYKKSELADIVEKSLKGANLWNEVKdrlNKPgSGLSGGQQQRLCIARAIAVEPKV 169
Cdd:PRK13640 90 FQNPdNQFVGATVGDDVAFGLE-NRAVPRPEMIKIVRDVLADVGMLDYID---SEP-ANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 512057730 170 LLMDEPCSALDPISTLAIEDLIGELKER--FTIVIVTHNMQQAARVSDrtaffnlAAVGQPGKLIEIDDTERIFSNPSV 246
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIRKLKKKnnLTVISITHDIDEANMADQ-------VLVLDDGKLLAQGSPVEIFSKVEM 236
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
2.88e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 108.67 E-value: 2.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 1 MAKRIDVSGLTAYY-GSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTPGG-RVEGKVLLDDEDLYgagi 78
Cdd:PRK13647 1 MDNIIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRvKVMGREVNAENEKW---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 79 dpvsVRREIGMVFQRPNP--FpTMSIFDNVAAGlRLNGSYKKSELADIVEKSLKGANLWnevkDRLNKPGSGLSGGQQQR 156
Cdd:PRK13647 77 ----VRSKVGLVFQDPDDqvF-SSTVWDDVAFG-PVNMGLDKDEVERRVEEALKAVRMW----DFRDKPPYHLSYGQKKR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 512057730 157 LCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGEL-KERFTIVIVTHNMQQAARVSDR 216
Cdd:PRK13647 147 VAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDLAAEWADQ 207
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
13-210 |
4.57e-28 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 105.97 E-value: 4.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 13 YYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAGIDPVSVRREIGMVFQ 92
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQ-----SGAVLIDGEPLDYSRKGLLERRQRVGLVFQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 93 RPNP--FPTmSIFDNVAAGLRlNGSYKKSELADIVEKSLKGANLwnevKDRLNKPGSGLSGGQQQRLCIARAIAVEPKVL 170
Cdd:TIGR01166 76 DPDDqlFAA-DVDQDVAFGPL-NLGLSEAEVERRVREALTAVGA----SGLRERPTHCLSGGEKKRVAIAGAVAMRPDVL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 512057730 171 LMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQA 210
Cdd:TIGR01166 150 LLDEPTAGLDPAGREQMLAILRRLRAEgMTVVISTHDVDLA 190
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-246 |
5.84e-28 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 107.38 E-value: 5.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 1 MAKRIDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEvtPGGrveGKVLLDDEDLygAGIDP 80
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYK--PTG---GTILLRGQHI--EGLPG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 81 VSVRREiGMV--FQRPNPFPTMSIFDN--VA----------AGLRLNGSYKKSEladivEKSLKGANLWNEV---KDRLN 143
Cdd:PRK11300 75 HQIARM-GVVrtFQHVRLFREMTVIENllVAqhqqlktglfSGLLKTPAFRRAE-----SEALDRAATWLERvglLEHAN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 144 KPGSGLSGGQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDRTAFFN 221
Cdd:PRK11300 149 RQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGISDRIYVVN 228
|
250 260
....*....|....*....|....*
gi 512057730 222 laavgqPGKLIEIDDTERIFSNPSV 246
Cdd:PRK11300 229 ------QGTPLANGTPEEIRNNPDV 247
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
19-243 |
6.47e-28 |
|
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: 106.80 E-value: 6.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 19 AIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVSVRREIGMVFQRpNPFP 98
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPE-----NGRVLVDGHDL--ALADPAWLRRQVGVVLQE-NVLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 99 TMSIFDNVAA---GLRLNGSYKKSELADIVEKSLKGANLWNEVkdrLNKPGSGLSGGQQQRLCIARAIAVEPKVLLMDEP 175
Cdd:cd03252 89 NRSIRDNIALadpGMSMERVIEAAKLAGAHDFISELPEGYDTI---VGEQGAGLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 512057730 176 CSALDPISTLAIEDLIGELKERFTIVIVTHNMqQAARVSDRTAFFNLAAVGQPGKLIEIDDTERIFSN 243
Cdd:cd03252 166 TSALDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELLAENGLYAY 232
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-207 |
9.39e-28 |
|
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: 105.75 E-value: 9.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 4 RIDVSGLTAYY--GSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPV 81
Cdd:cd03245 2 RIEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPT-----SGSVLLDGTDI--RQLDPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 82 SVRREIGMVFQRPNPFpTMSIFDNVAAGL------RLNGSYKKSELADIVEKSLKGANLwnEVKDRlnkpGSGLSGGQQQ 155
Cdd:cd03245 75 DLRRNIGYVPQDVTLF-YGTLRDNITLGApladdeRILRAAELAGVTDFVNKHPNGLDL--QIGER----GRGLSGGQRQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 512057730 156 RLCIARAIAVEPKVLLMDEPCSALDPIS-TLAIEDLIGELKERfTIVIVTHNM 207
Cdd:cd03245 148 AVALARALLNDPPILLLDEPTSAMDMNSeERLKERLRQLLGDK-TLIIITHRP 199
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
20-234 |
1.12e-27 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 111.35 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 20 IEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVSVRREIGMVFQRPNPFpT 99
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPT-----GGQVLLDGVPL--VQYDHHYLHRQVALVGQEPVLF-S 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 100 MSIFDNVAAGLR------LNGSYKKSELADIVEKSLKGANlwNEVKDRlnkpGSGLSGGQQQRLCIARAIAVEPKVLLMD 173
Cdd:TIGR00958 569 GSVRENIAYGLTdtpdeeIMAAAKAANAHDFIMEFPNGYD--TEVGEK----GSQLSGGQKQRIAIARALVRKPRVLILD 642
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 512057730 174 EPCSALDpistLAIEDLIGELKER--FTIVIVTHNMQQAARvSDRTAFFNLAAVGQPGKLIEI 234
Cdd:TIGR00958 643 EATSALD----AECEQLLQESRSRasRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQL 700
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-243 |
1.32e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 106.61 E-value: 1.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLT-AYYGSHK-AIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAGIDpvS 82
Cdd:PRK13632 8 IKVENVSfSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQ-----SGEIKIDGITISKENLK--E 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 83 VRREIGMVFQRP-NPFPTMSIFDNVAAGLRlNGSYKKSELADIVEKSLKGANLwnevKDRLNKPGSGLSGGQQQRLCIAR 161
Cdd:PRK13632 81 IRKKIGIIFQNPdNQFIGATVEDDIAFGLE-NKKVPPKKMKDIIDDLAKKVGM----EDYLDKEPQNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 162 AIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARvSDRTAFFNlaavgqPGKLIEIDDTER 239
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAIL-ADKVIVFS------EGKLIAQGKPKE 228
|
....
gi 512057730 240 IFSN 243
Cdd:PRK13632 229 ILNN 232
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
7-210 |
1.45e-27 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 106.32 E-value: 1.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 7 VSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMheVTPGGrveGKVLLDDEDLYGAGIdpvsvrrE 86
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGF--VPYQH---GSITLDGKPVEGPGA-------E 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 87 IGMVFQRPNPFPTMSIFDNVAAGLRLNGsYKKSELADIVEKSLKGANLWNEVKDRLNKpgsgLSGGQQQRLCIARAIAVE 166
Cdd:PRK11248 72 RGVVFQNEGLLPWRNVQDNVAFGLQLAG-VEKMQRLEIAHQMLKKVGLEGAEKRYIWQ----LSGGQRQRVGIARALAAN 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 512057730 167 PKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQA 210
Cdd:PRK11248 147 PQLLLLDEPFGALDAFTREQMQTLLLKLWQETgkQVLLITHDIEEA 192
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
17-212 |
1.82e-27 |
|
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: 105.25 E-value: 1.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 17 HKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpGGRV--EGKVLLDDEDLYgagidpvsVRREIGMVFQRP 94
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQ-GGQVllDGKPISQYEHKY--------LHSKVSLVGQEP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 95 NPFpTMSIFDNVAAGL------RLNGSYKKSELADIVEKSLKGanLWNEVKDRlnkpGSGLSGGQQQRLCIARAIAVEPK 168
Cdd:cd03248 98 VLF-ARSLQDNIAYGLqscsfeCVKEAAQKAHAHSFISELASG--YDTEVGEK----GSQLSGGQKQRVAIARALIRNPQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 512057730 169 VLLMDEPCSALDPISTLAIEDLIGELKERFTIVIVTHNMQQAAR 212
Cdd:cd03248 171 VLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVER 214
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-246 |
1.88e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 106.32 E-value: 1.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 19 AIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAGIDPVSVRREIGMVFQRPNP-- 96
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPT-----SGEVLIKGEPIKYDKKSLLEVRKTVGIVFQNPDDql 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 97 -FPTMSifDNVAAGlRLNGSYKKSELADIVEKSLKGANLwnevKDRLNKPGSGLSGGQQQRLCIARAIAVEPKVLLMDEP 175
Cdd:PRK13639 92 fAPTVE--EDVAFG-PLNLGLSKEEVEKRVKEALKAVGM----EGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512057730 176 CSALDPISTLAIEDLIGEL-KERFTIVIVTHNMQQAARVSDRTAFFNlaavgqPGKLIEIDDTERIFSNPSV 246
Cdd:PRK13639 165 TSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVYADKVYVMS------DGKIIKEGTPKEVFSDIET 230
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
5-215 |
2.00e-27 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 106.39 E-value: 2.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLnrmhevtpGGRVE---GKVLLDDED--------L 73
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLI--------GGQIApdhGEILFDGENipamsrsrL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 74 YgagidpvSVRREIGMVFQRPNPFPTMSIFDNVAAGLRLNGSYKKSELADIVEKSLKGANLWNEVKdrlNKPgSGLSGGQ 153
Cdd:PRK11831 80 Y-------TVRKRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAK---LMP-SELSGGM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 512057730 154 QQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSD 215
Cdd:PRK11831 149 ARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALgvTCVVVSHDVPEVLSIAD 212
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
18-244 |
3.91e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 106.59 E-value: 3.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 18 KAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAgiDPVSV---RREIGMVFQrp 94
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPT-----GGELYYQGQDLLKA--DPEAQkllRQKIQIVFQ-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 95 NPF----PTMSIFDNVAAGLRLNGSYKKSELADIVEKSLKGANLWNEVKDRLnkPGSgLSGGQQQRLCIARAIAVEPKVL 170
Cdd:PRK11308 100 NPYgslnPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRY--PHM-FSGGQRQRIAIARALMLDPDVV 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 512057730 171 LMDEPCSALDpISTLA-IEDLIGELKERFTI--VIVTHNMQQAARVSDRTAFFNLaavgqpGKLIEIDDTERIFSNP 244
Cdd:PRK11308 177 VADEPVSALD-VSVQAqVLNLMMDLQQELGLsyVFISHDLSVVEHIADEVMVMYL------GRCVEKGTKEQIFNNP 246
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
3-216 |
5.57e-27 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 105.15 E-value: 5.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 3 KRIDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYG-AGIDPV 81
Cdd:PRK10419 11 HHYAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPS-----QGNVSWRGEPLAKlNRAQRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 82 SVRREIGMVFQ-RPNPF-PTMSIFDNVAAGLRLNGSYKKSELADIVEKSLKGANLWNEVKDRLnkPGSgLSGGQQQRLCI 159
Cdd:PRK10419 86 AFRRDIQMVFQdSISAVnPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKR--PPQ-LSGGQLQRVCL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 512057730 160 ARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERFTI--VIVTHNMQQAARVSDR 216
Cdd:PRK10419 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERFCQR 221
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-213 |
6.22e-27 |
|
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: 102.29 E-value: 6.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKA--IEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVS 82
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPT-----SGRVRLDGADI--SQWDPNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 83 VRREIGMVFQRPNPFPTmSIFDNVaaglrlngsykkseladivekslkganlwnevkdrlnkpgsgLSGGQQQRLCIARA 162
Cdd:cd03246 74 LGDHVGYLPQDDELFSG-SIAENI------------------------------------------LSGGQRQRLGLARA 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 512057730 163 IAVEPKVLLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNM---QQAARV 213
Cdd:cd03246 111 LYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAgATRIVIAHRPetlASADRI 165
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-217 |
6.66e-27 |
|
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: 103.67 E-value: 6.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 1 MAKRIDVSGLTAYYGSH-------KAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDE-- 71
Cdd:COG4778 1 MTTLLEVENLSKTFTLHlqggkrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPD-----SGSILVRHDgg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 72 --DLygAGIDPVSV----RREIGMVFQRPNPFPTMSIFDNVAAGLRLNGsYKKSELADIVEKSLKGANLwnevKDRL-NK 144
Cdd:COG4778 76 wvDL--AQASPREIlalrRRTIGYVSQFLRVIPRVSALDVVAEPLLERG-VDREEARARARELLARLNL----PERLwDL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 512057730 145 PGSGLSGGQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERFT-IVIVTHNMQQAARVSDRT 217
Cdd:COG4778 149 PPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTaIIGIFHDEEVREAVADRV 222
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
12-208 |
8.71e-27 |
|
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: 108.80 E-value: 8.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 12 AYYGS-HKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVSVRREIGMV 90
Cdd:TIGR03375 472 AYPGQeTPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPT-----EGSVLLDGVDI--RQIDPADLRRNIGYV 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 91 FQRPNPFpTMSIFDNVAAGlrlNGSYKKSELADIVEKSlkGA-NLWNEVKDRLNKP----GSGLSGGQQQRLCIARAIAV 165
Cdd:TIGR03375 545 PQDPRLF-YGTLRDNIALG---APYADDEEILRAAELA--GVtEFVRRHPDGLDMQigerGRSLSGGQRQAVALARALLR 618
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 512057730 166 EPKVLLMDEPCSALDPIS-TLAIEDLIGELKERfTIVIVTHNMQ 208
Cdd:TIGR03375 619 DPPILLLDEPTSAMDNRSeERFKDRLKRWLAGK-TLVLVTHRTS 661
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-216 |
9.31e-27 |
|
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: 106.35 E-value: 9.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 22 DISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMheVTPGgrvEGKVLLDDEDLY--GAGIDPVSVRREIGMVFQRPNPFPT 99
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGL--TRPD---EGEIVLNGRTLFdsRKGIFLPPEKRRIGYVFQEARLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 100 MSIFDNVAAGL-RLNGSYKKSELADIVEksLKGanlwneVKDRLNKPGSGLSGGQQQRLCIARAIAVEPKVLLMDEPCSA 178
Cdd:TIGR02142 90 LSVRGNLRYGMkRARPSERRISFERVIE--LLG------IGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 512057730 179 LDPISTLAI----EDLIGELkeRFTIVIVTHNMQQAARVSDR 216
Cdd:TIGR02142 162 LDDPRKYEIlpylERLHAEF--GIPILYVSHSLQEVLRLADR 201
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-234 |
1.15e-26 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 106.08 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 1 MAKrIDVSGLT-AYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGID 79
Cdd:PRK11650 1 MAG-LKLQAVRkSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERIT-----SGEIWIGGRVV--NELE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 80 PVSvrREIGMVFQRPNPFPTMSIFDNVAAGLRLNGsYKKSELADIVEKSLKGANLwNEVKDRlnKPgSGLSGGQQQRLCI 159
Cdd:PRK11650 73 PAD--RDIAMVFQNYALYPHMSVRENMAYGLKIRG-MPKAEIEERVAEAARILEL-EPLLDR--KP-RELSGGQRQRVAM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 160 ARAIAVEPKVLLMDEPCSALDpistlA-------IEdlIGELKERF--TIVIVTHNMQQAARVSDRTAFFNLAAVGQPGK 230
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLD-----AklrvqmrLE--IQRLHRRLktTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGT 218
|
....
gi 512057730 231 LIEI 234
Cdd:PRK11650 219 PVEV 222
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
10-256 |
1.36e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 103.56 E-value: 1.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 10 LTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMheVTPggrVEGKVLLDDEDLygAGIDPVSVRREIGM 89
Cdd:PRK11231 8 LTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARL--LTP---QSGTVFLGDKPI--SMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 90 VFQRPNPFPTMSIFDNVAAGL--------RLNGSYKKseladIVEKSLKGAnlwnEVKDRLNKPGSGLSGGQQQRLCIAR 161
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYGRspwlslwgRLSAEDNA-----RVNQAMEQT----RINHLADRRLTDLSGGQRQRAFLAM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 162 AIAVEPKVLLMDEPCSALDPISTLAIEDLIGELK-ERFTIVIVTHNMQQAARVSDRTAFF---NLAAVGQPGKLIEIDDT 237
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNtQGKTVVTVLHDLNQASRYCDHLVVLangHVMAQGTPEEVMTPGLL 231
|
250
....*....|....*....
gi 512057730 238 ERIFSnPSVQATEDYISGR 256
Cdd:PRK11231 232 RTVFD-VEAEIHPEPVSGT 249
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-202 |
1.38e-26 |
|
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: 107.88 E-value: 1.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 4 RIDVSGLTAYYGSH--KAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPV 81
Cdd:TIGR02203 330 DVEFRNVTFRYPGRdrPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPD-----SGQILLDGHDL--ADYTLA 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 82 SVRREIGMVFQRPNPFPTmSIFDNVAAGLRlnGSYKKSEladiVEKSLKGANLwNEVKDRLNK--------PGSGLSGGQ 153
Cdd:TIGR02203 403 SLRRQVALVSQDVVLFND-TIANNIAYGRT--EQADRAE----IERALAAAYA-QDFVDKLPLgldtpigeNGVLLSGGQ 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 512057730 154 QQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGEL-KERFTIVI 202
Cdd:TIGR02203 475 RQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLmQGRTTLVI 524
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-241 |
1.74e-26 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 103.91 E-value: 1.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 2 AKRIDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMheVTPggrVEGKVLLDDEDLYGAGIDPV 81
Cdd:PRK10253 5 VARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRL--MTP---AHGHVWLDGEHIQHYASKEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 82 SvrREIGMVFQRPNPFPTMSIFDNVAAGLR----LNGSYKKsELADIVEKSLKGANlwneVKDRLNKPGSGLSGGQQQRL 157
Cdd:PRK10253 80 A--RRIGLLAQNATTPGDITVQELVARGRYphqpLFTRWRK-EDEEAVTKAMQATG----ITHLADQSVDTLSGGQRQRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 158 CIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKER--FTIVIVTHNMQQAARVSDRTAFF---NLAAVGQPGKLI 232
Cdd:PRK10253 153 WIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREkgYTLAAVLHDLNQACRYASHLIALregKIVAQGAPKEIV 232
|
....*....
gi 512057730 233 EIDDTERIF 241
Cdd:PRK10253 233 TAELIERIY 241
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
15-216 |
1.82e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 104.16 E-value: 1.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 15 GSHkAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMheVTPggrVEGKVLLDDEDLYGAGIDPVSVRREIGMVFQRP 94
Cdd:PRK13636 18 GTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGI--LKP---SSGRILFDGKPIDYSRKGLMKLRESVGMVFQDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 95 -NPFPTMSIFDNVAAGLrLNGSYKKSELADIVEKSLKGANlwneVKDRLNKPGSGLSGGQQQRLCIARAIAVEPKVLLMD 173
Cdd:PRK13636 92 dNQLFSASVYQDVSFGA-VNLKLPEDEVRKRVDNALKRTG----IEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 512057730 174 EPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDR 216
Cdd:PRK13636 167 EPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDIDIVPLYCDN 211
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-228 |
3.37e-26 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 102.50 E-value: 3.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRmhEVTPGgrvEGKVLLDDEDLygAGIDPV--S 82
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTG--ELTPS---SGEVRLNGRPL--AAWSPWelA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 83 VRR-----EIGMVFqrpnPFPTMSIfdnVAAGlRLNGSYKKSELADIVEKSLKGANLWnEVKDRLNkpgSGLSGGQQQRL 157
Cdd:COG4559 75 RRRavlpqHSSLAF----PFTVEEV---VALG-RAPHGSSAAQDRQIVREALALVGLA-HLAGRSY---QTLSGGEQQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 158 CIARAIA-------VEPKVLLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSDRTAFFN---LAAVG 226
Cdd:COG4559 143 QLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRgGGVVAVLHDLNLAAQYADRILLLHqgrLVAQG 222
|
..
