|
Name |
Accession |
Description |
Interval |
E-value |
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-269 |
0e+00 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 508.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 4 TNKKTPKNIILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDLIPNCSLKGTVLFDGTNIY 83
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGARVEGEILLDGEDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 84 DKRVDPVEVRRRIGMVFQQPNPFPKSIYENIAFGARINGFT--GDMDELVESSLRKAALWDECKDKLNDSGYSLSGGQQQ 161
Cdd:COG1117 82 DPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGLRLHGIKskSELDEIVEESLRKAALWDEVKDRLKKSALGLSGGQQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 162 RLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTHNMQQALRVSDMTAFFNaveyedgdggkVGY 241
Cdd:COG1117 162 RLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFY-----------LGE 230
|
250 260
....*....|....*....|....*...
gi 123755092 242 LAEFNSTKKIFNSPKEKTTQEYISGKFG 269
Cdd:COG1117 231 LVEFGPTEQIFTNPKDKRTEDYITGRFG 258
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
11-269 |
1.60e-164 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 456.17 E-value: 1.60e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 11 NIILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDLIPNCSLKGTVLFDGTNIYDKRVDPV 90
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFHGKNLYAPDVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 91 EVRRRIGMVFQQPNPFPKSIYENIAFGARINGFTGDMDELVESSLRKAALWDECKDKLNDSGYSLSGGQQQRLCIARTIA 170
Cdd:PRK14243 88 EVRRRIGMVFQKPNPFPKSIYDNIAYGARINGYKGDMDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 171 IEPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTHNMQQALRVSDMTAFFNAVEYEdgDGGKVGYLAEFNSTKK 250
Cdd:PRK14243 168 VQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTE--GGGRYGYLVEFDRTEK 245
|
250
....*....|....*....
gi 123755092 251 IFNSPKEKTTQEYISGKFG 269
Cdd:PRK14243 246 IFNSPQQQATRDYVSGRFG 264
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
13-268 |
2.29e-152 |
|
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: 424.79 E-value: 2.29e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDLIPNCSLKGTVLFDGTNIYDKRVDPVEV 92
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPGVRIEGKVLFDGQDIYDKKIDVVEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 93 RRRIGMVFQQPNPFPKSIYENIAFGARINGFT--GDMDELVESSLRKAALWDECKDKLNDSGYSLSGGQQQRLCIARTIA 170
Cdd:TIGR00972 81 RRRVGMVFQKPNPFPMSIYDNIAYGPRLHGIKdkKELDEIVEESLKKAALWDEVKDRLHDSALGLSGGQQQRLCIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 171 IEPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTHNMQQALRVSDMTAFFnaveyedgdggKVGYLAEFNSTKK 250
Cdd:TIGR00972 161 VEPEVLLLDEPTSALDPIATGKIEELIQELKKKYTIVIVTHNMQQAARISDRTAFF-----------YDGELVEYGPTEQ 229
|
250
....*....|....*...
gi 123755092 251 IFNSPKEKTTQEYISGKF 268
Cdd:TIGR00972 230 IFTNPKEKRTEDYISGRF 247
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
14-251 |
5.45e-131 |
|
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: 369.97 E-value: 5.45e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDLIPNCSLKGTVLFDGTNIYDKRVDPVEVR 93
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 94 RRIGMVFQQPNPFPKSIYENIAFGARINGF--TGDMDELVESSLRKAALWDECKDKLNdsGYSLSGGQQQRLCIARTIAI 171
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVAYGLRLHGIklKEELDERVEEALRKAALWDEVKDRLH--ALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 172 EPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTHNMQQALRVSDMTAFFNAveyedgdggkvGYLAEFNSTKKI 251
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLN-----------GRLVEFGPTEQI 227
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
13-269 |
5.95e-126 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 358.32 E-value: 5.95e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDLIPNCSLKGTVLFDGTNIYDKRVDPVEV 92
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 93 RRRIGMVFQQPNPFPKSIYENIAFGARINGFTGD--MDELVESSLRKAALWDECKDKLNDSGYSLSGGQQQRLCIARTIA 170
Cdd:PRK14239 85 RKEIGMVFQQPNPFPMSIYENVVYGLRLKGIKDKqvLDEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIARVLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 171 IEPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTHNMQQALRVSDMTAFFnaveyEDGDggkvgyLAEFNSTKK 250
Cdd:PRK14239 165 TSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFF-----LDGD------LIEYNDTKQ 233
|
250
....*....|....*....
gi 123755092 251 IFNSPKEKTTQEYISGKFG 269
Cdd:PRK14239 234 MFMNPKHKETEDYISGKFG 252
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-269 |
6.86e-93 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 274.61 E-value: 6.86e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDLIPNCSLKGTVLFDGTNIYDKRVDPVEVR 93
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 94 RRIGMVFQQPNPFPKSIYENIAFGARINGFTG--DMDELVESSLRKAALWDECKDKLNDSGYSLSGGQQQRLCIARTIAI 171
Cdd:PRK14258 88 RQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPklEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 172 EPEIILMDEPCSALDPISTLKIEETMHELKM--NYTIIIVTHNMQQALRVSDMTAFFNaveyedGDGGKVGYLAEFNSTK 249
Cdd:PRK14258 168 KPKVLLMDEPCFGLDPIASMKVESLIQSLRLrsELTMVIVSHNLHQVSRLSDFTAFFK------GNENRIGQLVEFGLTK 241
|
250 260
....*....|....*....|
gi 123755092 250 KIFNSPKEKTTQEYISGKFG 269
Cdd:PRK14258 242 KIFNSPHDSRTREYVLSRLG 261
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-269 |
1.77e-90 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 268.25 E-value: 1.77e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 10 KNIILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDLIPNCSLKGTVLFDGTNIYDKRVDP 89
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 90 VEVRRRIGMVFQQPNPFPK-SIYENIAFGARINGFT---GDMDELVESSLRKAALWDECKDKLNDSGYSLSGGQQQRLCI 165
Cdd:PRK14267 81 IEVRREVGMVFQYPNPFPHlTIYDNVAIGVKLNGLVkskKELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 166 ARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTHNMQQALRVSDMTAFFnaveyedgdggKVGYLAEF 245
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFL-----------YLGKLIEV 229
|
250 260
....*....|....*....|....
gi 123755092 246 NSTKKIFNSPKEKTTQEYISGKFG 269
Cdd:PRK14267 230 GPTRKVFENPEHELTEKYVTGALG 253
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-267 |
4.93e-81 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 244.05 E-value: 4.93e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDLIPNCSLKGTVLFDGTNIYdkRVDPVEVR 93
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIF--KMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 94 RRIGMVFQQPNPFPK-SIYENIAFGARINGFTGDMDEL---VESSLRKAALWDECKDKLNDSGYSLSGGQQQRLCIARTI 169
Cdd:PRK14247 82 RRVQMVFQIPNPIPNlSIFENVALGLKLNRLVKSKKELqerVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 170 AIEPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTHNMQQALRVSDMTAFFnaveYEdgdggkvGYLAEFNSTK 249
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFL----YK-------GQIVEWGPTR 230
|
250
....*....|....*...
gi 123755092 250 KIFNSPKEKTTQEYISGK 267
Cdd:PRK14247 231 EVFTNPRHELTEKYVTGR 248
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-269 |
3.88e-69 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 214.96 E-value: 3.88e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 18 NVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDLIPNCSLKGTVLFDGTNIYDKRvDPVEVRRRIG 97
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYR-DVLEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 98 MVFQQPNPFPKSIYENIAFGARINGFT--GDMDELVESSLRKAALWDECKDKLNDSGYSLSGGQQQRLCIARTIAIEPEI 175
Cdd:PRK14271 105 MLFQRPNPFPMSIMDNVLAGVRAHKLVprKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 176 ILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTHNMQQALRVSDMTAFFNAveyedgdggkvGYLAEFNSTKKIFNSP 255
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFD-----------GRLVEEGPTEQLFSSP 253
|
250
....*....|....
gi 123755092 256 KEKTTQEYISGKFG 269
Cdd:PRK14271 254 KHAETARYVAGLSG 267
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
13-265 |
1.16e-66 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 207.15 E-value: 1.16e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDliPNcslKGTVLFDGTNIYDKRVDPVEV 92
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEE--PD---SGTITVDGEDLTDSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 93 RRRIGMVFQQPNPFP-KSIYENIAFG-----------ARingftgdmdELVESSLRKAALwdecKDKLNDSGYSLSGGQQ 160
Cdd:COG1126 76 RRKVGMVFQQFNLFPhLTVLENVTLApikvkkmskaeAE---------ERAMELLERVGL----ADKADAYPAQLSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 161 QRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL---KMnyTIIIVTHNMQQALRVSDMTAFFnaveyedgDGG 237
Cdd:COG1126 143 QRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLakeGM--TMVVVTHEMGFAREVADRVVFM--------DGG 212
|
250 260
....*....|....*....|....*...
gi 123755092 238 KVgylAEFNSTKKIFNSPKEKTTQEYIS 265
Cdd:COG1126 213 RI---VEEGPPEEFFENPQHERTRAFLS 237
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
29-267 |
1.19e-61 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 194.88 E-value: 1.19e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 29 VRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDLIPN-CSLKGTVLFDGTNIYdkRVDPVEVRRRIGMVFQQPNPFP 107
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSkIKVDGKVLYFGKDIF--QIDAIKLRKEVGMVFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 108 K-SIYENIAFGARINGFTG--DMDELVESSLRKAALWDECKDKLNDSGYSLSGGQQQRLCIARTIAIEPEIILMDEPCSA 184
Cdd:PRK14246 104 HlSIYDNIAYPLKSHGIKEkrEIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 185 LDPISTLKIEETMHELKMNYTIIIVTHNMQQALRVSDMTAFFNAveyedgdggkvGYLAEFNSTKKIFNSPKEKTTQEYI 264
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYN-----------GELVEWGSSNEIFTSPKNELTEKYV 252
|
...
gi 123755092 265 SGK 267
Cdd:PRK14246 253 IGR 255
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
14-228 |
1.25e-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: 189.71 E-value: 1.25e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDLIpncslKGTVLFDGTNIYDKRVDPVEVR 93
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPD-----SGSILIDGEDLTDLEDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 94 RRIGMVFQQPNPFP-KSIYENIAFGaringftgdmdelvesslrkaalwdeckdklndsgysLSGGQQQRLCIARTIAIE 172
Cdd:cd03229 76 RRIGMVFQDFALFPhLTVLENIALG-------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 123755092 173 PEIILMDEPCSALDPISTLKIEETMHELK--MNYTIIIVTHNMQQALRVSDMTAFFNA 228
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLQaqLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
14-221 |
1.67e-57 |
|
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: 183.30 E-value: 1.67e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISY-GTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNcslKGTVLFDGTNIYDKrvDPVEV 92
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGL--LKPT---SGEVLVDGKDITKK--NLREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 93 RRRIGMVFQqpNP----FPKSIYENIAFGARINGFTGD-MDELVESSLRKAALWDeckdKLNDSGYSLSGGQQQRLCIAR 167
Cdd:COG1122 74 RRKVGLVFQ--NPddqlFAPTVEEDVAFGPENLGLPREeIRERVEEALELVGLEH----LADRPPHELSGGQKQRVAIAG 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 123755092 168 TIAIEPEIILMDEPCSALDPISTLKIEETMHEL-KMNYTIIIVTHNMQQALRVSD 221
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAELAD 202
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
14-227 |
1.09e-56 |
|
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: 180.79 E-value: 1.09e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRmndLIPNCSlkGTVLFDGTNIYDKrvdPVEvR 93
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAG---LERPDS--GEILIDGRDVTGV---PPE-R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 94 RRIGMVFQQPNPFP-KSIYENIAFGARINGF-TGDMDELVESSLRKAALwdecKDKLNDSGYSLSGGQQQRLCIARTIAI 171
Cdd:cd03259 72 RNIGMVFQDYALFPhLTVAENIAFGLKLRGVpKAEIRARVRELLELVGL----EGLLNRYPHELSGGQQQRVALARALAR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123755092 172 EPEIILMDEPCSALDPISTlkiEETMHELK-----MNYTIIIVTHNMQQALRVSDMTAFFN 227
Cdd:cd03259 148 EPSLLLLDEPLSALDAKLR---EELREELKelqreLGITTIYVTHDQEEALALADRIAVMN 205
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
14-239 |
9.71e-55 |
|
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: 175.80 E-value: 9.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDliPNcslKGTVLFDGTNIYDKRVDPVEVR 93
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEE--PD---SGTIIIDGLKLTDDKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 94 RRIGMVFQQPNPFP-KSIYENIAFGAR-INGFT-GDMDELVESSLRKAALwdecKDKLNDSGYSLSGGQQQRLCIARTIA 170
Cdd:cd03262 76 QKVGMVFQQFNLFPhLTVLENITLAPIkVKGMSkAEAEERALELLEKVGL----ADKADAYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 171 IEPEIILMDEPCSALDPISTLKIEETMHEL-KMNYTIIIVTHNMQQALRVSDMTAFFnaveyedgDGGKV 239
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMKDLaEEGMTMVVVTHEMGFAREVADRVIFM--------DDGRI 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
15-221 |
5.00e-54 |
|
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: 173.81 E-value: 5.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 15 SLENVSISYGTFE--AVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPncsLKGTVLFDGTNIYDKRVdpVEV 92
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGL--LGP---TSGEVLVDGKDLTKLSL--KEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 93 RRRIGMVFQQPNP--FPKSIYENIAFGARINGFTGD-MDELVESSLRKAALWDeckdKLNDSGYSLSGGQQQRLCIARTI 169
Cdd:cd03225 74 RRKVGLVFQNPDDqfFGPTVEEEVAFGLENLGLPEEeIEERVEEALELVGLEG----LRDRSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 123755092 170 AIEPEIILMDEPCSALDPISTLKIEETMHELK-MNYTIIIVTHNMQQALRVSD 221
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKaEGKTIIIVTHDLDLLLELAD 202
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
14-221 |
1.15e-53 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 172.69 E-value: 1.15e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNrmnDLIPNCSlkGTVLFDGTNIYDkrVDPVEVR 93
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALA---DLDPPTS--GEIYLDGKPLSA--MPPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 94 RRIGMVFQQPNPFPKSIYENIAFGARINGFTGDMDELVESsLRKAALWDECKDKlndSGYSLSGGQQQRLCIARTIAIEP 173
Cdd:COG4619 74 RQVAYVPQEPALWGGTVRDNLPFPFQLRERKFDRERALEL-LERLGLPPDILDK---PVERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 123755092 174 EIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHNMQQALRVSD 221
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYlaEEGRAVLWVSHDPEQIERVAD 199
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
16-227 |
3.55e-52 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 172.20 E-value: 3.55e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 16 LENVSISY-GTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDliPNcslKGTVLFDGTNIYDkrVDPVEVRR 94
Cdd:COG1125 4 FENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIE--PT---SGRILIDGEDIRD--LDPVELRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 95 RIGMVFQQPNPFP-KSIYENIAFGARINGFTGD-----MDELVES-SLRKAALWDEckdklndsgY--SLSGGQQQRLCI 165
Cdd:COG1125 77 RIGYVIQQIGLFPhMTVAENIATVPRLLGWDKErirarVDELLELvGLDPEEYRDR---------YphELSGGQQQRVGV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 123755092 166 ARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHNMQQALRVSDMTAFFN 227
Cdd:COG1125 148 ARALAADPPILLMDEPFGALDPITREQLQDELLRLqrELGKTIVFVTHDIDEALKLGDRIAVMR 211
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
14-255 |
5.85e-52 |
|
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: 169.79 E-value: 5.85e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISY-GTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNcslKGTVLFDGTNIydKRVDPVEV 92
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRL--IEPT---SGEIFIDGEDI--REQDPVEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 93 RRRIGMVFQQPNPFP-KSIYENIAFGARINGFTGD-----MDELVE-SSLRKAALWDECKDKlndsgysLSGGQQQRLCI 165
Cdd:cd03295 74 RRKIGYVIQQIGLFPhMTVEENIALVPKLLKWPKEkirerADELLAlVGLDPAEFADRYPHE-------LSGGQQQRVGV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 166 ARTIAIEPEIILMDEPCSALDPISTLKIEETMHELK--MNYTIIIVTHNMQQALRVSDMTAFFNAveyedgdggkvGYLA 243
Cdd:cd03295 147 ARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQqeLGKTIVFVTHDIDEAFRLADRIAIMKN-----------GEIV 215
|
250
....*....|..
gi 123755092 244 EFNSTKKIFNSP 255
Cdd:cd03295 216 QVGTPDEILRSP 227
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
13-228 |
1.11e-51 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 172.20 E-value: 1.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRslnrmndLI-----PNcslKGTVLFDGTNIYDKrv 87
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLR-------MIagfetPD---SGRILLDGRDVTGL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 88 dPVEvRRRIGMVFQQPNPFP-KSIYENIAFGARINGFT-GDMDELVESSLRKAALwdeckdklndSGYS------LSGGQ 159
Cdd:COG3842 73 -PPE-KRNVGMVFQDYALFPhLTVAENVAFGLRMRGVPkAEIRARVAELLELVGL----------EGLAdryphqLSGGQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 123755092 160 QQRLCIARTIAIEPEIILMDEPCSALDPisTLKiEETMHELK-----MNYTIIIVTHNMQQALRVSDMTAFFNA 228
Cdd:COG3842 141 QQRVALARALAPEPRVLLLDEPLSALDA--KLR-EEMREELRrlqreLGITFIYVTHDQEEALALADRIAVMND 211
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
8-224 |
1.31e-51 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 169.11 E-value: 1.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 8 TPKNIILSLENVSISY----GTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNrmnDLIPNCSlkGTVLFDGTNIy 83
Cdd:COG1116 2 SAAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIA---GLEKPTS--GEVLVDGKPV- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 84 dkrvdpVEVRRRIGMVFQQPNPFP-KSIYENIAFGARINGFT-GDMDELVESSLRKAALwDECKDKLndsGYSLSGGQQQ 161
Cdd:COG1116 76 ------TGPGPDRGVVFQEPALLPwLTVLDNVALGLELRGVPkAERRERARELLELVGL-AGFEDAY---PHQLSGGMRQ 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 123755092 162 RLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHNMQQALRVSD----MTA 224
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHDVDEAVFLADrvvvLSA 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
13-265 |
1.37e-51 |
|
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: 175.86 E-value: 1.37e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISY-----GTFEAVRNVfcNF--KKGNITSLIGPSGCGKSTVLRSLNRMNDliPNcslKGTVLFDGTNIYD- 84
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDV--SLtlRRGETLGLVGESGSGKSTLARLLLGLLR--PT---SGSILFDGKDLTKl 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 85 KRVDPVEVRRRIGMVFQQP----NPFpKSIYENIAFGARINGFTG--DMDELVESSLRKAALWDECKDKlndSGYSLSGG 158
Cdd:COG1123 333 SRRSLRELRRRVQMVFQDPysslNPR-MTVGDIIAEPLRLHGLLSraERRERVAELLERVGLPPDLADR---YPHELSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 159 QQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELK--MNYTIIIVTHNMQQALRVSDMTAFFNAveyedgdg 236
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQreLGLTYLFISHDLAVVRYIADRVAVMYD-------- 480
|
250 260
....*....|....*....|....*....
gi 123755092 237 gkvGYLAEFNSTKKIFNSPKEKTTQEYIS 265
Cdd:COG1123 481 ---GRIVEDGPTEEVFANPQHPYTRALLA 506
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
14-221 |
3.18e-51 |
|
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: 167.29 E-value: 3.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSlnrMNDLIPncSLKGTVLFDGTNIYD-KRVDPVEV 92
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRL---IVGLLR--PDSGEVLIDGEDISGlSEAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 93 RRRIGMVFQQPNPF-PKSIYENIAFGARINGftgdmdELVESSLRKAALwdeckDKLNDSG---------YSLSGGQQQR 162
Cdd:cd03261 76 RRRMGMLFQSGALFdSLTVFENVAFPLREHT------RLSEEEIREIVL-----EKLEAVGlrgaedlypAELSGGMKKR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123755092 163 LCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNY--TIIIVTHNMQQALRVSD 221
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELglTSIMVTHDLDTAFAIAD 205
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
14-262 |
4.46e-51 |
|
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: 167.67 E-value: 4.46e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGT----FEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDliPNcslKGTVLFDGTNIYDKRvdP 89
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLER--PW---SGEVTFDGRPVTRRR--R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 90 VEVRRRIGMVFQQP----NPFpKSIYENIAFGARINGFtGDMDELVESSLRKAALWDECKDKLndsGYSLSGGQQQRLCI 165
Cdd:COG1124 75 KAFRRRVQMVFQDPyaslHPR-HTVDRILAEPLRIHGL-PDREERIAELLEQVGLPPSFLDRY---PHQLSGGQRQRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 166 ARTIAIEPEIILMDEPCSALDPISTLKIEETMHELK--MNYTIIIVTHNMQQALRVSDMTAFFNAveyedgdggkvGYLA 243
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILNLLKDLReeRGLTYLFVSHDLAVVAHLCDRVAVMQN-----------GRIV 218
|
250
....*....|....*....