gi 512057730 227 QP 228
Cdd:COG4559 223 TP 224
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
18-244 |
4.61e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 103.18 E-value: 4.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 18 KAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLyGAGIDPV---SVRREIGMVFQrp 94
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPT-----SGTVTIGERVI-TAGKKNKklkPLRKKVGIVFQ-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 95 npFPTMSIFD-----NVAAGlRLNGSYKKSELADIVEKSLKGANLWNEVKDRlnKPGSgLSGGQQQRLCIARAIAVEPKV 169
Cdd:PRK13634 93 --FPEHQLFEetvekDICFG-PMNFGVSEEDAKQKAREMIELVGLPEELLAR--SPFE-LSGGQMRRVAIAGVLAMEPEV 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 512057730 170 LLMDEPCSALDPISTLAIEDLIGEL-KER-FTIVIVTHNMQQAARVSDRTaffnlaAVGQPGKLIEIDDTERIFSNP 244
Cdd:PRK13634 167 LVLDEPTAGLDPKGRKEMMEMFYKLhKEKgLTTVLVTHSMEDAARYADQI------VVMHKGTVFLQGTPREIFADP 237
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
4-246 |
6.02e-26 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 101.64 E-value: 6.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 4 RIDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKST-FlrtlnRMheVTpgGRV---EGKVLLDDEDLYGagiD 79
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTtF-----YM--IV--GLVkpdSGRIFLDGEDITH---L 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 80 PVSVR--REIGMVFQRPNPFPTMSIFDNVAAGLRLNGsYKKSELADIVEKSLKGANLwNEVKDRlnkPGSGLSGGQQQRL 157
Cdd:COG1137 71 PMHKRarLGIGYLPQEASIFRKLTVEDNILAVLELRK-LSKKEREERLEELLEEFGI-THLRKS---KAYSLSGGERRRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 158 CIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSDRtaffnlAAVGQPGKLIEIDD 236
Cdd:COG1137 146 EIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERgIGVLITDHNVRETLGICDR------AYIISEGKVLAEGT 219
|
250
....*....|
gi 512057730 237 TERIFSNPSV 246
Cdd:COG1137 220 PEEILNNPLV 229
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
5-205 |
7.47e-26 |
|
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: 101.70 E-value: 7.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTPGGRVEgkvLLDDEdlYGaGIDPVSVR 84
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVR---LFGER--RG-GEDVWELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIGMV---FQRPNPfPTMSIFDNVAAGLrlNGS---YKKSELADIvEKSLKGANLWnEVKDRLNKPGSGLSGGQQQRLC 158
Cdd:COG1119 78 KRIGLVspaLQLRFP-RDETVLDVVLSGF--FDSiglYREPTDEQR-ERARELLELL-GLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 512057730 159 IARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGEL--KERFTIVIVTH 205
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLaaEGAPTLVLVTH 201
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
18-215 |
9.13e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 102.13 E-value: 9.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 18 KAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAGI--DPVSVRREIGMVFQrpn 95
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPT-----QGSVRVDDTLITSTSKnkDIKQIRKKVGLVFQ--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 96 pFPTMSIFD-----NVAAGLRlNGSYKKSELADIVEKSLKGANLWNEVKDRlnKPGSgLSGGQQQRLCIARAIAVEPKVL 170
Cdd:PRK13649 93 -FPESQLFEetvlkDVAFGPQ-NFGVSQEEAEALAREKLALVGISESLFEK--NPFE-LSGGQMRRVAIAGILAMEPKIL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 512057730 171 LMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSD 215
Cdd:PRK13649 168 VLDEPTAGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVANYAD 213
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-217 |
1.04e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 101.70 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 17 HKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAgidPVSVR-REIGMVFQrpN 95
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPD-----SGSILIDGKDVTKL---PEYKRaKYIGRVFQ--D 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 96 PF----PTMSIFDNVA-AGLR-----LNGSYKKSELADIVEKsLKGANLWNEvkDRLNKPGSGLSGGQQQRLCIARAIAV 165
Cdd:COG1101 89 PMmgtaPSMTIEENLAlAYRRgkrrgLRRGLTKKRRELFREL-LATLGLGLE--NRLDTKVGLLSGGQRQALSLLMATLT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 512057730 166 EPKVLLMDEPCSALDPISTLAIEDLIGEL--KERFTIVIVTHNMQQAARVSDRT 217
Cdd:COG1101 166 KPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNMEQALDYGNRL 219
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-208 |
1.70e-25 |
|
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: 99.79 E-value: 1.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 4 RIDVSGLTAYYGSH--KAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPV 81
Cdd:cd03369 6 EIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAE-----EGKIEIDGIDI--STIPLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 82 SVRREIGMVFQRPNPFptmsifdnvAAGLRLN----GSYKKSELADIVEKSLKGANlwnevkdrlnkpgsgLSGGQQQRL 157
Cdd:cd03369 79 DLRSSLTIIPQDPTLF---------SGTIRSNldpfDEYSDEEIYGALRVSEGGLN---------------LSQGQRQLL 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 512057730 158 CIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERFTIVIVTHNMQ 208
Cdd:cd03369 135 CLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLR 185
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-249 |
2.60e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 101.85 E-value: 2.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSH-----KAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTPGG-RVEGKVLLDDEDLYGAGI 78
Cdd:PRK13631 22 LRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTiQVGDIYIGDKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 79 DPVS--------VRREIGMVFQrpnpFPTMSIFDN----------VAAGLrlngsyKKSELADIVEKSLKGANLWNEVKD 140
Cdd:PRK13631 102 NPYSkkiknfkeLRRRVSMVFQ----FPEYQLFKDtiekdimfgpVALGV------KKSEAKKLAKFYLNKMGLDDSYLE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 141 RlnKPgSGLSGGQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELK-ERFTIVIVTHNMQQAARVSDRtaf 219
Cdd:PRK13631 172 R--SP-FGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKaNNKTVFVITHTMEHVLEVADE--- 245
|
250 260 270
....*....|....*....|....*....|
gi 512057730 220 fnlAAVGQPGKLIEIDDTERIFSNPSVQAT 249
Cdd:PRK13631 246 ---VIVMDKGKILKTGTPYEIFTDQHIINS 272
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
24-230 |
4.23e-25 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 98.78 E-value: 4.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 24 SMTVEPRTVTAFIGPSGCGKSTFLRTLNRMheVTPggrVEGKVLLDDEDLYGAGidpvSVRREIGMVFQRPNPFPTMSIF 103
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGF--IEP---ASGSIKVNDQSHTGLA----PYQRPVSMLFQENNLFAHLTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 104 DNVAAG----LRLNgSYKKSELADIVeKSLKGANLWnevkDRLnkPGSgLSGGQQQRLCIARAIAVEPKVLLMDEPCSAL 179
Cdd:TIGR01277 89 QNIGLGlhpgLKLN-AEQQEKVVDAA-QQVGIADYL----DRL--PEQ-LSGGQRQRVALARCLVRPNPILLLDEPFSAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 512057730 180 DPISTLAIEDLIGEL--KERFTIVIVTHNMQQAARVSDRTAFFNLAAVGQPGK 230
Cdd:TIGR01277 160 DPLLREEMLALVKQLcsERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSD 212
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
16-243 |
6.47e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 99.78 E-value: 6.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 16 SHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMheVTPggrVEGKVLLDDEDLYGAGiDPVSVRREIGMVFQRP- 94
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNAL--LIP---SEGKVYVDGLDTSDEE-NLWDIRNKAGMVFQNPd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 95 NPFPTMSIFDNVAAGLRlNGSYKKSELADIVEKSLKGANLWnEVKDRlnkPGSGLSGGQQQRLCIARAIAVEPKVLLMDE 174
Cdd:PRK13633 96 NQIVATIVEEDVAFGPE-NLGIPPEEIRERVDESLKKVGMY-EYRRH---APHLLSGGQKQRVAIAGILAMRPECIIFDE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512057730 175 PCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARvSDRTaffnlaAVGQPGKLIeIDDTER-IFSN 243
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVE-ADRI------IVMDSGKVV-MEGTPKeIFKE 234
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
15-205 |
7.17e-25 |
|
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: 97.62 E-value: 7.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 15 GSHKAI-EDISMTVEPRTVTAFIGPSGCGKSTFLRTL-NRmhevTPGGRVEGKVLLDdedlyGAGIDPVSVRREIGMVFQ 92
Cdd:cd03213 19 KSGKQLlKNVSGKAKPGELTAIMGPSGAGKSTLLNALaGR----RTGLGVSGEVLIN-----GRPLDKRSFRKIIGYVPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 93 RPNPFPTMSIFDN--VAAGLRlngsykkseladivekslkganlwnevkdrlnkpgsGLSGGQQQRLCIARAIAVEPKVL 170
Cdd:cd03213 90 DDILHPTLTVRETlmFAAKLR------------------------------------GLSGGERKRVSIALELVSNPSLL 133
|
170 180 190
....*....|....*....|....*....|....*.
gi 512057730 171 LMDEPCSALDPISTLAIEDLIGEL-KERFTIVIVTH 205
Cdd:cd03213 134 FLDEPTSGLDSSSALQVMSLLRRLaDTGRTIICSIH 169
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
13-233 |
7.38e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 102.73 E-value: 7.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 13 YYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVSVRREIGMVFQ 92
Cdd:PRK13657 344 YDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQ-----SGRILIDGTDI--RTVTRASLRRNIAVVFQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 93 RPNPFpTMSIFDNVAAG--------LRLngSYKKSELADIVEKSLKGANlwNEVKDRlnkpGSGLSGGQQQRLCIARAIA 164
Cdd:PRK13657 417 DAGLF-NRSIEDNIRVGrpdatdeeMRA--AAERAQAHDFIERKPDGYD--TVVGER----GRQLSGGERQRLAIARALL 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 512057730 165 VEPKVLLMDEPCSALDPISTLAIEDLIGELKERFTIVIVTHNMqQAARVSDRTAFFnlaavgQPGKLIE 233
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRL-STVRNADRILVF------DNGRVVE 549
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-217 |
8.97e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 98.50 E-value: 8.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 24 SMTVEPRTVTAFIGPSGCGKSTFLrtlNRMHEVTPGGRveGKVLLDDEDLYGAgidPVSvRREIGMVFQRPNPFPTMSIF 103
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLL---NLIAGFLTPAS--GSLTLNGQDHTTT---PPS-RRPVSMLFQENNLFSHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 104 DNVA----AGLRLNgSYKKSELADIVEKSLKGANLwnevkDRLnkPGSgLSGGQQQRLCIARAIAVEPKVLLMDEPCSAL 179
Cdd:PRK10771 90 QNIGlglnPGLKLN-AAQREKLHAIARQMGIEDLL-----ARL--PGQ-LSGGQRQRVALARCLVREQPILLLDEPFSAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 512057730 180 DPISTLAIEDLIGEL-KER-FTIVIVTHNMQQAARVSDRT 217
Cdd:PRK10771 161 DPALRQEMLTLVSQVcQERqLTLLMVSHSLEDAARIAPRS 200
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-216 |
1.32e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 99.04 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 1 MAKRIDVSGLTAYYGS---HKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygaG 77
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE-----SGQIIIDGDLL---T 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 78 IDPV-SVRREIGMVFQRP-NPFPTMSIFDNVAAGLRlNGSYKKSELADIVEKSLKGANLwNEVKDRlnKPgSGLSGGQQQ 155
Cdd:PRK13650 73 EENVwDIRHKIGMVFQNPdNQFVGATVEDDVAFGLE-NKGIPHEEMKERVNEALELVGM-QDFKER--EP-ARLSGGQKQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 512057730 156 RLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAArVSDR 216
Cdd:PRK13650 148 RVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVA-LSDR 209
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
4-216 |
1.54e-24 |
|
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: 101.75 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 4 RIDVSGLT-AYYGSHKAI-EDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGagIDPV 81
Cdd:COG4618 330 RLSVENLTvVPPGSKRPIlRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPT-----AGSVRLDGADLSQ--WDRE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 82 SVRREIGMVFQRPNPFPTmSIFDNVA----------------AG-----LRLNGSYkkseladivekslkganlwnevkD 140
Cdd:COG4618 403 ELGRHIGYLPQDVELFDG-TIAENIArfgdadpekvvaaaklAGvhemiLRLPDGY-----------------------D 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 512057730 141 -RLNKPGSGLSGGQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMqQAARVSDR 216
Cdd:COG4618 459 tRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHRP-SLLAAVDK 535
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1-249 |
6.87e-24 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 96.69 E-value: 6.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 1 MAKRIDVSGLTAYygSHKA-IEDISMTVEPRTVTAFIGPSGCGKS-TFLRTLnrmhEVTPGG--RVEGKVLLDdedlyGA 76
Cdd:PRK10418 1 MPQQIELRNIALQ--AAQPlVHGVSLTLQRGRVLALVGGSGSGKSlTCAAAL----GILPAGvrQTAGRVLLD-----GK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 77 GIDPVSVR-REIGMVFQRP----NPFPTMSifDNVAAGLRLNGsyKKSELADIVEkSLKGANLwNEVKDRLNKPGSGLSG 151
Cdd:PRK10418 70 PVAPCALRgRKIATIMQNPrsafNPLHTMH--THARETCLALG--KPADDATLTA-ALEAVGL-ENAARVLKLYPFEMSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 152 GQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKER--FTIVIVTHNMQQAARVSDRTaffnlaAVGQPG 229
Cdd:PRK10418 144 GMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKraLGMLLVTHDMGVVARLADDV------AVMSHG 217
|
250 260
....*....|....*....|
gi 512057730 230 KLIEIDDTERIFSNPSVQAT 249
Cdd:PRK10418 218 RIVEQGDVETLFNAPKHAVT 237
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-245 |
7.06e-24 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 97.85 E-value: 7.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 18 KAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAGIDPV-SVRREIGMVFQRP-- 94
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKAT-----DGEVAWLGKDLLGMKDDEWrAVRSDIQMIFQDPla 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 95 --NPfpTMSIFDNVAAGLRlngSY----KKSELADIVEKSLKGANLWNEVkdrLNKPGSGLSGGQQQRLCIARAIAVEPK 168
Cdd:PRK15079 110 slNP--RMTIGEIIAEPLR---TYhpklSRQEVKDRVKAMMLKVGLLPNL---INRYPHEFSGGQCQRIGIARALILEPK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 169 VLLMDEPCSALDpISTLA-IEDLIGEL-KE-RFTIVIVTHNMQQAARVSDRTAFFNLaavgqpGKLIEIDDTERIFSNPS 245
Cdd:PRK15079 182 LIICDEPVSALD-VSIQAqVVNLLQQLqREmGLSLIFIAHDLAVVKHISDRVLVMYL------GHAVELGTYDEVYHNPL 254
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-244 |
1.10e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 99.54 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 19 AIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDdedlyGAGIDPVS------VRREIGMVFQ 92
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQ-----GGEIIFN-----GQRIDTLSpgklqaLRRDIQFIFQ 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 93 RPNPF--PTMSIFDNVAAGLR----LNGSYKKSELADIVEK-SLKGANLWNEVKDrlnkpgsgLSGGQQQRLCIARAIAV 165
Cdd:PRK10261 409 DPYASldPRQTVGDSIMEPLRvhglLPGKAAAARVAWLLERvGLLPEHAWRYPHE--------FSGGQRQRICIARALAL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 166 EPKVLLMDEPCSALDPISTLAIEDLIGELKERFTI--VIVTHNMQQAARVSDRTAFFNLaavgqpGKLIEIDDTERIFSN 243
Cdd:PRK10261 481 NPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERISHRVAVMYL------GQIVEIGPRRAVFEN 554
|
.
gi 512057730 244 P 244
Cdd:PRK10261 555 P 555
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-216 |
1.49e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 96.32 E-value: 1.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 1 MAKRIDVSGLTAYYGSHKAIED---ISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEvtpggRVEGKVLLDDEDLYGAG 77
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDVNQlngVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFE-----EFEGKVKIDGELLTAEN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 78 IdpVSVRREIGMVFQRP-NPFPTMSIFDNVAAGLRlNGSYKKSELADIVEKSLKGANLWnevkDRLNKPGSGLSGGQQQR 156
Cdd:PRK13642 76 V--WNLRRKIGMVFQNPdNQFVGATVEDDVAFGME-NQGIPREEMIKRVDEALLAVNML----DFKTREPARLSGGQKQR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512057730 157 LCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARvSDR 216
Cdd:PRK13642 149 VAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAAS-SDR 209
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-205 |
1.54e-23 |
|
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: 94.87 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 4 RIDVSGLTAYYGSHK--AIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPV 81
Cdd:cd03244 2 DIEFKNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELS-----SGSILIDGVDI--SKIGLH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 82 SVRREIGMVFQRPNPFptmsifdnvAAGLRLN----GSYKKSELADIVEKSlKGANLWNEVKDRLNKP----GSGLSGGQ 153
Cdd:cd03244 75 DLRSRISIIPQDPVLF---------SGTIRSNldpfGEYSDEELWQALERV-GLKEFVESLPGGLDTVveegGENLSVGQ 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 512057730 154 QQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIgelKERF---TIVIVTH 205
Cdd:cd03244 145 RQLLCLARALLRKSKILVLDEATASVDPETDALIQKTI---REAFkdcTVLTIAH 196
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-251 |
1.66e-23 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 99.03 E-value: 1.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 1 MAKRIDVSGLTAYY----GSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTPGG-RVEGK--VLLDDEDL 73
Cdd:PRK10535 1 MTALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTyRVAGQdvATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 74 ygagidpVSVRRE-IGMVFQRPNPFPTMSIFDNVAAGLRLNGSYKKSELADIVEKSLKGAnlwneVKDRLNKPGSGLSGG 152
Cdd:PRK10535 81 -------AQLRREhFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLG-----LEDRVEYQPSQLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 153 QQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAArvsdrtaffnlaavgQPGKL 231
Cdd:PRK10535 149 QQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAA---------------QAERV 213
|
250 260
....*....|....*....|
gi 512057730 232 IEIDDTErIFSNPSVQATED 251
Cdd:PRK10535 214 IEIRDGE-IVRNPPAQEKVN 232
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-206 |
1.80e-23 |
|
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: 98.59 E-value: 1.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 4 RIDVSGLTAYY-GSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVS 82
Cdd:TIGR02868 334 TLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL-----QGEVTLDGVPV--SSLDQDE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 83 VRREIGMVFQRPNPFPTmSIFDNVAAGlrlNGSYKKSELADIVEKsLKGANLWNEVKDRLNKP----GSGLSGGQQQRLC 158
Cdd:TIGR02868 407 VRRRVSVCAQDAHLFDT-TVRENLRLA---RPDATDEELWAALER-VGLADWLRALPDGLDTVlgegGARLSGGERQRLA 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 512057730 159 IARAIAVEPKVLLMDEPCSALDPISTLA-IEDLIGELKERfTIVIVTHN 206
Cdd:TIGR02868 482 LARALLADAPILLLDEPTEHLDAETADElLEDLLAALSGR-TVVLITHH 529
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
18-243 |
2.04e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 96.31 E-value: 2.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 18 KAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRM-------------HEVTPGGRVEGKVLLDDEDL---YGAGIDPV 81
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALllpdtgtiewifkDEKNKKKTKEKEKVLEKLVIqktRFKKIKKI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 82 -SVRREIGMVFQrpnpFPTMSIFD-----NVAAGLRLNGSyKKSELADIVEKSLKGANLWNEVkdrLNKPGSGLSGGQQQ 155
Cdd:PRK13651 101 kEIRRRVGVVFQ----FAEYQLFEqtiekDIIFGPVSMGV-SKEEAKKRAAKYIELVGLDESY---LQRSPFELSGGQKR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 156 RLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGEL-KERFTIVIVTHNMQQAARVSDRTAFFNlaavgqPGKLIEI 234
Cdd:PRK13651 173 RVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVLEWTKRTIFFK------DGKIIKD 246
|
....*....