gi 123755092 244 EFNSTKKIFNSPKEKTTQE 262
Cdd:COG1124 219 EELTVADLLAGPKHPYTRE 237
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
14-221 |
5.41e-51 |
|
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: 166.49 E-value: 5.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGT----FEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRmndLIPNCSlkGTVLFDGTNIydkrvdp 89
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAG---LERPTS--GEVLVDGEPV------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 90 VEVRRRIGMVFQQPNPFP-KSIYENIAFGARINGF-TGDMDELVESSLRKAALwdecKDKLNDSGYSLSGGQQQRLCIAR 167
Cdd:cd03293 69 TGPGPDRGYVFQQDALLPwLTVLDNVALGLELQGVpKAEARERAEELLELVGL----SGFENAYPHQLSGGMRQRVALAR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 123755092 168 TIAIEPEIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHNMQQALRVSD 221
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIwrETGKTVLLVTHDIDEAVFLAD 200
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
11-221 |
6.97e-50 |
|
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: 164.00 E-value: 6.97e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 11 NIILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNcslKGTVLFDGTNIYD-KRVDP 89
Cdd:COG1127 3 EPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGL--LRPD---SGEILVDGQDITGlSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 90 VEVRRRIGMVFQQPNPF-PKSIYENIAFGARINGftgDMDElveSSLRKAALwdeckDKLNDSGYS---------LSGGQ 159
Cdd:COG1127 78 YELRRRIGMLFQGGALFdSLTVFENVAFPLREHT---DLSE---AEIRELVL-----EKLELVGLPgaadkmpseLSGGM 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 123755092 160 QQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHNMQQALRVSD 221
Cdd:COG1127 147 RKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELrdELGLTSVVVTHDLDSAFAIAD 210
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
13-221 |
4.45e-49 |
|
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: 162.52 E-value: 4.45e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRmndLIPncSLKGTVLFDGTNIydKRVDPVEV 92
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAG---LLK--PSSGEVLLDGRDL--ASLSRREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 93 RRRIGMVFQQPN-PFPKSIYENIAFG-----ARINGFTGDMDELVESSLRKAALWDeCKDKLNDsgySLSGGQQQRLCIA 166
Cdd:COG1120 74 ARRIAYVPQEPPaPFGLTVRELVALGryphlGLFGRPSAEDREAVEEALERTGLEH-LADRPVD---ELSGGERQRVLIA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 123755092 167 RTIAIEPEIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHNMQQALRVSD 221
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNLAARYAD 206
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
14-221 |
1.26e-48 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 160.61 E-value: 1.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVfcNF--KKGNITSLIGPSGCGKSTVLRSLnrMNDLIPNcslKGTVLFDGTNIYDkrvDPVE 91
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGV--SLtvEPGEIFGLLGPNGAGKTTTIRML--LGLLRPT---SGEVRVLGEDVAR---DPAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 92 VRRRIGMVFQQPNPFPK-SIYENIAFGARINGFTG-DMDELVESSLRKAALWDECKDKLNDsgysLSGGQQQRLCIARTI 169
Cdd:COG1131 71 VRRRIGYVPQEPALYPDlTVRENLRFFARLYGLPRkEARERIDELLELFGLTDAADRKVGT----LSGGMKQRLGLALAL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 123755092 170 AIEPEIILMDEPCSALDPISTLKIEETMHELK-MNYTIIIVTHNMQQALRVSD 221
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAaEGKTVLLSTHYLEEAERLCD 199
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
14-214 |
1.44e-48 |
|
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: 159.96 E-value: 1.44e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYG----TFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDliPNcslKGTVLFDGTNIY---DKR 86
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDR--PT---SGEVRVDGTDISklsEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 87 VDPvEVRRRIGMVFQQPNPFPK-SIYENIAFGARINGFTG-DMDELVESSLRKAALwdecKDKLNDSGYSLSGGQQQRLC 164
Cdd:cd03255 76 LAA-FRRRHIGFVFQSFNLLPDlTALENVELPLLLAGVPKkERRERAEELLERVGL----GDRLNHYPSELSGGQQQRVA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 123755092 165 IARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHNMQ 214
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPE 202
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-211 |
4.03e-48 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 169.63 E-value: 4.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFE--AVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNcslKGTVLFDGTNIydKRVDPVE 91
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGL--YEPT---SGRILIDGIDL--RQIDPAS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 92 VRRRIGMVFQQPNPFPKSIYENIAFGARingfTGDMDELVESsLRKAALWDECKD-------KLNDSGYSLSGGQQQRLC 164
Cdd:COG2274 547 LRRQIGVVLQDVFLFSGTIRENITLGDP----DATDEEIIEA-ARLAGLHDFIEAlpmgydtVVGEGGSNLSGGQRQRLA 621
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 123755092 165 IARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTH 211
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAH 668
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
14-219 |
1.72e-47 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 155.62 E-value: 1.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTF--EAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDliPNcslKGTVLFDGTNIYDkrVDPVE 91
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYD--PT---SGEILIDGVDLRD--LDLES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 92 VRRRIGMVFQQPNPFPKSIYENIafgaringftgdmdelvesslrkaalwdeckdklndsgysLSGGQQQRLCIARTIAI 171
Cdd:cd03228 74 LRKNIAYVPQDPFLFSGTIRENI----------------------------------------LSGGQRQRIAIARALLR 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 123755092 172 EPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTHNMQQALRV 219
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDA 161
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
14-221 |
2.71e-47 |
|
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: 158.77 E-value: 2.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISY--GT-FE--AVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNcslKGTVLFDGTNIY-DKRV 87
Cdd:TIGR04521 1 IKLKNVSYIYqpGTpFEkkALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGL--LKPT---SGTVTIDGRDITaKKKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 88 DPVEVRRRIGMVFQQPNP--FPKSIYENIAFGARINGFTGDM-DELVESSLRKAALWDECKDKlndSGYSLSGGQQQRLC 164
Cdd:TIGR04521 76 KLKDLRKKVGLVFQFPEHqlFEETVYKDIAFGPKNLGLSEEEaEERVKEALELVGLDEEYLER---SPFELSGGQMRRVA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 123755092 165 IARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHNMQQALRVSD 221
Cdd:TIGR04521 153 IAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLhkEKGLTVILVTHSMEDVAEYAD 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
14-256 |
1.31e-46 |
|
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: 155.47 E-value: 1.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDliPNcslKGTVLFDGTNIYDkrVDPVevR 93
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFET--PT---SGEILLDGKDITN--LPPH--K 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 94 RRIGMVFQQPNPFPK-SIYENIAFGARINGFTGD-MDELVESSLRKAALwdecKDKLNDSGYSLSGGQQQRLCIARTIAI 171
Cdd:cd03300 72 RPVNTVFQNYALFPHlTVFENIAFGLRLKKLPKAeIKERVAEALDLVQL----EGYANRKPSQLSGGQQQRVAIARALVN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 172 EPEIILMDEPCSALDpistLKIEETMH-ELK-----MNYTIIIVTHNMQQALRVSDMTAFFNAveyedgdggkvGYLAEF 245
Cdd:cd03300 148 EPKVLLLDEPLGALD----LKLRKDMQlELKrlqkeLGITFVFVTHDQEEALTMSDRIAVMNK-----------GKIQQI 212
|
250
....*....|.
gi 123755092 246 NSTKKIFNSPK 256
Cdd:cd03300 213 GTPEEIYEEPA 223
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
14-221 |
2.84e-46 |
|
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: 155.03 E-value: 2.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGT-FEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNcslKGTVLFDGTNI-YDKRVDPVE 91
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGL--VEPT---SGSVLIDGTDInKLKGKALRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 92 VRRRIGMVFQQPNPFPK-SIYENIAFG--ARINGFTGdMDELVESSLRKAALwdECKDKLNDSGYS------LSGGQQQR 162
Cdd:cd03256 76 LRRQIGMIFQQFNLIERlSVLENVLSGrlGRRSTWRS-LFGLFPKEEKQRAL--AALERVGLLDKAyqradqLSGGQQQR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123755092 163 LCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHNMQQALRVSD 221
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREYAD 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
14-221 |
2.81e-45 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 155.62 E-value: 2.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRslnrmndLI-----PNcslKGTVLFDGtniydKRVD 88
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLR-------MIagledPT---SGEILIGG-----RDVT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 89 PVEVRRR-IGMVFQQPNPFP-KSIYENIAFGARINGFTGD-MDELVesslRKAAlwdeckDKLNDSGY------SLSGGQ 159
Cdd:COG3839 69 DLPPKDRnIAMVFQSYALYPhMTVYENIAFPLKLRKVPKAeIDRRV----REAA------ELLGLEDLldrkpkQLSGGQ 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 123755092 160 QQRLCIARTIAIEPEIILMDEPCSALDPisTLKiEETMHELK-----MNYTIIIVTHNMQQALRVSD 221
Cdd:COG3839 139 RQRVALGRALVREPKVFLLDEPLSNLDA--KLR-VEMRAEIKrlhrrLGTTTIYVTHDQVEAMTLAD 202
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
11-218 |
2.98e-45 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 151.73 E-value: 2.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 11 NIILSLENVSISYGT----FEAVRNVFCNFKKGNITSLIGPSGCGKSTVLrslnrmndlipNC-SL-----KGTVLFDGT 80
Cdd:COG1136 2 SPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLL-----------NIlGGldrptSGEVLIDGQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 81 NIY---DKRVDpvEVRRR-IGMVFQQPNPFPK-SIYENIAFGARINGFT-GDMDELVESSLRKAALwdecKDKLNDSGYS 154
Cdd:COG1136 71 DISslsERELA--RLRRRhIGFVFQFFNLLPElTALENVALPLLLAGVSrKERRERARELLERVGL----GDRLDHRPSQ 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 123755092 155 LSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHNMQQALR 218
Cdd:COG1136 145 LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAAR 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
13-257 |
3.95e-45 |
|
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: 158.53 E-value: 3.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISY--GTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRmndLIP-NCSLKGTVLFDGTNIydKRVDP 89
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG---LLPhGGRISGEVLLDGRDL--LELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 90 VEVRRRIGMVFQQP--NPFPKSIYENIAFGARINGFTGD-MDELVESSLRKAALwdecKDKLNDSGYSLSGGQQQRLCIA 166
Cdd:COG1123 79 ALRGRRIGMVFQDPmtQLNPVTVGDQIAEALENLGLSRAeARARVLELLEAVGL----ERRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 167 RTIAIEPEIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHNMQQALRVSDMTAFFNAveyedgdggkvGYLAE 244
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELqrERGTTVLLITHDLGVVAEIADRVVVMDD-----------GRIVE 223
|
250
....*....|...
gi 123755092 245 FNSTKKIFNSPKE 257
Cdd:COG1123 224 DGPPEEILAAPQA 236
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
13-221 |
7.01e-45 |
|
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: 150.73 E-value: 7.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISY----GTFEAVRNVfcNF--KKGNITSLIGPSGCGKSTVLRSLNRMNDLIpncslKGTVLFDGTNIYDKR 86
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDV--SFsiKKGETLGLVGESGSGKSTLARAILGLLKPT-----SGSIIFDGKDLLKLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 87 VDPVEVRRR-IGMVFQQP----NPFpKSIYENIAFGARINGFTGDMDELVESSLRKAALWDECKDKLNDSGYSLSGGQQQ 161
Cdd:cd03257 74 RRLRKIRRKeIQMVFQDPmsslNPR-MTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQ 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123755092 162 RLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELK--MNYTIIIVTHNMQQALRVSD 221
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQeeLGLTLLFITHDLGVVAKIAD 214
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
13-221 |
8.20e-45 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 151.36 E-value: 8.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISY-GTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDliPNcslKGTVLFDGTNI-YDKRVDPV 90
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVE--PT---SGEILVDGQDVtALRGRALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 91 EVRRRIGMVFQQPNPFPK-SIYENIAFG--ARINGFTGdMDELVESSLRKAALwdEC------KDKLNDSGYSLSGGQQQ 161
Cdd:COG3638 77 RLRRRIGMIFQQFNLVPRlSVLTNVLAGrlGRTSTWRS-LLGLFPPEDRERAL--EAlervglADKAYQRADQLSGGQQQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123755092 162 RLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHNMQQALRVSD 221
Cdd:COG3638 154 RVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIarEDGITVVVNLHQVDLARRYAD 215
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
13-214 |
1.37e-44 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 149.82 E-value: 1.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGT-FEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRmnDLIPNcslKGTVLFDGTNIydKRVDPVE 91
Cdd:COG2884 1 MIRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYG--EERPT---SGQVLVNGQDL--SRLKRRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 92 V---RRRIGMVFQQ----PNpfpKSIYENIAFGARINGFT-GDMDELVESSLRKAALwdecKDKLNDSGYSLSGGQQQRL 163
Cdd:COG2884 74 IpylRRRIGVVFQDfrllPD---RTVYENVALPLRVTGKSrKEIRRRVREVLDLVGL----SDKAKALPHELSGGEQQRV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 123755092 164 CIARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL-KMNYTIIIVTHNMQ 214
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLE 198
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
13-219 |
3.16e-44 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 149.47 E-value: 3.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDLIpncslKGTVLFDGTNIYDKRVDPVEV 92
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEIT-----SGDLIVDGLKVNDPKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 93 RRRIGMVFQQPNPFPK-SIYENIAFGA-RINGFT-GDMDELVESSLRKAALwdecKDKLNDSGYSLSGGQQQRLCIARTI 169
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHlTALENVMFGPlRVRGASkEEAEKQARELLAKVGL----AERAHHYPSELSGGQQQRVAIARAL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 123755092 170 AIEPEIILMDEPCSALDP---ISTLKIEETMHELKMnyTIIIVTHNMQQALRV 219
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDPelrHEVLKVMQDLAEEGM--TMVIVTHEIGFAEKV 202
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-211 |
1.02e-43 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 155.71 E-value: 1.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISY-GTFEAVRNVfcNF--KKGNITSLIGPSGCGKSTVLRSLNRMNDliPNcslKGTVLFDGTNIydKRVDPV 90
Cdd:COG1132 340 IEFENVSFSYpGDRPVLKDI--SLtiPPGETVALVGPSGSGKSTLVNLLLRFYD--PT---SGRILIDGVDI--RDLTLE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 91 EVRRRIGMVFQQPNPFPKSIYENIAFGAriNGFTgdmDELVESSLRKAALWD---ECKDKLN----DSGYSLSGGQQQRL 163
Cdd:COG1132 411 SLRRQIGVVPQDTFLFSGTIRENIRYGR--PDAT---DEEVEEAAKAAQAHEfieALPDGYDtvvgERGVNLSGGQRQRI 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 123755092 164 CIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTH 211
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAH 533
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
13-221 |
2.12e-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: 147.44 E-value: 2.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGT-FEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDliPNcslKGTVLFDGTNIYD-KRVDPV 90
Cdd:TIGR02315 1 MLEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVE--PS---SGSILLEGTDITKlRGKKLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 91 EVRRRIGMVFQQPNPFP-KSIYENIAFG--ARINGFTGDMDELVESSLRKAAlwdECKDKLNDSGYS------LSGGQQQ 161
Cdd:TIGR02315 76 KLRRRIGMIFQHYNLIErLTVLENVLHGrlGYKPTWRSLLGRFSEEDKERAL---SALERVGLADKAyqradqLSGGQQQ 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123755092 162 RLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHNMQQALRVSD 221
Cdd:TIGR02315 153 RVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRInkEDGITVIINLHQVDLAKKYAD 214
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
15-227 |
3.20e-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: 144.31 E-value: 3.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 15 SLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNCslkGTVLFDGTNIydKRVDPVEVRR 94
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGL--LKPTS---GEILIDGKDI--AKLPLEELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 95 RIGMVFQqpnpfpksiyeniafgaringftgdmdelvesslrkaalwdeckdklndsgysLSGGQQQRLCIARTIAIEPE 174
Cdd:cd00267 74 RIGYVPQ-----------------------------------------------------LSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 123755092 175 IILMDEPCSALDPISTLKIEETMHEL-KMNYTIIIVTHNMQQALRVSDMTAFFN 227
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAELAADRVIVLK 154
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
13-265 |
5.54e-43 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 149.07 E-value: 5.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISY----GTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRmndlipncsL----KGTVLFDGTNI-- 82
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL---------LerptSGSVLVDGVDLta 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 83 YDKRvDPVEVRRRIGMVFQQPNPFP-KSIYENIAFGARINGFTG-DMDELVESSLRKAALwdecKDKLNDsgY--SLSGG 158
Cdd:COG1135 72 LSER-ELRAARRKIGMIFQHFNLLSsRTVAENVALPLEIAGVPKaEIRKRVAELLELVGL----SDKADA--YpsQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 159 QQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHNMQ--QAL--RVSDMtaffnaveye 232
Cdd:COG1135 145 QKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDInrELGLTIVLITHEMDvvRRIcdRVAVL---------- 214
|
250 260 270
....*....|....*....|....*....|...
gi 123755092 233 dgDGGKVgylAEFNSTKKIFNSPKEKTTQEYIS 265
Cdd:COG1135 215 --ENGRI---VEQGPVLDVFANPQSELTRRFLP 242
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
14-256 |
3.60e-42 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 147.22 E-value: 3.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRslnrmndLI-----PNcslKGTVLFDGTNIYdkrVD 88
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLR-------IIagletPD---SGRIVLNGRDLF---TN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 89 pVEVR-RRIGMVFQQPNPFPK-SIYENIAFGARING-FTGDMDELVESSLRKAALwdeckdklndSGYS------LSGGQ 159
Cdd:COG1118 70 -LPPReRRVGFVFQHYALFPHmTVAENIAFGLRVRPpSKAEIRARVEELLELVQL----------EGLAdrypsqLSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 160 QQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHNMQQALRVSD----Mtaffnaveyed 233
Cdd:COG1118 139 RQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLhdELGGTTVFVTHDQEEALELADrvvvM----------- 207
|
250 260
....*....|....*....|...
gi 123755092 234 gDGGKVgylAEFNSTKKIFNSPK 256
Cdd:COG1118 208 -NQGRI---EQVGTPDEVYDRPA 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
14-221 |
1.36e-41 |
|
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: 140.61 E-value: 1.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLnrMNDLIPNcslKGTVLFDGTNIYDkrvDPVEVR 93
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKII--LGLLKPD---SGEIKVLGKDIKK---EPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 94 RRIGMVFQQPNPFPK-SIYENIafgaringftgdmdelvesslrkaalwdeckdklndsgySLSGGQQQRLCIARTIAIE 172
Cdd:cd03230 73 RRIGYLPEEPSLYENlTVRENL---------------------------------------KLSGGMKQRLALAQALLHD 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 123755092 173 PEIILMDEPCSALDPISTLKIEETMHEL-KMNYTIIIVTHNMQQALRVSD 221
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRELkKEGKTILLSSHILEEAERLCD 163
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
13-256 |
3.22e-41 |
|
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: 141.56 E-value: 3.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGT----FEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDliPNcslKGTVLFDGTNIYD-KRV 87
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLER--PT---SGSVLVDGTDLTLlSGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 88 DPVEVRRRIGMVFQQPNPF-PKSIYENIAFGARINGFtgDMDELVESSLRKAALWDeCKDKLNDSGYSLSGGQQQRLCIA 166
Cdd:cd03258 76 ELRKARRRIGMIFQHFNLLsSRTVFENVALPLEIAGV--PKAEIEERVLELLELVG-LEDKADAYPAQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 167 RTIAIEPEIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHNMQQALRVSDMTAFFnaveyedgDGGKVgylAE 244
Cdd:cd03258 153 RALANNPKVLLCDEATSALDPETTQSILALLRDInrELGLTIVLITHEMEVVKRICDRVAVM--------EKGEV---VE 221
|
250
....*....|..
gi 123755092 245 FNSTKKIFNSPK 256
Cdd:cd03258 222 EGTVEEVFANPQ 233
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
14-219 |
4.26e-41 |
|
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: 148.37 E-value: 4.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISY-GTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDlipncSLKGTVLFDGTNIYDkrVDPVEV 92
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP-----PYSGSILINGVDLSD--LDPASW 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 93 RRRIGMVFQQPNPFPKSIYENIAFGARinGFTgdmDELVESSLRKAALWDECKD-------KLNDSGYSLSGGQQQRLCI 165
Cdd:COG4988 410 RRQIAWVPQNPYLFAGTIRENLRLGRP--DAS---DEELEAALEAAGLDEFVAAlpdgldtPLGEGGRGLSGGQAQRLAL 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 123755092 166 ARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTH---NMQQALRV 219
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHrlaLLAQADRI 541
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
24-266 |
8.77e-41 |
|
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: 144.22 E-value: 8.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 24 GTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRmndLIPNCSlkGTVLFDGTNIYDkrVDPVEV----RRRIGMV 99
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNR---LIEPTA--GQIFIDGENIMK--QSPVELrevrRKKIGMV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 100 FQQPNPFP-KSIYENIAFGARINGFtgDMDELVESSLRKAALWD--ECKDKLNDSgysLSGGQQQRLCIARTIAIEPEII 176
Cdd:TIGR01186 77 FQQFALFPhMTILQNTSLGPELLGW--PEQERKEKALELLKLVGleEYEHRYPDE---LSGGMQQRVGLARALAAEPDIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 177 LMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHNMQQALRVSDMTAFFnaveyedgdggKVGYLAEFNSTKKIFNS 254
Cdd:TIGR01186 152 LMDEAFSALDPLIRDSMQDELKKLqaTLQKTIVFITHDLDEAIRIGDRIVIM-----------KAGEIVQVGTPDEILRN 220
|
250
....*....|..
gi 123755092 255 PKEKTTQEYISG 266
Cdd:TIGR01186 221 PANEYVEEFIGK 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
14-221 |
1.38e-40 |
|
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: 139.88 E-value: 1.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNcslKGTVLFDGTNIYDKRVDPVeVR 93
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGF--LRPT---SGSVLFDGEDITGLPPHEI-AR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 94 RRIGMVFQQPNPFPK-SIYENIAFGARI---NGFTGDMDELVESSLRKAALW--DECK--DKLNDSGYSLSGGQQQRLCI 165
Cdd:cd03219 75 LGIGRTFQIPRLFPElTVLENVMVAAQArtgSGLLLARARREEREARERAEEllERVGlaDLADRPAGELSYGQQRRLEI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 123755092 166 ARTIAIEPEIILMDEPCSALDPISTLKIEETMHELK-MNYTIIIVTHNMQQALRVSD 221
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLNPEETEELAELIRELReRGITVLLVEHDMDVVMSLAD 211
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
14-228 |
4.26e-40 |
|
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: 138.16 E-value: 4.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDLIpncslKGTVLFDGTNIYDkrVDPVEvr 93
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPT-----SGRIYIGGRDVTD--LPPKD-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 94 RRIGMVFQQPNPFP-KSIYENIAFGARINGFTGD-MDELVESSLRKAALwDECKDKLNDSgysLSGGQQQRLCIARTIAI 171
Cdd:cd03301 72 RDIAMVFQNYALYPhMTVYDNIAFGLKLRKVPKDeIDERVREVAELLQI-EHLLDRKPKQ---LSGGQRQRVALGRAIVR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123755092 172 EPEIILMDEPCSALDPistlKIEETMH-ELK-----MNYTIIIVTHNMQQALRVSDMTAFFNA 228
Cdd:cd03301 148 EPKVFLMDEPLSNLDA----KLRVQMRaELKrlqqrLGTTTIYVTHDQVEAMTMADRIAVMND 206
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
14-217 |
4.65e-40 |
|
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: 139.49 E-value: 4.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISY--GTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNcslKGTVLFDGTNIYD-KRVDpv 90
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGL--LLPT---SGKVTVDGLDTLDeENLW-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 91 EVRRRIGMVFQQP-NPFPKSIYEN-IAFGARINGF-TGDMDELVESSLRKAALWDeckdKLNDSGYSLSGGQQQRLCIAR 167
Cdd:TIGR04520 74 EIRKKVGMVFQNPdNQFVGATVEDdVAFGLENLGVpREEMRKRVDEALKLVGMED----FRDREPHLLSGGQKQRVAIAG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 123755092 168 TIAIEPEIILMDEPCSALDPISTLKIEETMHELK--MNYTIIIVTHNMQQAL 217
Cdd:TIGR04520 150 VLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAV 201
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-211 |
8.92e-40 |
|
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: 138.06 E-value: 8.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 16 LENVSISYGT---FEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDLIpncslKGTVLFDGTNIydKRVDPVEV 92
Cdd:cd03249 3 FKNVSFRYPSrpdVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPT-----SGEILLDGVDI--RDLNLRWL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 93 RRRIGMVFQQPNPFPKSIYENIAFGARingftGDMDELVESSLRKAALWD---ECKDKLN----DSGYSLSGGQQQRLCI 165
Cdd:cd03249 76 RSQIGLVSQEPVLFDGTIAENIRYGKP-----DATDEEVEEAAKKANIHDfimSLPDGYDtlvgERGSQLSGGQKQRIAI 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 123755092 166 ARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTH 211
Cdd:cd03249 151 ARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAH 196
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
35-183 |
1.31e-39 |
|
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: 134.70 E-value: 1.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 35 NFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPncsLKGTVLFDGTNIYDKRVDPVevRRRIGMVFQQPNPFP-KSIYEN 113
Cdd:pfam00005 7 TLNPGEILALVGPNGAGKSTLLKLIAGL--LSP---TEGTILLDGQDLTDDERKSL--RKEIGYVFQDPQLFPrLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123755092 114 IAFGARINGFTGD-MDELVESSLRKAALWDECKDKLNDSGYSLSGGQQQRLCIARTIAIEPEIILMDEPCS 183
Cdd:pfam00005 80 LRLGLLLKGLSKReKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
24-225 |
2.37e-39 |
|
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: 137.77 E-value: 2.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 24 GTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRmndLIPNCSlkGTVLFDGTNIYD-KRVDPVEVRR-RIGMVFQ 101
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINR---LIEPTS--GKVLIDGQDIAAmSRKELRELRRkKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 102 QPNPFP-KSIYENIAFGARINGftgdMDElvESSLRKAAlwdECKDKLNDSGYS------LSGGQQQRLCIARTIAIEPE 174
Cdd:cd03294 110 SFALLPhRTVLENVAFGLEVQG----VPR--AEREERAA---EALELVGLEGWEhkypdeLSGGMQQRVGLARALAVDPD 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 123755092 175 IILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHNMQQALRVSDMTAF 225
Cdd:cd03294 181 ILLMDEAFSALDPLIRREMQDELLRLqaELQKTIVFITHDLDEALRLGDRIAI 233
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
14-221 |
5.66e-39 |
|
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: 135.64 E-value: 5.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVfcNF--KKGNITSLIGPSGCGKSTVLRSLnrMNdLIPNCSlkGTVLFDGTNIydKRVDPVE 91
Cdd:cd03224 1 LEVENLNAGYGKSQILFGV--SLtvPEGEIVALLGRNGAGKTTLLKTI--MG-LLPPRS--GSIRFDGRDI--TGLPPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 92 -VRRRIGMVFQQPNPFPK-SIYENIAFGARI---NGFTGDMDELVEsslrkaaLWDECKDKLNDSGYSLSGGQQQRLCIA 166
Cdd:cd03224 72 rARAGIGYVPEGRRIFPElTVEENLLLGAYArrrAKRKARLERVYE-------LFPRLKERRKQLAGTLSGGEQQMLAIA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 123755092 167 RTIAIEPEIILMDEPCSALDPISTLKIEETMHELK-MNYTIIIVTHNMQQALRVSD 221
Cdd:cd03224 145 RALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRdEGVTILLVEQNARFALEIAD 200
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
9-227 |
1.56e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 134.83 E-value: 1.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 9 PKNIILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSlnrMNDLIPNcsLKGTVLFDGTniydkrvD 88
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKA---ILGLLPP--TSGTVRLFGK-------P 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 89 PVEVRRRIGMVFQQPN---PFPKSIYENIAFGAR-----INGFTGDMDELVESSLRKAALWDECKDKLNDsgysLSGGQQ 160
Cdd:COG1121 70 PRRARRRIGYVPQRAEvdwDFPITVRDVVLMGRYgrrglFRRPSRADREAVDEALERVGLEDLADRPIGE----LSGGQQ 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 123755092 161 QRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL-KMNYTIIIVTHNMQQALRVSDMTAFFN 227
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREYFDRVLLLN 213
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
13-256 |
2.44e-38 |
|
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: 136.34 E-value: 2.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISY----GTFEAVRNVfcNF--KKGNITSLIGPSGCGKSTVLRSLnrMNDLIPNCSLKGTVLFDGTNIYdkR 86
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGV--SFdvRRGETLGLVGESGSGKSTLARAI--LGLLPPPGITSGEILFDGEDLL--K 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 87 VDPVEVR----RRIGMVFQQP----NPFpKSIYENIAFGARINGftgdmdelvesSLRKAALWDECKDKLNDSG------ 152
Cdd:COG0444 75 LSEKELRkirgREIQMIFQDPmtslNPV-MTVGDQIAEPLRIHG-----------GLSKAEARERAIELLERVGlpdper 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 153 ----YS--LSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELK--MNYTIIIVTHNMQQALRVSDMTa 224
Cdd:COG0444 143 rldrYPheLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQreLGLAILFITHDLGVVAEIADRV- 221
|
250 260 270
....*....|....*....|....*....|..