gi 512057730 235 DDTERIFSN 243
Cdd:PRK13651 247 GDTYDILSD 255
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
5-216 |
2.55e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 94.84 E-value: 2.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNrmHEVTPGgrvEGKVLLDDEDLygAGIDPVSVR 84
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALS--GELSPD---SGEVRLNGRPL--ADWSPAELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIGMVFQRPN---PFPTMSIfdnVAAGlRLNGSYKKSELADIVEKSLKGANLWnEVKDRLNkpgSGLSGGQQQRLCIAR 161
Cdd:PRK13548 76 RRRAVLPQHSSlsfPFTVEEV---VAMG-RAPHGLSRAEDDALVAAALAQVDLA-HLAGRDY---PQLSGGEQQRVQLAR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 512057730 162 AIA------VEPKVLLMDEPCSALDPISTLAIEDLIGEL--KERFTIVIVTHNMQQAARVSDR 216
Cdd:PRK13548 148 VLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLahERGLAVIVVLHDLNLAARYADR 210
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
18-243 |
2.87e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 95.46 E-value: 2.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 18 KAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTPGGRVEGKVLLDdedlygAGIDPVS----VRREIGMVFQr 93
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIP------ANLKKIKevkrLRKEIGLVFQ- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 94 pnpFPTMSIFDN----------VAAGLRLNGSYKK-SELADIVEKSlkganlwnevKDRLNKPGSGLSGGQQQRLCIARA 162
Cdd:PRK13645 98 ---FPEYQLFQEtiekdiafgpVNLGENKQEAYKKvPELLKLVQLP----------EDYVKRSPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 163 IAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERFT--IVIVTHNMQQAARVSDRTaffnlaAVGQPGKLIEIDDTERI 240
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKkrIIMVTHNMDQVLRIADEV------IVMHEGKVISIGSPFEI 238
|
...
gi 512057730 241 FSN 243
Cdd:PRK13645 239 FSN 241
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-216 |
3.59e-23 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 94.69 E-value: 3.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 1 MAKRIDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRM--HEVTPGGRVE--GKVLLDDEDLYGa 76
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitGDKSAGSHIEllGRTVQREGRLAR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 77 giDPVSVRREIGMVFQRPNPFPTMSIFDNVAAGL-------RLNGSYKKSELADIVEKSLKGANLWNEVKDRLnkpgSGL 149
Cdd:PRK09984 80 --DIRKSRANTGYIFQQFNLVNRLSVLENVLIGAlgstpfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRV----STL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 512057730 150 SGGQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKER--FTIVIVTHNMQQAARVSDR 216
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDYALRYCER 222
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-242 |
8.39e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 94.46 E-value: 8.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 17 HKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAGIDPV--SVRREIGMVFQrp 94
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPT-----TGTVTVDDITITHKTKDKYirPVRKRIGMVFQ-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 95 npFPTMSIF-DNVAAGLRLNGSYKKSELADIVEKSLKGANLWNEVKDRLNKPGSGLSGGQQQRLCIARAIAVEPKVLLMD 173
Cdd:PRK13646 93 --FPESQLFeDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 512057730 174 EPCSALDPISTLAIEDLIGEL--KERFTIVIVTHNMQQAARVSDRTaffnlaAVGQPGKLIEIDDTERIFS 242
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLKSLqtDENKTIILVSHDMNEVARYADEV------IVMKEGSIVSQTSPKELFK 235
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
18-244 |
1.29e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 93.74 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 18 KAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVllddeDLYGAGIDPVS-------VRREIGMV 90
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPS-----SGTI-----TIAGYHITPETgnknlkkLRKKVSLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 91 FQrpnpFPTMSIFDN-----VAAGLRlNGSYKKSELADIVEKSLKGANLWNEVkdrLNKPGSGLSGGQQQRLCIARAIAV 165
Cdd:PRK13641 91 FQ----FPEAQLFENtvlkdVEFGPK-NFGFSEDEAKEKALKWLKKVGLSEDL---ISKSPFELSGGQMRRVAIAGVMAY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 166 EPKVLLMDEPCSALDPISTLAIEDLIGEL-KERFTIVIVTHNMQQAARVSDRTaffnlaAVGQPGKLIEIDDTERIFSNP 244
Cdd:PRK13641 163 EPEILCLDEPAAGLDPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEYADDV------LVLEHGKLIKHASPKEIFSDK 236
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
12-202 |
1.32e-22 |
|
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: 96.43 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 12 AYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVSVRREIGMVF 91
Cdd:COG5265 366 GYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVT-----SGRILIDGQDI--RDVTQASLRAAIGIVP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 92 QRPNPFPTmSIFDNVAAGlRLNGSY-------KKSELADIVEKSLKGANlwNEVKDRlnkpGSGLSGGQQQRLCIARAIA 164
Cdd:COG5265 439 QDTVLFND-TIAYNIAYG-RPDASEeeveaaaRAAQIHDFIESLPDGYD--TRVGER----GLKLSGGEKQRVAIARTLL 510
|
170 180 190
....*....|....*....|....*....|....*....
gi 512057730 165 VEPKVLLMDEPCSALDPISTLAIEDLIGEL-KERFTIVI 202
Cdd:COG5265 511 KNPPILIFDEATSALDSRTERAIQAALREVaRGRTTLVI 549
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
13-234 |
1.61e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 93.33 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 13 YYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMheVTPggrVEGKVLLDDEDLYGAGIDpvSVRREIGMVFQ 92
Cdd:PRK13652 13 YSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGI--LKP---TSGSVLIRGEPITKENIR--EVRKFVGLVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 93 RPNP--FPTmSIFDNVAAGlRLNGSYKKSELADIVEKSLKGANLwNEVKDRLNKpgsGLSGGQQQRLCIARAIAVEPKVL 170
Cdd:PRK13652 86 NPDDqiFSP-TVEQDIAFG-PINLGLDEETVAHRVSSALHMLGL-EELRDRVPH---HLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512057730 171 LMDEPCSALDPISTLAIEDLIGELKER--FTIVIVTHNMQQAARVSDRTAFFNLAAVGQPGKLIEI 234
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
5-233 |
2.18e-22 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 95.96 E-value: 2.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYG-SHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTPGGRVEGKVLLDDedlygagIDPVSV 83
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKD-------IDRHTL 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 84 RREIGMVFQRPNPFpTMSIFDNVAAGLRLNGSYKK-SELADIVEKSLKGANLWNEVKDRLNKPGSGLSGGQQQRLCIARA 162
Cdd:TIGR01193 547 RQFINYLPQEPYIF-SGSILENLLLGAKENVSQDEiWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARA 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 512057730 163 IAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERfTIVIVTHNMQQAARvSDRTaffnlaAVGQPGKLIE 233
Cdd:TIGR01193 626 LLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK-TIIFVAHRLSVAKQ-SDKI------IVLDHGKIIE 688
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
10-255 |
2.22e-22 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 92.25 E-value: 2.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 10 LTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAGIDPVsVRREIGM 89
Cdd:PRK11614 11 VSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRAT-----SGRIVFDGKDITDWQTAKI-MREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 90 VFQRPNPFPTMSIFDNVAAGlrlnGSYKKSELADivEKSLKGANLWNEVKDRLNKPGSGLSGGQQQRLCIARAIAVEPKV 169
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMG----GFFAERDQFQ--ERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 170 LLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSDRtaffnlAAVGQPGKLIEIDDTERIFSNPSVQA 248
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLREQgMTIFLVEQNANQALKLADR------GYVLENGHVVLEDTGDALLANEAVRS 232
|
....*..
gi 512057730 249 TedYISG 255
Cdd:PRK11614 233 A--YLGG 237
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-242 |
2.95e-22 |
|
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: 95.25 E-value: 2.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYY-----GSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTPGgrvEGKVLLDDE--DLYGAG 77
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSG---EVNVRVGDEwvDMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 78 IDPVS-VRREIGMVFQRPNPFPTMSIFDNV--AAGLRLNGSYKKSElADIVeksLKGANLWNE-VKDRLNKPGSGLSGGQ 153
Cdd:TIGR03269 357 PDGRGrAKRYIGILHQEYDLYPHRTVLDNLteAIGLELPDELARMK-AVIT---LKMVGFDEEkAEEILDKYPDELSEGE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 154 QQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDRtaffnlAAVGQPGKL 231
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMeqTFIIVSHDMDFVLDVCDR------AALMRDGKI 506
|
250
....*....|.
gi 512057730 232 IEIDDTERIFS 242
Cdd:TIGR03269 507 VKIGDPEEIVE 517
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-233 |
3.10e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 93.74 E-value: 3.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMheVTPGgrvEGKVLLDDEdlygagidPV--- 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGM--TSPD---AGKITVLGV--------PVpar 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 82 --SVRREIGMVFQRPNPFPTMSIFDNvaagLRLNGSY---KKSELADIVEKSLKGANLWNEVKDRLnkpgSGLSGGQQQR 156
Cdd:PRK13536 109 arLARARIGVVPQFDNLDLEFTVREN----LLVFGRYfgmSTREIEAVIPSLLEFARLESKADARV----SDLSGGMKRR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 157 LCIARAIAVEPKVLLMDEPCSALDPISTLAI-EDLIGELKERFTIVIVTHNMQQAARVSDRTAFFNLA---AVGQPGKLI 232
Cdd:PRK13536 181 LTLARALINDPQLLILDEPTTGLDPHARHLIwERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGrkiAEGRPHALI 260
|
.
gi 512057730 233 E 233
Cdd:PRK13536 261 D 261
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
7-244 |
6.57e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 91.14 E-value: 6.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 7 VSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRmhEVTPGgrvEGKVLLDDE-----DLYGAGidpV 81
Cdd:PRK11701 9 VRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSA--RLAPD---AGEVHYRMRdgqlrDLYALS---E 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 82 SVRR-----EIGMVFQRPnpfptmsifdnvAAGLRLNGSYKkselADIVEKSLK-GANLWNEVK--------------DR 141
Cdd:PRK11701 81 AERRrllrtEWGFVHQHP------------RDGLRMQVSAG----GNIGERLMAvGARHYGDIRatagdwlerveidaAR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 142 LNKPGSGLSGGQQQRLCIARAIAVEPKVLLMDEPCSALDpISTLA-IEDLIGELKERF--TIVIVTHNMQQAARVSDRTa 218
Cdd:PRK11701 145 IDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD-VSVQArLLDLLRGLVRELglAVVIVTHDLAVARLLAHRL- 222
|
250 260
....*....|....*....|....*.
gi 512057730 219 ffnlaAVGQPGKLIEIDDTERIFSNP 244
Cdd:PRK11701 223 -----LVMKQGRVVESGLTDQVLDDP 243
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
19-234 |
1.01e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 90.97 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 19 AIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTPGGRVEGKVLLDDEDLygagidpVSVRREIGMVFQRP-NPF 97
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNF-------EKLRKHIGIVFQNPdNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 98 PTMSIFDNVAAGLRlNGSYKKSELADIVEKSLKGANLWnevkDRLNKPGSGLSGGQQQRLCIARAIAVEPKVLLMDEPCS 177
Cdd:PRK13648 97 VGSIVKYDVAFGLE-NHAVPYDEMHRRVSEALKQVDML----ERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 512057730 178 ALDPISTLAIEDLIGELKE--RFTIVIVTHNMQQAARvSDRTAFFNLAAVGQPGKLIEI 234
Cdd:PRK13648 172 MLDPDARQNLLDLVRKVKSehNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
16-215 |
1.12e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 91.33 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 16 SHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTPGGRVEGKVLLDDEDLYGAgIDPVsvRREIGMVFQrpn 95
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKE-IKPV--RKKVGVVFQ--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 96 pFPTMSIFD-----NVAAGLRlNGSYKKSELADIVEKSLKGANLWNEVKDrlnKPGSGLSGGQQQRLCIARAIAVEPKVL 170
Cdd:PRK13643 92 -FPESQLFEetvlkDVAFGPQ-NFGIPKEKAEKIAAEKLEMVGLADEFWE---KSPFELSGGQMRRVAIAGILAMEPEVL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 512057730 171 LMDEPCSALDPISTLAIEDLIGELKERF-TIVIVTHNMQQAARVSD 215
Cdd:PRK13643 167 VLDEPTAGLDPKARIEMMQLFESIHQSGqTVVLVTHLMDDVADYAD 212
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-204 |
1.32e-21 |
|
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: 89.64 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 18 KAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMheVTPGGRVEGKVLLDDEDLygagiDPVSVRREIGMVFQRPNPF 97
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR--VEGGGTTSGQILFNGQPR-----KPDQFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 98 PTMSIFDNV--AAGLRL----NGSYKKSELADIVEKSLKGANLWNEVKdrlnkpgSGLSGGQQQRLCIARAIAVEPKVLL 171
Cdd:cd03234 94 PGLTVRETLtyTAILRLprksSDAIRKKRVEDVLLRDLALTRIGGNLV-------KGISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190
....*....|....*....|....*....|...
gi 512057730 172 MDEPCSALDPISTLAIEDLIGELKERFTIVIVT 204
Cdd:cd03234 167 LDEPTSGLDSFTALNLVSTLSQLARRNRIVILT 199
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-216 |
2.58e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 92.40 E-value: 2.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 1 MAKRIDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEdlygagidP 80
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPD-----SGEILIDGK--------P 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 81 VSVR--RE-----IGMVFQRPNPFPTMSIFDNVAAGL--RLNGSYKKSELADIVEkslkganlwnEVKDR------LNKP 145
Cdd:COG3845 69 VRIRspRDaialgIGMVHQHFMLVPNLTVAENIVLGLepTKGGRLDRKAARARIR----------ELSERygldvdPDAK 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 512057730 146 GSGLSGGQQQRLCIARAIAVEPKVLLMDEPCSALDPistLAIEDLIGELK----ERFTIVIVTHNMQQAARVSDR 216
Cdd:COG3845 139 VEDLSVGEQQRVEILKALYRGARILILDEPTAVLTP---QEADELFEILRrlaaEGKSIIFITHKLREVMAIADR 210
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
20-214 |
3.00e-21 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 89.10 E-value: 3.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 20 IEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDL--YGAGIDPVSVRREIGMVFQRPNPF 97
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPT-----SGDVIFNGQPMskLSSAAKAELRNQKLGFIYQFHHLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 98 PTMSIFDNVAAGLrLNGSYKKSELADIVEKSLKGANLwnevKDRLNKPGSGLSGGQQQRLCIARAIAVEPKVLLMDEPCS 177
Cdd:PRK11629 100 PDFTALENVAMPL-LIGKKKPAEINSRALEMLAAVGL----EHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTG 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 512057730 178 ALDPISTLAIEDLIGELKER--FTIVIVTHNMQQAARVS 214
Cdd:PRK11629 175 NLDARNADSIFQLLGELNRLqgTAFLVVTHDLQLAKRMS 213
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-217 |
3.01e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 88.06 E-value: 3.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 14 YGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpGGRVEgkvllddedlygagidpVSVRREIGMVFQR 93
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPT-SGTVR-----------------RAGGARVAYVPQR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 94 ---PNPFPtMSIFDNVAAGL-RLNGSYKKSELAD--IVEKSLKGANLwnevKDRLNKPGSGLSGGQQQRLCIARAIAVEP 167
Cdd:NF040873 64 sevPDSLP-LTVRDLVAMGRwARRGLWRRLTRDDraAVDDALERVGL----ADLAGRQLGELSGGQRQRALLAQGLAQEA 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 512057730 168 KVLLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSDRT 217
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLAEEHARgATVVVVTHDLELVRRADPCV 189
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-233 |
3.08e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 90.25 E-value: 3.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMheVTPGGrveGKVLLDDEDLYGAGidpVSVR 84
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGL--THPDA---GSISLCGEPVPSRA---RHAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIGMVFQRPNPFPTMSIFDNvaagLRLNGSY---KKSELADIVEKSLKGANLWNevkdRLNKPGSGLSGGQQQRLCIAR 161
Cdd:PRK13537 80 QRVGVVPQFDNLDPDFTVREN----LLVFGRYfglSAAAARALVPPLLEFAKLEN----KADAKVGELSGGMKRRLTLAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512057730 162 AIAVEPKVLLMDEPCSALDPIST-LAIEDLIGELKERFTIVIVTHNMQQAARVSDRTAFFNLA---AVGQPGKLIE 233
Cdd:PRK13537 152 ALVNDPDVLVLDEPTTGLDPQARhLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGrkiAEGAPHALIE 227
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
5-243 |
4.79e-21 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 88.22 E-value: 4.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDD-----EDLygagid 79
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPT-----SGEIIFDGhpwtrKDL------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 80 pvsvrREIGMVFQRPNPFPTMSIFDNVAAGLRLNGsYKKSEladiVEKSLKGANLWNEVKdrlnKPGSGLSGGQQQRLCI 159
Cdd:TIGR03740 70 -----HKIGSLIESPPLYENLTARENLKVHTTLLG-LPDSR----IDEVLNIVDLTNTGK----KKAKQFSLGMKQRLGI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 160 ARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSDRTAFFNLAAVGQPGKLIEIDDTE 238
Cdd:TIGR03740 136 AIALLNHPKLLILDEPTNGLDPIGIQELRELIRSFPEQgITVILSSHILSEVQQLADHIGIISEGVLGYQGKINKSENLE 215
|
....*
gi 512057730 239 RIFSN 243
Cdd:TIGR03740 216 KLFVE 220
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
5-244 |
8.57e-21 |
|
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: 88.35 E-value: 8.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLnrmhevtpGGRV---EGKVLLDDEDLYGAGIDPV 81
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCL--------AGRLapdHGTATYIMRSGAELELYQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 82 S-------VRREIGMVFQRPnpfptmsifdnvAAGLRLNGSYKkselADIVEKSL-----------KGANLW-NEVK--- 139
Cdd:TIGR02323 76 SeaerrrlMRTEWGFVHQNP------------RDGLRMRVSAG----ANIGERLMaigarhygnirATAQDWlEEVEidp 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 140 DRLNKPGSGLSGGQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERFTI--VIVTHNMQQAARVSDRT 217
Cdd:TIGR02323 140 TRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLavIIVTHDLGVARLLAQRL 219
|
250 260
....*....|....*....|....*..
gi 512057730 218 affnlaAVGQPGKLIEIDDTERIFSNP 244
Cdd:TIGR02323 220 ------LVMQQGRVVESGLTDQVLDDP 240
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-258 |
9.13e-21 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 88.31 E-value: 9.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 18 KAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDL-YGagiDPVSVRREIGMVFQRP-- 94
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPT-----SGELLIDDHPLhFG---DYSYRSQRIRMIFQDPst 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 95 --NPFPTMS-IFDnvaAGLRLNGSYKKSELADIVEKSLKGANLwneVKDRLNKPGSGLSGGQQQRLCIARAIAVEPKVLL 171
Cdd:PRK15112 99 slNPRQRISqILD---FPLRLNTDLEPEQREKQIIETLRQVGL---LPDHASYYPHMLAPGQKQRLGLARALILRPKVII 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 172 MDEPCSALDPISTLAIEDLIGELKERFTI--VIVTHNMQQAARVSDRTaffnlaAVGQPGKLIEIDDTERIFSNPSVQAT 249
Cdd:PRK15112 173 ADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHISDQV------LVMHQGEVVERGSTADVLASPLHELT 246
|
....*....
gi 512057730 250 EDYISGRFG 258
Cdd:PRK15112 247 KRLIAGHFG 255
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
5-208 |
1.09e-20 |
|
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: 86.75 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGS-----HKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLnrMHEVTpggRVEGKVllddedlygagid 79
Cdd:cd03250 1 ISVEDASFTWDSgeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL--LGELE---KLSGSV------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 80 pvSVRREIGMVFQrpNPF-PTMSIFDNVAAGLRLNGS-YKK-----SELADIveKSLKGANLwNEVKDRlnkpGSGLSGG 152
Cdd:cd03250 63 --SVPGSIAYVSQ--EPWiQNGTIRENILFGKPFDEErYEKvikacALEPDL--EILPDGDL-TEIGEK----GINLSGG 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 512057730 153 QQQRLCIARAIAVEPKVLLMDEPCSALDP-ISTLAIEDLI-GELKERFTIVIVTHNMQ 208
Cdd:cd03250 132 QKQRISLARAVYSDADIYLLDDPLSAVDAhVGRHIFENCIlGLLLNNKTRILVTHQLQ 189
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
16-220 |
2.19e-20 |
|
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: 85.44 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 16 SHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRmhEVTPGgrvEGKVLLDDEDLYGAGidpVSVRREIGMVFQRPN 95
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG--DLKPQ---QGEITLDGVPVSDLE---KALSSLISVLNQRPY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 96 PFPTmSIFDNVaaGLRLngsykkseladivekslkganlwnevkdrlnkpgsglSGGQQQRLCIARAIAVEPKVLLMDEP 175
Cdd:cd03247 86 LFDT-TLRNNL--GRRF-------------------------------------SGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 512057730 176 CSALDPISTLAIEDLIGELKERFTIVIVTHNMQQAARVsDRTAFF 220
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHM-DKILFL 169
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
20-205 |
2.66e-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: 89.62 E-value: 2.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 20 IEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVSVRREIGMVFQRPNPF-- 97
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPW-----SGEILFDGIPR--EEIPREVLANSVAMVDQDIFLFeg 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 98 ----------PTMSIFDNVAAGlrlngsyKKSELADIVeKSLKGAnlwneVKDRLNKPGSGLSGGQQQRLCIARAIAVEP 167
Cdd:TIGR03796 568 tvrdnltlwdPTIPDADLVRAC-------KDAAIHDVI-TSRPGG-----YDAELAEGGANLSGGQRQRLEIARALVRNP 634
|
170 180 190
....*....|....*....|....*....|....*....