gi 123755092 225 ffnAVEYedgdGGKVgylAEFNSTKKIFNSPK 256
Cdd:COG0444 222 ---AVMY----AGRI---VEEGPVEELFENPR 243
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
15-227 |
2.69e-38 |
|
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: 133.43 E-value: 2.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 15 SLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNrmnDLIPNCSlkGTVLFDGtniydkrVDPVEVRR 94
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAIL---GLLKPTS--GSIRVFG-------KPLEKERK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 95 RIGMVFQQPN---PFPKSIYENIAFG--ARINGF---TGDMDELVESSLRK---AALWDECKDklndsgySLSGGQQQRL 163
Cdd:cd03235 69 RIGYVPQRRSidrDFPISVRDVVLMGlyGHKGLFrrlSKADKAKVDEALERvglSELADRQIG-------ELSGGQQQRV 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 123755092 164 CIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELK-MNYTIIIVTHNMQQALRVSDMTAFFN 227
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRrEGMTILVVTHDLGLVLEYFDRVLLLN 206
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
12-221 |
7.97e-38 |
|
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: 133.63 E-value: 7.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 12 IILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNcslKGTVLFDGTNIydKRVDPVE 91
Cdd:COG0411 3 PLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGF--YRPT---SGRILFDGRDI--TGLPPHR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 92 VRRRiGMV--FQQPNPFPK-SIYENIAFGARIN---GFTGDMDELVESSLRKAALWDEC---------KDKLNDSGYSLS 156
Cdd:COG0411 76 IARL-GIArtFQNPRLFPElTVLENVLVAAHARlgrGLLAALLRLPRARREEREARERAeellervglADRADEPAGNLS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 123755092 157 GGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELK--MNYTIIIVTHNMQQALRVSD 221
Cdd:COG0411 155 YGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRdeRGITILLIEHDMDLVMGLAD 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
15-221 |
8.48e-38 |
|
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: 131.02 E-value: 8.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 15 SLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRmndLIPncSLKGTVLFDGTNIydKRVDPVEVRR 94
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAG---LLK--PSSGEILLDGKDL--ASLSPKELAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 95 RIGMVFQqpnpfpksIYENIafgaringftgDMDELVESSLRkaalwdeckdklndsgySLSGGQQQRLCIARTIAIEPE 174
Cdd:cd03214 74 KIAYVPQ--------ALELL-----------GLAHLADRPFN-----------------ELSGGERQRVLLARALAQEPP 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 123755092 175 IILMDEPCSALDPISTLKIEETMHELK--MNYTIIIVTHNMQQALRVSD 221
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLELLRRLAreRGKTVVMVLHDLNLAARYAD 166
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
17-221 |
1.02e-37 |
|
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: 132.85 E-value: 1.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 17 ENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDliPNcslKGTVLFDGtniydKRVDPVEVRRR- 95
Cdd:cd03296 6 RNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLER--PD---SGTILFGG-----EDATDVPVQERn 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 96 IGMVFQQPNPFPK-SIYENIAFGARINGFTG-----DMDELVESSLRKAALwdeckDKLNDSgY--SLSGGQQQRLCIAR 167
Cdd:cd03296 76 VGFVFQHYALFRHmTVFDNVAFGLRVKPRSErppeaEIRAKVHELLKLVQL-----DWLADR-YpaQLSGGQRQRVALAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123755092 168 TIAIEPEIILMDEPCSALDPistlKIEETM-------HElKMNYTIIIVTHNMQQALRVSD 221
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALDA----KVRKELrrwlrrlHD-ELHVTTVFVTHDQEEALEVAD 205
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
28-221 |
1.76e-37 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 136.00 E-value: 1.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 28 AVRNVfcNF--KKGNITSLIGPSGCGKSTVLRSLNRmndLIPNCSlkGTVLFDGTNIYdkRVDP---VEVRR-RIGMVFQ 101
Cdd:COG4175 42 GVNDA--SFdvEEGEIFVIMGLSGSGKSTLVRCLNR---LIEPTA--GEVLIDGEDIT--KLSKkelRELRRkKMSMVFQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 102 Q----PNpfpKSIYENIAFGARINGftgdMDElvESSLRKAALW------DECKDKLNDSgysLSGGQQQRLCIARTIAI 171
Cdd:COG4175 113 HfallPH---RTVLENVAFGLEIQG----VPK--AERRERAREAlelvglAGWEDSYPDE---LSGGMQQRVGLARALAT 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 123755092 172 EPEIILMDEPCSALDPIstlkIEETMH-EL-----KMNYTIIIVTHNMQQALRVSD 221
Cdd:COG4175 181 DPDILLMDEAFSALDPL----IRREMQdELlelqaKLKKTIVFITHDLDEALRLGD 232
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
17-224 |
3.45e-37 |
|
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: 130.95 E-value: 3.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 17 ENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNrmnDLIPNCSLKGTVlfdgtNIYDKRVDPVEVRRRI 96
Cdd:cd03265 4 ENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLT---TLLKPTSGRATV-----AGHDVVREPREVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 97 GMVFQQPNPFPK-SIYENIAFGARINGFTGD-MDELVESSLRKAALWdECKDKLNDSgysLSGGQQQRLCIARTIAIEPE 174
Cdd:cd03265 76 GIVFQDLSVDDElTGWENLYIHARLYGVPGAeRRERIDELLDFVGLL-EAADRLVKT---YSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 123755092 175 IILMDEPCSALDPISTLKIEETMHELK--MNYTIIIVTHNMQQALRVSDMTA 224
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKeeFGMTILLTTHYMEEAEQLCDRVA 203
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-213 |
2.42e-36 |
|
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: 129.27 E-value: 2.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGT-FEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDlipncSLKGTVLFDGTNIydKRVDPVEV 92
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYD-----VSSGSILIDGQDI--REVTLDSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 93 RRRIGMVFQQPNPFPKSIYENIAFGaRINGftgdMDELVESSLRKAALWDECKdKLNDsGYS---------LSGGQQQRL 163
Cdd:cd03253 74 RRAIGVVPQDTVLFNDTIGYNIRYG-RPDA----TDEEVIEAAKAAQIHDKIM-RFPD-GYDtivgerglkLSGGEKQRV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 123755092 164 CIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTHNM 213
Cdd:cd03253 147 AIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRL 196
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
16-221 |
1.14e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 128.63 E-value: 1.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 16 LENVSISY--GT-FE--AVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNcslKGTVLFDGTNIYDKRVDPV 90
Cdd:PRK13637 5 IENLTHIYmeGTpFEkkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGL--LKPT---SGKIIIDGVDITDKKVKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 91 EVRRRIGMVFQQP--NPFPKSIYENIAFGARINGFT-GDMDELVESSLRKAAL-WDECKDKlndSGYSLSGGQQQRLCIA 166
Cdd:PRK13637 80 DIRKKVGLVFQYPeyQLFEETIEKDIAFGPINLGLSeEEIENRVKRAMNIVGLdYEDYKDK---SPFELSGGQKRRVAIA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 123755092 167 RTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNY--TIIIVTHNMQQALRVSD 221
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKLAD 213
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
16-213 |
2.31e-35 |
|
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: 126.16 E-value: 2.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 16 LENVSISYGTFE--AVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNcslKGTVLFDGTNIydKRVDPVEVR 93
Cdd:cd03245 5 FRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGL--YKPT---SGSVLLDGTDI--RQLDPADLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 94 RRIGMVFQQPNPFPKSIYENIAFGARIngftGDmDELVESSLRKAALWDECKD-------KLNDSGYSLSGGQQQRLCIA 166
Cdd:cd03245 78 RNIGYVPQDVTLFYGTLRDNITLGAPL----AD-DERILRAAELAGVTDFVNKhpngldlQIGERGRGLSGGQRQAVALA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 123755092 167 RTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTHNM 213
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRP 199
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
16-265 |
3.26e-35 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 128.77 E-value: 3.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 16 LENVSISY----GTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDliPNcslKGTVLFDGTNI--YDKRvDP 89
Cdd:PRK11153 4 LKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLER--PT---SGRVLVDGQDLtaLSEK-EL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 90 VEVRRRIGMVFQQPNPFP-KSIYENIAFGARINGFT-GDMDELVESSLRKAALWDEcKDKlndsgY--SLSGGQQQRLCI 165
Cdd:PRK11153 78 RKARRQIGMIFQHFNLLSsRTVFDNVALPLELAGTPkAEIKARVTELLELVGLSDK-ADR-----YpaQLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 166 ARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHNMQQALRVSDMTAFFnaveyedgDGGKVgylA 243
Cdd:PRK11153 152 ARALASNPKVLLCDEATSALDPATTRSILELLKDInrELGLTIVLITHEMDVVKRICDRVAVI--------DAGRL---V 220
|
250 260
....*....|....*....|..
gi 123755092 244 EFNSTKKIFNSPKEKTTQEYIS 265
Cdd:PRK11153 221 EQGTVSEVFSHPKHPLTREFIQ 242
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
38-221 |
3.86e-35 |
|
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: 125.49 E-value: 3.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 38 KGNITSLIGPSGCGKSTVLRSLNRMNDLIpncslKGTVLFDGTNIYDKRVD---PVEvRRRIGMVFQQPNPFPK-SIYEN 113
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPD-----GGTIVLNGTVLFDSRKKinlPPQ-QRKIGLVFQQYALFPHlNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 114 IAFGARINGFTGDMDeLVESSLRKAALwdeckDKLNDSG-YSLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLK 192
Cdd:cd03297 96 LAFGLKRKRNREDRI-SVDELLDLLGL-----DHLLNRYpAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190
....*....|....*....|....*....|.
gi 123755092 193 IEETMHELKMNYTI--IIVTHNMQQALRVSD 221
Cdd:cd03297 170 LLPELKQIKKNLNIpvIFVTHDLSEAEYLAD 200
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
14-228 |
4.49e-35 |
|
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: 125.31 E-value: 4.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFE--AVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLnrMNDLIPNCslkGTVLFDGtniYDKRVDPVE 91
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKML--TGELRPTS---GTAYING---YSIRTDRKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 92 VRRRIGMVFQQPNPFPK-SIYENIAFGARINGFT-GDMDELVESSLRKAALwdecKDKLNDSGYSLSGGQQQRLCIARTI 169
Cdd:cd03263 73 ARQSLGYCPQFDALFDElTVREHLRFYARLKGLPkSEIKEEVELLLRVLGL----TDKANKRARTLSGGMKRKLSLAIAL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 123755092 170 AIEPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTHNMQQALRVSDMTAFFNA 228
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSD 207
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
9-211 |
4.72e-35 |
|
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: 131.81 E-value: 4.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 9 PKNIILSLENVSISY--GTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNcslKGTVLFDGTNIYDkr 86
Cdd:COG4987 329 PGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRF--LDPQ---SGSITLGGVDLRD-- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 87 VDPVEVRRRIGMVFQQPNPFPKSIYENIAFGARingfTGDMDELVESsLRKAALWD---ECKDKLN----DSGYSLSGGQ 159
Cdd:COG4987 402 LDEDDLRRRIAVVPQRPHLFDTTLRENLRLARP----DATDEELWAA-LERVGLGDwlaALPDGLDtwlgEGGRRLSGGE 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 123755092 160 QQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTH 211
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITH 528
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
14-268 |
7.74e-35 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 125.68 E-value: 7.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNdlIPNcslKGTVLFDGTNIYDKR------- 86
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLE--TPD---SGEIRVGGEEIRLKPdrdgelv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 87 -VDPVEVRR---RIGMVFQQPNPFP-KSIYENIAFG-ARINGFtgDMDELVESS---LRKAALWDEcKDKlndsgY--SL 155
Cdd:COG4598 84 pADRRQLQRirtRLGMVFQSFNLWShMTVLENVIEApVHVLGR--PKAEAIERAealLAKVGLADK-RDA-----YpaHL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 156 SGGQQQRLCIARTIAIEPEIILMDEPCSALDP---------ISTLKiEE--TMhelkmnytiIIVTHNMQQALRVSDMTA 224
Cdd:COG4598 156 SGGQQQRAAIARALAMEPEVMLFDEPTSALDPelvgevlkvMRDLA-EEgrTM---------LVVTHEMGFARDVSSHVV 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 123755092 225 FFNAveyedgdggkvGYLAEFNSTKKIFNSPKEKTTQEYISGKF 268
Cdd:COG4598 226 FLHQ-----------GRIEEQGPPAEVFGNPKSERLRQFLSSSL 258
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
14-211 |
8.40e-35 |
|
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: 125.04 E-value: 8.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYG--TFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDLIpncslKGTVLFDGTNIYDkrVDPVE 91
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVD-----SGRILIDGHDVRD--YTLAS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 92 VRRRIGMVFQQPNPFPKSIYENIAFGARingftGDMDELVESSLRKAALWDECKD-------KLNDSGYSLSGGQQQRLC 164
Cdd:cd03251 74 LRRQIGLVSQDVFLFNDTVAENIAYGRP-----GATREEVEEAARAANAHEFIMElpegydtVIGERGVKLSGGQRQRIA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 123755092 165 IARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTH 211
Cdd:cd03251 149 IARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAH 195
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-227 |
9.79e-35 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 128.14 E-value: 9.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 1 MIKTNKKTPkniILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRslnrmndLI-----PNcslKGTV 75
Cdd:PRK09452 5 NKQPSSLSP---LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLR-------LIagfetPD---SGRI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 76 LFDGTNIYDKrvdPVEvRRRIGMVFQQPNPFPK-SIYENIAFGARINGF-TGDMDELVESSLRKAALWDECKDKLNDsgy 153
Cdd:PRK09452 72 MLDGQDITHV---PAE-NRHVNTVFQSYALFPHmTVFENVAFGLRMQKTpAAEITPRVMEALRMVQLEEFAQRKPHQ--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 154 sLSGGQQQRLCIARTIAIEPEIILMDEPCSALDpistLKIEETM-HELKM-----NYTIIIVTHNMQQALRVSDMTAFFN 227
Cdd:PRK09452 145 -LSGGQQQRVAIARAVVNKPKVLLLDESLSALD----YKLRKQMqNELKAlqrklGITFVFVTHDQEEALTMSDRIVVMR 219
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
13-220 |
1.11e-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: 124.28 E-value: 1.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGT-FEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNcslKGTVLFDGTNI--YDKRVDP 89
Cdd:TIGR02673 1 MIEFHNVSKAYPGgVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGA--LTPS---RGQVRIAGEDVnrLRGRQLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 90 VeVRRRIGMVFQQPNPFP-KSIYENIAFGARINGFTG-DMDELVESSLRKAALwdecKDKLNDSGYSLSGGQQQRLCIAR 167
Cdd:TIGR02673 76 L-LRRRIGVVFQDFRLLPdRTVYENVALPLEVRGKKErEIQRRVGAALRQVGL----EHKADAFPEQLSGGEQQRVAIAR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 123755092 168 TIAIEPEIILMDEPCSALDPISTLKIEETMHEL-KMNYTIIIVTHNMQQALRVS 220
Cdd:TIGR02673 151 AIVNSPPLLLADEPTGNLDPDLSERILDLLKRLnKRGTTVIVATHDLSLVDRVA 204
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
13-221 |
2.10e-34 |
|
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: 123.94 E-value: 2.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGTFEAVRNVfcNF--KKGNITSLIGPSGCGKSTVLRSLnrMNdLIPNCSlkGTVLFDGTNIydKRVDPV 90
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGV--SLevEEGEIVALLGRNGAGKTTLLKAI--SG-LLPPRS--GSIRFDGEDI--TGLPPH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 91 E-VRRRIGMVFQQPNPFPK-SIYENIAFGARINGFTGDMDELVESSLrkaALWDECKDKLNDSGYSLSGGQQQRLCIART 168
Cdd:COG0410 74 RiARLGIGYVPEGRRIFPSlTVEENLLLGAYARRDRAEVRADLERVY---ELFPRLKERRRQRAGTLSGGEQQMLAIGRA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 123755092 169 IAIEPEIILMDEPCSALDPISTLKIEETMHELK-MNYTIIIVTHNMQQALRVSD 221
Cdd:COG0410 151 LMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNrEGVTILLVEQNARFALEIAD 204
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
44-264 |
5.67e-34 |
|
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: 125.30 E-value: 5.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 44 LIGPSGCGKSTVLRSLNRMNDLIpncslKGTVLFDGTNIYDKrvdPVEvRRRIGMVFQQPNPFPK-SIYENIAFGARING 122
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPD-----SGSIMLDGEDVTNV---PPH-LRHINMVFQSYALFPHmTVEENVAFGLKMRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 123 F-TGDMDELVESSLRKAALWDECKDKLNDsgysLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPistlKIEETM-HEL 200
Cdd:TIGR01187 72 VpRAEIKPRVLEALRLVQLEEFADRKPHQ----LSGGQQQRVALARALVFKPKILLLDEPLSALDK----KLRDQMqLEL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 123755092 201 KM-----NYTIIIVTHNMQQALRVSDMTAFFNaveyedgdGGKvgyLAEFNSTKKIFNSPKEKTTQEYI 264
Cdd:TIGR01187 144 KTiqeqlGITFVFVTHDQEEAMTMSDRIAIMR--------KGK---IAQIGTPEEIYEEPANLFVARFI 201
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
14-187 |
8.19e-34 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 121.82 E-value: 8.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNrmNDLIPNCSLKGTVLFDGTNIYDKrvdPVEvR 93
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIA--GTLSPAFSASGEVLLNGRRLTAL---PAE-Q 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 94 RRIGMVFQQPNPFPK-SIYENIAFG--ARINGftGDMDELVESSLRKAALwdeckdklndSGY------SLSGGQQQRLC 164
Cdd:COG4136 76 RRIGILFQDDLLFPHlSVGENLAFAlpPTIGR--AQRRARVEQALEEAGL----------AGFadrdpaTLSGGQRARVA 143
|
170 180
....*....|....*....|...
gi 123755092 165 IARTIAIEPEIILMDEPCSALDP 187
Cdd:COG4136 144 LLRALLAEPRALLLDEPFSKLDA 166
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
14-265 |
1.37e-33 |
|
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: 122.06 E-value: 1.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEaVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLnrMNDLIPNcslKGTVLFDGTNIYDKrvdPVEvR 93
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETI--AGFIKPD---SGKILLNGKDITNL---PPE-K 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 94 RRIGMVFQQPNPFP-KSIYENIAFGARINGFtgdMDELVESSLRKAALWDECKDKLNDSGYSLSGGQQQRLCIARTIAIE 172
Cdd:cd03299 71 RDISYVPQNYALFPhMTVYKNIAYGLKKRKV---DKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 173 PEIILMDEPCSALDPISTLKIEETMHELKMNY--TIIIVTHNMQQALRVSDMTAFFNaveyedgdGGKvgyLAEFNSTKK 250
Cdd:cd03299 148 PKILLLDEPFSALDVRTKEKLREELKKIRKEFgvTVLHVTHDFEEAWALADKVAIML--------NGK---LIQVGKPEE 216
|
250
....*....|....*
gi 123755092 251 IFNSPKEKTTQEYIS 265
Cdd:cd03299 217 VFKKPKNEFVAEFLG 231
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
14-265 |
1.45e-33 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 122.04 E-value: 1.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNdlIPNcslKGTVL-----FD-GTNIYDKRV 87
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLE--TPD---SGQLNiaghqFDfSQKPSEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 88 dpVEVRRRIGMVFQQPNPFPKsiyeniafgaringFTGdMDELVESSLR-----KAALWDECK---------DKLNDSGY 153
Cdd:COG4161 78 --RLLRQKVGMVFQQYNLWPH--------------LTV-MENLIEAPCKvlglsKEQAREKAMkllarlrltDKADRFPL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 154 SLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELK-MNYTIIIVTHNMQQALRVSDMTAFFnaveyE 232
Cdd:COG4161 141 HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSqTGITQVIVTHEVEFARKVASQVVYM-----E 215
|
250 260 270
....*....|....*....|....*....|...