gi 512057730 168 KVLLMDEPCSALDPISTLAIEDligELKER-FTIVIVTH 205
Cdd:TIGR03796 635 SILILDEATSALDPETEKIIDD---NLRRRgCTCIIVAH 670
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-215 |
5.33e-20 |
|
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: 88.73 E-value: 5.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHevtPGGRVEGKVLLDDEDLYGAGIDPVSvR 84
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY---PHGTWDGEIYWSGSPLKASNIRDTE-R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIGMVFQRPNPFPTMSIFDNVAAG--LRLNGSykkseLADIVEKSLKGANLWNEVK---DRLNKPGSGLSGGQQQRLCI 159
Cdd:TIGR02633 78 AGIVIIHQELTLVPELSVAENIFLGneITLPGG-----RMAYNAMYLRAKNLLRELQldaDNVTRPVGDYGGGQQQLVEI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 512057730 160 ARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSD 215
Cdd:TIGR02633 153 AKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHgVACVYISHKLNEVKAVCD 209
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
15-206 |
1.23e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 84.38 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 15 GSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVSVRREIGMVFQRP 94
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPT-----SGTLLFEGEDI--STLKPEIYRQQVSYCAQTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 95 NPFPTmSIFDNVAAGLRLNgsyKKSELADIVEKSLKGANLWNEVkdrLNKPGSGLSGGQQQRLCIARAIAVEPKVLLMDE 174
Cdd:PRK10247 91 TLFGD-TVYDNLIFPWQIR---NQQPDPAIFLDDLERFALPDTI---LTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190
....*....|....*....|....*....|....
gi 512057730 175 PCSALDPISTLAIEDLIGELKERFTIVI--VTHN 206
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVREQNIAVlwVTHD 197
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
23-216 |
1.27e-19 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 84.45 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 23 ISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAGIDPVSVRR--EIGMVFQRPNPFPTM 100
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGS-----SGEVSLVGQPLHQMDEEARAKLRakHVGFVFQSFMLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 101 SIFDNVAAGLRLNGSYKKSELADIVEKsLKGANLwnevKDRLNKPGSGLSGGQQQRLCIARAIAVEPKVLLMDEPCSALD 180
Cdd:PRK10584 104 NALENVELPALLRGESSRQSRNGAKAL-LEQLGL----GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 512057730 181 PISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDR 216
Cdd:PRK10584 179 RQTGDKIADLLFSLNREHgtTLILVTHDLQLAARCDRR 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-217 |
1.35e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.43 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLnrMHEVTP-GGRVEgkvllddedlYGAGIdpvsv 83
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLL--AGELEPdSGTVK----------LGETV----- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 84 rrEIGMVFQRPNPF-PTMSIFDNVAAGLRlNGsyKKSELADIVEKSL-KGanlwnevkDRLNKPGSGLSGGQQQRLCIAR 161
Cdd:COG0488 379 --KIGYFDQHQEELdPDKTVLDELRDGAP-GG--TEQEVRGYLGRFLfSG--------DDAFKPVGVLSGGEKARLALAK 445
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 512057730 162 AIAVEPKVLLMDEPCSALDpISTL-AIEDLIgelkERF--TIVIVTHNMQQAARVSDRT 217
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLD-IETLeALEEAL----DDFpgTVLLVSHDRYFLDRVATRI 499
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-221 |
2.01e-19 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 87.39 E-value: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 4 RIDVSGLTAYYGSHKAI---EDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEV------------------------ 56
Cdd:PTZ00265 1165 KIEIMDVNFRYISRPNVpiyKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtndmtneqdyqg 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 57 -----------------TPGGRVE--------GKVLLDDEDLYGAGIDpvSVRREIGMVFQRPNPFpTMSIFDNVAAGlr 111
Cdd:PTZ00265 1245 deeqnvgmknvnefsltKEGGSGEdstvfknsGKILLDGVDICDYNLK--DLRNLFSIVSQEPMLF-NMSIYENIKFG-- 1319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 112 lngsyKKSELADIVEKSLKGA-------NLWNEVKDRLNKPGSGLSGGQQQRLCIARAIAVEPKVLLMDEPCSALDPIST 184
Cdd:PTZ00265 1320 -----KEDATREDVKRACKFAaidefieSLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSE 1394
|
250 260 270
....*....|....*....|....*....|....*....
gi 512057730 185 LAIEDLIGELKERF--TIVIVTHNMQQAARvSDRTAFFN 221
Cdd:PTZ00265 1395 KLIEKTIVDIKDKAdkTIITIAHRIASIKR-SDKIVVFN 1432
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-241 |
2.19e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 84.36 E-value: 2.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVSVR 84
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPD-----SGEVLVDGLDV--ATTPSRELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIGMVFQRPNPFPTMSIFDNVAAGL------RLNgsykkSELADIVEKSLKGANLwNEVKDR-LNKpgsgLSGGQQQRL 157
Cdd:COG4604 75 KRLAILRQENHINSRLTVRELVAFGRfpyskgRLT-----AEDREIIDEAIAYLDL-EDLADRyLDE----LSGGQRQRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 158 CIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDR-TAFFN--LAAVGQPGKLI 232
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELgkTVVIVLHDINFASCYADHiVAMKDgrVVAQGTPEEII 224
|
....*....
gi 512057730 233 EIDDTERIF 241
Cdd:COG4604 225 TPEVLSDIY 233
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
12-217 |
2.99e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 83.39 E-value: 2.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 12 AYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAGIDPVS-VRREIGMV 90
Cdd:PRK10908 10 AYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPS-----AGKIWFSGHDITRLKNREVPfLRRQIGMI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 91 FQRPNPFPTMSIFDNVAAGLRLNGSyKKSELADIVEKSLKGANLWNEVKdrlNKPGSgLSGGQQQRLCIARAIAVEPKVL 170
Cdd:PRK10908 85 FQDHHLLMDRTVYDNVAIPLIIAGA-SGDDIRRRVSAALDKVGLLDKAK---NFPIQ-LSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 512057730 171 LMDEPCSALDPistlAIEDLIGELKERF-----TIVIVTHNMQQAARVSDRT 217
Cdd:PRK10908 160 LADEPTGNLDD----ALSEGILRLFEEFnrvgvTVLMATHDIGLISRRSYRM 207
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
12-205 |
3.54e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 86.23 E-value: 3.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 12 AYYGSHK-AIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDL--YGAGidpvSVRREIG 88
Cdd:PRK11176 350 TYPGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDID-----EGEILLDGHDLrdYTLA----SLRNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 89 MVFQRPNPFPTmSIFDNVAAGLrlNGSYKKSEladiVEKSLKGA---NLWNEVKDRLN----KPGSGLSGGQQQRLCIAR 161
Cdd:PRK11176 421 LVSQNVHLFND-TIANNIAYAR--TEQYSREQ----IEEAARMAyamDFINKMDNGLDtvigENGVLLSGGQRQRIAIAR 493
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 512057730 162 AIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERFTIVIVTH 205
Cdd:PRK11176 494 ALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAH 537
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-249 |
4.33e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 85.91 E-value: 4.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 15 GSHKAIEDISMTVEPRTVTAFIGPSGCGKST----FLRTLNRmhevtpggrvEGKVLLDDEDLYGAGIDP-VSVRREIGM 89
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS----------QGEIWFDGQPLHNLNRRQlLPVRHRIQV 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 90 VFQRPNPF--PTMSIFDNVAAGLRLNgsykkseladivEKSLKGANLWNEVKDRLNKPG----------SGLSGGQQQRL 157
Cdd:PRK15134 367 VFQDPNSSlnPRLNVLQIIEEGLRVH------------QPTLSAAQREQQVIAVMEEVGldpetrhrypAEFSGGQRQRI 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 158 CIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGEL--KERFTIVIVTHNMqQAARvsdrtAFFNLAAVGQPGKLIEID 235
Cdd:PRK15134 435 AIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLqqKHQLAYLFISHDL-HVVR-----ALCHQVIVLRQGEVVEQG 508
|
250
....*....|....
gi 512057730 236 DTERIFSNPSVQAT 249
Cdd:PRK15134 509 DCERVFAAPQQEYT 522
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-244 |
5.04e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 85.91 E-value: 5.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 17 HKAIEDISMTVEPRTVTAFIGPSGCGKS----TFLRTLNRMHEVTPGG--RVEGKVLL--DDEDLYGagidpvsVR-REI 87
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVYPSGdiRFHGESLLhaSEQTLRG-------VRgNKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 88 GMVFQRP----NPFPTmsIFDNVAAGLRLN-GSYKKSELADIVEkSLKGANLWNEVKdRLNKPGSGLSGGQQQRLCIARA 162
Cdd:PRK15134 95 AMIFQEPmvslNPLHT--LEKQLYEVLSLHrGMRREAARGEILN-CLDRVGIRQAAK-RLTDYPHQLSGGERQRVMIAMA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 163 IAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDRTaffnlaAVGQPGKLIEIDDTERI 240
Cdd:PRK15134 171 LLTRPELLIADEPTTALDVSVQAQILQLLRELQQELnmGLLFITHNLSIVRKLADRV------AVMQNGRCVEQNRAATL 244
|
....
gi 512057730 241 FSNP 244
Cdd:PRK15134 245 FSAP 248
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
20-206 |
8.13e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 82.42 E-value: 8.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 20 IEDISMTVEPRTVTAFIGPSGCGKSTFLRTL--NRMHEVTpggrvEGKVLLDDEDLYGAGIDPVSvRREIGMVFQRPNPF 97
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVT-----SGSILLDGEDILELSPDERA-RAGIFLAFQYPVEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 98 P--TMSIFDNVAAGLRLNGSYKKSELADIVEKSLKGANLWNEVKDR-LNkpgSGLSGGQQQRLCIARAIAVEPKVLLMDE 174
Cdd:COG0396 90 PgvSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLDEDFLDRyVN---EGFSGGEKKRNEILQMLLLEPKLAILDE 166
|
170 180 190
....*....|....*....|....*....|....
gi 512057730 175 PCSALDpISTLAI-EDLIGELK-ERFTIVIVTHN 206
Cdd:COG0396 167 TDSGLD-IDALRIvAEGVNKLRsPDRGILIITHY 199
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-206 |
1.16e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 84.88 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYY--GSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVS 82
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQ-----QGEILLNGQPI--ADYSEAA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 83 VRREIGMVFQRPNPFPTmSIFDNVAAGL------RLNGSYKKSELADIVEkSLKGANLWnevkdrLNKPGSGLSGGQQQR 156
Cdd:PRK11160 412 LRQAISVVSQRVHLFSA-TLRDNLLLAApnasdeALIEVLQQVGLEKLLE-DDKGLNAW------LGEGGRQLSGGEQRR 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 512057730 157 LCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERFTIVIVTHN 206
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHR 533
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-215 |
1.27e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 84.12 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMheVTPGGrveGKVLLDDEDLygAGIDPVSVR 84
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGT--LTPTA---GTVLVAGDDV--EALSARAAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIGMVfqrpnPFPTMSIFD-NVAAGLRLNGSYKKSELAD-------IVEKSLKGAnlwnEVKDRLNKPGSGLSGGQQQR 156
Cdd:PRK09536 77 RRVASV-----PQDTSLSFEfDVRQVVEMGRTPHRSRFDTwtetdraAVERAMERT----GVAQFADRPVTSLSGGERQR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 512057730 157 LCIARAIAVEPKVLLMDEPCSALD---PISTLA-IEDLIGELKerfTIVIVTHNMQQAARVSD 215
Cdd:PRK09536 148 VLLARALAQATPVLLLDEPTASLDinhQVRTLElVRRLVDDGK---TAVAAIHDLDLAARYCD 207
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-205 |
1.42e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 84.77 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 4 RIDVSGLT-AYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVS 82
Cdd:PRK10790 340 RIDIDNVSfAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLT-----EGEIRLDGRPL--SSLSHSV 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 83 VRREIGMVFQRPNPFPTmSIFDNVAAGLRLN-----GSYKKSELADIVEKSLKGANlwnevkDRLNKPGSGLSGGQQQRL 157
Cdd:PRK10790 413 LRQGVAMVQQDPVVLAD-TFLANVTLGRDISeeqvwQALETVQLAELARSLPDGLY------TPLGEQGNNLSVGQKQLL 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 512057730 158 CIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERFTIVIVTH 205
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAH 533
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
19-247 |
1.43e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 82.73 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 19 AIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLddedlygAGIDPVS------VRREIGMVFQ 92
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQ-----KGKVLV-------SGIDTGDfsklqgIRKLVGIVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 93 RPNP-FPTMSIFDNVAAGLRlNGSYKKSELADIVEKSLKGANLwneVKDRLNKPGSgLSGGQQQRLCIARAIAVEPKVLL 171
Cdd:PRK13644 85 NPETqFVGRTVEEDLAFGPE-NLCLPPIEIRKRVDRALAEIGL---EKYRHRSPKT-LSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 512057730 172 MDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQaARVSDRTaffnlaAVGQPGKLIEIDDTERIFSNPSVQ 247
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEE-LHDADRI------IVMDRGKIVLEGEPENVLSDVSLQ 229
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
19-218 |
1.50e-18 |
|
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: 85.07 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 19 AIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYgAGIDpvSVRREIGMVFQRPNPFP 98
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPT-----SGTVLVGGKDIE-TNLD--AVRQSLGMCPQHNILFH 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 99 TMSIFDNVAAGLRLNG-SYKKSELAdiVEKSLKGANLWNevkdRLNKPGSGLSGGQQQRLCIARAIAVEPKVLLMDEPCS 177
Cdd:TIGR01257 1017 HLTVAEHILFYAQLKGrSWEEAQLE--MEAMLEDTGLHH----KRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 512057730 178 ALDPISTLAIEDLIGELKERFTIVIVTHNMQQAARVSDRTA 218
Cdd:TIGR01257 1091 GVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIA 1131
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
3-238 |
1.56e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 81.67 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 3 KRIDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpGGRVE--GKV--LLDdedlYGAGI 78
Cdd:COG1134 25 KELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPT-SGRVEvnGRVsaLLE----LGAGF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 79 DP-VSVRreigmvfqrpnpfptmsifDNVaaglRLNGS---YKKSE----LADIVEKSlkganlwnEVKDRLNKPGSGLS 150
Cdd:COG1134 100 HPeLTGR-------------------ENI----YLNGRllgLSRKEidekFDEIVEFA--------ELGDFIDQPVKTYS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 151 GGQQQRLCIARAIAVEPKVLLMDEpcsaldpisTLAI---------EDLIGELKERF-TIVIVTHNMQQAARVSDRtaff 220
Cdd:COG1134 149 SGMRARLAFAVATAVDPDILLVDE---------VLAVgdaafqkkcLARIRELRESGrTVIFVSHSMGAVRRLCDR---- 215
|
250
....*....|....*...
gi 512057730 221 nlAAVGQPGKLIEIDDTE 238
Cdd:COG1134 216 --AIWLEKGRLVMDGDPE 231
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-205 |
2.47e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.96 E-value: 2.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 7 VSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLnrMHEVTP-GGRvegkvllddedlygagidpVSVRR 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKIL--AGELEPdSGE-------------------VSIPK 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 86 --EIGMVFQRPNPFPTMSIFDNVAAGL--------RLNGSYKK--------SELADIVEKsLKGANLWN---EVK----- 139
Cdd:COG0488 60 glRIGYLPQEPPLDDDLTVLDTVLDGDaelraleaELEELEAKlaepdedlERLAELQEE-FEALGGWEaeaRAEeilsg 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 512057730 140 -----DRLNKPGSGLSGGQQQRLCIARAIAVEPKVLLMDEPCSALDpistL-AIEDLIGELKER-FTIVIVTH 205
Cdd:COG0488 139 lgfpeEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD----LeSIEWLEEFLKNYpGTVLVVSH 207
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
14-216 |
2.62e-18 |
|
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: 81.22 E-value: 2.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 14 YGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMheVTP-GGRVegKVllddedlygAGIDPVSVRRE----IG 88
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGL--LQPtSGEV--RV---------AGLVPWKRRKKflrrIG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 89 MVF-QRpnpfpTMSIFD-NVAAGLRLN--------GSYKKS--ELADIVEkslkganlwneVKDRLNKPGSGLSGGQQQR 156
Cdd:cd03267 98 VVFgQK-----TQLWWDlPVIDSFYLLaaiydlppARFKKRldELSELLD-----------LEELLDTPVRQLSLGQRMR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512057730 157 LCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGEL-KERFTIVIVT-HNMQQAARVSDR 216
Cdd:cd03267 162 AEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTsHYMKDIEALARR 223
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
7-206 |
2.87e-18 |
|
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: 80.26 E-value: 2.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 7 VSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTL--NRMHEVTpggrvEGKVLLDDEDLYGAGIDpVSVR 84
Cdd:cd03217 3 IKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVT-----EGEILFKGEDITDLPPE-ERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIGMVFQRPNPFPtmsifdnvaaGLRlngsykkseladivekslkganlwneVKDRLNKPGSGLSGGQQQRLCIARAIA 164
Cdd:cd03217 77 LGIFLAFQYPPEIP----------GVK--------------------------NADFLRYVNEGFSGGEKKRNEILQLLL 120
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 512057730 165 VEPKVLLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHN 206
Cdd:cd03217 121 LEPDLAILDEPDSGLDIDALRLVAEVINKLREEgKSVLIITHY 163
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
23-244 |
3.20e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 81.37 E-value: 3.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 23 ISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygAGIDPVSVRREIGMVFQRPNPFPTMSI 102
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPS-----EGEILLDAQPL--ESWSSKAFARKVAYLPQQLPAAEGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 103 FDNVAAG-LRLNGSYKKSELAD--IVEKSLKGANLwnevKDRLNKPGSGLSGGQQQRLCIARAIAVEPKVLLMDEPCSAL 179
Cdd:PRK10575 103 RELVAIGrYPWHGALGRFGAADreKVEEAISLVGL----KPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSAL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 180 DPISTLAIEDLIGEL-KER-FTIVIVTHNMQQAARVSDRTAFF---NLAAVGQPGKLIEIDDTERIFSNP 244
Cdd:PRK10575 179 DIAHQVDVLALVHRLsQERgLTVIAVLHDINMAARYCDYLVALrggEMIAQGTPAELMRGETLEQIYGIP 248
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
15-205 |
7.13e-18 |
|
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: 82.40 E-value: 7.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 15 GSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLnrmheVTPGGRVEGKVLLDDEDLYGagIDPVSVRREIGMVFQRP 94
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLI-----VGIWPPTSGSVRLDGADLKQ--WDRETFGKHIGYLPQDV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 95 NPFPTmSIFDNVAaglRLNGS------YKKSELADIVEKSLKGANLWNEVkdrLNKPGSGLSGGQQQRLCIARAIAVEPK 168
Cdd:TIGR01842 402 ELFPG-TVAENIA---RFGENadpekiIEAAKLAGVHELILRLPDGYDTV---IGPGGATLSGGQRQRIALARALYGDPK 474
|
170 180 190
....*....|....*....|....*....|....*...