gi 123755092 233 DgdggkvGYLAEFnSTKKIFNSPKEKTTQEYIS 265
Cdd:COG4161 216 K------GRIIEQ-GDASHFTQPQTEAFAHYLS 241
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
14-211 |
1.57e-33 |
|
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: 127.40 E-value: 1.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISY-GTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRmndLIPNCSlkGTVLFDGTNIYDkrVDPVEV 92
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLG---FVDPTE--GSIAVNGVPLAD--ADADSW 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 93 RRRIGMVFQQPNPFPKSIYENIAFGARingftGDMDELVESSLRKAALWDECKD-------KLNDSGYSLSGGQQQRLCI 165
Cdd:TIGR02857 395 RDQIAWVPQHPFLFAGTIAENIRLARP-----DASDAEIREALERAGLDEFVAAlpqgldtPIGEGGAGLSGGQAQRLAL 469
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 123755092 166 ARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTH 211
Cdd:TIGR02857 470 ARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTH 515
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-218 |
2.56e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 122.43 E-value: 2.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGTFE--AVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNcslKGTVLFDGTNIYDKRVdpV 90
Cdd:PRK13635 5 IIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGL--LLPE---AGTITVGGMVLSEETV--W 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 91 EVRRRIGMVFQQP-NPFPKSIYEN-IAFGARINGFTGD-MDELVESSLRKAALwdecKDKLNDSGYSLSGGQQQRLCIAR 167
Cdd:PRK13635 78 DVRRQVGMVFQNPdNQFVGATVQDdVAFGLENIGVPREeMVERVDQALRQVGM----EDFLNREPHRLSGGQKQRVAIAG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 123755092 168 TIAIEPEIILMDEPCSALDPISTLKIEETMHELK--MNYTIIIVTHNMQQALR 218
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKeqKGITVLSITHDLDEAAQ 206
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
14-264 |
2.78e-33 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 121.02 E-value: 2.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNvfCNFKKGNITSLIGPSGCGKSTVLrslnrmnDLI-----PNcslKGTVLFDGTNIYDKRVD 88
Cdd:COG3840 2 LRLDDLTYRYGDFPLRFD--LTIAAGERVAILGPSGAGKSTLL-------NLIagflpPD---SGRILWNGQDLTALPPA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 89 pvevRRRIGMVFQQPNPFPK-SIYENIAFGARING-FTGDMDELVESSLRKAALwDECKDKLNDsgySLSGGQQQRLCIA 166
Cdd:COG3840 70 ----ERPVSMLFQENNLFPHlTVAQNIGLGLRPGLkLTAEQRAQVEQALERVGL-AGLLDRLPG---QLSGGQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 167 RTIAIEPEIILMDEPCSALDPIstLKIEetMHEL------KMNYTIIIVTHNMQQALRVSDMTAFfnaveyedGDGGKVg 240
Cdd:COG3840 142 RCLVRKRPILLLDEPFSALDPA--LRQE--MLDLvdelcrERGLTVLMVTHDPEDAARIADRVLL--------VADGRI- 208
|
250 260
....*....|....*....|....
gi 123755092 241 ylAEFNSTKKIFNSPKEKTTQEYI 264
Cdd:COG3840 209 --AADGPTAALLDGEPPPALAAYL 230
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
37-268 |
7.91e-33 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 120.24 E-value: 7.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 37 KKGNITSLIGPSGCGKSTVLRSLNRMNDLIPNCSLKGTVLFDGTNIYDKRVDPV-EVRRRIGMVFQQPNPFP-KSIYENI 114
Cdd:PRK11264 27 KPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLIrQLRQHVGFVFQNFNLFPhRTVLENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 115 AFGARINGFT--GDMDELVESSLRKAALwdecKDKLNDSGYSLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLK 192
Cdd:PRK11264 107 IEGPVIVKGEpkEEATARARELLAKVGL----AGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 123755092 193 IEETMHEL-KMNYTIIIVTHNMQQALRVSDMTAFFnaveyedgDGGKVgylAEFNSTKKIFNSPKEKTTQEYISgKF 268
Cdd:PRK11264 183 VLNTIRQLaQEKRTMVIVTHEMSFARDVADRAIFM--------DQGRI---VEQGPAKALFADPQQPRTRQFLE-KF 247
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
17-211 |
8.06e-33 |
|
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: 119.64 E-value: 8.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 17 ENVSISY-GTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDliPNcslKGTVLFDGTNIydKRVDPVEVRRR 95
Cdd:cd03254 6 ENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYD--PQ---KGQILIDGIDI--RDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 96 IGMVFQQPNPFPKSIYENIAFGARINgftgdMDELVESSLRKAALWDECKD-------KLNDSGYSLSGGQQQRLCIART 168
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNA-----TDEEVIEAAKEAGAHDFIMKlpngydtVLGENGGNLSQGERQLLAIARA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 123755092 169 IAIEPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTH 211
Cdd:cd03254 154 MLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAH 196
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
15-221 |
1.15e-32 |
|
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: 118.51 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 15 SLENVSISYG-TFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDlipncSLKGTVLFDGtniydKRVDPVEVR 93
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIK-----ESSGSILLNG-----KPIKAKERR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 94 RRIGMVFQQPNP--FPKSIYENIAFGARIngfTGDMDELVESSLRKAALWDEcKDKLNdsgYSLSGGQQQRLCIARTIAI 171
Cdd:cd03226 71 KSIGYVMQDVDYqlFTDSVREELLLGLKE---LDAGNEQAETVLKDLDLYAL-KERHP---LSLSGGQKQRLAIAAALLS 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 123755092 172 EPEIILMDEPCSALDPISTLKIEETMHEL-KMNYTIIIVTHNMQQALRVSD 221
Cdd:cd03226 144 GKDLLIFDEPTSGLDYKNMERVGELIRELaAQGKAVIVITHDYEFLAKVCD 194
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
14-264 |
1.17e-32 |
|
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: 122.45 E-value: 1.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDLIpncslKGTVLFDGTNIYDKrvdPVEvR 93
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQT-----AGTIYQGGRDITRL---PPQ-K 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 94 RRIGMVFQQPNPFPK-SIYENIAFG--------ARINGFTGDMDELVEsslrkaalwdeckdkLNDSG--Y--SLSGGQQ 160
Cdd:TIGR03265 76 RDYGIVFQSYALFPNlTVADNIAYGlknrgmgrAEVAERVAELLDLVG---------------LPGSErkYpgQLSGGQQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 161 QRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHNMQQALRVSDMTAFFNAVEYEdgdggK 238
Cdd:TIGR03265 141 QRVALARALATSPGLLLLDEPLSALDARVREHLRTEIRQLqrRLGVTTIMVTHDQEEALSMADRIVVMNHGVIE-----Q 215
|
250 260
....*....|....*....|....*.
gi 123755092 239 VGYLAEfnstkkIFNSPKEKTTQEYI 264
Cdd:TIGR03265 216 VGTPQE------IYRHPATPFVADFV 235
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1-212 |
2.13e-32 |
|
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: 118.28 E-value: 2.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 1 MIKTNKKTPKNIiLSLENVSISygtfeavrnvfcnFKKGNITSLIGPSGCGKSTVLRSLNRMNdlIPNcslKGTVLFDGT 80
Cdd:cd03292 3 FINVTKTYPNGT-AALDGINIS-------------ISAGEFVFLVGPSGAGKSTLLKLIYKEE--LPT---SGTIRVNGQ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 81 NI--YDKRVDPVeVRRRIGMVFQQPNPFPK-SIYENIAFGARINGFTG-DMDELVESSLRKAALwdecKDKLNDSGYSLS 156
Cdd:cd03292 64 DVsdLRGRAIPY-LRRKIGVVFQDFRLLPDrNVYENVAFALEVTGVPPrEIRKRVPAALELVGL----SHKHRALPAELS 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 123755092 157 GGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL-KMNYTIIIVTHN 212
Cdd:cd03292 139 GGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATHA 195
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
14-211 |
2.33e-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: 118.06 E-value: 2.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGnITSLIGPSGCGKSTVLRSLNrmnDLIPNCSlkGTVLFDGtniYDKRVDPVEVR 93
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILA---TLTPPSS--GTIRIDG---QDVLKQPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 94 RRIGMVFQQPNPFPK-SIYENIAFGARINGFT-GDMDELVESSLRKAALWDECKDKLNdsgySLSGGQQQRLCIARTIAI 171
Cdd:cd03264 72 RRIGYLPQEFGVYPNfTVREFLDYIAWLKGIPsKEVKARVDEVLELVNLGDRAKKKIG----SLSGGMRRRVGIAQALVG 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 123755092 172 EPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTH 211
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTH 187
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
27-216 |
6.15e-32 |
|
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: 116.37 E-value: 6.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 27 EAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNcslKGTVLFDGTNI-YDKRvDPVEVRRRIGMVFQQPNP 105
Cdd:TIGR01166 6 EVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGL--LRPQ---SGAVLIDGEPLdYSRK-GLLERRQRVGLVFQDPDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 106 --FPKSIYENIAFGARINGFTGDMdelVESSLRKAAlwdeckDKLNDSGYS------LSGGQQQRLCIARTIAIEPEIIL 177
Cdd:TIGR01166 80 qlFAADVDQDVAFGPLNLGLSEAE---VERRVREAL------TAVGASGLRerpthcLSGGEKKRVAIAGAVAMRPDVLL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 123755092 178 MDEPCSALDPISTLKIEETMHELK-MNYTIIIVTHNMQQA 216
Cdd:TIGR01166 151 LDEPTAGLDPAGREQMLAILRRLRaEGMTVVISTHDVDLA 190
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
11-221 |
1.09e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 117.91 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 11 NIILSLENVSISY--GTfEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNdlIPNcslKGTVLFDGTNIYDKRVD 88
Cdd:PRK13647 2 DNIIEVEDLHFRYkdGT-KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIY--LPQ---RGRVKVMGREVNAENEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 89 pvEVRRRIGMVFQQPNP--FPKSIYENIAFGARINGFTGD-MDELVESSLRKAALWDeCKDKlndSGYSLSGGQQQRLCI 165
Cdd:PRK13647 76 --WVRSKVGLVFQDPDDqvFSSTVWDDVAFGPVNMGLDKDeVERRVEEALKAVRMWD-FRDK---PPYHLSYGQKKRVAI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 123755092 166 ARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL-KMNYTIIIVTHNMQQALRVSD 221
Cdd:PRK13647 150 AGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDLAAEWAD 206
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
23-221 |
1.17e-31 |
|
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: 118.65 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 23 YGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNrmnDLIPNCSLKGTVLfdGtniYDKRVDPVEVRRRIGMVFQQ 102
Cdd:TIGR01188 3 YGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLT---TLLRPTSGTARVA--G---YDVVREPRKVRRSIGIVPQY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 103 PNPFPK-SIYENIAFGARINGFTGDM-DELVESSLRKAALWDECKDKLNdsgySLSGGQQQRLCIARTIAIEPEIILMDE 180
Cdd:TIGR01188 75 ASVDEDlTGRENLEMMGRLYGLPKDEaEERAEELLELFELGEAADRPVG----TYSGGMRRRLDIAASLIHQPDVLFLDE 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 123755092 181 PCSALDPISTLKIEETMHELK-MNYTIIIVTHNMQQALRVSD 221
Cdd:TIGR01188 151 PTTGLDPRTRRAIWDYIRALKeEGVTILLTTHYMEEADKLCD 192
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
14-219 |
1.51e-31 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 116.65 E-value: 1.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNdlIPNcslKGTV-----LFD-GTNIYDKRV 87
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLE--MPR---SGTLniagnHFDfSKTPSDKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 88 dpVEVRRRIGMVFQQPNPFPK-SIYEN-IAFGARINGftgdmdeLVESSLRKAAlwDECKDKLNDSGYS------LSGGQ 159
Cdd:PRK11124 78 --RELRRNVGMVFQQYNLWPHlTVQQNlIEAPCRVLG-------LSKDQALARA--EKLLERLRLKPYAdrfplhLSGGQ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123755092 160 QQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL-KMNYTIIIVTHNMQQALRV 219
Cdd:PRK11124 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELaETGITQVIVTHEVEVARKT 207
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
16-211 |
2.48e-31 |
|
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: 121.99 E-value: 2.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 16 LENVSISYGTFEAV--RNVFCNFKKGNITSLIGPSGCGKSTVLRSLnrmndLIPNCSLKGTVLFDGTNIydKRVDPVEVR 93
Cdd:TIGR03797 454 VDRVTFRYRPDGPLilDDVSLQIEPGEFVAIVGPSGSGKSTLLRLL-----LGFETPESGSVFYDGQDL--AGLDVQAVR 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 94 RRIGMVFQQPNPFPKSIYENIAFGARINgftgdMDELVESsLRKAALWDECKDK-------LNDSGYSLSGGQQQRLCIA 166
Cdd:TIGR03797 527 RQLGVVLQNGRLMSGSIFENIAGGAPLT-----LDEAWEA-ARMAGLAEDIRAMpmgmhtvISEGGGTLSGGQRQRLLIA 600
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 123755092 167 RTIAIEPEIILMDEPCSALDPISTLKIEETMHelKMNYTIIIVTH 211
Cdd:TIGR03797 601 RALVRKPRILLFDEATSALDNRTQAIVSESLE--RLKVTRIVIAH 643
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
41-221 |
4.48e-31 |
|
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: 118.28 E-value: 4.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 41 ITSLIGPSGCGKSTVLRS---LNRmndliP---NCSLKGTVLFDGTniydKRVD-PVEvRRRIGMVFQQPNPFP-KSIYE 112
Cdd:COG4148 27 VTALFGPSGSGKTTLLRAiagLER-----PdsgRIRLGGEVLQDSA----RGIFlPPH-RRRIGYVFQEARLFPhLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 113 NIAFGARINGF---TGDMDELVE----SSL--RKAAlwdeckdklndsgySLSGGQQQRLCIARTIAIEPEIILMDEPCS 183
Cdd:COG4148 97 NLLYGRKRAPRaerRISFDEVVEllgiGHLldRRPA--------------TLSGGERQRVAIGRALLSSPRLLLMDEPLA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 123755092 184 ALDpiSTLKIE-----ETMH-ELKMnyTIIIVTHNMQQALRVSD 221
Cdd:COG4148 163 ALD--LARKAEilpylERLRdELDI--PILYVSHSLDEVARLAD 202
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
10-217 |
1.68e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 114.70 E-value: 1.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 10 KNIILSLENVSISYGTFE--AVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNcslKGTVLFDGTNIYDKRV 87
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGL--LKPQ---SGEIKIDGITISKENL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 88 DpvEVRRRIGMVFQQP-NPFPKSIYE-NIAFGARINGFT-GDMDELVESSLRKAALwdecKDKLNDSGYSLSGGQQQRLC 164
Cdd:PRK13632 79 K--EIRKKIGIIFQNPdNQFIGATVEdDIAFGLENKKVPpKKMKDIIDDLAKKVGM----EDYLDKEPQNLSGGQKQRVA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 123755092 165 IARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHNMQQAL 217
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLrkTRKKTLISITHDMDEAI 207
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
13-212 |
1.78e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 114.79 E-value: 1.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISY--GTfEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNcslKGTVLFDGTNI-YDKRvDP 89
Cdd:PRK13639 1 ILETRDLKYSYpdGT-EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGI--LKPT---SGEVLIKGEPIkYDKK-SL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 90 VEVRRRIGMVFQQPNP--FPKSIYENIAFGARINGFtgDMDEL---VESSLRKAALwdeckdklndSGYS------LSGG 158
Cdd:PRK13639 74 LEVRKTVGIVFQNPDDqlFAPTVEEDVAFGPLNLGL--SKEEVekrVKEALKAVGM----------EGFEnkpphhLSGG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 123755092 159 QQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL-KMNYTIIIVTHN 212
Cdd:PRK13639 142 QKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHD 196
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
13-213 |
1.95e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 114.94 E-value: 1.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISY--GTfEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNcslKGTVLFDGTNIYDKRVDPV 90
Cdd:PRK13636 5 ILKVEELNYNYsdGT-HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGI--LKPS---SGRILFDGKPIDYSRKGLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 91 EVRRRIGMVFQQPNP--FPKSIYENIAFGARINGFTGD-MDELVESSLRKAALwDECKDKlndSGYSLSGGQQQRLCIAR 167
Cdd:PRK13636 79 KLRESVGMVFQDPDNqlFSASVYQDVSFGAVNLKLPEDeVRKRVDNALKRTGI-EHLKDK---PTHCLSFGQKKRVAIAG 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 123755092 168 TIAIEPEIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHNM 213
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMqkELGLTIIIATHDI 202
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
14-217 |
3.14e-30 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 113.80 E-value: 3.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYG----TFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLrslNRMNDLIPNCSlkGTVLFDGTniydkrvdP 89
Cdd:COG4525 4 LTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLL---NLIAGFLAPSS--GEITLDGV--------P 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 90 VE---VRRriGMVFQQPNPFP-KSIYENIAFGARINGFT-GDMDELVESSLRKAALWDECKDKLndsgYSLSGGQQQRLC 164
Cdd:COG4525 71 VTgpgADR--GVVFQKDALLPwLNVLDNVAFGLRLRGVPkAERRARAEELLALVGLADFARRRI----WQLSGGMRQRVG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 123755092 165 IARTIAIEPEIILMDEPCSALDPIStlkiEETMHEL------KMNYTIIIVTHNMQQAL 217
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALDALT----REQMQELlldvwqRTGKGVFLITHSVEEAL 199
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
10-227 |
3.72e-30 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 115.59 E-value: 3.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 10 KNIILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDliPNcslKGTVLFDGTNIYDKRVDp 89
Cdd:PRK11432 3 QKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEK--PT---EGQIFIDGEDVTHRSIQ- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 90 vevRRRIGMVFQQPNPFPK-SIYENIAFGARINGFT-GDMDELVESSLRKAALwDECKDKLNDsgySLSGGQQQRLCIAR 167
Cdd:PRK11432 77 ---QRDICMVFQSYALFPHmSLGENVGYGLKMLGVPkEERKQRVKEALELVDL-AGFEDRYVD---QISGGQQQRVALAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123755092 168 TIAIEPEIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHNMQQALRVSDMTAFFN 227
Cdd:PRK11432 150 ALILKPKVLLFDEPLSNLDANLRRSMREKIRELqqQFNITSLYVTHDQSEAFAVSDTVIVMN 211
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
14-213 |
4.59e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 113.69 E-value: 4.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISY--GT-FE--AVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNdlIPNcslKGTVLFDGTNI--YDKR 86
Cdd:PRK13649 3 INLQNVSYTYqaGTpFEgrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLH--VPT---QGSVRVDDTLItsTSKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 87 VDPVEVRRRIGMVFQQPNP--FPKSIYENIAFGARINGFTGDMDE-LVESSLRKAALWDECKDKlndSGYSLSGGQQQRL 163
Cdd:PRK13649 78 KDIKQIRKKVGLVFQFPESqlFEETVLKDVAFGPQNFGVSQEEAEaLAREKLALVGISESLFEK---NPFELSGGQMRRV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 123755092 164 CIARTIAIEPEIILMDEPCSALDPI---STLKIEETMHELKMnyTIIIVTHNM 213
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKgrkELMTLFKKLHQSGM--TIVLVTHLM 205
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
15-221 |
5.62e-30 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 115.51 E-value: 5.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 15 SLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDLIpncslKGTVLfdgtnIYDKRVDPVE-VR 93
Cdd:PRK11000 5 TLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDIT-----SGDLF-----IGEKRMNDVPpAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 94 RRIGMVFQQPNPFPK-SIYENIAFGARINGFT-GDMDELVESS---LRKAALWDEcKDKlndsgySLSGGQQQRLCIART 168
Cdd:PRK11000 75 RGVGMVFQSYALYPHlSVAENMSFGLKLAGAKkEEINQRVNQVaevLQLAHLLDR-KPK------ALSGGQRQRVAIGRT 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 123755092 169 IAIEPEIILMDEPCSALDPI--STLKIEETMHELKMNYTIIIVTHNMQQALRVSD 221
Cdd:PRK11000 148 LVAEPSVFLLDEPLSNLDAAlrVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLAD 202
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
26-227 |
6.42e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 114.03 E-value: 6.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 26 FEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNcslKGTVLFDGTNIYDKRVDPV--------------- 90
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNAL--LLPD---TGTIEWIFKDEKNKKKTKEkekvleklviqktrf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 91 -------EVRRRIGMVFQ--QPNPFPKSIYENIAFGARINGFTGdmdelvESSLRKAALWDEC----KDKLNDSGYSLSG 157
Cdd:PRK13651 95 kkikkikEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSK------EEAKKRAAKYIELvgldESYLQRSPFELSG 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123755092 158 GQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL-KMNYTIIIVTHNMQQALRVSDMTAFFN 227
Cdd:PRK13651 169 GQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVLEWTKRTIFFK 239
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
14-266 |
2.62e-29 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 111.21 E-value: 2.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDliPNcslKGTVLFDGTNI----------- 82
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEK--PS---EGSIVVNGQTInlvrdkdgqlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 83 -YDKRVDPVeVRRRIGMVFQQPNPFPK-SIYENIAFG-ARINGFT-GDMDELVESSLRKAALWDECKDKLNdsgYSLSGG 158
Cdd:PRK10619 81 vADKNQLRL-LRTRLTMVFQHFNLWSHmTVLENVMEApIQVLGLSkQEARERAVKYLAKVGIDERAQGKYP---VHLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 159 QQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL-KMNYTIIIVTHNMQQALRVSDMTAFFNAveyedgdgg 237
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLaEEGKTMVVVTHEMGFARHVSSHVIFLHQ--------- 227
|
250 260
....*....|....*....|....*....