gi 512057730 169 VLLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTH 205
Cdd:TIGR01842 475 LVVLDEPNSNLDEEGEQALANAIKALKARgITVVVITH 512
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
19-245 |
7.15e-18 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 81.31 E-value: 7.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 19 AIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLnrMHEVTPGGRVEGKVLLDDEDLYGAGIDPVSVRR--EIGMVFQRP-- 94
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFAL--MGLLAANGRIGGSATFNGREILNLPEKELNKLRaeQISMIFQDPmt 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 95 --NPFptMSIFDNVAAGLRLNGSYKKSEladIVEKSLK--GANLWNEVKDRLNKPGSGLSGGQQQRLCIARAIAVEPKVL 170
Cdd:PRK09473 109 slNPY--MRVGEQLMEVLMLHKGMSKAE---AFEESVRmlDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 512057730 171 LMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDRTaffnlaAVGQPGKLIEIDDTERIFSNPS 245
Cdd:PRK09473 184 IADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKV------LVMYAGRTMEYGNARDVFYQPS 254
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-216 |
1.16e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 79.50 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 23 ISMTVEPRTVTAFIGPSGCGKSTFlrtLNRMHEVTPGgrvEGKVLLDDEDLygAGIDPVSVRREIGMVFQRPNPFPTMSI 102
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTL---LARMAGLLPG---QGEILLNGRPL--SDWSAAELARHRAYLSQQQSPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 103 FDNVAAGLRLNGS--YKKSELADIVEKsLKganlwneVKDRLNKPGSGLSGGQQQRLCIARAI-----AVEP--KVLLMD 173
Cdd:COG4138 87 FQYLALHQPAGASseAVEQLLAQLAEA-LG-------LEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPegQLLLLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 512057730 174 EPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSDR 216
Cdd:COG4138 159 EPMNSLDVAQQAALDRLLRELCQQgITVVMSSHDLNHTLRHADR 202
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-234 |
2.16e-17 |
|
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: 81.00 E-value: 2.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTP-GGRV--------------------- 62
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPtSGRIiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 63 -----EGKVLLDDEDLYGAGiDPV--SVRREIGMVFQRPNP-FPTMSIFDNVAAGLRLNGsYKKSELADIVEKSLKGANL 134
Cdd:TIGR03269 81 pcpvcGGTLEPEEVDFWNLS-DKLrrRIRKRIAIMLQRTFAlYGDDTVLDNVLEALEEIG-YEGKEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 135 wnevKDRLNKPGSGLSGGQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGEL--KERFTIVIVTHNMQQAAR 212
Cdd:TIGR03269 159 ----SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIED 234
|
250 260
....*....|....*....|..
gi 512057730 213 VSDRTAFFNLAAVGQPGKLIEI 234
Cdd:TIGR03269 235 LSDKAIWLENGEIKEEGTPDEV 256
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-216 |
4.06e-17 |
|
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: 76.70 E-value: 4.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 4 RIDVSGLTAyygsHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygaGIDPVSV 83
Cdd:cd03215 4 VLEVRGLSV----KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPA-----SGEITLDGKPV---TRRSPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 84 RREIGMVF-----QRPNPFPTMSIFDNVAAGlrlngsykkseladivekslkganlwnevkdrlnkpgSGLSGGQQQRLC 158
Cdd:cd03215 72 AIRAGIAYvpedrKREGLVLDLSVAENIALS-------------------------------------SLLSGGNQQKVV 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 512057730 159 IARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSDR 216
Cdd:cd03215 115 LARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAgKAVLLISSELDELLGLCDR 173
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-202 |
4.42e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 80.46 E-value: 4.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 3 KRIDVSGLTAYYGSHKAIE---DISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDlygaGID 79
Cdd:PTZ00265 381 KKIQFKNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPT-----EGDIIINDSH----NLK 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 80 PVSV---RREIGMVFQRPNPFpTMSIFDNVAAGL---------------RLNGSY------------------------- 116
Cdd:PTZ00265 452 DINLkwwRSKIGVVSQDPLLF-SNSIKNNIKYSLyslkdlealsnyyneDGNDSQenknkrnscrakcagdlndmsnttd 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 117 --------------KKSELADIVEKSLKG---ANLWNEVKDRLNKPGSGLSGGQQQRLCIARAIAVEPKVLLMDEPCSAL 179
Cdd:PTZ00265 531 sneliemrknyqtiKDSEVVDVSKKVLIHdfvSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSL 610
|
250 260
....*....|....*....|....*.
gi 512057730 180 DPISTLAIEDLIGELK---ERFTIVI 202
Cdd:PTZ00265 611 DNKSEYLVQKTINNLKgneNRITIII 636
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
23-209 |
4.48e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 80.27 E-value: 4.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 23 ISMTVEPRTVTAFIGPSGCGKSTFLRTLNrmhevtpgGRV--EGKVLLDDEDLygAGIDPVSVRREIGMVFQRPNPFPTm 100
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALL--------GFLpyQGSLKINGIEL--RELDPESWRKHLSWVGQNPQLPHG- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 101 SIFDNVAAG------LRLNGSYKKSELADIVEKSLKGANLwnEVKDRlnkpGSGLSGGQQQRLCIARAIAVEPKVLLMDE 174
Cdd:PRK11174 438 TLRDNVLLGnpdasdEQLQQALENAWVSEFLPLLPQGLDT--PIGDQ----AAGLSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190
....*....|....*....|....*....|....*
gi 512057730 175 PCSALDPISTLAIEDLIGELKERFTIVIVTHNMQQ 209
Cdd:PRK11174 512 PTASLDAHSEQLVMQALNAASRRQTTLMVTHQLED 546
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
8-231 |
3.09e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 76.20 E-value: 3.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 8 SGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMheVTPGgrvEGKVLLDDEDLYGAGIDPVSVRREI 87
Cdd:PRK13638 5 SDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGL--LRPQ---KGAVLWQGKPLDYSKRGLLALRQQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 88 GMVFQRPNP--FPTmSIFDNVAAGLRlNGSYKKSELADIVEKSLkgaNLWNEVKDRlNKPGSGLSGGQQQRLCIARAIAV 165
Cdd:PRK13638 80 ATVFQDPEQqiFYT-DIDSDIAFSLR-NLGVPEAEITRRVDEAL---TLVDAQHFR-HQPIQCLSHGQKKRVAIAGALVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 166 EPKVLLMDEPCSALDPISTLAIEDLIGELKERFT-IVIVTHNMQQAARVSDRTAFF---NLAAVGQPGKL 231
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNhVIISSHDIDLIYEISDAVYVLrqgQILTHGAPGEV 223
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-205 |
3.22e-16 |
|
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: 73.25 E-value: 3.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLnrMHEVTPggrVEGKVLLDDedlygagidpvsvR 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLI--AGELEP---DEGIVTWGS-------------T 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIGMVFQrpnpfptmsifdnvaaglrlngsykkseladivekslkganlwnevkdrlnkpgsgLSGGQQQRLCIARAIA 164
Cdd:cd03221 63 VKIGYFEQ--------------------------------------------------------LSGGEKMRLALAKLLL 86
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 512057730 165 VEPKVLLMDEPCSALDPIStlaIEDLIGELKE-RFTIVIVTH 205
Cdd:cd03221 87 ENPNLLLLDEPTNHLDLES---IEALEEALKEyPGTVILVSH 125
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
5-244 |
3.70e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 76.70 E-value: 3.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSH----KAIEDISMTVEPRTVTAFIGPSGCGKStfLRTLNRMHEVTPGGRVEG-KVLLDDEDLygAGID 79
Cdd:PRK11022 4 LNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKS--VSSLAIMGLIDYPGRVMAeKLEFNGQDL--QRIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 80 PVSVRR----EIGMVFQRP----NPFPTMSiFDNVAAGLRLNGSYKKSELADIVEkslkganLWNEV-----KDRLNKPG 146
Cdd:PRK11022 80 EKERRNlvgaEVAMIFQDPmtslNPCYTVG-FQIMEAIKVHQGGNKKTRRQRAID-------LLNQVgipdpASRLDVYP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 147 SGLSGGQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGEL--KERFTIVIVTHNMQQAARVSDRTaffnlaA 224
Cdd:PRK11022 152 HQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALVLITHDLALVAEAAHKI------I 225
|
250 260
....*....|....*....|
gi 512057730 225 VGQPGKLIEIDDTERIFSNP 244
Cdd:PRK11022 226 VMYAGQVVETGKAHDIFRAP 245
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
22-244 |
4.29e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 76.45 E-value: 4.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 22 DISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMheVTPG-GRV--EGKVLLDDEdlygAGIDPVSVRREIGMVFQRPNPFP 98
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGL--TRPQkGRIvlNGRVLFDAE----KGICLPPEKRRIGYVFQDARLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 99 TMSIFDNVAAGLRlngSYKKSELADIVEksLKGanlwneVKDRLNKPGSGLSGGQQQRLCIARAIAVEPKVLLMDEPCSA 178
Cdd:PRK11144 90 HYKVRGNLRYGMA---KSMVAQFDKIVA--LLG------IEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLAS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 512057730 179 LD-P--------ISTLAIEDLIgelkerfTIVIVTHNMQQAARVSDrtaffNLAAVGQpGKLIEIDDTERIFSNP 244
Cdd:PRK11144 159 LDlPrkrellpyLERLAREINI-------PILYVSHSLDEILRLAD-----RVVVLEQ-GKVKAFGPLEEVWASS 220
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-205 |
5.10e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 77.15 E-value: 5.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 20 IEDISMTVEPRTVTAFIGPSGCGKSTFLRTLnrmhevtpggrvegkvllddedlygAGIDP-----VSVRREIGMVF--Q 92
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAI-------------------------AGLWPygsgrIARPAGARVLFlpQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 93 RPNpFPTMSifdnvaagLR-------LNGSYKKSELADIVEKslkgANLwNEVKDRLNKP---GSGLSGGQQQRLCIARA 162
Cdd:COG4178 434 RPY-LPLGT--------LReallypaTAEAFSDAELREALEA----VGL-GHLAERLDEEadwDQVLSLGEQQRLAFARL 499
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 512057730 163 IAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERFTIVIVTH 205
Cdd:COG4178 500 LLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGH 542
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-207 |
8.21e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 74.38 E-value: 8.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 1 MAKRIDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTPGgrvegkVLLDDEDLygagidp 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG------VIKRNGKL------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 81 vsvrrEIGMVFQRPNPFPTMSIfdNVAAGLRLNGSYKKselADIVE--KSLKGANLwnevkdrLNKPGSGLSGGQQQRLC 158
Cdd:PRK09544 68 -----RIGYVPQKLYLDTTLPL--TVNRFLRLRPGTKK---EDILPalKRVQAGHL-------IDAPMQKLSGGETQRVL 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 512057730 159 IARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNM 207
Cdd:PRK09544 131 LARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELdcAVLMVSHDL 181
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
20-204 |
1.06e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 76.24 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 20 IEDISMTVEPRTVTAFIGPSGCGKSTFLRTLnrMHEVTPGGRVEGKVLLDdedlyGAGIDPVSVRREIGMVFQRPNPFPT 99
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNAL--AFRSPKGVKGSGSVLLN-----GMPIDAKEMRAISAYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 100 MSIFD--NVAAGLRLNGSYKKSELADIVEKSLKGANLWNEVKDRLNKPGS--GLSGGQQQRLCIARAIAVEPKVLLMDEP 175
Cdd:TIGR00955 114 LTVREhlMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180
....*....|....*....|....*....
gi 512057730 176 CSALDPISTLAIEDLIGELKERFTIVIVT 204
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGLAQKGKTIICT 222
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-215 |
1.27e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 76.14 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNrmhevtpggrveGKVLLDDEDLYGAGiDPVSVR 84
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILN------------GEVLLDDGRIIYEQ-DLIVAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REigmvfQRPNPFPTMSIFDNVAAGLRLNGSYKK------------------SELADIVEKsLKGANLW------NEVKD 140
Cdd:PRK11147 71 LQ-----QDPPRNVEGTVYDFVAEGIEEQAEYLKryhdishlvetdpseknlNELAKLQEQ-LDHHNLWqlenriNEVLA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 141 RL----NKPGSGLSGGQQQRLCIARAIAVEPKVLLMDEPCSALDpISTlaIEDLIGELKE-RFTIVIVTH------NMqq 209
Cdd:PRK11147 145 QLgldpDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD-IET--IEWLEGFLKTfQGSIIFISHdrsfirNM-- 219
|
....*.
gi 512057730 210 AARVSD 215
Cdd:PRK11147 220 ATRIVD 225
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-244 |
1.60e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 75.66 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 19 AIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpGGRVE-GKVLLDDEDLYGAGIDPVS---VRR----EIGMV 90
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQA-GGLVQcDKMLLRRRSRQVIELSEQSaaqMRHvrgaDMAMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 91 FQRP--NPFPTMSIFDNVAAGLRLNGSYKKSELADIVEKSLKGANLwNEVKDRLNKPGSGLSGGQQQRLCIARAIAVEPK 168
Cdd:PRK10261 110 FQEPmtSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRI-PEAQTILSRYPHQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 512057730 169 VLLMDEPCSALDPISTLAIEDLIGELKERFT--IVIVTHNMQQAARVSDRTaffnlaAVGQPGKLIEIDDTERIFSNP 244
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRV------LVMYQGEAVETGSVEQIFHAP 260
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
3-216 |
2.23e-15 |
|
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: 72.95 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 3 KRIDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpGGRVE--GKV--LLDdedlYGAGI 78
Cdd:cd03220 21 KKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPD-SGTVTvrGRVssLLG----LGGGF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 79 DP-VSVRREIGMvfqrpnpfptmsifdnVAAGLRLNGSYKKSELADIVEKSlkganlwnEVKDRLNKPGSGLSGGQQQRL 157
Cdd:cd03220 96 NPeLTGRENIYL----------------NGRLLGLSRKEIDEKIDEIIEFS--------ELGDFIDLPVKTYSSGMKARL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 158 CIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERFTIVI-VTHNMQQAARVSDR 216
Cdd:cd03220 152 AFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVIlVSHDPSSIKRLCDR 211
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-216 |
3.16e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 73.97 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 18 KAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMheVTP-GGRVEgkVLlddedlygaGIDPVSVRRE----IGMVF- 91
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGI--LVPtSGEVR--VL---------GYVPFKRRKEfarrIGVVFg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 92 QRpnpfpTMSIFD-NVAAGLRLNGS--------YKK--SELADIVekslkganlwnEVKDRLNKPGSGLSGGQQQRLCIA 160
Cdd:COG4586 103 QR-----SQLWWDlPAIDSFRLLKAiyripdaeYKKrlDELVELL-----------DLGELLDTPVRQLSLGQRMRCELA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 512057730 161 RAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDR 216
Cdd:COG4586 167 AALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMDDIEALCDR 224
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
20-205 |
3.32e-15 |
|
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: 71.03 E-value: 3.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 20 IEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpGGRVEgkvLLDDEDLYgagidpvsvrreigMVFQRPNpFPT 99
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWG-SGRIG---MPEGEDLL--------------FLPQRPY-LPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 100 msifdnvaaglrlnGSykkseLADIVekslkgANLWNEVkdrlnkpgsgLSGGQQQRLCIARAIAVEPKVLLMDEPCSAL 179
Cdd:cd03223 78 --------------GT-----LREQL------IYPWDDV----------LSGGEQQRLAFARLLLHKPKFVFLDEATSAL 122
|
170 180
....*....|....*....|....*..
gi 512057730 180 DPISTLAIEDLigeLKERFTIVI-VTH 205
Cdd:cd03223 123 DEESEDRLYQL---LKELGITVIsVGH 146
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
10-241 |
6.46e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 72.55 E-value: 6.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 10 LTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTL--NRMHEVTPGG-RVEGKVLLDDEDLygAGIDPVSVRRE 86
Cdd:PRK13547 7 LHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALagDLTGGGAPRGaRVTGDVTLNGEPL--AAIDAPRLARL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 87 IGMVFQRPNPFPTMSIFDNVAAGlRLNGSYKKSELA----DIVEKSLKGANlwneVKDRLNKPGSGLSGGQQQRLCIARA 162
Cdd:PRK13547 85 RAVLPQAAQPAFAFSAREIVLLG-RYPHARRAGALThrdgEIAWQALALAG----ATALVGRDVTTLSGGELARVQFARV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 163 IA---------VEPKVLLMDEPCSALDPISTLAIEDLIGELKE--RFTIVIVTHNMQQAARVSDRTAFF---NLAAVGQP 228
Cdd:PRK13547 160 LAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNLAARHADRIAMLadgAIVAHGAP 239
|
250
....*....|...
gi 512057730 229 GKLIEIDDTERIF 241
Cdd:PRK13547 240 ADVLTPAHIARCY 252
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
27-194 |
1.10e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 73.60 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 27 VEPRTVTAFIGPSGCGKSTFLRTLnrmhevtpGGRVEGKVLLDDEDLYGAGIDPVSVRREIGMVFQRPNPFPTMSIFDNV 106
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVL--------AERVTTGVITGGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRESL 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 107 --AAGLRLNGSYKKSELADIVEKSLKGANLwNEVKDRL-NKPGSGLSGGQQQRLCIARAIAVEPKVLL-MDEPCSALDPI 182
Cdd:TIGR00956 858 rfSAYLRQPKSVSKSEKMEYVEEVIKLLEM-ESYADAVvGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQ 936
|
170
....*....|..
gi 512057730 183 STLAIEDLIGEL 194
Cdd:TIGR00956 937 TAWSICKLMRKL 948
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
9-253 |
1.62e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 72.65 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 9 GLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNrmhEVTPGGRVEGKVLLDDEDLYGAGIDPvSVRREIG 88
Cdd:PRK13549 10 NITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLS---GVYPHGTYEGEIIFEGEELQASNIRD-TERAGIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 89 MVFQRPNPFPTMSIFDNVAAGLRLNgsykKSELADIVEKSLKGANLWNEVKDRLN--KPGSGLSGGQQQRLCIARAIAVE 166
Cdd:PRK13549 86 IIHQELALVKELSVLENIFLGNEIT----PGGIMDYDAMYLRAQKLLAQLKLDINpaTPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 167 PKVLLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSDrtaffnlaavgqpgKLIEIDDTERIFSNPS 245
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRDLKAHgIACIYISHKLNEVKAISD--------------TICVIRDGRHIGTRPA 227
|
....*...
gi 512057730 246 VQATEDYI 253
Cdd:PRK13549 228 AGMTEDDI 235
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-216 |
1.68e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.51 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 1 MAKRIDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDlYGAGIDP 80
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPT-----KGTITINNIN-YNKLDHK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 81 VSVRREIGMVFQRPNPFPTMSIFDNVAAGLRLNGSYKKSELADIVEKSLKGANLWNEV--KDRLNKPGSGLSGGQQQRLC 158
Cdd:PRK09700 76 LAAQLGIGIIYQELSVIDELTVLENLYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVglKVDLDEKVANLSISHKQMLE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 512057730 159 IARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGEL-KERFTIVIVTHNMQQAARVSDR 216
Cdd:PRK09700 156 IAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLrKEGTAIVYISHKLAEIRRICDR 214
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-205 |
1.74e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 72.44 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 16 SHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAGIDpvSVRREIGMVFQRPN 95
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVS-----EGDIRFHDIPLTKLQLD--SWRSRLAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 96 PFpTMSIFDNVAAGlRLNGSYKKSE----LADIVEKSLKGANLWN-EVKDRlnkpGSGLSGGQQQRLCIARAIAVEPKVL 170
Cdd:PRK10789 400 LF-SDTVANNIALG-RPDATQQEIEhvarLASVHDDILRLPQGYDtEVGER----GVMLSGGQKQRISIARALLLNAEIL 473
|
170 180 190
....*....|....*....|....*....|....*
gi 512057730 171 LMDEPCSALDPISTLAIEDLIGELKERFTIVIVTH 205
Cdd:PRK10789 474 ILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAH 508
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-208 |
4.47e-14 |
|
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: 71.87 E-value: 4.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 4 RIDVSGLTAYY--GSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMhevtpgGRVEGKVLLDdedlyGAGIDPV 81
Cdd:TIGR01271 1217 QMDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL------LSTEGEIQID-----GVSWNSV 1285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 82 SV---RREIGMVFQRpnpfptMSIFdnvAAGLRLN----GSYKKSELADIVEK-SLKgaNLWNEVKDRLN----KPGSGL 149
Cdd:TIGR01271 1286 TLqtwRKAFGVIPQK------VFIF---SGTFRKNldpyEQWSDEEIWKVAEEvGLK--SVIEQFPDKLDfvlvDGGYVL 1354
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512057730 150 SGGQQQRLCIARAIAVEPKVLLMDEPCSALDPIsTLAIedLIGELKERF---TIVIVTHNMQ 208
Cdd:TIGR01271 1355 SNGHKQLMCLARSILSKAKILLLDEPSAHLDPV-TLQI--IRKTLKQSFsncTVILSEHRVE 1413
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-205 |
5.15e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.22 E-value: 5.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 17 HKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTPggrVEGKVLLDDEDLY--GAGIDPVSVRREIGMVFQRP 94
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTP---VAGCVDVPDNQFGreASLIDAIGRKGDFKDAVELL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 95 NpfptmsifdnvAAGLRLNGSYKKSeladivekslkganlWNEvkdrlnkpgsgLSGGQQQRLCIARAIAVEPKVLLMDE 174
Cdd:COG2401 120 N-----------AVGLSDAVLWLRR---------------FKE-----------LSTGQKFRFRLALLLAERPKLLVIDE 162
|
170 180 190
....*....|....*....|....*....|...