gi 123755092 238 kvGYLAEFNSTKKIFNSPKEKTTQEYISG 266
Cdd:PRK10619 228 --GKIEEEGAPEQLFGNPQSPRLQQFLKG 254
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
24-221 |
3.39e-29 |
|
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: 109.76 E-value: 3.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 24 GTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNcslKGTVLFDGtniYDKRVDPVEVRRRIGMVFQQP 103
Cdd:cd03266 16 KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGL--LEPD---AGFATVDG---FDVVKEPAEARRRLGFVSDST 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 104 NPFPK-SIYENIAFGARINGFTGD-----MDELVESSlrkaalwdECKDKLNDSGYSLSGGQQQRLCIARTIAIEPEIIL 177
Cdd:cd03266 88 GLYDRlTARENLEYFAGLYGLKGDeltarLEELADRL--------GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 123755092 178 MDEPCSALDPISTLKIEETMHELK-MNYTIIIVTHNMQQALRVSD 221
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLRaLGKCILFSTHIMQEVERLCD 204
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
13-221 |
4.12e-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: 4.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTvlrSLNRMNDLIPNCSlkGTVLFDGTNIYDKrvdPVEV 92
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTT---SFYMIVGLVRPDA--GKILIDGQDITHL---PMHE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 93 RRRIGMVF--QQPNPFPK-SIYENIAfgaRINGFTGDMDELVESSLRKAALWD-ECKDKLNDSGYSLSGGQQQRLCIART 168
Cdd:TIGR04406 73 RARLGIGYlpQEASIFRKlTVEENIM---AVLEIRKDLDRAEREERLEALLEEfQISHLRDNKAMSLSGGERRRVEIARA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 123755092 169 IAIEPEIILMDEPCSALDPISTLKIEETMHELK-MNYTIIIVTHNMQQALRVSD 221
Cdd:TIGR04406 150 LATNPKFILLDEPFAGVDPIAVGDIKKIIKHLKeRGIGVLITDHNVRETLDICD 203
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
14-211 |
5.46e-29 |
|
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: 109.11 E-value: 5.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLnrmndlipnCSL----KGTVLFDGTNIydkRVDP 89
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRIL---------AGLlppsAGEVLWNGEPI---RDAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 90 VEVRRRIGMVFQQPNPFPK-SIYENIAFGARINGFTGDmDELVESSLRKAALwDECKDKLndsGYSLSGGQQQRLCIART 168
Cdd:COG4133 71 EDYRRRLAYLGHADGLKPElTVRENLRFWAALYGLRAD-REAIDEALEAVGL-AGLADLP---VRQLSAGQKRRVALARL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 123755092 169 IAIEPEIILMDEPCSALDPISTLKIEETMHELKMN-YTIIIVTH 211
Cdd:COG4133 146 LLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARgGAVLLTTH 189
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
11-221 |
6.62e-29 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 109.58 E-value: 6.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 11 NIILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndliPNCSlKGTVLFDGTNIYDKRVDPV 90
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGD----PRAT-SGRIVFDGKDITDWQTAKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 91 eVRRRIGMVFQQPNPFPK-SIYENIAFGarinGFTGDMDELVESSLRKAALWDECKDKLNDSGYSLSGGQQQRLCIARTI 169
Cdd:PRK11614 78 -MREAVAIVPEGRRVFSRmTVEENLAMG----GFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRAL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 123755092 170 AIEPEIILMDEPCSALDPISTLKIEETMHELKMN-YTIIIVTHNMQQALRVSD 221
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQgMTIFLVEQNANQALKLAD 205
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
14-213 |
7.97e-29 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 109.50 E-value: 7.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAV--RNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNcslKGTVLFDGTNIydKRVDPVE 91
Cdd:cd03252 1 ITFEHVRFRYKPDGPVilDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRF--YVPE---NGRVLVDGHDL--ALADPAW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 92 VRRRIGMVFQQPNPFPKSIYENIAFGAringfTG-DMDELVESSLRKAA------LWDECKDKLNDSGYSLSGGQQQRLC 164
Cdd:cd03252 74 LRRQVGVVLQENVLFNRSIRDNIALAD-----PGmSMERVIEAAKLAGAhdfiseLPEGYDTIVGEQGAGLSGGQRQRIA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 123755092 165 IARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTHNM 213
Cdd:cd03252 149 IARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRL 197
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
10-216 |
9.42e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 110.18 E-value: 9.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 10 KNIILSLENVSISYGTFE------AVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNcslKGTVLFDGTNIY 83
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEesteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNAL--LIPS---EGKVYVDGLDTS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 84 DKRvDPVEVRRRIGMVFQQP-NPFPKSIYE-NIAFGARINGFTGD-MDELVESSLRKAALWdECKDKlndSGYSLSGGQQ 160
Cdd:PRK13633 76 DEE-NLWDIRNKAGMVFQNPdNQIVATIVEeDVAFGPENLGIPPEeIRERVDESLKKVGMY-EYRRH---APHLLSGGQK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 123755092 161 QRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNY--TIIIVTHNMQQA 216
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEA 208
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-221 |
1.14e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 110.58 E-value: 1.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLnrMNDLIPNcslKGTVLFDGtniydKRVDPvEV 92
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRII--LGILAPD---SGEVLWDG-----EPLDP-ED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 93 RRRIG-MvfqqpnP-----FPK-SIYENIAFGARINGftgdMDElvESSLRKAALWDE---CKDKLNDSGYSLSGGQQQR 162
Cdd:COG4152 70 RRRIGyL------PeerglYPKmKVGEQLVYLARLKG----LSK--AEAKRRADEWLErlgLGDRANKKVEELSKGNQQK 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 163 LCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMN-YTIIIVTHNMQQALRVSD 221
Cdd:COG4152 138 VQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKgTTVIFSSHQMELVEELCD 197
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
16-222 |
2.14e-28 |
|
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: 107.32 E-value: 2.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 16 LENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDliPNcslKGTVLFDGTNIYD-KRVDPVEVRR 94
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEK--FD---SGQVYLNGQETPPlNSKKASKFRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 95 -RIGMVFQQpnpFP----KSIYENIAFG-ARINGFTGDMDELVESSLRKAALWDECKDKLndsgYSLSGGQQQRLCIART 168
Cdd:TIGR03608 76 eKLGYLFQN---FAlienETVEENLDLGlKYKKLSKKEKREKKKEALEKVGLNLKLKQKI----YELSGGEQQRVALARA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 123755092 169 IAIEPEIILMDEPCSALDPISTLKIEETMHEL-KMNYTIIIVTHNM---QQALRVSDM 222
Cdd:TIGR03608 149 ILKPPPLILADEPTGSLDPKNRDEVLDLLLELnDEGKTIIIVTHDPevaKQADRVIEL 206
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
18-264 |
2.18e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 109.48 E-value: 2.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 18 NVSISY--GT---FEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNcslKGTVLFDGTNIYDKRVDPV-- 90
Cdd:PRK13646 7 NVSYTYqkGTpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINAL--LKPT---TGTVTVDDITITHKTKDKYir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 91 EVRRRIGMVFQQPNP--FPKSIYENIAFGARinGFTGDMDELVESSLRKAALWDECKDKLNDSGYSLSGGQQQRLCIART 168
Cdd:PRK13646 82 PVRKRIGMVFQFPESqlFEDTVEREIIFGPK--NFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 169 IAIEPEIILMDEPCSALDPISTLKIEETMHELKM--NYTIIIVTHNMQQALRVSDMTAFFNAveyedgdggkvGYLAEFN 246
Cdd:PRK13646 160 LAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTdeNKTIILVSHDMNEVARYADEVIVMKE-----------GSIVSQT 228
|
250
....*....|....*...
gi 123755092 247 STKKIFNSpKEKTTQEYI 264
Cdd:PRK13646 229 SPKELFKD-KKKLADWHI 245
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
9-222 |
3.27e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 109.12 E-value: 3.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 9 PKNIILSLENVSISYGTFE--AVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNCSLKGTVLFDGTNIYDKR 86
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGL--LLPDDNPNSKITVDGITLTAKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 87 VdpVEVRRRIGMVFQQP-NPF-PKSIYENIAFGARINGFT-GDMDELVESSLRKAALWDECKDKLNDsgysLSGGQQQRL 163
Cdd:PRK13640 79 V--WDIREKVGIVFQNPdNQFvGATVGDDVAFGLENRAVPrPEMIKIVRDVLADVGMLDYIDSEPAN----LSGGQKQRV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123755092 164 CIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKM--NYTIIIVTHNMQQALRVSDM 222
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQV 213
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
8-214 |
3.66e-28 |
|
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: 107.56 E-value: 3.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 8 TPKNI--ILSLENVSISYGTFEAV---RNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDLipncsLKGTVLFDGTNI 82
Cdd:cd03248 4 APDHLkgIVKFQNVTFAYPTRPDTlvlQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQP-----QGGQVLLDGKPI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 83 --YDKRVdpveVRRRIGMVFQQPNPFPKSIYENIAFGARingfTGDMDELVESSLRKAA------LWDECKDKLNDSGYS 154
Cdd:cd03248 79 sqYEHKY----LHSKVSLVGQEPVLFARSLQDNIAYGLQ----SCSFECVKEAAQKAHAhsfiseLASGYDTEVGEKGSQ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 155 LSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTHNMQ 214
Cdd:cd03248 151 LSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLS 210
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
14-214 |
4.94e-28 |
|
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: 112.65 E-value: 4.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISY--GTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLnrMNDLIPNcslKGTVLFDGTNIydKRVDPVE 91
Cdd:TIGR03375 464 IEFRNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLL--LGLYQPT---EGSVLLDGVDI--RQIDPAD 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 92 VRRRIGMVFQQPNPFPKSIYENIAFGARingFTGDmDELVESsLRKAALWDECKD-------KLNDSGYSLSGGQQQRLC 164
Cdd:TIGR03375 537 LRRNIGYVPQDPRLFYGTLRDNIALGAP---YADD-EEILRA-AELAGVTEFVRRhpdgldmQIGERGRSLSGGQRQAVA 611
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 123755092 165 IARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTHNMQ 214
Cdd:TIGR03375 612 LARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHRTS 661
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
13-221 |
8.82e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 107.02 E-value: 8.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPncsLKGTVLFDGTNIYDkrVDPVEV 92
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARL--LTP---QSGTVFLGDKPISM--LSSRQL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 93 RRRIGMVFQQPnPFPK--SIYENIAFG--------ARIngfTGDMDELVESSLRKAALwDECKDKLNDsgySLSGGQQQR 162
Cdd:PRK11231 75 ARRLALLPQHH-LTPEgiTVRELVAYGrspwlslwGRL---SAEDNARVNQAMEQTRI-NHLADRRLT---DLSGGQRQR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 163 LCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMN-YTIIIVTHNMQQALRVSD 221
Cdd:PRK11231 147 AFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQgKTVVTVLHDLNQASRYCD 206
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
13-264 |
1.24e-27 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 109.15 E-value: 1.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNdlIPNcslKGTVLFDGTNIydKRVDPVev 92
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFE--QPT---AGQIMLDGVDL--SHVPPY-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 93 RRRIGMVFQQPNPFPK-SIYENIAFG--------ARINGFTGDMDELV---ESSLRKAalwdeckdklndsgYSLSGGQQ 160
Cdd:PRK11607 90 QRPINMMFQSYALFPHmTVEQNIAFGlkqdklpkAEIASRVNEMLGLVhmqEFAKRKP--------------HQLSGGQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 161 QRLCIARTIAIEPEIILMDEPCSALDPistlKIEETM-HEL-----KMNYTIIIVTHNMQQALRVSDMTAFFNAveyedg 234
Cdd:PRK11607 156 QRVALARSLAKRPKLLLLDEPMGALDK----KLRDRMqLEVvdileRVGVTCVMVTHDQEEAMTMAGRIAIMNR------ 225
|
250 260 270
....*....|....*....|....*....|
gi 123755092 235 dggkvGYLAEFNSTKKIFNSPKEKTTQEYI 264
Cdd:PRK11607 226 -----GKFVQIGEPEEIYEHPTTRYSAEFI 250
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
28-186 |
1.44e-27 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 108.28 E-value: 1.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 28 AVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRmndLIPNCSlkGTVLFDGTNIYD-KRVDPVEVRRRIGMVFQQP--- 103
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLR---LEEPTS--GEILFDGQDITGlSGRELRPLRRRMQMVFQDPyas 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 104 -NPfPKSIYENIAFGARINGFT--GDMDELVESSLRKAALWDECKDKlndsgYS--LSGGQQQRLCIARTIAIEPEIILM 178
Cdd:COG4608 108 lNP-RMTVGDIIAEPLRIHGLAskAERRERVAELLELVGLRPEHADR-----YPheFSGGQRQRIGIARALALNPKLIVC 181
|
....*...
gi 123755092 179 DEPCSALD 186
Cdd:COG4608 182 DEPVSALD 189
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
26-221 |
1.53e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 107.41 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 26 FE--AVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNcslKGTVLFDGTNIY----DKRVDPVevRRRIGMV 99
Cdd:PRK13634 18 FErrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGL--LQPT---SGTVTIGERVITagkkNKKLKPL--RKKVGIV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 100 FQQPNP--FPKSIYENIAFGARINGFTgdmdelVESSLRKAALW------DEckDKLNDSGYSLSGGQQQRLCIARTIAI 171
Cdd:PRK13634 91 FQFPEHqlFEETVEKDICFGPMNFGVS------EEDAKQKAREMielvglPE--ELLARSPFELSGGQMRRVAIAGVLAM 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 123755092 172 EPEIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHNMQQALRVSD 221
Cdd:PRK13634 163 EPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAARYAD 214
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
17-226 |
2.35e-27 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 110.44 E-value: 2.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 17 ENVSISY-GTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDliPNcslKGTVLFDGTNIYDkrVDPVEVRRR 95
Cdd:PRK13657 338 DDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFD--PQ---SGRILIDGTDIRT--VTRASLRRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 96 IGMVFQQPNPFPKSIYENIafgaRInGFTGDMDELVESSLRKAALWDECKDKLN-------DSGYSLSGGQQQRLCIART 168
Cdd:PRK13657 411 IAVVFQDAGLFNRSIEDNI----RV-GRPDATDEEMRAAAERAQAHDFIERKPDgydtvvgERGRQLSGGERQRLAIARA 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 123755092 169 IAIEPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTHNMqQALRVSDMTAFF 226
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRL-STVRNADRILVF 542
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
14-221 |
2.37e-27 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 105.32 E-value: 2.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTvlrSLNRMNDLI-PNcslKGTVLFDGTNIYDKrvdPVEV 92
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTT---TFYMIVGLVkPD---SGKILLDGQDITKL---PMHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 93 RRRIGMVF--QQPNPFPK-SIYENIAFGARINGFTGDmdelvESSLRKAALWDECK-DKLNDS-GYSLSGGQQQRLCIAR 167
Cdd:cd03218 72 RARLGIGYlpQEASIFRKlTVEENILAVLEIRGLSKK-----EREEKLEELLEEFHiTHLRKSkASSLSGGERRRVEIAR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 123755092 168 TIAIEPEIILMDEPCSALDPISTLKIEETMHELK-MNYTIIIVTHNMQQALRVSD 221
Cdd:cd03218 147 ALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKdRGIGVLITDHNVRETLSITD 201
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
9-212 |
4.18e-27 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 109.37 E-value: 4.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 9 PKNIILSLENVSISY-GTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRmndLIPncSLKGTVLFDGTNIYDKRV 87
Cdd:TIGR02868 330 LGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAG---LLD--PLQGEVTLDGVPVSSLDQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 88 DpvEVRRRIGMVFQQPNPFPKSIYENIAFGAringftGDM-DELVESSLRKAAL--W-DECKDKLNDS----GYSLSGGQ 159
Cdd:TIGR02868 405 D--EVRRRVSVCAQDAHLFDTTVRENLRLAR------PDAtDEELWAALERVGLadWlRALPDGLDTVlgegGARLSGGE 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 123755092 160 QQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTHN 212
Cdd:TIGR02868 477 RQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
14-221 |
5.22e-27 |
|
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: 103.90 E-value: 5.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNcslKGTVLFDGtniydKRVDPvEVR 93
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGI--ILPD---SGEVLFDG-----KPLDI-AAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 94 RRIGMVFQQPNPFPK-SIYENIAFGARINGFT-GDMDELVESSLRKAALWDECKDKLNDsgysLSGGQQQRLCIARTIAI 171
Cdd:cd03269 70 NRIGYLPEERGLYPKmKVIDQLVYLAQLKGLKkEEARRRIDEWLERLELSEYANKRVEE----LSKGNQQKVQFIAAVIH 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 123755092 172 EPEIILMDEPCSALDPISTLKIEETMHELKMN-YTIIIVTHNMQQALRVSD 221
Cdd:cd03269 146 DPELLILDEPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEELCD 196
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-222 |
6.40e-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: 102.68 E-value: 6.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEA--VRNVFCNFKKGNITSLIGPSGCGKSTVLRSLnrMNDLIPncsLKGTVLFDGTNIydKRVDPVE 91
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLI--LGLLRP---TSGRVRLDGADI--SQWDPNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 92 VRRRIGMVFQQPNPFPKSIYENIafgaringftgdmdelvesslrkaalwdeckdklndsgysLSGGQQQRLCIARTIAI 171
Cdd:cd03246 74 LGDHVGYLPQDDELFSGSIAENI----------------------------------------LSGGQRQRLGLARALYG 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 123755092 172 EPEIILMDEPCSALDPISTLKIEETMHELKM-NYTIIIVTHNM---QQALRVSDM 222
Cdd:cd03246 114 NPRILVLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPetlASADRILVL 168
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
10-211 |
8.33e-27 |
|
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: 103.01 E-value: 8.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 10 KNIILSLENvSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNrmnDLIPNCSLKGTVLFDGTNIYDKrvdp 89
Cdd:cd03213 7 RNLTVTVKS-SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALA---GRRTGLGVSGEVLINGRPLDKR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 90 vEVRRRIGMVFQQPNPFPK-SIYENIAFGARINGftgdmdelvesslrkaalwdeckdklndsgysLSGGQQQRLCIART 168
Cdd:cd03213 79 -SFRKIIGYVPQDDILHPTlTVRETLMFAAKLRG--------------------------------LSGGERKRVSIALE 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 123755092 169 IAIEPEIILMDEPCSALDPISTLKIEETMHEL-KMNYTIIIVTH 211
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLaDTGRTIICSIH 169
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
14-256 |
8.52e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 105.30 E-value: 8.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYG---TFEA--VRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNcslKGTVlfdgtNIYDKRVD 88
Cdd:PRK13641 3 IKFENVDYIYSpgtPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNAL--LKPS---SGTI-----TIAGYHIT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 89 P-------VEVRRRIGMVFQQPNP--FPKSIYENIAFGARINGFTGD-MDELVESSLRKAALWDECKDKlndSGYSLSGG 158
Cdd:PRK13641 73 PetgnknlKKLRKKVSLVFQFPEAqlFENTVLKDVEFGPKNFGFSEDeAKEKALKWLKKVGLSEDLISK---SPFELSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 159 QQQRLCIARTIAIEPEIILMDEPCSALDPIStlkiEETMHELKMNY-----TIIIVTHNMQQalrVSDMTAFFNAVEYed 233
Cdd:PRK13641 150 QMRRVAIAGVMAYEPEILCLDEPAAGLDPEG----RKEMMQLFKDYqkaghTVILVTHNMDD---VAEYADDVLVLEH-- 220
|
250 260
....*....|....*....|...
gi 123755092 234 gdggkvGYLAEFNSTKKIFNSPK 256
Cdd:PRK13641 221 ------GKLIKHASPKEIFSDKE 237
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-221 |
9.02e-27 |
|
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: 101.74 E-value: 9.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLnrMNDLIPNcslKGTVLFDGTNIydKRVDPVEVR 93
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKIL--SGLYKPD---SGEILVDGKEV--SFASPRDAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 94 RR-IGMVFQqpnpfpksiyeniafgaringftgdmdelvesslrkaalwdeckdklndsgysLSGGQQQRLCIARTIAIE 172
Cdd:cd03216 74 RAgIAMVYQ-----------------------------------------------------LSVGERQMVEIARALARN 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 123755092 173 PEIILMDEPCSALDPISTLKIEETMHELK-MNYTIIIVTHNMQQALRVSD 221
Cdd:cd03216 101 ARLLILDEPTAALTPAEVERLFKVIRRLRaQGVAVIFISHRLDEVFEIAD 150
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
14-211 |
1.14e-26 |
|
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: 103.34 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISY--GTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndlIPNCSlkGTVLFDGTNIydKRVDPVE 91
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRL---VELSS--GSILIDGVDI--SKIGLHD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 92 VRRRIGMVFQQPNPFPKSIYENIAFgarINGFTgdmDELVESSLRKAALWDECK-------DKLNDSGYSLSGGQQQRLC 164
Cdd:cd03244 76 LRSRISIIPQDPVLFSGTIRSNLDP---FGEYS---DEELWQALERVGLKEFVEslpggldTVVEEGGENLSVGQRQLLC 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 123755092 165 IARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTH 211
Cdd:cd03244 150 LARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAH 196
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
17-218 |
1.54e-26 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 104.30 E-value: 1.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 17 ENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPncsLKGTVLFDGTNIydKRVDPVEVRRRI 96
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRL--MTP---AHGHVWLDGEHI--QHYASKEVARRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 97 GMVFQQP-NPFPKSIYENIAFGARING--FT---GDMDELVESSLRKAALWDECKDKLNdsgySLSGGQQQRLCIARTIA 170
Cdd:PRK10253 84 GLLAQNAtTPGDITVQELVARGRYPHQplFTrwrKEDEEAVTKAMQATGITHLADQSVD----TLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 123755092 171 IEPEIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHNMQQALR 218
Cdd:PRK10253 160 QETAIMLLDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNQACR 209
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
14-214 |
2.66e-26 |
|
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: 101.24 E-value: 2.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFE--AVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRmnDLIPNcslKGTVLFDGTNIYDKRVdpvE 91
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG--DLKPQ---QGEITLDGVPVSDLEK---A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 92 VRRRIGMVFQQPNPFPKSIYENIafGARingftgdmdelvesslrkaalwdeckdklndsgysLSGGQQQRLCIARTIAI 171
Cdd:cd03247 73 LSSLISVLNQRPYLFDTTLRNNL--GRR-----------------------------------FSGGERQRLALARILLQ 115
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 123755092 172 EPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTHNMQ 214
Cdd:cd03247 116 DAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLT 158
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
37-221 |
3.13e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 104.05 E-value: 3.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 37 KKGNITSLIGPSGCGKSTVLRSLNRMNDLIPNCSLKGTVLFDGTNiYDKRVDPVevRRRIGMVFQQPNP--FPKSIYENI 114
Cdd:PRK13643 30 KKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTS-KQKEIKPV--RKKVGVVFQFPESqlFEETVLKDV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 115 AFGARINGFTGD-MDELVESSLRKAALWDECKDKlndSGYSLSGGQQQRLCIARTIAIEPEIILMDEPCSALDP---IST 190
Cdd:PRK13643 107 AFGPQNFGIPKEkAEKIAAEKLEMVGLADEFWEK---SPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPkarIEM 183
|
170 180 190
....*....|....*....|....*....|.
gi 123755092 191 LKIEETMHElkMNYTIIIVTHNMQQALRVSD 221
Cdd:PRK13643 184 MQLFESIHQ--SGQTVVLVTHLMDDVADYAD 212
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
10-234 |
4.21e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 102.91 E-value: 4.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 10 KNIILSLENVSISYGTFEA--VRNVFCNFKKGNITSLIGPSGCGKSTVLRSLnrMNDLIPNcslKGTVLFDGTNIYDKrv 87
Cdd:PRK13648 4 KNSIIVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLM--IGIEKVK---SGEIFYNNQAITDD-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 88 DPVEVRRRIGMVFQQP-NPFPKSIYE-NIAFGARINGF-TGDMDELVESSLRKAALWDeckdKLNDSGYSLSGGQQQRLC 164
Cdd:PRK13648 77 NFEKLRKHIGIVFQNPdNQFVGSIVKyDVAFGLENHAVpYDEMHRRVSEALKQVDMLE----RADYEPNALSGGQKQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123755092 165 IARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKM--NYTIIIVTHNMQQALRVSDMTAFFNAVEYEDG 234
Cdd:PRK13648 153 IAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSehNITIISITHDLSEAMEADHVIVMNKGTVYKEG 224
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
14-211 |
6.91e-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: 106.34 E-value: 6.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYG--TFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDliPNcslKGTVLFDGTNIYDKRVDpvE 91
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYE--PD---SGQILLDGHDLADYTLA--S 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 92 VRRRIGMVFQQPNPFPKSIYENIAFGARingfTGDMDELVESSLRKAALWDECkDKL--------NDSGYSLSGGQQQRL 163
Cdd:TIGR02203 404 LRRQVALVSQDVVLFNDTIANNIAYGRT----EQADRAEIERALAAAYAQDFV-DKLplgldtpiGENGVLLSGGQRQRL 478
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 123755092 164 CIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTH 211
Cdd:TIGR02203 479 AIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAH 526
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
14-266 |
8.30e-26 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 104.73 E-value: 8.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDlipncSLKGTVLFDGTNIydKRVDPVEVR 93
Cdd:PRK10070 29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE-----PTRGQVLIDGVDI--AKISDAELR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 94 ----RRIGMVFQQPNPFPK-SIYENIAFGARINGFTG-DMDELVESSLRKAALWDECKdklndsGY--SLSGGQQQRLCI 165
Cdd:PRK10070 102 evrrKKIAMVFQSFALMPHmTVLDNTAFGMELAGINAeERREKALDALRQVGLENYAH------SYpdELSGGMRQRVGL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 166 ARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNY--TIIIVTHNMQQALRVSDMTAFFnaveyEDGDGGKVGyla 243
Cdd:PRK10070 176 ARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHqrTIVFISHDLDEAMRIGDRIAIM-----QNGEVVQVG--- 247
|
250 260
....*....|....*....|...
gi 123755092 244 efnSTKKIFNSPKEKTTQEYISG 266
Cdd:PRK10070 248 ---TPDEILNNPANDYVRTFFRG 267
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
10-221 |
1.47e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 102.62 E-value: 1.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 10 KNIILSLENVSISYGT-----FEAVRNVFCNFKKGNITSLIGPSGCGKSTVLrslNRMNDLIPncSLKGTVLFDGTNIYD 84
Cdd:PRK13631 18 DDIILRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLV---THFNGLIK--SKYGTIQVGDIYIGD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 85 KRVDPV--------------EVRRRIGMVFQQP--NPFPKSIYENIAFGARINGFTG-DMDELVESSLRKAALWDeckDK 147
Cdd:PRK13631 93 KKNNHElitnpyskkiknfkELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKsEAKKLAKFYLNKMGLDD---SY 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 123755092 148 LNDSGYSLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPistlKIEETMHEL-----KMNYTIIIVTHNMQQALRVSD 221
Cdd:PRK13631 170 LERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDP----KGEHEMMQLildakANNKTVFVITHTMEHVLEVAD 244
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
9-214 |
2.76e-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: 99.41 E-value: 2.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 9 PKNIILSLENVSISYGTF--EAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDLIpncslKGTVLFDGTNIydKR 86
Cdd:cd03369 2 PEHGEIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAE-----EGKIEIDGIDI--ST 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 87 VDPVEVRRRIGMVFQQPNPFPKSIYENIAfgaRINGFTgdmDELVESSLRkaalwdeckdkLNDSGYSLSGGQQQRLCIA 166
Cdd:cd03369 75 IPLEDLRSSLTIIPQDPTLFSGTIRSNLD---PFDEYS---DEEIYGALR-----------VSEGGLNLSQGQRQLLCLA 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 123755092 167 RTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTHNMQ 214
Cdd:cd03369 138 RALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLR 185
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
7-221 |
2.90e-25 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 100.99 E-value: 2.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 7 KTPKNIIlSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNrmNDLIPNcslKGTVLFDGTNIYD-K 85
Cdd:PRK11831 2 QSVANLV-DMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIG--GQIAPD---HGEILFDGENIPAmS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 86 RVDPVEVRRRIGMVFQQPNPFPK-SIYENIAFGARINgfTGDMDELVESS---------LRKAAlwdeckdKLNDSgySL 155
Cdd:PRK11831 76 RSRLYTVRKRMSMLFQSGALFTDmNVFDNVAYPLREH--TQLPAPLLHSTvmmkleavgLRGAA-------KLMPS--EL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 156 SGGQQQRLCIARTIAIEPEIILMDEPCSALDPIST---LK-IEETMHELKMnyTIIIVTHNMQQALRVSD 221
Cdd:PRK11831 145 SGGMARRAALARAIALEPDLIMFDEPFVGQDPITMgvlVKlISELNSALGV--TCVVVSHDVPEVLSIAD 212
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
14-221 |
4.16e-25 |
|
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: 98.83 E-value: 4.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSlnrMNDLIPNCSlkGTVLFDGTNIydkrVDPVEVR 93
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKI---ILGLIKPDS--GEITFDGKSY----QKNIEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 94 RRIGMVFQQPNPFPK-SIYENIAFGARINGFTgdmDELVESSLRKAALWDECKDKLndSGYSLsgGQQQRLCIARTIAIE 172
Cdd:cd03268 72 RRIGALIEAPGFYPNlTARENLRLLARLLGIR---KKRIDEVLDVVGLKDSAKKKV--KGFSL--GMKQRLGIALALLGN 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 123755092 173 PEIILMDEPCSALDPISTLKIEETMHEL-KMNYTIIIVTHNMQQALRVSD 221
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELILSLrDQGITVLISSHLLSEIQKVAD 194
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
14-241 |
1.02e-24 |
|
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: 97.95 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGtfEAVRNVFCNFKKGNITSLIGPSGCGKSTVLrslnrmnDLIPNCSL--KGTVLFDGTNIydKRVDPVE 91
Cdd:cd03298 1 VRLDKIRFSYG--EQPMHFDLTFAQGEITAIVGPSGSGKSTLL-------NLIAGFETpqSGRVLINGVDV--TAAPPAD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 92 vrRRIGMVFQQPNPFPK-SIYENIAFGARIN-GFTGDMDELVESSLRKAALwDECKDKLNDSgysLSGGQQQRLCIARTI 169
Cdd:cd03298 70 --RPVSMLFQENNLFAHlTVEQNVGLGLSPGlKLTAEDRQAIEVALARVGL-AGLEKRLPGE---LSGGERQRVALARVL 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 123755092 170 AIEPEIILMDEPCSALDPI---STLKIEETMH-ELKMnyTIIIVTHNMQQALRVSDMTAFFnaveyedgDGGKVGY 241
Cdd:cd03298 144 VRDKPVLLLDEPFAALDPAlraEMLDLVLDLHaETKM--TVLMVTHQPEDAKRLAQRVVFL--------DNGRIAA 209
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
11-212 |
1.20e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 98.25 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 11 NIILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLR---SLnrmndLIPNcslKGTVLFDGTNIydKRV 87
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKivaSL-----ISPT---SGTLLFEGEDI--STL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 88 DPVEVRRRIGMVFQQPNPFPKSIYENIAFGARINGFTGDMDELVESsLRKAALWDECKDK-LNDsgysLSGGQQQRLCIA 166
Cdd:PRK10247 75 KPEIYRQQVSYCAQTPTLFGDTVYDNLIFPWQIRNQQPDPAIFLDD-LERFALPDTILTKnIAE----LSGGEKQRISLI 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 123755092 167 RTIAIEPEIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHN 212
Cdd:PRK10247 150 RNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYvrEQNIAVLWVTHD 197
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
11-221 |
1.33e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 102.02 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 11 NIILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLN---RMNDlipncslkGTVLFDGTNIydKRV 87
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSgvyQPDS--------GEILLDGEPV--RFR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 88 DPVEVRRR-IGMVFQQPNPFPK-SIYENIAFG--ARINGFtgdmdelvessLRKAALWDECKDKLNDSGY---------S 154
Cdd:COG1129 72 SPRDAQAAgIAIIHQELNLVPNlSVAENIFLGrePRRGGL-----------IDWRAMRRRARELLARLGLdidpdtpvgD 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 123755092 155 LSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELK-MNYTIIIVTHNMQQALRVSD 221
Cdd:COG1129 141 LSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKaQGVAIIYISHRLDEVFEIAD 208
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-186 |
1.71e-24 |
|
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: 102.07 E-value: 1.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 12 IILSLENVSISY-----------GTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRmndLIPNcslKGTVLFDGT 80
Cdd:COG4172 274 PLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR---LIPS---EGEIRFDGQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 81 NIYD-KRVDPVEVRRRIGMVFQqpNPF----PK-SIYENIAFGARINGFTGD---MDELVESSLRKAALWDECKDKlnds 151
Cdd:COG4172 348 DLDGlSRRALRPLRRRMQVVFQ--DPFgslsPRmTVGQIIAEGLRVHGPGLSaaeRRARVAEALEEVGLDPAARHR---- 421
|
170 180 190
....*....|....*....|....*....|....*..
gi 123755092 152 gY--SLSGGQQQRLCIARTIAIEPEIILMDEPCSALD 186
Cdd:COG4172 422 -YphEFSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
10-221 |
1.77e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 99.31 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 10 KNIILslENVSISYGT-----FEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNCSlkGTVLFD---GTN 81
Cdd:PRK13645 5 KDIIL--DNVSYTYAKktpfeFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGL--IISETG--QTIVGDyaiPAN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 82 IydKRVDPV-EVRRRIGMVFQQP--NPFPKSIYENIAFGArINgFTGDMDELVESSLRKAALWDECKDKLNDSGYSLSGG 158
Cdd:PRK13645 79 L--KKIKEVkRLRKEIGLVFQFPeyQLFQETIEKDIAFGP-VN-LGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 123755092 159 QQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNYT--IIIVTHNMQQALRVSD 221
Cdd:PRK13645 155 QKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKkrIIMVTHNMDQVLRIAD 219
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
13-221 |
2.08e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 97.79 E-value: 2.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTvlrSLNRMNDLI-PNcslKGTVLFDGTNIYDKrvdPVE 91
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTT---TFYMIVGLVkPD---SGRIFLDGEDITHL---PMH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 92 VRRRIGMVF--QQPNPFPK-SIYENIAFGARINGFTGD-----MDELVE----SSLRKAalwdeckdklndSGYSLSGGQ 159
Cdd:COG1137 74 KRARLGIGYlpQEASIFRKlTVEDNILAVLELRKLSKKereerLEELLEefgiTHLRKS------------KAYSLSGGE 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123755092 160 QQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELK-MNYTIIIVTHNMQQALRVSD 221
Cdd:COG1137 142 RRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKeRGIGVLITDHNVRETLGICD 204
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
14-214 |
2.83e-24 |
|
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: 96.38 E-value: 2.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYG-----TFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLnrMNDLIPncsLKGTVlfdgtniydkrvd 88
Cdd:cd03250 1 ISVEDASFTWDsgeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL--LGELEK---LSGSV------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 89 pvEVRRRIGMVFQQPNPFPKSIYENIAFGARINgftgdmDELVESSLRKAALwDECKDKLND--------SGYSLSGGQQ 160
Cdd:cd03250 63 --SVPGSIAYVSQEPWIQNGTIRENILFGKPFD------EERYEKVIKACAL-EPDLEILPDgdlteigeKGINLSGGQK 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 123755092 161 QRLCIARTIAIEPEIILMDEPCSALDPISTLKIEET--MHELKMNYTIIIVTHNMQ 214
Cdd:cd03250 134 QRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENciLGLLLNNKTRILVTHQLQ 189
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
13-218 |
3.50e-24 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 97.78 E-value: 3.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRM--NDLIPNCS---LKGTVLFDGTNIYDKRv 87
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitGDKSAGSHielLGRTVQREGRLARDIR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 88 dpvEVRRRIGMVFQQPNPFPK-SIYENIAFGAR---------INGFTGDMDELVESSLRKAALWDECKDKLNdsgySLSG 157
Cdd:PRK09984 83 ---KSRANTGYIFQQFNLVNRlSVLENVLIGALgstpfwrtcFSWFTREQKQRALQALTRVGMVHFAHQRVS----TLSG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123755092 158 GQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMN--YTIIIVTHNMQQALR 218
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDYALR 218
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
10-215 |
7.85e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 97.11 E-value: 7.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 10 KNIIlSLENVSISYGTFE---AVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNcslKGTVLFDGTNIYDKR 86
Cdd:PRK13650 2 SNII-EVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGL--LEAE---SGQIIIDGDLLTEEN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 87 VdpVEVRRRIGMVFQQP-NPFPKSIYEN-IAFGARINGFT-GDMDELVESSLRKAALWDeCKDKlndSGYSLSGGQQQRL 163
Cdd:PRK13650 76 V--WDIRHKIGMVFQNPdNQFVGATVEDdVAFGLENKGIPhEEMKERVNEALELVGMQD-FKER---EPARLSGGQKQRV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 123755092 164 CIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNY--TIIIVTHNMQQ 215
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDE 203
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
14-221 |
1.12e-23 |
|
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: 95.67 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLnrMNdLIPNCSlkGTVLFDGTNIYDKRvdPVE-V 92
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTL--MG-LLPVKS--GSIRLDGEDITKLP--PHErA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 93 RRRIGMVFQQPNPFPK-SIYENIAFGAringftgdmdELVESSLRKA-----ALWDECKDKLNDSGYSLSGGQQQRLCIA 166
Cdd:TIGR03410 74 RAGIAYVPQGREIFPRlTVEENLLTGL----------AALPRRSRKIpdeiyELFPVLKEMLGRRGGDLSGGQQQQLAIA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 123755092 167 RTIAIEPEIILMDEPCSALDPISTLKIEETMHELK--MNYTIIIVTHNMQQALRVSD 221
Cdd:TIGR03410 144 RALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRaeGGMAILLVEQYLDFARELAD 200
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
11-216 |
1.50e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 96.32 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 11 NIILSLENVSISY---GTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDlipncSLKGTVLFDGTNIYDKRV 87
Cdd:PRK13642 2 NKILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFE-----EFEGKVKIDGELLTAENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 88 dpVEVRRRIGMVFQQP-NPF-PKSIYENIAFGARINGFTgdMDELVESsLRKAALWDECKDKLNDSGYSLSGGQQQRLCI 165
Cdd:PRK13642 77 --WNLRRKIGMVFQNPdNQFvGATVEDDVAFGMENQGIP--REEMIKR-VDEALLAVNMLDFKTREPARLSGGQKQRVAV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 123755092 166 ARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNY--TIIIVTHNMQQA 216
Cdd:PRK13642 152 AGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEA 204
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-222 |
1.53e-23 |
|
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: 99.44 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISY-GTFEAV-RNVfcNF--KKGNITSLIGPSGCGKSTVLRSLnrMNDLIPncsLKGTVLFDGTNIYdkRVDP 89
Cdd:COG4618 331 LSVENLTVVPpGSKRPIlRGV--SFslEPGEVLGVIGPSGSGKSTLARLL--VGVWPP---TAGSVRLDGADLS--QWDR 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 90 VEVRRRIGMVFQQPNPFPKSIYENIAfgaRingFTGDMDELVESSLRKAAlwdeCKD-----------KLNDSGYSLSGG 158
Cdd:COG4618 402 EELGRHIGYLPQDVELFDGTIAENIA---R---FGDADPEKVVAAAKLAG----VHEmilrlpdgydtRIGEGGARLSGG 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 123755092 159 QQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELK-MNYTIIIVTHNMqQALRVSDM 222
Cdd:COG4618 472 QRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKaRGATVVVITHRP-SLLAAVDK 535
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
14-211 |
1.82e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 99.32 E-value: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFE--AVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDLipncsLKGTVLFDGTNIYDKRVDpvE 91
Cdd:PRK11176 342 IEFRNVTFTYPGKEvpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDI-----DEGEILLDGHDLRDYTLA--S 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 92 VRRRIGMVFQQPNPFPKSIYENIAFgARINGFTgdmDELVESSLRKAALWD---ECKDKLN----DSGYSLSGGQQQRLC 164
Cdd:PRK11176 415 LRNQVALVSQNVHLFNDTIANNIAY-ARTEQYS---REQIEEAARMAYAMDfinKMDNGLDtvigENGVLLSGGQRQRIA 490
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 123755092 165 IARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTH 211
Cdd:PRK11176 491 IARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAH 537
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
13-234 |
2.41e-23 |
|
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: 95.15 E-value: 2.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNdliPNCSLKGTVLFD---GtniydkRVDP 89
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDL---PPTYGNDVRLFGerrG------GEDV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 90 VEVRRRIGMV---FQQPNPFPKSIYENIAFGA-----RINGFTGDMDELVESSLrkaALWDeCKDKLNDSGYSLSGGQQQ 161
Cdd:COG1119 74 WELRKRIGLVspaLQLRFPRDETVLDVVLSGFfdsigLYREPTDEQRERARELL---ELLG-LAHLADRPFGTLSQGEQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 123755092 162 RLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNY--TIIIVTHnmqqalRVSDMTAFFN-AVEYEDG 234
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGapTLVLVTH------HVEEIPPGIThVLLLKDG 219
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
15-221 |
3.25e-23 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 94.76 E-value: 3.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 15 SLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRmndLIPncSLKGTVLFDGTNIydKRVDPVEVRR 94
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISR---LLP--PDSGEVLVDGLDV--ATTPSRELAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 95 RIGmVFQQPNPFPK--SIYENIAFG------ARIngfTGDMDELVESSLRKAALwDECKDKLNDsgySLSGGQQQRLCIA 166
Cdd:COG4604 76 RLA-ILRQENHINSrlTVRELVAFGrfpyskGRL---TAEDREIIDEAIAYLDL-EDLADRYLD---ELSGGQRQRAFIA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 123755092 167 RTIAIEPEIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHNMQQALRVSD 221
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLadELGKTVVIVLHDINFASCYAD 204
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
16-221 |
3.74e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 96.69 E-value: 3.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 16 LENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLR---SLNRMNdlipncslKGTVLFDGTNiydkrVDPVEV 92
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRiiaGLEHQT--------SGHIRFHGTD-----VSRLHA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 93 R-RRIGMVFQQPNPFPK-SIYENIAFG-------ARINGFTgdMDELVESSLRKAALwdeckDKLNDSGYS-LSGGQQQR 162
Cdd:PRK10851 72 RdRKVGFVFQHYALFRHmTVFDNIAFGltvlprrERPNAAA--IKAKVTQLLEMVQL-----AHLADRYPAqLSGGQKQR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 123755092 163 LCIARTIAIEPEIILMDEPCSALDpiSTLKIE-----ETMHElKMNYTIIIVTHNMQQALRVSD 221
Cdd:PRK10851 145 VALARALAVEPQILLLDEPFGALD--AQVRKElrrwlRQLHE-ELKFTSVFVTHDQEEAMEVAD 205
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
41-249 |
3.75e-23 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 96.72 E-value: 3.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 41 ITSLIGPSGCGKSTVLRSlnrMNDLIP----NCSLKGTVLFDGTniydKRVD-PVEvRRRIGMVFQQPNPFPK-SIYENI 114
Cdd:TIGR02142 25 VTAIFGRSGSGKTTLIRL---IAGLTRpdegEIVLNGRTLFDSR----KGIFlPPE-KRRIGYVFQEARLFPHlSVRGNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 115 AFGARingftgdmdeLVESSLRKAAlWDECKDKLNDSGY------SLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPI 188
Cdd:TIGR02142 97 RYGMK----------RARPSERRIS-FERVIELLGIGHLlgrlpgRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 123755092 189 STLKI----EETMHELKMnyTIIIVTHNMQQALRVSDmtaffNAVEYEDGDGGKVGYLAEFNSTK 249
Cdd:TIGR02142 166 RKYEIlpylERLHAEFGI--PILYVSHSLQEVLRLAD-----RVVVLEDGRVAAAGPIAEVWASP 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-262 |
5.51e-23 |
|
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: 97.45 E-value: 5.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGT----FEAVRNVfcNF--KKGNITSLIGPSGCGKS----TVLRSLNRmndliPNCSLKGTVLFDGTNI 82
Cdd:COG4172 6 LLSVEDLSVAFGQgggtVEAVKGV--SFdiAAGETLALVGESGSGKSvtalSILRLLPD-----PAAHPSGSILFDGQDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 83 YDKrvDPVEVRR----RIGMVFQQP----NPFpKSIYENIAFGARINGftgdmdelvesSLRKAALWDECKDKLNDSG-- 152
Cdd:COG4172 79 LGL--SERELRRirgnRIAMIFQEPmtslNPL-HTIGKQIAEVLRLHR-----------GLSGAAARARALELLERVGip 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 153 ----------YSLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELK--MNYTIIIVTHNM----QQA 216
Cdd:COG4172 145 dperrldaypHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQreLGMALLLITHDLgvvrRFA 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 123755092 217 LRVSDMTAffnaveyedgdggkvGYLAEFNSTKKIFNSPKEKTTQE 262
Cdd:COG4172 225 DRVAVMRQ---------------GEIVEQGPTAELFAAPQHPYTRK 255
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
29-221 |
9.12e-23 |
|
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: 93.30 E-value: 9.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 29 VRNVFCNFKKGNITSLIGPSGCGKSTVLrslnrmnDLIPNCSL--KGTVLFDGTNIYDKRVDPVevrrrigMVFQQPNPF 106
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLL-------NLISGLAQptSGGVILEGKQITEPGPDRM-------VVFQNYSLL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 107 P-KSIYENIAFG---ARINGFTGDMDELVESSLRKAALwDECKDKLNDSgysLSGGQQQRLCIARTIAIEPEIILMDEPC 182
Cdd:TIGR01184 67 PwLTVRENIALAvdrVLPDLSKSERRAIVEEHIALVGL-TEAADKRPGQ---LSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 123755092 183 SALDPISTLKIEETMHEL--KMNYTIIIVTHNMQQALRVSD 221
Cdd:TIGR01184 143 GALDALTRGNLQEELMQIweEHRVTVLMVTHDVDEALLLSD 183
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
13-213 |
1.65e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 93.71 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISY-GTFEAVRNVfcNFKKGNIT--SLIGPSGCGKSTVLRSLNRMndLIPNcslKGTVLFDGTNIYDKRVDp 89
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNI--NFIAPRNSriAVIGPNGAGKSTLFRHFNGI--LKPT---SGSVLIRGEPITKENIR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 90 vEVRRRIGMVFQQPNP--FPKSIYENIAFGARINGF-TGDMDELVESSLRKAALwDECKDKLNdsgYSLSGGQQQRLCIA 166
Cdd:PRK13652 75 -EVRKFVGLVFQNPDDqiFSPTVEQDIAFGPINLGLdEETVAHRVSSALHMLGL-EELRDRVP---HHLSGGEKKRVAIA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 123755092 167 RTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNY--TIIIVTHNM 213
Cdd:PRK13652 150 GVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYgmTVIFSTHQL 198
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
13-213 |
2.63e-22 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 91.86 E-value: 2.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISY-GTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRslnrmndLIpnCSLK----GTVLFDGTNIydKRV 87
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLK-------LI--CGIErpsaGKIWFSGHDI--TRL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 88 DPVEV---RRRIGMVFQQPNPF-PKSIYENIAFGARINGFTG-DMDELVESSLRKAALWDECKDklndSGYSLSGGQQQR 162
Cdd:PRK10908 70 KNREVpflRRQIGMIFQDHHLLmDRTVYDNVAIPLIIAGASGdDIRRRVSAALDKVGLLDKAKN----FPIQLSGGEQQR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 123755092 163 LCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL-KMNYTIIIVTHNM 213
Cdd:PRK10908 146 VGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFnRVGVTVLMATHDI 197
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
39-211 |
2.67e-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: 95.66 E-value: 2.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 39 GNITSLIGPSGCGKSTVLRSLNRMNDliPNcslKGTVLFDGTNIYDkrVDPVEVRRRIGMVFQQPNPFPKSIYENIAFGa 118
Cdd:COG5265 384 GKTVAIVGPSGAGKSTLARLLFRFYD--VT---SGRILIDGQDIRD--VTQASLRAAIGIVPQDTVLFNDTIAYNIAYG- 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 119 RINGftgDMDElVESSLRKAALwDECKDKLNDsGYS---------LSGGQQQRLCIARTIAIEPEIILMDEPCSALDPIS 189
Cdd:COG5265 456 RPDA---SEEE-VEAAARAAQI-HDFIESLPD-GYDtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRT 529
|
170 180
....*....|....*....|..