gi 512057730 175 PCSALDPISTLAIEDLIGELKERF--TIVIVTH 205
Cdd:COG2401 163 FCSHLDRQTAKRVARNLQKLARRAgiTLVVATH 195
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
17-187 |
1.18e-13 |
|
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: 67.67 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 17 HKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEvtPGGRVEGKVLLDDEDLYGAGIDPvsvRREIGMVFQRPNP 96
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTE--GNVSVEGDIHYNGIPYKEFAEKY---PGEIIYVSEEDVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 97 FPTMSIFDNVAAGLRLNGSykkselaDIVekslkganlwnevkdrlnkpgSGLSGGQQQRLCIARAIAVEPKVLLMDEPC 176
Cdd:cd03233 95 FPTLTVRETLDFALRCKGN-------EFV---------------------RGISGGERKRVSIAEALVSRASVLCWDNST 146
|
170
....*....|.
gi 512057730 177 SALDPISTLAI 187
Cdd:cd03233 147 RGLDSSTALEI 157
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-208 |
3.89e-13 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 67.57 E-value: 3.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 4 RIDVSGLTAYY--GSHKAIEDISMTVEPRTVTAFIGPSGCGKST----FLRTLNrmhevtpggrVEGKVLLDdedlyGAG 77
Cdd:cd03289 2 QMTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTllsaFLRLLN----------TEGDIQID-----GVS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 78 IDPVSV---RREIGMVFQRPNPFpTMSIFDNvaagLRLNGSYKKSELADIVEK-SLKgaNLWNEVKDRLN----KPGSGL 149
Cdd:cd03289 67 WNSVPLqkwRKAFGVIPQKVFIF-SGTFRKN----LDPYGKWSDEEIWKVAEEvGLK--SVIEQFPGQLDfvlvDGGCVL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512057730 150 SGGQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLigeLKERF---TIVIVTHNMQ 208
Cdd:cd03289 140 SHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKT---LKQAFadcTVILSEHRIE 198
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-213 |
6.54e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.49 E-value: 6.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 23 ISMTVEPRTVTAFIGPSGCGKSTFlrtLNRMHEVTPGgrvEGKVLLDDEDLYGAGIDPVSVRReiGMVFQRPNPFPTMSI 102
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTL---LARMAGLLPG---SGSIQFAGQPLEAWSAAELARHR--AYLSQQQTPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 103 FD----NVAAGLRLNGSykKSELADIVEkSLKganlwneVKDRLNKPGSGLSGGQQQR-------LCIARAIAVEPKVLL 171
Cdd:PRK03695 87 FQyltlHQPDKTRTEAV--ASALNEVAE-ALG-------LDDKLGRSVNQLSGGEWQRvrlaavvLQVWPDINPAGQLLL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 512057730 172 MDEPCSALDPISTLAIEDLIGELKERFTIVIVT-----HNMQQAARV 213
Cdd:PRK03695 157 LDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSshdlnHTLRHADRV 203
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
23-213 |
2.69e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.06 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 23 ISMTVEPRTVTAFIGPSGCGKSTFLRTL-NRMHevtpGGRVEGKVLLDDEDLYGagidpvSVRREIGMVFQRPNPFPTMS 101
Cdd:PLN03211 87 VTGMASPGEILAVLGPSGSGKSTLLNALaGRIQ----GNNFTGTILANNRKPTK------QILKRTGFVTQDDILYPHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 102 IFDNV--AAGLRLNGSYKKSE---LADIVEKSLKGANLWNEVKDrlNKPGSGLSGGQQQRLCIARAIAVEPKVLLMDEPC 176
Cdd:PLN03211 157 VRETLvfCSLLRLPKSLTKQEkilVAESVISELGLTKCENTIIG--NSFIRGISGGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190
....*....|....*....|....*....|....*..
gi 512057730 177 SALDPISTLAIEDLIGELKERFTiVIVTHNMQQAARV 213
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSLAQKGK-TIVTSMHQPSSRV 270
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
20-208 |
6.12e-12 |
|
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: 63.12 E-value: 6.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 20 IEDISMTVEPRTVTAFIGPSGCGKSTFL-RTLNRMHevtpggRVEGKVLLDDEDLYGAGIDPVSVRREIGMVFQRPNPFP 98
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQ------TLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 99 -TMSIFDNVAAGLRLNGS-YKKSELADIVEKSLKGANLWNEVKdrLNKPGSGLSGGQQQRLCIARAIAVEPKVLLMDEPC 176
Cdd:cd03290 91 lNATVEENITFGSPFNKQrYKAVTDACSLQPDIDLLPFGDQTE--IGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190
....*....|....*....|....*....|....*
gi 512057730 177 SALD-PISTLAIEDLIGEL--KERFTIVIVTHNMQ 208
Cdd:cd03290 169 SALDiHLSDHLMQEGILKFlqDDKRTLVLVTHKLQ 203
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-217 |
1.15e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.04 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 18 KAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHevtPGGRVEGKVLLDDE--------DLYGAGIdpVSVRREIGM 89
Cdd:NF040905 15 KALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY---PHGSYEGEILFDGEvcrfkdirDSEALGI--VIIHQELAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 90 VfqrpnpfPTMSIFDNVAAGlrlNgsykkseladivEKSLKGANLWNEVKDR----LNKPG---------SGLSGGQQQR 156
Cdd:NF040905 90 I-------PYLSIAENIFLG---N------------ERAKRGVIDWNETNRRarelLAKVGldespdtlvTDIGVGKQQL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512057730 157 LCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSDRT 217
Cdd:NF040905 148 VEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQgITSIIISHKLNEIRRVADSI 209
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
20-187 |
1.56e-11 |
|
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: 61.49 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 20 IEDISMTVEPRTVTAFIGPSGCGKSTFLRTL-NRMHevtpGGRVEGKVLLDdedlyGAGIDPvSVRREIGMVFQRPNPFP 98
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKT----AGVITGEILIN-----GRPLDK-NFQRSTGYVEQQDVHSP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 99 TMSifdnvaaglrlngsykkseladiVEKSLK-GANLwnevkdrlnkpgSGLSGGQQQRLCIARAIAVEPKVLLMDEPCS 177
Cdd:cd03232 93 NLT-----------------------VREALRfSALL------------RGLSVEQRKRLTIGVELAAKPSILFLDEPTS 137
|
170
....*....|
gi 512057730 178 ALDPISTLAI 187
Cdd:cd03232 138 GLDSQAAYNI 147
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
7-216 |
1.77e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 63.50 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 7 VSGLTAyygsHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDlygagIDPVS---- 82
Cdd:COG1129 259 VEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPAD-----SGEIRLDGKP-----VRIRSprda 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 83 VRREIGMVfqrpnP--------FPTMSIFDNVAAG----LRLNGSYKKSELADIVEkslkganlwnEVKDRLN-KPGS-- 147
Cdd:COG1129 325 IRAGIAYV-----PedrkgeglVLDLSIRENITLAsldrLSRGGLLDRRRERALAE----------EYIKRLRiKTPSpe 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 148 ----GLSGGQQQRLCIARAIAVEPKVLLMDEPcsaldpisT--------LAIEDLIGELKER-FTIVIVTHNMQQAARVS 214
Cdd:COG1129 390 qpvgNLSGGNQQKVVLAKWLATDPKVLILDEP--------TrgidvgakAEIYRLIRELAAEgKAVIVISSELPELLGLS 461
|
..
gi 512057730 215 DR 216
Cdd:COG1129 462 DR 463
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-209 |
1.85e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.48 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 18 KAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTPGG-RVEGKvlldDEDLYG------AGIdpvsvrreiGMV 90
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSiLYLGK----EVTFNGpkssqeAGI---------GII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 91 FQRPNPFPTMSIFDNVAAGLRLNGSYkkseladivekslkGANLWNEVKD-------RLNKPGSG------LSGGQQQRL 157
Cdd:PRK10762 85 HQELNLIPQLTIAENIFLGREFVNRF--------------GRIDWKKMYAeadkllaRLNLRFSSdklvgeLSIGEQQMV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 512057730 158 CIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQ 209
Cdd:PRK10762 151 EIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQgRGIVYISHRLKE 203
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4-206 |
2.51e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.43 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 4 RIDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVtpggrVEGKVLLDDEDlygagIDPVSV 83
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPP-----AAGTIKLDGGD-----IDDPDV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 84 RREIGMVFQRPNPFPTMSIFDNVAAGLRLNGSykksELADIVEkSLKGANLwnevKDRLNKPGSGLSGGQQQRLCIARAI 163
Cdd:PRK13539 72 AEACHYLGHRNAMKPALTVAENLEFWAAFLGG----EELDIAA-ALEAVGL----APLAHLPFGYLSAGQKRRVALARLL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 512057730 164 AVEPKVLLMDEPCSALDPISTLAIEDLIGE-LKERFTIVIVTHN 206
Cdd:PRK13539 143 VSNRPIWILDEPTAALDAAAVALFAELIRAhLAQGGIVIAATHI 186
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-220 |
2.60e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.01 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 18 KAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDE--------DLYGAGidpvsvrreIGM 89
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPD-----AGSILIDGQemrfasttAALAAG---------VAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 90 VFQRPNPFPTMSIFDNVAAGlRLNGSykkselADIVEKSLkganLWNEVKDRLNKPG---------SGLSGGQQQRLCIA 160
Cdd:PRK11288 84 IYQELHLVPEMTVAENLYLG-QLPHK------GGIVNRRL----LNYEAREQLEHLGvdidpdtplKYLSIGQRQMVEIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 512057730 161 RAIAVEPKVLLMDEPCSALdpiSTLAIEDL---IGELKERFTIVI-VTHNMQQAARVSDRTAFF 220
Cdd:PRK11288 153 KALARNARVIAFDEPTSSL---SAREIEQLfrvIRELRAEGRVILyVSHRMEEIFALCDAITVF 213
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
15-244 |
4.94e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 61.85 E-value: 4.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 15 GSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLR------------TLNRMHevtpggrvegkvlLDDEDLYGagIDPVS 82
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKaicgitkdnwhvTADRFR-------------WNGIDLLK--LSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 83 ----VRREIGMVFQRPNPF--PTMSIFDnvaaglRLNGSykkseladIVEKSLKGaNLWNEVKDR-------LNKPG--- 146
Cdd:COG4170 83 rrkiIGREIAMIFQEPSSCldPSAKIGD------QLIEA--------IPSWTFKG-KWWQRFKWRkkraielLHRVGikd 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 147 ---------SGLSGGQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKE--RFTIVIVTHNMQQAARVSD 215
Cdd:COG4170 148 hkdimnsypHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlqGTSILLISHDLESISQWAD 227
|
250 260
....*....|....*....|....*....
gi 512057730 216 RtafFNLAAVGQpgkLIEIDDTERIFSNP 244
Cdd:COG4170 228 T---ITVLYCGQ---TVESGPTEQILKSP 250
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-243 |
5.29e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.69 E-value: 5.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 23 ISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAGIdpVSVRREIGMVFQRPNPFPTMSI 102
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELE-----KGRIMIDDCDVAKFGL--TDLRRVLSIIPQSPVLFSGTVR 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 103 FD-------NVAAglrLNGSYKKSELADIVEKSLKGANLwnevkdRLNKPGSGLSGGQQQRLCIARAIAVEPKVLLMDEP 175
Cdd:PLN03232 1328 FNidpfsehNDAD---LWEALERAHIKDVIDRNPFGLDA------EVSEGGENFSVGQRQLLSLARALLRRSKILVLDEA 1398
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 512057730 176 CSALDPISTLAIEDLIGELKERFTIVIVTHNMQQaarVSDRTAFFNLAAvgqpGKLIEIDDTERIFSN 243
Cdd:PLN03232 1399 TASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNT---IIDCDKILVLSS----GQVLEYDSPQELLSR 1459
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-242 |
5.78e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.05 E-value: 5.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 1 MAKRIDVSGLT-AYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTPGgrvegkvlldDEDLYGAGID 79
Cdd:PRK15056 3 QQAGIVVNDVTvTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASG----------KISILGQPTR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 80 PVSVRREIGMVFQRPN---PFPTMsIFDNVAAG-------LRLngsyKKSELADIVEKSLKGANLwneVKDRLNKPGSgL 149
Cdd:PRK15056 73 QALQKNLVAYVPQSEEvdwSFPVL-VEDVVMMGryghmgwLRR----AKKRDRQIVTAALARVDM---VEFRHRQIGE-L 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 150 SGGQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELK-ERFTIVIVTHNMQQAARVSDRTAFF--NLAAVG 226
Cdd:PRK15056 144 SGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTVMVkgTVLASG 223
|
250
....*....|....*.
gi 512057730 227 QPGKLIEIDDTERIFS 242
Cdd:PRK15056 224 PTETTFTAENLELAFS 239
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-205 |
1.11e-10 |
|
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: 61.10 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 3 KRIDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLnrMHEVTPGgrvEGKVLLDDedlygagidpvS 82
Cdd:TIGR03719 321 KVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMI--TGQEQPD---SGTIEIGE-----------T 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 83 VRreIGMVFQ-RPNPFPTMSIFDNVAAG---LRLnGSYKKSELADIVEKSLKGANLWNEVKDrlnkpgsgLSGGQQQRLC 158
Cdd:TIGR03719 385 VK--LAYVDQsRDALDPNKTVWEEISGGldiIKL-GKREIPSRAYVGRFNFKGSDQQKKVGQ--------LSGGERNRVH 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 512057730 159 IARAIAVEPKVLLMDEPCSALDpISTL-AIEDLIgelkERF--TIVIVTH 205
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLD-VETLrALEEAL----LNFagCAVVISH 498
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-212 |
1.37e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 61.29 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 7 VSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFL------RTLNRmhevtpgGRVEgkVLlddedlyGAGIDP 80
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLsliagaRKIQQ-------GRVE--VL-------GGDMAD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 81 VSVRREIG-----MvfqrP-----NPFPTMSIFDNVAAGLRLNGsYKKSELADIVEKSLKGANLWnEVKDRlnkPGSGLS 150
Cdd:NF033858 68 ARHRRAVCpriayM----PqglgkNLYPTLSVFENLDFFGRLFG-QDAAERRRRIDELLRATGLA-PFADR---PAGKLS 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 512057730 151 GGQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKER---FTIVIVTHNMQQAAR 212
Cdd:NF033858 139 GGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpgMSVLVATAYMEEAER 203
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-205 |
3.97e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.52 E-value: 3.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLnrMHEVTPGgrvEGKVllddedlygagidPVSVR 84
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL--VGELEPD---SGTV-------------KWSEN 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIGMVFQRPNP-FPT-MSIFDNVaaglrlnGSYKKSELADIVEKSLKGANLWNEvkDRLNKPGSGLSGGQQQRLCIARA 162
Cdd:PRK15064 382 ANIGYYAQDHAYdFENdLTLFDWM-------SQWRQEGDDEQAVRGTLGRLLFSQ--DDIKKSVKVLSGGEKGRMLFGKL 452
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 512057730 163 IAVEPKVLLMDEPCSALDPIStlaIEDLIGELkERF--TIVIVTH 205
Cdd:PRK15064 453 MMQKPNVLVMDEPTNHMDMES---IESLNMAL-EKYegTLIFVSH 493
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
9-205 |
6.64e-10 |
|
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: 58.79 E-value: 6.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 9 GLTAYYGSHKAI-EDISMTVEPRTVTAFIGPSGCGKSTFLRTLnrmhevtpggrvegkvllddedlygAGIDP------- 80
Cdd:TIGR03719 9 RVSKVVPPKKEIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------------------------AGVDKdfngear 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 81 VSVRREIGMVFQRPNPFPTMSIFDNVAAGL--------RLNGSYKK---------------SELADIVEkslkGANLWN- 136
Cdd:TIGR03719 64 PQPGIKVGYLPQEPQLDPTKTVRENVEEGVaeikdaldRFNEISAKyaepdadfdklaaeqAELQEIID----AADAWDl 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 512057730 137 ----EVK-DRLNKPG-----SGLSGGQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKErfTIVIVTH 205
Cdd:TIGR03719 140 dsqlEIAmDALRCPPwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG--TVVAVTH 216
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-212 |
8.45e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.02 E-value: 8.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 22 DISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLY---GAGIDPVSVRREIgmVFqrpnpfp 98
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEIS-----EGRVWAERSIAYvpqQAWIMNATVRGNI--LF------- 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 99 tmsiFDNVAAGlRLNGSYKKSEL-ADIvekSLKGANLWNEVKDRlnkpGSGLSGGQQQRLCIARAIAVEPKVLLMDEPCS 177
Cdd:PTZ00243 744 ----FDEEDAA-RLADAVRVSQLeADL---AQLGGGLETEIGEK----GVNLSGGQKARVSLARAVYANRDVYLLDDPLS 811
|
170 180 190
....*....|....*....|....*....|....*..
gi 512057730 178 ALDP-ISTLAIEDLI-GELKERfTIVIVTHNMQQAAR 212
Cdd:PTZ00243 812 ALDAhVGERVVEECFlGALAGK-TRVLATHQVHVVPR 847
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-207 |
8.62e-10 |
|
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: 58.80 E-value: 8.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 23 ISMTVEPRTVTAFIGPSGCGKSTFLRTLnrMHEVTpggRVEGKVLLDDEDLY---GAGIDPVSVRreigmvfqrpnpfpt 99
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMD---KVEGHVHMKGSVAYvpqQAWIQNDSLR--------------- 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 100 msifDNVAAGLRLNGSYKKSE------LADIveKSLKGANlwnevKDRLNKPGSGLSGGQQQRLCIARAIAVEPKVLLMD 173
Cdd:TIGR00957 717 ----ENILFGKALNEKYYQQVleacalLPDL--EILPSGD-----RTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFD 785
|
170 180 190
....*....|....*....|....*....|....*...
gi 512057730 174 EPCSALDP-ISTLAIEDLIGE---LKERfTIVIVTHNM 207
Cdd:TIGR00957 786 DPLSAVDAhVGKHIFEHVIGPegvLKNK-TRILVTHGI 822
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-207 |
9.62e-10 |
|
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: 58.80 E-value: 9.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 20 IEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAGIDpvSVRREIGMVFQRPNPFpt 99
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESA-----EGEIIIDGLNIAKIGLH--DLRFKITIIPQDPVLF-- 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 100 msifdnvAAGLRLN----GSYKKSELADIVEKS-LKGanLWNEVKDRLN----KPGSGLSGGQQQRLCIARAIAVEPKVL 170
Cdd:TIGR00957 1373 -------SGSLRMNldpfSQYSDEEVWWALELAhLKT--FVSALPDKLDhecaEGGENLSVGQRQLVCLARALLRKTKIL 1443
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 512057730 171 LMDEPCSALDpistLAIEDLI-GELKERF---TIVIVTHNM 207
Cdd:TIGR00957 1444 VLDEATAAVD----LETDNLIqSTIRTQFedcTVLTIAHRL 1480
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-243 |
1.59e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.21 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 23 ISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAGIdpVSVRREIGMVFQRPNPFPTMSI 102
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELE-----RGRILIDGCDISKFGL--MDLRKVLGIIPQAPVLFSGTVR 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 103 FD----NVAAGLRLNGSYKKSELADIVEKSLKGanLWNEVKDrlnkPGSGLSGGQQQRLCIARAIAVEPKVLLMDEPCSA 178
Cdd:PLN03130 1331 FNldpfNEHNDADLWESLERAHLKDVIRRNSLG--LDAEVSE----AGENFSVGQRQLLSLARALLRRSKILVLDEATAA 1404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 512057730 179 LDPISTLAIEDLIGELKERFTIVIVTHNMQQAARvSDRTaffnlaAVGQPGKLIEIDDTERIFSN 243
Cdd:PLN03130 1405 VDVRTDALIQKTIREEFKSCTMLIIAHRLNTIID-CDRI------LVLDAGRVVEFDTPENLLSN 1462
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-215 |
1.68e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.82 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 18 KAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEvtpggRVEGKVLLDdedlyGAGIDPVSVRRE----IGMVFQR 93
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQ-----KDSGSILFQ-----GKEIDFKSSKEAlengISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 94 PNPFPTMSIFDNVAAGlrlngSY-KKSELADIVEKSLKGANLWNEVKDRLN--KPGSGLSGGQQQRLCIARAIAVEPKVL 170
Cdd:PRK10982 82 LNLVLQRSVMDNMWLG-----RYpTKGMFVDQDKMYRDTKAIFDELDIDIDprAKVATLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 512057730 171 LMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSD 215
Cdd:PRK10982 157 IMDEPTSSLTEKEVNHLFTIIRKLKERgCGIVYISHKMEEIFQLCD 202
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
7-204 |
1.70e-09 |
|
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: 55.83 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 7 VSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMheVTPggrVEGKVLLDDEDLYGAGIDPvsvRRE 86
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGL--LRP---DSGEVRWNGTPLAEQRDEP---HEN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 87 IGMVFQRPNPFPTMSIFDNVAAGLRLNGSYKKSeladiVEKSLKGANLwnevKDRLNKPGSGLSGGQQQRLCIARAIAVE 166
Cdd:TIGR01189 75 ILYLGHLPGLKPELSALENLHFWAAIHGGAQRT-----IEDALAAVGL----TGFEDLPAAQLSAGQQRRLALARLWLSR 145
|
170 180 190
....*....|....*....|....*....|....*...