gi 123755092 190 TLKIEETMHELKMNYTIIIVTH 211
Cdd:COG5265 530 ERAIQAALREVARGRTTLVIAH 551
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
13-221 |
6.56e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 91.97 E-value: 6.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISY--GTfEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNcslKGTVLFDGTNIYDKRVDPv 90
Cdd:PRK13644 1 MIRLENVSYSYpdGT-PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGL--LRPQ---KGKVLVSGIDTGDFSKLQ- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 91 EVRRRIGMVFQQPNP--FPKSIYENIAFGARINGFTG-DMDELVESSLRKAALwdecKDKLNDSGYSLSGGQQQRLCIAR 167
Cdd:PRK13644 74 GIRKLVGIVFQNPETqfVGRTVEEDLAFGPENLCLPPiEIRKRVDRALAEIGL----EKYRHRSPKTLSGGQGQCVALAG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 123755092 168 TIAIEPEIILMDEPCSALDPISTLKIEETMHEL-KMNYTIIIVTHNMQQaLRVSD 221
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEE-LHDAD 203
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-221 |
1.45e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 90.51 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 5 NKKTPkniiLSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDliPNcslKGTVLFDGTNIYD 84
Cdd:PRK11247 8 NQGTP----LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLET--PS---AGELLAGTAPLAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 85 KRVDpvevrrrIGMVFQQPNPFP-KSIYENIAFGARingftGDMDELVESSLRKAALwdecKDKLNDSGYSLSGGQQQRL 163
Cdd:PRK11247 79 ARED-------TRLMFQDARLLPwKKVIDNVGLGLK-----GQWRDAALQALAAVGL----ADRANEWPAALSGGQKQRV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 164 CIARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHNMQQALRVSD 221
Cdd:PRK11247 143 ALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwqQHGFTVLLVTHDVSEAVAMAD 202
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
13-217 |
2.09e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 90.14 E-value: 2.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLrslNRMNDLIPNCSlkGTVLFDGtniydKRVDPVEV 92
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLL---NLIAGFVPYQH--GSITLDG-----KPVEGPGA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 93 RRriGMVFQQPNPFP-KSIYENIAFGARINGFT-GDMDELVESSLRKAALWDECKDKLndsgYSLSGGQQQRLCIARTIA 170
Cdd:PRK11248 71 ER--GVVFQNEGLLPwRNVQDNVAFGLQLAGVEkMQRLEIAHQMLKKVGLEGAEKRYI----WQLSGGQRQRVGIARALA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 123755092 171 IEPEIILMDEPCSALDPIStlkiEETMHELKMNY------TIIIVTHNMQQAL 217
Cdd:PRK11248 145 ANPQLLLLDEPFGALDAFT----REQMQTLLLKLwqetgkQVLLITHDIEEAV 193
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
12-221 |
2.69e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 89.83 E-value: 2.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 12 IILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNrmNDLIPNCslkGTVLFDGTNIydKRVDPVE 91
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALS--GELSPDS---GEVRLNGRPL--ADWSPAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 92 VRRRIGMVFQQPN-PFPKSIYENIAFGARINGFTGDMD-ELVESSLRKAALWDeckdkLNDSGY-SLSGGQQQRLCIART 168
Cdd:PRK13548 74 LARRRAVLPQHSSlSFPFTVEEVVAMGRAPHGLSRAEDdALVAAALAQVDLAH-----LAGRDYpQLSGGEQQRVQLARV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123755092 169 IA------IEPEIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHNMQQALRVSD 221
Cdd:PRK13548 149 LAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLahERGLAVIVVLHDLNLAARYAD 209
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
14-219 |
3.83e-21 |
|
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: 92.50 E-value: 3.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYG-TFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDlipncSLKGTVLFDGTNIYDkrVDPVEV 92
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQ-----ARSGEILLNGFSLKD--IDRHTL 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 93 RRRIGMVFQQPNPFPKSIYENIAFGARINGFTGDMDELVESslrkAALWDECKD-------KLNDSGYSLSGGQQQRLCI 165
Cdd:TIGR01193 547 RQFINYLPQEPYIFSGSILENLLLGAKENVSQDEIWAACEI----AEIKDDIENmplgyqtELSEEGSSISGGQKQRIAL 622
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 123755092 166 ARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKmNYTIIIVTHNMQQALRV 219
Cdd:TIGR01193 623 ARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQ-DKTIIFVAHRLSVAKQS 675
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-262 |
6.96e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 91.69 E-value: 6.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGTFEAVRNVFCNF----KKGNITSLIGPSGCGKSTVLRSLNRMNDLIPNCSLKGTVLFDGTNIYDkrVD 88
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVRTVVNDVslqiEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGESLLH--AS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 89 PVEVRR----RIGMVFQQP----NPF---PKSIYENIAF--GARINGFTGDM-DELVESSLRKAAlwdeckDKLNDSGYS 154
Cdd:PRK15134 83 EQTLRGvrgnKIAMIFQEPmvslNPLhtlEKQLYEVLSLhrGMRREAARGEIlNCLDRVGIRQAA------KRLTDYPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 155 LSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELK--MNYTIIIVTHNMQQALRVSDMTAFFNAveye 232
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQqeLNMGLLFITHNLSIVRKLADRVAVMQN---- 232
|
250 260 270
....*....|....*....|....*....|
gi 123755092 233 dgdggkvGYLAEFNSTKKIFNSPKEKTTQE 262
Cdd:PRK15134 233 -------GRCVEQNRAATLFSAPTHPYTQK 255
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
14-211 |
1.76e-20 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 89.13 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISY-GTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRS---LNRMNDlipncslkGTVLFDgtniyDKRVDP 89
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMvagLERITS--------GEIWIG-----GRVVNE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 90 VEVRRR-IGMVFQQPNPFPK-SIYENIAFGARINGFtgDMDElVESSLRKAALWDECKDKLNDSGYSLSGGQQQRLCIAR 167
Cdd:PRK11650 71 LEPADRdIAMVFQNYALYPHmSVRENMAYGLKIRGM--PKAE-IEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 123755092 168 TIAIEPEIILMDEPCSALDPistlKIEETMH-ELK-----MNYTIIIVTH 211
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLDA----KLRVQMRlEIQrlhrrLKTTSLYVTH 193
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
14-225 |
3.80e-20 |
|
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: 85.68 E-value: 3.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVfcNFKKGNITSLIGPSGCGKSTVLrslNRMNDLIPNCSlkGTVLFDGTNIydKRVDPVevR 93
Cdd:TIGR01277 1 LALDKVRYEYEHLPMEFDL--NVADGEIVAIMGPSGAGKSTLL---NLIAGFIEPAS--GSIKVNDQSH--TGLAPY--Q 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 94 RRIGMVFQQPNPFPK-SIYENIAFGARIN-GFTGDMDELVESSLRKAALwDECKDKLNDSgysLSGGQQQRLCIARTIAI 171
Cdd:TIGR01277 70 RPVSMLFQENNLFAHlTVRQNIGLGLHPGlKLNAEQQEKVVDAAQQVGI-ADYLDRLPEQ---LSGGQRQRVALARCLVR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123755092 172 EPEIILMDEPCSALDP---------ISTLKIEETMhelkmnyTIIIVTHNMQQALRVSDMTAF 225
Cdd:TIGR01277 146 PNPILLLDEPFSALDPllreemlalVKQLCSERQR-------TLLMVTHHLSDARAIASQIAV 201
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
13-221 |
3.89e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 86.49 E-value: 3.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTvlrSLNRMNDLIPNCSlkGTVLFDGTNIydkRVDPVEV 92
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTT---TFYMVVGIVPRDA--GNIIIDDEDI---SLLPLHA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 93 RRR--IGMVFQQPNPFPK-SIYENIAFGARINgftgdmDELVESSLRKAA--LWDECK-DKLNDS-GYSLSGGQQQRLCI 165
Cdd:PRK10895 75 RARrgIGYLPQEASIFRRlSVYDNLMAVLQIR------DDLSAEQREDRAneLMEEFHiEHLRDSmGQSLSGGERRRVEI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 123755092 166 ARTIAIEPEIILMDEPCSALDPISTLKIEETMHELK-MNYTIIIVTHNMQQALRVSD 221
Cdd:PRK10895 149 ARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVRETLAVCE 205
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
14-211 |
4.52e-20 |
|
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: 89.33 E-value: 4.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISY--GTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSlnrMNDLIPNCSlkGTVLFDGTNIydKRVDPVE 91
Cdd:TIGR01842 317 LSVENVTIVPpgGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARL---IVGIWPPTS--GSVRLDGADL--KQWDRET 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 92 VRRRIGMVFQQPNPFPKSIYENIA-FGARIngftgDMDELVESSlrKAA--------LWDECKDKLNDSGYSLSGGQQQR 162
Cdd:TIGR01842 390 FGKHIGYLPQDVELFPGTVAENIArFGENA-----DPEKIIEAA--KLAgvhelilrLPDGYDTVIGPGGATLSGGQRQR 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 123755092 163 LCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKM-NYTIIIVTH 211
Cdd:TIGR01842 463 IALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKArGITVVVITH 512
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
34-227 |
4.91e-20 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 89.70 E-value: 4.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 34 CNFKKgnITSLIGPSGCGKSTVLRSLNRMNDLI--------------------------PNCSLK--------------- 72
Cdd:PTZ00265 1191 CDSKK--TTAIVGETGSGKSTVMSLLMRFYDLKndhhivfknehtndmtneqdyqgdeeQNVGMKnvnefsltkeggsge 1268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 73 --------GTVLFDGTNIYDKRVDpvEVRRRIGMVFQQPNPFPKSIYENIAFG---------ARINGFTGdMDELVESsl 135
Cdd:PTZ00265 1269 dstvfknsGKILLDGVDICDYNLK--DLRNLFSIVSQEPMLFNMSIYENIKFGkedatredvKRACKFAA-IDEFIES-- 1343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 136 rkaaLWDECKDKLNDSGYSLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHNM 213
Cdd:PTZ00265 1344 ----LPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRI 1419
|
250
....*....|....
gi 123755092 214 qQALRVSDMTAFFN 227
Cdd:PTZ00265 1420 -ASIKRSDKIVVFN 1432
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
10-224 |
5.05e-20 |
|
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: 89.09 E-value: 5.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 10 KNIILSLENVSISY-----GTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLnrMNDLIPNcslKGTVLF----DGT 80
Cdd:TIGR03269 276 GEPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKII--AGVLEPT---SGEVNVrvgdEWV 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 81 NIYDKRVDPV-EVRRRIGMVFQQPNPFP-KSIYENI--AFGARINGFTGDMDELVessLRKAALWDECKDK--LNDSGYS 154
Cdd:TIGR03269 351 DMTKPGPDGRgRAKRYIGILHQEYDLYPhRTVLDNLteAIGLELPDELARMKAVI---TLKMVGFDEEKAEeiLDKYPDE 427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123755092 155 LSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELK--MNYTIIIVTHNMQQALRVSDMTA 224
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAReeMEQTFIIVSHDMDFVLDVCDRAA 499
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
13-211 |
5.64e-20 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 85.54 E-value: 5.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGT----FEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNrMNDLIPNcslkGTVLFDGTNI----YD 84
Cdd:NF038007 1 MLNMQNAEKCYITktikTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIG-MFDSLDS----GSLTLAGKEVtnlsYS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 85 KRVdpvEVRRR-IGMVFQQPNPFPK-SIYENIAFGARINGFTgdMDELVESSLRKAALWDeCKDKLNDSGYSLSGGQQQR 162
Cdd:NF038007 76 QKI---ILRRElIGYIFQSFNLIPHlSIFDNVALPLKYRGVA--KKERIERVNQVLNLFG-IDNRRNHKPMQLSGGQQQR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 123755092 163 LCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL-KMNYTIIIVTH 211
Cdd:NF038007 150 VAIARAMVSNPALLLADEPTGNLDSKNARAVLQQLKYInQKGTTIIMVTH 199
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
13-221 |
6.19e-20 |
|
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: 86.40 E-value: 6.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGTFEAVR---------NVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDliPNcslKGTVLFDGTNIY 83
Cdd:TIGR02769 2 LLEVRDVTHTYRTGGLFGakqrapvltNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEK--PA---QGTVSFRGQDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 84 D-KRVDPVEVRRRIGMVFQQ-PNPF-PKSIYENIaFGARINGFTgDMDEL-----VESSLRKAALWDECKDKLNDSgysL 155
Cdd:TIGR02769 77 QlDRKQRRAFRRDVQLVFQDsPSAVnPRMTVRQI-IGEPLRHLT-SLDESeqkarIAELLDMVGLRSEDADKLPRQ---L 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 123755092 156 SGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNYTI--IIVTHNMQQALRVSD 221
Cdd:TIGR02769 152 SGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSFCQ 219
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
16-211 |
6.24e-20 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 88.85 E-value: 6.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 16 LENVSISYGTFEA--VRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDlipncSLKGTVLFDGtnIYDKRVDPVEVR 93
Cdd:TIGR03796 480 LRNITFGYSPLEPplIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQ-----PWSGEILFDG--IPREEIPREVLA 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 94 RRIGMVFQQPNPFPKSIYENIAfgaringftgdmdeLVESSLRKAALWDECKD----------------KLNDSGYSLSG 157
Cdd:TIGR03796 553 NSVAMVDQDIFLFEGTVRDNLT--------------LWDPTIPDADLVRACKDaaihdvitsrpggydaELAEGGANLSG 618
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 123755092 158 GQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHelKMNYTIIIVTH 211
Cdd:TIGR03796 619 GQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLR--RRGCTCIIVAH 670
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-221 |
1.18e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 86.81 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 11 NIILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNdlipnCSLKGTVLFDGTNIYDK-RVdp 89
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMT-----SPDAGKITVLGVPVPARaRL-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 90 veVRRRIGMVFQQPNPFPK-SIYEN-IAFGARINGFTGDMDELVESSLRKAALWDECKDKLNDsgysLSGGQQQRLCIAR 167
Cdd:PRK13536 112 --ARARIGVVPQFDNLDLEfTVRENlLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSD----LSGGMKRRLTLAR 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 123755092 168 TIAIEPEIILMDEPCSALDPISTLKIEETMHE-LKMNYTIIIVTHNMQQALRVSD 221
Cdd:PRK13536 186 ALINDPQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAERLCD 240
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
39-219 |
1.39e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 87.86 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 39 GNITSLIGPSGCGKSTVLRSLNRMNDliPNcslKGTVLFDGTNIydKRVDPVEVRRRIGMVFQQPNPFPKSIYENIAFGa 118
Cdd:TIGR00958 507 GEVVALVGPSGSGKSTVAALLQNLYQ--PT---GGQVLLDGVPL--VQYDHHYLHRQVALVGQEPVLFSGSVRENIAYG- 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 119 ringFTGDMDELVESSLRKAALWD-----------ECKDKlndsGYSLSGGQQQRLCIARTIAIEPEIILMDEPCSALDp 187
Cdd:TIGR00958 579 ----LTDTPDEEIMAAAKAANAHDfimefpngydtEVGEK----GSQLSGGQKQRIAIARALVRKPRVLILDEATSALD- 649
|
170 180 190
....*....|....*....|....*....|....*..
gi 123755092 188 istLKIEETMHELKMNY--TIIIVTHNM---QQALRV 219
Cdd:TIGR00958 650 ---AECEQLLQESRSRAsrTVLLIAHRLstvERADQI 683
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-212 |
2.44e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 87.19 E-value: 2.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 3 KTNKKTPKNIILSLENVSISY--GTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDliPNCslkGTVLFDGT 80
Cdd:PRK11160 328 TTSTAAADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWD--PQQ---GEILLNGQ 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 81 NIYDkrVDPVEVRRRIGMVFQQPNPFPKSIYENIAFGAringFTGDMDELVESsLRKAALWD--ECKDKLN----DSGYS 154
Cdd:PRK11160 403 PIAD--YSEAALRQAISVVSQRVHLFSATLRDNLLLAA----PNASDEALIEV-LQQVGLEKllEDDKGLNawlgEGGRQ 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 123755092 155 LSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTHN 212
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHR 533
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-218 |
2.89e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 84.37 E-value: 2.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISY--GTFE---AVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNrmNDLIPNcslKGTVLFDGTNIYDKrv 87
Cdd:COG1101 1 MLELKNLSKTFnpGTVNekrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIA--GSLPPD---SGSILIDGKDVTKL-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 88 dPVEVR-RRIGMVFQqpNPF----PK-SIYENIA--------FGARInGFTGDMDELVESSLRKAALWDEckDKLNDSGY 153
Cdd:COG1101 74 -PEYKRaKYIGRVFQ--DPMmgtaPSmTIEENLAlayrrgkrRGLRR-GLTKKRRELFRELLATLGLGLE--NRLDTKVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 123755092 154 SLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHNMQQALR 218
Cdd:COG1101 148 LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNMEQALD 214
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
13-221 |
4.89e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 84.47 E-value: 4.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNdlIPNCslkGTVLFDGTNIYDKrvdPVEV 92
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLT--HPDA---GSISLCGEPVPSR---ARHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 93 RRRIGMVFQQPNPFPK-SIYENIAFGARINGFT-GDMDELVESSLRKAALWDECKDKLNDsgysLSGGQQQRLCIARTIA 170
Cdd:PRK13537 79 RQRVGVVPQFDNLDPDfTVRENLLVFGRYFGLSaAAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 123755092 171 IEPEIILMDEPCSALDPISTLKIEETMHEL-KMNYTIIIVTHNMQQALRVSD 221
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMWERLRSLlARGKTILLTTHFMEEAERLCD 206
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
12-213 |
7.78e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 83.58 E-value: 7.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 12 IILSLENVSISYGTF---------EAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDliPNcslKGTVLFDGTNI 82
Cdd:PRK10419 2 TLLNVSGLSHHYAHGglsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLES--PS---QGNVSWRGEPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 83 YD-KRVDPVEVRRRIGMVFQQP----NPfPKSIYENIAFGARingFTGDMDEL-----VESSLRKAALWDECKDKLNDSg 152
Cdd:PRK10419 77 AKlNRAQRKAFRRDIQMVFQDSisavNP-RKTVREIIREPLR---HLLSLDKAerlarASEMLRAVDLDDSVLDKRPPQ- 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123755092 153 ysLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNYTI--IIVTHNM 213
Cdd:PRK10419 152 --LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDL 212
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
28-265 |
1.38e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 84.91 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 28 AVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDlipncSLKGTVLFDGTNI---YDKRVDPVevRRRIGMVFQQP- 103
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVE-----SQGGEIIFNGQRIdtlSPGKLQAL--RRDIQFIFQDPy 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 104 ---NPfPKSIYENIAFGARINGF-TGD-MDELVESSLRKAALWDECKDKLNdsgYSLSGGQQQRLCIARTIAIEPEIILM 178
Cdd:PRK10261 412 aslDP-RQTVGDSIMEPLRVHGLlPGKaAAARVAWLLERVGLLPEHAWRYP---HEFSGGQRQRICIARALALNPKVIIA 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 179 DEPCSALDPISTLKIEETMHELKMNYTI--IIVTHNMQQALRVSDMTaffnAVEYedgdggkVGYLAEFNSTKKIFNSPK 256
Cdd:PRK10261 488 DEAVSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERISHRV----AVMY-------LGQIVEIGPRRAVFENPQ 556
|
....*....
gi 123755092 257 EKTTQEYIS 265
Cdd:PRK10261 557 HPYTRKLMA 565
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
28-211 |
1.99e-18 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 84.38 E-value: 1.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 28 AVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDLIpncslKGTVLFDGTNIYDKRVDpvEVRRRIGMVFQQPNPFP 107
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVS-----EGDIRFHDIPLTKLQLD--SWRSRLAVVSQTPFLFS 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 108 KSIYENIAFGAringfTGDMDELVESSLRKAALWDEC-------KDKLNDSGYSLSGGQQQRLCIARTIAIEPEIILMDE 180
Cdd:PRK10789 403 DTVANNIALGR-----PDATQQEIEHVARLASVHDDIlrlpqgyDTEVGERGVMLSGGQKQRISIARALLLNAEILILDD 477
|
170 180 190
....*....|....*....|....*....|.
gi 123755092 181 PCSALDPISTLKIEETMHELKMNYTIIIVTH 211
Cdd:PRK10789 478 ALSAVDGRTEHQILHNLRQWGEGRTVIISAH 508
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
31-211 |
2.99e-18 |
|
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: 80.78 E-value: 2.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 31 NVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDLIPNCSlkGTVLFDGtniydKRVDPVEVRRRIGMVFQQPNPFPK-S 109
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTS--GQILFNG-----QPRKPDQFQKCVAYVRQDDILLPGlT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 110 IYENIAFGARINgftgdMDELVESSLRKAALWDECKDKLNDS---GY---SLSGGQQQRLCIARTIAIEPEIILMDEPCS 183
Cdd:cd03234 98 VRETLTYTAILR-----LPRKSSDAIRKKRVEDVLLRDLALTrigGNlvkGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180
....*....|....*....|....*....
gi 123755092 184 ALDPISTLKIEETMHEL-KMNYTIIIVTH 211
Cdd:cd03234 173 GLDSFTALNLVSTLSQLaRRNRIVILTIH 201
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
14-187 |
3.97e-18 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 81.32 E-value: 3.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRmnDLIPNcslKGTVLFDGTNIydKRVDPVEVR 93
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTG--ELTPS---SGEVRLNGRPL--AAWSPWELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 94 RRIGMVFQQPN-PFPKSIYENIAFGaRINGFTG--DMDELVESSLRKAALWDeckdkLNDSGY-SLSGGQQQRLCIARTI 169
Cdd:COG4559 75 RRRAVLPQHSSlAFPFTVEEVVALG-RAPHGSSaaQDRQIVREALALVGLAH-----LAGRSYqTLSGGEQQRVQLARVL 148
|
170 180
....*....|....*....|....*
gi 123755092 170 A-------IEPEIILMDEPCSALDP 187
Cdd:COG4559 149 AqlwepvdGGPRWLFLDEPTSALDL 173
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-224 |
5.95e-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: 83.52 E-value: 5.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 28 AVRNVFCNFKKGNITSLIGPSGCGKSTvlrSLNRMNDLIPNCSlkGTVLFDGTNIyDKRVDPVevRRRIGMVFQQPNPFP 107
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTT---TLSILTGLLPPTS--GTVLVGGKDI-ETNLDAV--RQSLGMCPQHNILFH 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 108 K-SIYENIAFGARINGFTGDMDEL-VESSLRKAALwdecKDKLNDSGYSLSGGQQQRLCIARTIAIEPEIILMDEPCSAL 185
Cdd:TIGR01257 1017 HlTVAEHILFYAQLKGRSWEEAQLeMEAMLEDTGL----HHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGV 1092
|
170 180 190
....*....|....*....|....*....|....*....