gi 512057730 167 PKVLLMDEPCSALDPISTLAIEDLIGELKERFTIVIVT 204
Cdd:TIGR01189 146 RPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLT 183
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-243 |
1.80e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.87 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 23 ISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTPGG-RVEGKvlldDEDLYGAGidpvSVRREIGMVFQRP------- 94
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEiRVNGR----EIGAYGLR----ELRRQFSMIPQDPvlfdgtv 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 95 ----NPFPTMSIFDnVAAGLRLNGSYKK--SELADIVEKSLKGanlwnevkdrlnkpGSGLSGGQQQRLCIARAIAVE-P 167
Cdd:PTZ00243 1401 rqnvDPFLEASSAE-VWAALELVGLRERvaSESEGIDSRVLEG--------------GSNYSVGQRQLMCMARALLKKgS 1465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 168 KVLLMDEPCSALDPISTLAIEDLIGELKERFTIVIVTHNMQQAAR-----VSDRTAffnLAAVGQPGKLIEidDTERIFS 242
Cdd:PTZ00243 1466 GFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQydkiiVMDHGA---VAEMGSPRELVM--NRQSIFH 1540
|
.
gi 512057730 243 N 243
Cdd:PTZ00243 1541 S 1541
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
20-205 |
2.35e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 56.34 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 20 IEDISMTVEPRTVTAFIGPSGCGKSTFLRTL--NRMHEVTpGGRVE--GKVL--LDDEDLYGAGidpvsvrreIGMVFQR 93
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVT-GGTVEfkGKDLleLSPEDRAGEG---------IFMAFQY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 94 PNPFPTMS--IFDNVAAG----LRLNGSYKKSELADIVEKSLKganLWNEVKDRLNKP-GSGLSGGQQQRLCIARAIAVE 166
Cdd:PRK09580 87 PVEIPGVSnqFFLQTALNavrsYRGQEPLDRFDFQDLMEEKIA---LLKMPEDLLTRSvNVGFSGGEKKRNDILQMAVLE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 512057730 167 PKVLLMDEPCSALDPISTLAIEDLIGELK-ERFTIVIVTH 205
Cdd:PRK09580 164 PELCILDESDSGLDIDALKIVADGVNSLRdGKRSFIIVTH 203
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-207 |
5.34e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.36 E-value: 5.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 26 TVEPRTVTAFIGPSGCGKSTFLRTLNrmHEVTPG-GRVEGKVLLDD--------------EDLYGAGIDPVsvrREIGMV 90
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILS--GELIPNlGDYEEEPSWDEvlkrfrgtelqnyfKKLYNGEIKVV---HKPQYV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 91 FQRPNpfptmsifdnvaaglRLNGsyKKSELadiveksLKGAN---LWNEVKDRLN------KPGSGLSGGQQQRLCIAR 161
Cdd:PRK13409 170 DLIPK---------------VFKG--KVREL-------LKKVDergKLDEVVERLGlenildRDISELSGGELQRVAIAA 225
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 512057730 162 AIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERFTIVIVTHNM 207
Cdd:PRK13409 226 ALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-216 |
5.62e-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: 55.99 E-value: 5.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 18 KAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEvtpgGRVEGKVLLDDEDLygAGIDPV-SVRREIGMV---FQR 93
Cdd:TIGR02633 274 KRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYP----GKFEGNVFINGKPV--DIRNPAqAIRAGIAMVpedRKR 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 94 PNPFPTMSIFDNVAAGLrLNGSYKKSELADIVEKSLKGANLwNEVKDRLNKPG---SGLSGGQQQRLCIARAIAVEPKVL 170
Cdd:TIGR02633 348 HGIVPILGVGKNITLSV-LKSFCFKMRIDAAAELQIIGSAI-QRLKVKTASPFlpiGRLSGGNQQKAVLAKMLLTNPRVL 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 512057730 171 LMDEPCSALDPISTLAIEDLIGEL-KERFTIVIVTHNMQQAARVSDR 216
Cdd:TIGR02633 426 ILDEPTRGVDVGAKYEIYKLINQLaQEGVAIIVVSSELAEVLGLSDR 472
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-227 |
8.34e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.56 E-value: 8.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 6 DVSGLTAYygSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLrtlNRMHEVTPggRVEGKVLLDdedlyGAGIDPVS--- 82
Cdd:PRK09700 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELM---NCLFGVDK--RAGGEIRLN-----GKDISPRSpld 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 83 -VRREIGMVFQ--RPNPF-PTMSIFDNVAAGLRL-NGSYK-------KSELADIVEK-----SLKGANLwnevkdrlNKP 145
Cdd:PRK09700 335 aVKKGMAYITEsrRDNGFfPNFSIAQNMAISRSLkDGGYKgamglfhEVDEQRTAENqrellALKCHSV--------NQN 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 146 GSGLSGGQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSDRTAFFNLAA 224
Cdd:PRK09700 407 ITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVFCEGR 486
|
...
gi 512057730 225 VGQ 227
Cdd:PRK09700 487 LTQ 489
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-197 |
1.07e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.03 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 4 RIDVSGLTAY-YGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLYGAGidpVS 82
Cdd:COG3845 257 VLEVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPA-----SGSIRLDGEDITGLS---PR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 83 VRREIGMVF-----QRPNPFPTMSIFDNVAAGLRLNGSYKKS---------ELA-DIVEK-SLKGANLWNEVKdrlnkpg 146
Cdd:COG3845 329 ERRRLGVAYipedrLGRGLVPDMSVAENLILGRYRRPPFSRGgfldrkairAFAeELIEEfDVRTPGPDTPAR------- 401
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 512057730 147 sGLSGGQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKER 197
Cdd:COG3845 402 -SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA 451
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-216 |
1.09e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.01 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 3 KRIDVSGLTayyGShkAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLnrmHEVTPggRVEGKVLLDDEDLY-------- 74
Cdd:PRK10762 256 VRLKVDNLS---GP--GVNDVSFTLRKGEILGVSGLMGAGRTELMKVL---YGALP--RTSGYVTLDGHEVVtrspqdgl 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 75 GAGIDPVSV-RREIGMVFQrpnpfptMSIFDNVA---------AGLRLNGSYKKSELADIVEkslkganLWNEVKDRLNK 144
Cdd:PRK10762 326 ANGIVYISEdRKRDGLVLG-------MSVKENMSltalryfsrAGGSLKHADEQQAVSDFIR-------LFNIKTPSMEQ 391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 512057730 145 PGSGLSGGQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELK-ERFTIVIVTHNMQQAARVSDR 216
Cdd:PRK10762 392 AIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKaEGLSIILVSSEMPEVLGMSDR 464
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-233 |
1.16e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.52 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLddedlYGAGIDP--VS 82
Cdd:NF033858 267 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPAS-----EGEAWL-----FGQPVDAgdIA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 83 VRREIGMvfqrpnpfptMS----------IFDNVAAGLRLNGsYKKSELADIVEKSLKGANLwNEVKDRLnkPGSgLSGG 152
Cdd:NF033858 337 TRRRVGY----------MSqafslygeltVRQNLELHARLFH-LPAAEIAARVAEMLERFDL-ADVADAL--PDS-LPLG 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 153 QQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGEL--KERFTIVIVTHNMQQAARVsDRTAFFN----LaAVG 226
Cdd:NF033858 402 IRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELsrEDGVTIFISTHFMNEAERC-DRISLMHagrvL-ASD 479
|
....*..
gi 512057730 227 QPGKLIE 233
Cdd:NF033858 480 TPAALVA 486
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-240 |
1.22e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.06 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMheVTPGG---RVEGKVLlddedlygAGIDPV 81
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGI--VPPDSgtlEIGGNPC--------ARLTPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 82 SVRR-EIGMVFQRPNPFPTMSIFDNVAAGL-RLNGSYKKseladiVEKSLKGANlwneVKDRLNKPGSGLSGGQQQRLCI 159
Cdd:PRK15439 82 KAHQlGIYLVPQEPLLFPNLSVKENILFGLpKRQASMQK------MKQLLAALG----CQLDLDSSAGSLEVADRQIVEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 160 ARAIAVEPKVLLMDEPCSALDPISTlaiEDLIGELKERFT----IVIVTHNMQQAARVSDRTAFFNLAAVGQPGKLIEID 235
Cdd:PRK15439 152 LRGLMRDSRILILDEPTASLTPAET---ERLFSRIRELLAqgvgIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLS 228
|
....*
gi 512057730 236 DTERI 240
Cdd:PRK15439 229 TDDII 233
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
5-204 |
1.59e-08 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 53.27 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTpggrvEGKVLLDDEDLygaGIDPVSVR 84
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPL-----AGRVLLNGGPL---DFQRDSIA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIGMVFQRPNPFPTMSIFDNVAAGLRLNGSykkselaDIVEKSLKGANLwNEVKDRlnkPGSGLSGGQQQRLCIARAIA 164
Cdd:cd03231 73 RGLLYLGHAPGIKTTLSVLENLRFWHADHSD-------EQVEEALARVGL-NGFEDR---PVAQLSAGQQRRVALARLLL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 512057730 165 VEPKVLLMDEPCSALDPISTLAIEDLIGELKERFTIVIVT 204
Cdd:cd03231 142 SGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLT 181
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
18-230 |
1.78e-08 |
|
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: 53.57 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 18 KAIEDISMTVEPRT-----VTAFIGPSGCGKSTFLRTLnrmhevtpGGRVE---GKVLLDDEDL-----YGAGIDPVSVR 84
Cdd:cd03237 8 KTLGEFTLEVEGGSiseseVIGILGPNGIGKTTFIKML--------AGVLKpdeGDIEIELDTVsykpqYIKADYEGTVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 REIgmvfqrpnpfptMSIFDNVaaglrLNGSYKKSELAdiveKSLKGANLW-NEVKDrlnkpgsgLSGGQQQRLCIARAI 163
Cdd:cd03237 80 DLL------------SSITKDF-----YTHPYFKTEIA----KPLQIEQILdREVPE--------LSGGELQRVAIAACL 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 512057730 164 AVEPKVLLMDEPCSALDP----ISTLAIEDLIgeLKERFTIVIVTHNMQQAARVSDRTAFFNlaavGQPGK 230
Cdd:cd03237 131 SKDADIYLLDEPSAYLDVeqrlMASKVIRRFA--ENNEKTAFVVEHDIIMIDYLADRLIVFE----GEPSV 195
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-216 |
3.15e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 53.65 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYY----GSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNrmhEVTPGG-RVEG-KVLLDDEDLYGagI 78
Cdd:PRK15093 4 LDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAIC---GVTKDNwRVTAdRMRFDDIDLLR--L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 79 DPVSVRREIG----MVFQRPNPF--PTMSIfdnvaaGLRLNGS-----YKKSELADIVEKSLKGANLWNEV-----KDRL 142
Cdd:PRK15093 79 SPRERRKLVGhnvsMIFQEPQSCldPSERV------GRQLMQNipgwtYKGRWWQRFGWRKRRAIELLHRVgikdhKDAM 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512057730 143 NKPGSGLSGGQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKER--FTIVIVTHNMQQAARVSDR 216
Cdd:PRK15093 153 RSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnnTTILLISHDLQMLSQWADK 228
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-205 |
4.35e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.71 E-value: 4.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 2 AKRIDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLnRMHEVTPGGR------VEGKVLLDD----E 71
Cdd:PLN03073 175 IKDIHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYM-AMHAIDGIPKncqilhVEQEVVGDDttalQ 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 72 DLYGAGIDPVSVRREIGMVFQRPNPFPTMSIF-----------DNVAAGLRLNGSYKKSELADIVEKS------LKGANL 134
Cdd:PLN03073 254 CVLNTDIERTQLLEEEAQLVAQQRELEFETETgkgkgankdgvDKDAVSQRLEEIYKRLELIDAYTAEaraasiLAGLSF 333
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 512057730 135 WNEVKDRLNKPgsgLSGGQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIgeLKERFTIVIVTH 205
Cdd:PLN03073 334 TPEMQVKATKT---FSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSH 399
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
10-218 |
5.12e-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: 53.48 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 10 LTAYYG--SHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHEVTPG-GRVEGKVLLDDedlygagidpvsvrre 86
Cdd:TIGR01257 1943 LTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGdATVAGKSILTN---------------- 2006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 87 IGMVFQRPNPFPTMSIFDNVAAG-------LRLNGSYKKsELADIVEKSLKGANLwNEVKDRLnkpGSGLSGGQQQRLCI 159
Cdd:TIGR01257 2007 ISDVHQNMGYCPQFDAIDDLLTGrehlylyARLRGVPAE-EIEKVANWSIQSLGL-SLYADRL---AGTYSGGNKRKLST 2081
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 160 ARAIAVEPKVLLMDEPCSALDPISTLAIEDLI-GELKERFTIVIVTHNMQQAARVSDRTA 218
Cdd:TIGR01257 2082 AIALIGCPPLVLLDEPTTGMDPQARRMLWNTIvSIIREGRAVVLTSHSMEECEALCTRLA 2141
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
18-230 |
8.29e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.50 E-value: 8.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 18 KAIEDISMTVEPRT-----VTAFIGPSGCGKSTFLRTLNrmHEVTPggrVEGKVLLDDEdlygagidpVSVRReigmvfQ 92
Cdd:PRK13409 348 KKLGDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLA--GVLKP---DEGEVDPELK---------ISYKP------Q 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 93 RPNPFPTMSIFDNVA-AGLRLNGSYKKSELAdivekslKGANLwnevKDRLNKPGSGLSGGQQQRLCIARAIAVEPKVLL 171
Cdd:PRK13409 408 YIKPDYDGTVEDLLRsITDDLGSSYYKSEII-------KPLQL----ERLLDKNVKDLSGGELQRVAIAACLSRDADLYL 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 512057730 172 MDEPCSALDP----ISTLAIEDLIgELKERfTIVIVTHNMQQAARVSDRTAFFNlaavGQPGK 230
Cdd:PRK13409 477 LDEPSAHLDVeqrlAVAKAIRRIA-EEREA-TALVVDHDIYMIDYISDRLMVFE----GEPGK 533
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
7-216 |
1.04e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 50.96 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 7 VSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMheVTPggrVEGKVLLDDED------------LY 74
Cdd:PRK13538 4 ARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGL--ARP---DAGEVLWQGEPirrqrdeyhqdlLY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 75 -G--AGIDPVsvrreigmvfqrpnpfptMSIFDNVAAGLRLNGSYKKSELADIVEK-SLKGanlwnevkdRLNKPGSGLS 150
Cdd:PRK13538 79 lGhqPGIKTE------------------LTALENLRFYQRLHGPGDDEALWEALAQvGLAG---------FEDVPVRQLS 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 512057730 151 GGQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERFTIVIVT-HnmQQAARVSDR 216
Cdd:PRK13538 132 AGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTtH--QDLPVASDK 196
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
8-242 |
1.91e-07 |
|
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: 50.68 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 8 SGLTAYYGSHKaIEDISMTVEP------RTVTAFIGP---------SGCGKSTFLRTLNRMHEVtpggrVEGKVLLDDED 72
Cdd:cd03288 11 SGLVGLGGEIK-IHDLCVRYENnlkpvlKHVKAYIKPgqkvgicgrTGSGKSSLSLAFFRMVDI-----FDGKIVIDGID 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 73 LygAGIDPVSVRREIGMVFQRPNPFptmsifdnvAAGLRLNGSYKKSELADIVEKSLKGANLWNEVKDR-------LNKP 145
Cdd:cd03288 85 I--SKLPLHTLRSRLSIILQDPILF---------SGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLpggldavVTEG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 146 GSGLSGGQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERFTIVIVTHnmqqaaRVSDRTAfFNLAAV 225
Cdd:cd03288 154 GENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAH------RVSTILD-ADLVLV 226
|
250
....*....|....*..
gi 512057730 226 GQPGKLIEIDDTERIFS 242
Cdd:cd03288 227 LSRGILVECDTPENLLA 243
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-216 |
3.02e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.68 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 4 RIDVSGLTAyygsHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTL---NRMHEvtpggrveGKVLLDdedlyGAGIDP 80
Cdd:PRK11288 257 RLRLDGLKG----PGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLygaTRRTA--------GQVYLD-----GKPIDI 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 81 VSVRREI--GMVF-----QRPNPFPTMSIFDNVA---------AGLRLNGSyKKSELADIVEKSLKganlwneVKDR-LN 143
Cdd:PRK11288 320 RSPRDAIraGIMLcpedrKAEGIIPVHSVADNINisarrhhlrAGCLINNR-WEAENADRFIRSLN-------IKTPsRE 391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 512057730 144 KPGSGLSGGQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSDR 216
Cdd:PRK11288 392 QLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQgVAVLFVSSDLPEVLGVADR 465
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
5-234 |
6.02e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 49.73 E-value: 6.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGcgkSTFLRTLNRMHEVTP-GGRVEGKvllddedLYGAGIDPVSV 83
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*G---AA**RGALPAHV*GPdAGRRPWR-------F*TWCANRRAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 84 RREIG----MVFQRPNPFPTMSIFDNVAAGLRLNGSYKKSELADIVEKSlkganlwnEVKDRLNKPGSGLSGGQQQRLCI 159
Cdd:NF000106 84 RRTIG*hrpVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERF--------SLTEAAGRAAAKYSGGMRRRLDL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512057730 160 ARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGEL-KERFTIVIVTHNMQQAARVSDRTAFFNLAAVGQPGKLIEI 234
Cdd:NF000106 156 AASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMvRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-219 |
7.73e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.63 E-value: 7.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 4 RIDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMH------EVTPGGRVEGKvllddedlyGAG 77
Cdd:PRK10938 260 RIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHpqgysnDLTLFGRRRGS---------GET 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 78 I-DpvsVRREIGMVfqrpnpfptmsifdnvAAGLRLNGSYKKSELADIVEKSLKGANLWNEVKDRL-------------- 142
Cdd:PRK10938 331 IwD---IKKHIGYV----------------SSSLHLDYRVSTSVRNVILSGFFDSIGIYQAVSDRQqklaqqwldilgid 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 143 ----NKPGSGLSGGQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLA----IEDLIGELKERftIVIVTHNMQQAAR-V 213
Cdd:PRK10938 392 krtaDAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLvrrfVDVLISEGETQ--LLFVSHHAEDAPAcI 469
|
....*.
gi 512057730 214 SDRTAF 219
Cdd:PRK10938 470 THRLEF 475
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
5-205 |
9.05e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.48 E-value: 9.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRmHevtPGGRV-EGKVLLDDEDLYGAGIDPVSv 83
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-H---PAYKIlEGDILFKGESILDLEPEERA- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 84 RREIGMVFQRPNPFPTMSIFDNvaagLRL--NGSYKKSELAD---------IVEKsLKGANLWNEVKDR-LNKpgsGLSG 151
Cdd:CHL00131 83 HLGIFLAFQYPIEIPGVSNADF----LRLayNSKRKFQGLPEldplefleiINEK-LKLVGMDPSFLSRnVNE---GFSG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 512057730 152 GQQQRLCIARAIAVEPKVLLMDEPCSALDpISTL-AIEDLIGELKERFT-IVIVTH 205
Cdd:CHL00131 155 GEKKRNEILQMALLDSELAILDETDSGLD-IDALkIIAEGINKLMTSENsIILITH 209
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
20-180 |
1.07e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.46 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 20 IEDISMTVEPRTVTAFIGPSGCGKSTFLRTLnrmhevtpGGRVEGKVLLDDEDLYGAGIDPVSVRREIGMVFQRPNPFPT 99
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVL--------AGRKTGGYIEGDIRISGFPKKQETFARISGYCEQNDIHSPQ 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 100 MSIFDNV--AAGLRLNGSYKKSELADIVEKSLKGANLwNEVKDRL-NKPG-SGLSGGQQQRLCIARAIAVEPKVLLMDEP 175
Cdd:PLN03140 968 VTVRESLiySAFLRLPKEVSKEEKMMFVDEVMELVEL-DNLKDAIvGLPGvTGLSTEQRKRLTIAVELVANPSIIFMDEP 1046
|
....*
gi 512057730 176 CSALD 180
Cdd:PLN03140 1047 TSGLD 1051
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-203 |
1.08e-06 |
|
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: 49.40 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 26 TVEPRTVTAFIGPSGCGKSTFLRTLNrmHEVTPG-GRVEGKvllddedlygAGIDPVsVRREIGMVFQrpnpfptmSIFD 104
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILS--GELKPNlGDYDEE----------PSWDEV-LKRFRGTELQ--------DYFK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 105 NVAAGlRLNGSYKkSELADIVEKSLKG-----------ANLWNEVKDRLN------KPGSGLSGGQQQRLCIARAIAVEP 167
Cdd:COG1245 154 KLANG-EIKVAHK-PQYVDLIPKVFKGtvrellekvdeRGKLDELAEKLGlenildRDISELSGGELQRVAIAAALLRDA 231
|
170 180 190
....*....|....*....|....*....|....*.
gi 512057730 168 KVLLMDEPCSALDPISTLAIEDLIGELKERFTIVIV 203
Cdd:COG1245 232 DFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLV 267
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
20-208 |
1.13e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.18 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 20 IEDISMTVEPRTVTAFIGPSGCGKSTFLRTLnrMHEVTP-GGRVEGKVLLDDE--DLYGAGIDPvsvrreigmvfQRpnp 96
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLM--LGQLQAdSGRIHCGTKLEVAyfDQHRAELDP-----------EK--- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 97 fptmSIFDNVAAG---LRLNG------SYkkseLADIVeKSLKganlwnevkdRLNKPGSGLSGGQQQRLCIARAIAVEP 167
Cdd:PRK11147 399 ----TVMDNLAEGkqeVMVNGrprhvlGY----LQDFL-FHPK----------RAMTPVKALSGGERNRLLLARLFLKPS 459
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 512057730 168 KVLLMDEPCSALDpISTLaieDLIGELKERF--TIVIVTHNMQ 208
Cdd:PRK11147 460 NLLILDEPTNDLD-VETL---ELLEELLDSYqgTVLLVSHDRQ 498
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
18-230 |
1.18e-06 |
|
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: 49.01 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 18 KAIEDISMTVEPRT-----VTAFIGPSGCGKSTFLRTLNrmHEVTPggrVEGKVlldDEDLygagidPVSVRReigmvfQ 92
Cdd:COG1245 349 KSYGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILA--GVLKP---DEGEV---DEDL------KISYKP------Q 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 93 RPNPFPTMSIFDNV--AAGLRLNGSYKKSELAdiveKSLKganlwneVKDRLNKPGSGLSGGQQQRLCIARAIAVEPKVL 170
Cdd:COG1245 409 YISPDYDGTVEEFLrsANTDDFGSSYYKTEII----KPLG-------LEKLLDKNVKDLSGGELQRVAIAACLSRDADLY 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512057730 171 LMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDRTAFFNlaavGQPGK 230
Cdd:COG1245 478 LLDEPSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDHDIYLIDYISDRLMVFE----GEPGV 535
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
149-216 |
1.60e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.57 E-value: 1.60e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 512057730 149 LSGGQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGEL-KERFTIVIVTHNMQQAARVSDR 216
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEMPELLGITDR 460
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-207 |
1.70e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 47.75 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 26 TVEPRTVTAFIGPSGCGKSTFLRTLNrmHEVTPG-GRVEGKVLLDD--------------EDLYGAGIDPVsvrREIGMV 90
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILA--GKLKPNlGKFDDPPDWDEildefrgselqnyfTKLLEGDVKVI---VKPQYV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 91 FQRPNPFPTmsifdnvAAGLRLNGSYKKSELADIVEKSlkganlwnEVKDRLNKPGSGLSGGQQQRLCIARAIAVEPKVL 170
Cdd:cd03236 97 DLIPKAVKG-------KVGELLKKKDERGKLDELVDQL--------ELRHVLDRNIDQLSGGELQRVAIAAALARDADFY 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 512057730 171 LMDEPCSALDPISTLAIEDLIGEL-KERFTIVIVTHNM 207
Cdd:cd03236 162 FFDEPSSYLDIKQRLNAARLIRELaEDDNYVLVVEHDL 199
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
20-205 |
1.99e-06 |
|
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: 48.59 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 20 IEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNrmhEVTPggrvegkvllddedLYGaGIDPVSVRREIGMVFQRPNP--- 96
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILG---ELWP--------------VYG-GRLTKPAKGKLFYVPQRPYMtlg 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 97 -------FPtMSIFDNVAAGLR---LNGSYKKSELADIVEKSLKganlWNEVKDRLNKpgsgLSGGQQQRLCIARAIAVE 166
Cdd:TIGR00954 530 tlrdqiiYP-DSSEDMKRRGLSdkdLEQILDNVQLTHILEREGG----WSAVQDWMDV----LSGGEKQRIAMARLFYHK 600
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 512057730 167 PKVLLMDEPCSALDPistlAIEDLIGEL--KERFTIVIVTH 205
Cdd:TIGR00954 601 PQFAILDECTSAVSV----DVEGYMYRLcrEFGITLFSVSH 637
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
141-215 |
3.18e-06 |
|
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: 46.16 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 141 RLNKPGSGLSGGQQQRLCIARAIAVEPK--VLLMDEPCSALDPISTLAIEDLIGEL-KERFTIVIVTHN---MQQAARVS 214
Cdd:cd03238 80 TLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLiDLGNTVILIEHNldvLSSADWII 159
|
.
gi 512057730 215 D 215
Cdd:cd03238 160 D 160
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
149-216 |
4.81e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.23 E-value: 4.81e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 512057730 149 LSGGQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGEL-KERFTIVIVTHNMQQAARVSDR 216
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLvQQGVAIIVISSELPEVLGLSDR 474
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
149-230 |
9.19e-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: 44.87 E-value: 9.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 149 LSGGQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERF--TIVIVTHNMQQAARVSDRTAFFNlaavG 226
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGkkTALVVEHDLAVLDYLSDRIHVFE----G 147
|
....
gi 512057730 227 QPGK 230
Cdd:cd03222 148 EPGV 151
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
142-216 |
1.17e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 45.81 E-value: 1.17e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512057730 142 LNKPGSGLSGGQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIGELKERFTIVI-VTHNMQQAARVSDR 216
Cdd:PRK15439 397 AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLfISSDLEEIEQMADR 472
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-205 |
1.22e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.88 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 5 IDVSGLTAYYGSHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLnrMHEVTPGGrveGKVLLDDedlygagidpvSVR 84
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMI--TGQEQPDS---GTIKIGE-----------TVK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 reIGMVFQ-RPNPFPTMSIFDNVAAGL---RLnGSYKKSELADIVEKSLKGAnlwnevkDRlNKPGSGLSGGQQQRLCIA 160
Cdd:PRK11819 389 --LAYVDQsRDALDPNKTVWEEISGGLdiiKV-GNREIPSRAYVGRFNFKGG-------DQ-QKKVGVLSGGERNRLHLA 457
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 512057730 161 RAIAVEPKVLLMDEPCSALDpISTL-AIEDLIgelkERF--TIVIVTH 205
Cdd:PRK11819 458 KTLKQGGNVLLLDEPTNDLD-VETLrALEEAL----LEFpgCAVVISH 500
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-212 |
1.26e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 46.06 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 20 IEDISMTVEPRTVTAFIGPSGCGKSTFLRTLnrMHEVTPGgrvEGKVllddedlygagidpvsvrREIGMVFQRPNPFPT 99
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMI--MGELEPS---EGKI------------------KHSGRISFSPQTSWI 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 100 M--SIFDNVAAGLRLNgSYKKSELADIVEKSLKGANLWNEVKDRLNKPGSGLSGGQQQRLCIARAIAVEPKVLLMDEPCS 177
Cdd:TIGR01271 499 MpgTIKDNIIFGLSYD-EYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170 180 190
....*....|....*....|....*....|....*.
gi 512057730 178 ALDPISTLAI-EDLIGELKERFTIVIVTHNMQQAAR 212
Cdd:TIGR01271 578 HLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKK 613
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
129-216 |
1.63e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.88 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 129 LKGANLwNEVKDRlnkpGSGLSGGQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIED--LIGELKERfTIVIVTHN 206
Cdd:PLN03130 726 LPGGDL-TEIGER----GVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDkcIKDELRGK-TRVLVTNQ 799
|
90
....*....|
gi 512057730 207 MQQAARVsDR 216
Cdd:PLN03130 800 LHFLSQV-DR 808
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
20-187 |
2.75e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.10 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 20 IEDISMTVEPRTVTAFIGPSGCGKSTFLRTLnrmhevtpGGRVEGKVLLDDEDLYGAGIDPVSVRR----EIGMVFQRPN 95
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTI--------ASNTDGFHIGVEGVITYDGITPEEIKKhyrgDVVYNAETDV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 96 PFPTMSIFDNV--AA-----GLRLNG----SYKKSeLADIVEKSL-----KGANLWNE-VKdrlnkpgsGLSGGQQQRLC 158
Cdd:TIGR00956 149 HFPHLTVGETLdfAArcktpQNRPDGvsreEYAKH-IADVYMATYglshtRNTKVGNDfVR--------GVSGGERKRVS 219
|
170 180
....*....|....*....|....*....
gi 512057730 159 IARAIAVEPKVLLMDEPCSALDPISTLAI 187
Cdd:TIGR00956 220 IAEASLGGAKIQCWDNATRGLDSATALEF 248
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
3-239 |
4.62e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 44.19 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 3 KRIDVSGLTAYYGSHK-AIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLNRMHevTPggrVEGKVLLDDEDLYGAgiDPV 81
Cdd:PRK10522 321 QTLELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLY--QP---QSGEILLDGKPVTAE--QPE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 82 SVRREIGMVFQrpnpfpTMSIFDnvaaglRLNGSYKKSELADIVEKSLKGANLWNEVKDRLNK-PGSGLSGGQQQRLCIA 160
Cdd:PRK10522 394 DYRKLFSAVFT------DFHLFD------QLLGPEGKPANPALVEKWLERLKMAHKLELEDGRiSNLKLSKGQKKRLALL 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 161 RAIAVEPKVLLMDEPCSALDP-ISTLAIEDLIGELKER-FTIVIVTHN---MQQAARVsdrtaffnLAAvgQPGKLIEID 235
Cdd:PRK10522 462 LALAEERDILLLDEWAADQDPhFRREFYQVLLPLLQEMgKTIFAISHDdhyFIHADRL--------LEM--RNGQLSELT 531
|
....
gi 512057730 236 DTER 239
Cdd:PRK10522 532 GEER 535
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
9-205 |
4.74e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.34 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 9 GLTAYYGSHKAI-EDISMTVEPRTVTAFIGPSGCGKSTFLRTLnrmhevtpggrvegkvllddedlygAGIDPVS---VR 84
Cdd:PRK11819 11 RVSKVVPPKKQIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------------------------AGVDKEFegeAR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 85 RE----IGMVFQRPNPFPTMSIFDNVAAGL--------RLNGSYKK--------SELAD---IVEKSLKGANLWN----- 136
Cdd:PRK11819 66 PApgikVGYLPQEPQLDPEKTVRENVEEGVaevkaaldRFNEIYAAyaepdadfDALAAeqgELQEIIDAADAWDldsql 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 512057730 137 EVK-DRLNKPG-----SGLSGGQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIEDLIgelkERF--TIVIVTH 205
Cdd:PRK11819 146 EIAmDALRCPPwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFL----HDYpgTVVAVTH 218
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-241 |
1.22e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.04 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 16 SHKAIEDISMTVEPRTVTAFIGPSGCGKSTFLRTLnrMHEVTPggrvegkvllddedlygAGIDPVSVRREIGMVFQRPN 95
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAM--LGELSH-----------------AETSSVVIRGSVAYVPQVSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 96 PFpTMSIFDNVAAGLRLNGS-YKKSELADIVEKSLK---GANLwNEVKDRlnkpGSGLSGGQQQRLCIARAIAVEPKVLL 171
Cdd:PLN03232 690 IF-NATVRENILFGSDFESErYWRAIDVTALQHDLDllpGRDL-TEIGER----GVNISGGQKQRVSMARAVYSNSDIYI 763
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 512057730 172 MDEPCSALDP-ISTLAIEDLIGELKERFTIVIVTHNMQQAARVsDRTAFFNLAAVGQPGKLIEIDDTERIF 241
Cdd:PLN03232 764 FDDPLSALDAhVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSKSGSLF 833
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-212 |
1.77e-04 |
|
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: 42.15 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 20 IEDISMTVEPRTVTAFIGPSGCGKSTFLRTLnrMHEVTPGgrvEGKVllddedlygagidpvsvrREIGMVFQRPNPFPT 99
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLI--LGELEPS---EGKI------------------KHSGRISFSSQFSWI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 100 M--SIFDNVAAGLrlngSYKKSELADIVekslKGANLWNEV-----KDR--LNKPGSGLSGGQQQRLCIARAIAVEPKVL 170
Cdd:cd03291 110 MpgTIKENIIFGV----SYDEYRYKSVV----KACQLEEDItkfpeKDNtvLGEGGITLSGGQRARISLARAVYKDADLY 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 512057730 171 LMDEPCSALDPISTLAI-EDLIGELKERFTIVIVTHNMQQAAR 212
Cdd:cd03291 182 LLDSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKK 224
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-240 |
1.80e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 41.73 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 19 AIEDISMTVEPRTVTAFIGPSGCGKSTFlrtlnrmhevtpggrvegkvllddEDLYGAGIDPVS--VRR--EIGMVFQRP 94
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTL------------------------SNIIGGSLSPTVgkVDRngEVSVIAISA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 95 NPFPTMSIFDNVAAGLRLNGsYKKSELADIVEKSLKganlWNEVKDRLNKPGSGLSGGQQQRLCIARAIAVEPKVLLMDE 174
Cdd:PRK13546 95 GLSGQLTGIENIEFKMLCMG-FKRKEIKAMTPKIIE----FSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 512057730 175 PCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSDRTAFFnlaavgQPGKLIEIDDTERI 240
Cdd:PRK13546 170 ALSVGDQTFAQKCLDKIYEFKEQnKTIFFVSHNLGQVRQFCTKIAWI------EGGKLKDYGELDDV 230
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
18-205 |
3.68e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 41.14 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 18 KAIEDISMTVEPRtVTAFIGPSGCGKSTFLRTLNRMHEVTPGGRVegkvllDDEDLYGaGIDPVSVRREIGMVFQRP--- 94
Cdd:COG3593 12 RSIKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSRKF------DEEDFYL-GDDPDLPEIEIELTFGSLlsr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 95 --NPFPTMSIFDNVAAGLR-LNGSYKKS--ELADIVEKSLKGA------------------------NLWNEVKDRLNKP 145
Cdd:COG3593 84 llRLLLKEEDKEELEEALEeLNEELKEAlkALNELLSEYLKELldgldlelelsldeledllkslslRIEDGKELPLDRL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512057730 146 GSGlsggqQQRLCI---ARAIA-----VEPKVLLMDEPCSALDPIstlAIEDLIGELKE----RFTIVIVTH 205
Cdd:COG3593 164 GSG-----FQRLILlalLSALAelkraPANPILLIEEPEAHLHPQ---AQRRLLKLLKElsekPNQVIITTH 227
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-241 |
3.92e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.41 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 17 HKAIEDISMTVEPRTVTAFIGPSGCGKSTFLrtlNRMHEVT-PGgrvEGKVllddeDLYG-AGIDPVSVrreiGMVFQrp 94
Cdd:PRK13545 37 HYALNNISFEVPEGEIVGIIGLNGSGKSTLS---NLIAGVTmPN---KGTV-----DIKGsAALIAISS----GLNGQ-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 95 npfptMSIFDNVA-AGLRLngSYKKSELADIVEKSLKGAnlwnEVKDRLNKPGSGLSGGQQQRLCIARAIAVEPKVLLMD 173
Cdd:PRK13545 100 -----LTGIENIElKGLMM--GLTKEKIKEIIPEIIEFA----DIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVID 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 512057730 174 EPCSALDPISTLAIEDLIGELKER-FTIVIVTHNMQQAARVSDRTAFFNLAAVGQPGKLIEIDDTERIF 241
Cdd:PRK13545 169 EALSVGDQTFTKKCLDKMNEFKEQgKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDEF 237
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
148-212 |
4.27e-04 |
|
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: 39.65 E-value: 4.27e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 148 GLSGGQQQRLCIARAIA---VEPKVL-LMDEPCSALDPISTLAIEDLIGE-LKERFTIVIVTHNMQQAAR 212
Cdd:cd03227 77 QLSGGEKELSALALILAlasLKPRPLyILDEIDRGLDPRDGQALAEAILEhLVKGAQVIVITHLPELAEL 146
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
1-56 |
1.09e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 39.91 E-value: 1.09e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 512057730 1 MAKRIDVSGLtayygshKAIEDISMTVEPRTVtaFIGPSGCGKSTFLRTLNRMHEV 56
Cdd:COG4637 1 MITRIRIKNF-------KSLRDLELPLGPLTV--LIGANGSGKSNLLDALRFLSDA 47
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
36-205 |
1.67e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.49 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 36 IGPSGCGKSTFLRTLnrmhevtpGGRVE---GKVLLDdedlygagidpVSVRreIGMVFQRPNPFPTMSIFDNV------ 106
Cdd:PRK15064 33 IGANGCGKSTFMKIL--------GGDLEpsaGNVSLD-----------PNER--LGKLRQDQFAFEEFTVLDTVimghte 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 107 --AAGLRLNGSYKKSELADivEKSLKGANLwnEVK------------------------DRLNKPGSGLSGGQQQRLCIA 160
Cdd:PRK15064 92 lwEVKQERDRIYALPEMSE--EDGMKVADL--EVKfaemdgytaearagelllgvgipeEQHYGLMSEVAPGWKLRVLLA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 512057730 161 RAIAVEPKVLLMDEPCSALDpISTlaIEDLIGELKER-FTIVIVTH 205
Cdd:PRK15064 168 QALFSNPDILLLDEPTNNLD-INT--IRWLEDVLNERnSTMIIISH 210
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-207 |
2.08e-03 |
|
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: 37.74 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 29 PRTVTAFIGPSGCGKSTFLRTLNRmHEVTPGGRVegkVLLDDEDLYgagidpvsvrreigmvfqrpnpfptmsifdnvaa 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAR-ELGPPGGGV---IYIDGEDIL---------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 109 glrlngsykkseladivekslkGANLWNEVKDRLNKPGSGLSGGQQQRLCIARAIAVEPKVLLMDEPCSALDPISTLAIE 188
Cdd:smart00382 43 ----------------------EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLL 100
|
170 180
....*....|....*....|....*
gi 512057730 189 D------LIGELKERFTIVIVTHNM 207
Cdd:smart00382 101 LleelrlLLLLKSEKNLTVILTTND 125
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
113-206 |
3.83e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 38.14 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 113 NGSYKKSELADIVEKSLKGANLWNEVKDRLNKPGSGLSGGQQQRLCIA---RAIAVEPKVLLMDEPCSALDPistLAIED 189
Cdd:pfam13304 201 DLGEGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKRLLALLaalLSALPKGGLLLIDEPESGLHP---KLLRR 277
|
90 100
....*....|....*....|.
gi 512057730 190 LIGELKE----RFTIVIVTHN 206
Cdd:pfam13304 278 LLELLKElsrnGAQLILTTHS 298
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
142-215 |
4.64e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.27 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512057730 142 LNKPGSGLSGGQQQRLCIAR---AIAVEPKVLLMDEPCSALdpiSTLAIEDLIGELK----ERFTIVIVTHNMqQAARVS 214
Cdd:PRK00635 803 LGRPLSSLSGGEIQRLKLAYellAPSKKPTLYVLDEPTTGL---HTHDIKALIYVLQslthQGHTVVIIEHNM-HVVKVA 878
|
.
gi 512057730 215 D 215
Cdd:PRK00635 879 D 879
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
24-47 |
9.62e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 33.73 E-value: 9.62e-03
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| |