gi 123755092 186 DPISTLKIEETMHELKMNYTIIIVTHNMQQALRVSDMTA 224
Cdd:TIGR01257 1093 DPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIA 1131
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
13-221 |
6.66e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.77 E-value: 6.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVlrslnrMNDLI----PNcslKGTVLFDGtniydKRV- 87
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTL------MKILYglyqPD---SGEILIDG-----KPVr 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 88 --DPVEVRRR-IGMVFQQPNPFPK-SIYENIAFGaringftgdMDELVESSLRKAALWDECKDKLNDSG---------YS 154
Cdd:COG3845 71 irSPRDAIALgIGMVHQHFMLVPNlTVAENIVLG---------LEPTKGGRLDRKAARARIRELSERYGldvdpdakvED 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 123755092 155 LSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELK-MNYTIIIVTHNMQQALRVSD 221
Cdd:COG3845 142 LSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAaEGKSIIFITHKLREVMAIAD 209
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
37-223 |
7.18e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 80.01 E-value: 7.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 37 KKGNITSLIGPSGCGKSTVLrslNRMNDLIPNCSlkGTVLFDGTNiyDKRVDPVevRRRIGMVFQQPNPFPK-SIYENIA 115
Cdd:PRK10771 23 ERGERVAILGPSGAGKSTLL---NLIAGFLTPAS--GSLTLNGQD--HTTTPPS--RRPVSMLFQENNLFSHlTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 116 FGA----RINGftgDMDELVESSLRKAALwDECKDKLNDSgysLSGGQQQRLCIARTIAIEPEIILMDEPCSALDP---- 187
Cdd:PRK10771 94 LGLnpglKLNA---AQREKLHAIARQMGI-EDLLARLPGQ---LSGGQRQRVALARCLVREQPILLLDEPFSALDPalrq 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 123755092 188 -ISTLkIEETMHELKMnyTIIIVTHNMQQALRVSDMT 223
Cdd:PRK10771 167 eMLTL-VSQVCQERQL--TLLMVSHSLEDAARIAPRS 200
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
13-221 |
8.01e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 80.42 E-value: 8.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLrslnrmndlipNC------SLKGTVLFDGTNIYDKr 86
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVF-----------NCltgfykPTGGTILLRGQHIEGL- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 87 vdPVEVRRRIGMV--FQQPNPFPK-SIYEN--IAFGARINgfTGDMDELVES---------SLRKAALWDE---CKDKLN 149
Cdd:PRK11300 73 --PGHQIARMGVVrtFQHVRLFREmTVIENllVAQHQQLK--TGLFSGLLKTpafrraeseALDRAATWLErvgLLEHAN 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 123755092 150 DSGYSLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNY--TIIIVTHNMQQALRVSD 221
Cdd:PRK11300 149 RQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGISD 222
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
14-221 |
1.29e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 81.43 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNrmNDLIPNCslkGTVLFDGTNIydKRVDPVEVR 93
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAIN--GTLTPTA---GTVLVAGDDV--EALSARAAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 94 RRIGMVFQQPN-PFPKSIYENIAFG-----ARINGFTGDMDELVESSLRKAALwDECKDKLNDSgysLSGGQQQRLCIAR 167
Cdd:PRK09536 77 RRVASVPQDTSlSFEFDVRQVVEMGrtphrSRFDTWTETDRAAVERAMERTGV-AQFADRPVTS---LSGGERQRVLLAR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 123755092 168 TIAIEPEIILMDEPCSALD---PISTLKIEETMHElkMNYTIIIVTHNMQQALRVSD 221
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDinhQVRTLELVRRLVD--DGKTAVAAIHDLDLAARYCD 207
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
23-214 |
1.33e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 79.30 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 23 YGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNcslKGTVLFDGTNIYDKRvdpVEVRRRIGMVFQQ 102
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGL--LQPT---SGEVRVAGLVPWKRR---KKFLRRIGVVFGQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 103 PNP--FPKSIYENIAFGARING-----FTGDMDELVEsslrkaALwdECKDKLNDSGYSLSGGQQQRLCIARTIAIEPEI 175
Cdd:cd03267 103 KTQlwWDLPVIDSFYLLAAIYDlpparFKKRLDELSE------LL--DLEELLDTPVRQLSLGQRMRAEIAAALLHEPEI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 123755092 176 ILMDEPCSALDPISTLKIEETMHELKMNY--TIIIVTHNMQ 214
Cdd:cd03267 175 LFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMK 215
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
35-215 |
5.91e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 80.27 E-value: 5.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 35 NF--KKGNITSLIGPSGCGKStvlrSLnrMNDLIPNCSLKGTVLFDGTNIydKRVDPVEVRRRIGMVFQQPNPFPKSIYE 112
Cdd:PRK11174 370 NFtlPAGQRIALVGPSGAGKT----SL--LNALLGFLPYQGSLKINGIEL--RELDPESWRKHLSWVGQNPQLPHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 113 NIAFGAringftGDM-DELVESSLRKAALWDECKDKLN-------DSGYSLSGGQQQRLCIARTIAIEPEIILMDEPCSA 184
Cdd:PRK11174 442 NVLLGN------PDAsDEQLQQALENAWVSEFLPLLPQgldtpigDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTAS 515
|
170 180 190
....*....|....*....|....*....|.
gi 123755092 185 LDPISTLKIEETMHELKMNYTIIIVTHNMQQ 215
Cdd:PRK11174 516 LDAHSEQLVMQALNAASRRQTTLMVTHQLED 546
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
41-221 |
6.75e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 79.15 E-value: 6.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 41 ITSLIGPSGCGKSTVLrslNRMNDLI-PNC---SLKGTVLFD---GTNIydkrvdPVEvRRRIGMVFQQPNPFPK-SIYE 112
Cdd:PRK11144 26 ITAIFGRSGAGKTSLI---NAISGLTrPQKgriVLNGRVLFDaekGICL------PPE-KRRIGYVFQDARLFPHyKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 113 NIAFGARiNGFTGDMDELVESsLRKAALwdeckdkLNDSGYSLSGGQQQRLCIARTIAIEPEIILMDEPCSALD-Pistl 191
Cdd:PRK11144 96 NLRYGMA-KSMVAQFDKIVAL-LGIEPL-------LDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlP---- 162
|
170 180 190
....*....|....*....|....*....|....*
gi 123755092 192 KIEETMHEL-----KMNYTIIIVTHNMQQALRVSD 221
Cdd:PRK11144 163 RKRELLPYLerlarEINIPILYVSHSLDEILRLAD 197
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
14-212 |
1.06e-16 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 76.03 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLnrMNDLIPNCSlKGTVLFDGTNIYDKrvdPVEVR 93
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTI--MGHPKYEVT-EGEILFKGEDITDL---PPEER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 94 RR--IGMVFQQPNPFPksiyeniafGARINGFTGDMDElvesslrkaalwdeckdklndsgySLSGGQQQRLCIARTIAI 171
Cdd:cd03217 75 ARlgIFLAFQYPPEIP---------GVKNADFLRYVNE------------------------GFSGGEKKRNEILQLLLL 121
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 123755092 172 EPEIILMDEPCSALDpISTLK-IEETMHELK-MNYTIIIVTHN 212
Cdd:cd03217 122 EPDLAILDEPDSGLD-IDALRlVAEVINKLReEGKSVLIITHY 163
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
13-219 |
1.30e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 79.38 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISY----GTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVlrslnrMNdlIPNCSLK---GTVLFDGTNIYDK 85
Cdd:PRK10535 4 LLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTL------MN--ILGCLDKptsGTYRVAGQDVATL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 86 RVDPVEVRRR--IGMVFQQPNPFPK-SIYENIAFGARINGFtgdmdELVESSLRKAALWDEC--KDKLNDSGYSLSGGQQ 160
Cdd:PRK10535 76 DADALAQLRRehFGFIFQRYHLLSHlTAAQNVEVPAVYAGL-----ERKQRLLRAQELLQRLglEDRVEYQPSQLSGGQQ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123755092 161 QRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELK-MNYTIIIVTHNMQ---QALRV 219
Cdd:PRK10535 151 QRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQvaaQAERV 213
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
14-253 |
1.45e-16 |
|
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: 76.28 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNcslKGTVLFDGTNIYDKRVdpvevr 93
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGI--LRPT---SGEIIFDGHPWTRKDL------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 94 RRIGMVFQQPnpfpkSIYENIAfgARIN-----GFTGDMDELVESSLRKAALWDECKDKLNDsgysLSGGQQQRLCIART 168
Cdd:TIGR03740 70 HKIGSLIESP-----PLYENLT--ARENlkvhtTLLGLPDSRIDEVLNIVDLTNTGKKKAKQ----FSLGMKQRLGIAIA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 169 IAIEPEIILMDEPCSALDPISTLKIEETMHELKMN-YTIIIVTHNMQQALRVSDMTAFFNaveyedgdGGKVGYLAEFNS 247
Cdd:TIGR03740 139 LLNHPKLLILDEPTNGLDPIGIQELRELIRSFPEQgITVILSSHILSEVQQLADHIGIIS--------EGVLGYQGKINK 210
|
....*....
gi 123755092 248 T---KKIFN 253
Cdd:TIGR03740 211 SenlEKLFV 219
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-214 |
2.06e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.59 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISY-----------GTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRmndLIPNcslKGTVLFDGTN 81
Cdd:PRK15134 275 LLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLR---LINS---QGEIWFDGQP 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 82 IYD-KRVDPVEVRRRIGMVFQQPNPF--PK-SIYENIAFGARINGFT---GDMDELVESSLRKAALWDECKDKlndsgY- 153
Cdd:PRK15134 349 LHNlNRRQLLPVRHRIQVVFQDPNSSlnPRlNVLQIIEEGLRVHQPTlsaAQREQQVIAVMEEVGLDPETRHR-----Yp 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 123755092 154 -SLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNYTI--IIVTHNMQ 214
Cdd:PRK15134 424 aEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLH 487
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
13-265 |
3.31e-16 |
|
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: 76.02 E-value: 3.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNrmNDLIPNcslKGTVLFDgtniyDKRVDPVEV 92
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLA--GRLAPD---HGTATYI-----MRSGAELEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 93 -------RRRI-----GMVFQQPNPFPK---SIYENI-----AFGARingFTGDMDELVESSLRKAALwdeCKDKLNDSG 152
Cdd:TIGR02323 73 yqlseaeRRRLmrtewGFVHQNPRDGLRmrvSAGANIgerlmAIGAR---HYGNIRATAQDWLEEVEI---DPTRIDDLP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 153 YSLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHNMQQALRVSDMTAFFnave 230
Cdd:TIGR02323 147 RAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLvrDLGLAVIIVTHDLGVARLLAQRLLVM---- 222
|
250 260 270
....*....|....*....|....*....|....*
gi 123755092 231 yedgdggKVGYLAEFNSTKKIFNSPKEKTTQEYIS 265
Cdd:TIGR02323 223 -------QQGRVVESGLTDQVLDDPQHPYTQLLVS 250
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
8-261 |
3.77e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 77.97 E-value: 3.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 8 TPKNIILSLENVSISY----GTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDLIPNCSLKGTVLFDGTN-- 81
Cdd:PRK10261 7 LDARDVLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 82 -IYDKRVDPVEVRR----RIGMVFQQP----NP-FPksIYENIAFGARINGFTGDMDELVESS-LRKAALWDECKDKLND 150
Cdd:PRK10261 87 vIELSEQSAAQMRHvrgaDMAMIFQEPmtslNPvFT--VGEQIAESIRLHQGASREEAMVEAKrMLDQVRIPEAQTILSR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 151 SGYSLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELK--MNYTIIIVTHNMQQALRVSDMTaffnA 228
Cdd:PRK10261 165 YPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQkeMSMGVIFITHDMGVVAEIADRV----L 240
|
250 260 270
....*....|....*....|....*....|...
gi 123755092 229 VEYEdgdggkvGYLAEFNSTKKIFNSPKEKTTQ 261
Cdd:PRK10261 241 VMYQ-------GEAVETGSVEQIFHAPQHPYTR 266
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
24-265 |
4.34e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 76.54 E-value: 4.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 24 GTFEAVRNVFCNFKKGNITSLIGPSGCGKSTvlrsLNRMNDLIPNCSlKGTVLFDGTNIydKRVDPVEV---RRRIGMVF 100
Cdd:PRK11308 26 RLVKALDGVSFTLERGKTLAVVGESGCGKST----LARLLTMIETPT-GGELYYQGQDL--LKADPEAQkllRQKIQIVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 101 QQP----NPFPK--SIYE-----NIAFGARingftgDMDELVESSLRKAALWDECKDKlndsgYS--LSGGQQQRLCIAR 167
Cdd:PRK11308 99 QNPygslNPRKKvgQILEeplliNTSLSAA------ERREKALAMMAKVGLRPEHYDR-----YPhmFSGGQRQRIAIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 168 TIAIEPEIILMDEPCSALDPISTLKIEETM----HELKMNYTIIivTHNMQQALRVSD--MTAFFnaveyedgdggkvGY 241
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALDVSVQAQVLNLMmdlqQELGLSYVFI--SHDLSVVEHIADevMVMYL-------------GR 232
|
250 260
....*....|....*....|....
gi 123755092 242 LAEFNSTKKIFNSPKEKTTQEYIS 265
Cdd:PRK11308 233 CVEKGTKEQIFNNPRHPYTQALLS 256
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
14-186 |
5.85e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 75.26 E-value: 5.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSIS--YGTFEAVrnvfcnFKKGNITSLIGPSGCGKSTVlrsLNRMNDLIPNcslKGTVLFDGTNIYDkrVDPVE 91
Cdd:COG4138 1 LQLNDVAVAgrLGPISAQ------VNAGELIHLIGPNGAGKSTL---LARMAGLLPG---QGEILLNGRPLSD--WSAAE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 92 VRRRIGMVFQQ-PNPFPKSIYENIAFGARINGFTGDMDELVESSLRKAALwdecKDKLNDSGYSLSGGQQQRLCIARTI- 169
Cdd:COG4138 67 LARHRAYLSQQqSPPFAMPVFQYLALHQPAGASSEAVEQLLAQLAEALGL----EDKLSRPLTQLSGGEWQRVRLAAVLl 142
|
170 180
....*....|....*....|...
gi 123755092 170 ----AIEPE--IILMDEPCSALD 186
Cdd:COG4138 143 qvwpTINPEgqLLLLDEPMNSLD 165
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
10-265 |
6.69e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 76.28 E-value: 6.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 10 KNIILSLENVSISYG-------------TFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRmndLIPNCSlkGTVL 76
Cdd:PRK15079 5 KKVLLEVADLKVHFDikdgkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIG---LVKATD--GEVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 77 FDGTNIYD-KRVDPVEVRRRIGMVFQQP----NPfPKSIYENIAFGARIngFTGDMD-----ELVESSLRKAALwdeCKD 146
Cdd:PRK15079 80 WLGKDLLGmKDDEWRAVRSDIQMIFQDPlaslNP-RMTIGEIIAEPLRT--YHPKLSrqevkDRVKAMMLKVGL---LPN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 147 KLNDSGYSLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELK--MNYTIIIVTHNMQQALRVSDMTa 224
Cdd:PRK15079 154 LINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQreMGLSLIFIAHDLAVVKHISDRV- 232
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 123755092 225 ffnAVEYedgdggkVGYLAEFNSTKKIFNSPKEKTTQEYIS 265
Cdd:PRK15079 233 ---LVMY-------LGHAVELGTYDEVYHNPLHPYTKALMS 263
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
31-214 |
7.79e-16 |
|
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: 74.29 E-value: 7.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 31 NVFCNFKKGNITSLIGPSGCGKSTVLRS-LNRMNdlipncSLKGTVLFDGTNIYDKRVDPVEVRRRIGMVF--QQPNPFP 107
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAiLGEMQ------TLEGKVHWSNKNESEPSFEATRSRNRYSVAYaaQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 108 KSIYENIAFGARINgftgdmdelvesSLRKAALWDEC-------------KDKLNDSGYSLSGGQQQRLCIARTIAIEPE 174
Cdd:cd03290 93 ATVEENITFGSPFN------------KQRYKAVTDACslqpdidllpfgdQTEIGERGINLSGGQRQRICVARALYQNTN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 123755092 175 IILMDEPCSALD-PISTLKIEETMHELKMN--YTIIIVTHNMQ 214
Cdd:cd03290 161 IVFLDDPFSALDiHLSDHLMQEGILKFLQDdkRTLVLVTHKLQ 203
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
22-218 |
2.41e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 72.27 E-value: 2.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 22 SYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPncsLKGTVlfdgtniydkRVDPvevRRRIGMVFQ 101
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGV--LRP---TSGTV----------RRAG---GARVAYVPQ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 102 Q---PNPFPKSIYENIAFG--ARINGF---TGDMDELVESSLRKAALWDECKDKLNdsgySLSGGQQQRLCIARTIAIEP 173
Cdd:NF040873 63 RsevPDSLPLTVRDLVAMGrwARRGLWrrlTRDDRAAVDDALERVGLADLAGRQLG----ELSGGQRQRALLAQGLAQEA 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 123755092 174 EIILMDEPCSALDPISTLKIEETM-HELKMNYTIIIVTHNMQQALR 218
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRR 184
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
14-261 |
3.33e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 73.20 E-value: 3.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSIsYGTFEAVRNVFCNFKKGNITSLIGPSGCGKS-TVLRSLnrmnDLIPN--CSLKGTVLFDGtniydKRVDPV 90
Cdd:PRK10418 5 IELRNIAL-QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAAL----GILPAgvRQTAGRVLLDG-----KPVAPC 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 91 EVR-RRIGMVFQQP----NPFpksiyENIAFGAR----INGFTGDMDELVESsLRKAALwDECKDKLNDSGYSLSGGQQQ 161
Cdd:PRK10418 75 ALRgRKIATIMQNPrsafNPL-----HTMHTHARetclALGKPADDATLTAA-LEAVGL-ENAARVLKLYPFEMSGGMLQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 162 RLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHNMQQALRVSDMTAFFNAveyedgdggkv 239
Cdd:PRK10418 148 RMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvqKRALGMLLVTHDMGVVARLADDVAVMSH----------- 216
|
250 260
....*....|....*....|..
gi 123755092 240 GYLAEFNSTKKIFNSPKEKTTQ 261
Cdd:PRK10418 217 GRIVEQGDVETLFNAPKHAVTR 238
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
11-225 |
4.94e-15 |
|
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: 72.08 E-value: 4.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 11 NIILSLENVSISY------G-TFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRmNDLiPNcslKGTVLF--DGTN 81
Cdd:COG4778 2 TTLLEVENLSKTFtlhlqgGkRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG-NYL-PD---SGSILVrhDGGW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 82 IYDKRVDPVEV----RRRIGMVFQqpnpFPKSI-----YENIAFGARINGftgdMDElvESSLRKAA-----------LW 141
Cdd:COG4778 77 VDLAQASPREIlalrRRTIGYVSQ----FLRVIprvsaLDVVAEPLLERG----VDR--EEARARARellarlnlperLW 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 142 DeckdklndsgysL-----SGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNYTIII-VTHN--- 212
Cdd:COG4778 147 D------------LppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDeev 214
|
250
....*....|....
gi 123755092 213 MQQ-ALRVSDMTAF 225
Cdd:COG4778 215 REAvADRVVDVTPF 228
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
13-215 |
5.24e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 72.42 E-value: 5.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISY----------------------GTFEAVRNVfcNF--KKGNITSLIGPSGCGKSTVLRSLNRMndLIPN 68
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDV--SFevERGESVGIIGRNGAGKSTLLKLIAGI--LEPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 69 cslKGTVLFDGtniydkRVD-PVEVrrriGMVFQqpnpfPK-SIYENIAFGARINGFTG-DMDELVESSLRKAalwdECK 145
Cdd:COG1134 80 ---SGRVEVNG------RVSaLLEL----GAGFH-----PElTGRENIYLNGRLLGLSRkEIDEKFDEIVEFA----ELG 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123755092 146 DKLNDSGYSLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNY-TIIIVTHNMQQ 215
Cdd:COG1134 138 DFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGrTVIFVSHSMGA 208
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
7-213 |
5.27e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 74.68 E-value: 5.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 7 KTPKNII-LSLENVSISYGT---FEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDlipncSLKGTVLF-DGTN 81
Cdd:PTZ00265 375 KKLKDIKkIQFKNVRFHYDTrkdVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD-----PTEGDIIInDSHN 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 82 IYDkrVDPVEVRRRIGMVFQQPNPFPKSIYENIAFG--------------------------------ARINGFTGDM-- 127
Cdd:PTZ00265 450 LKD--INLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndsqenknkrnscrAKCAGDLNDMsn 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 128 ----DELVEssLRK-----------------------AALWDECKDKLNDSGYSLSGGQQQRLCIARTIAIEPEIILMDE 180
Cdd:PTZ00265 528 ttdsNELIE--MRKnyqtikdsevvdvskkvlihdfvSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDE 605
|
250 260 270
....*....|....*....|....*....|....*
gi 123755092 181 PCSALDPISTLKIEETMHELK--MNYTIIIVTHNM 213
Cdd:PTZ00265 606 ATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRL 640
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
14-211 |
1.46e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 70.47 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPncsLKGTVLFDGTNIYDKRVDPVEVR 93
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGL--LRP---DSGEVRWNGTPLAEQRDEPHENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 94 RRIGmvfQQPNPFPK-SIYENIAFGARINGFTgdmDELVESSLRKAALwdeckdklndSGYS------LSGGQQQRLCIA 166
Cdd:TIGR01189 76 LYLG---HLPGLKPElSALENLHFWAAIHGGA---QRTIEDALAAVGL----------TGFEdlpaaqLSAGQQRRLALA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 123755092 167 RTIAIEPEIILMDEPCSALDPISTLKIEETMHE-LKMNYTIIIVTH 211
Cdd:TIGR01189 140 RLWLSRRPLWILDEPTTALDKAGVALLAGLLRAhLARGGIVLLTTH 185
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
3-213 |
1.71e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 72.06 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 3 KTNKKTPKNIILSLENVSISYGTFE----AVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLnrMNDLIPNCSLKGTVLFD 78
Cdd:PRK09473 2 VPLAQQQADALLDVKDLRVTFSTPDgdvtAVNDLNFSLRAGETLGIVGESGSGKSQTAFAL--MGLLAANGRIGGSATFN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 79 GTNIY---DKRVDPVEVRRrIGMVFQQP----NPFPK---SIYENIAFGARINGftgdmDELVESSLR--KAALWDECKD 146
Cdd:PRK09473 80 GREILnlpEKELNKLRAEQ-ISMIFQDPmtslNPYMRvgeQLMEVLMLHKGMSK-----AEAFEESVRmlDAVKMPEARK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 123755092 147 KLNDSGYSLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELK--MNYTIIIVTHNM 213
Cdd:PRK09473 154 RMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKreFNTAIIMITHDL 222
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
12-211 |
2.22e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 70.37 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 12 IILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRmndLIPNCSLKGTVLFDGTNIYDKRvdpve 91
Cdd:COG2401 29 IVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG---ALKGTPVAGCVDVPDNQFGREA----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 92 vrrrigmvfqqpnpfpkSIYENIafgarinGFTGDMDELVESslrkaalwdeckdkLNDSGYS-----------LSGGQQ 160
Cdd:COG2401 101 -----------------SLIDAI-------GRKGDFKDAVEL--------------LNAVGLSdavlwlrrfkeLSTGQK 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 123755092 161 QRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTH 211
Cdd:COG2401 143 FRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLarRAGITLVVATH 195
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
25-269 |
2.48e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 70.97 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 25 TFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndlIPNCSlkGTVLFDGTNI----YDKRvdpvevRRRIGMVF 100
Cdd:PRK15112 25 TVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGM---IEPTS--GELLIDDHPLhfgdYSYR------SQRIRMIF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 101 QQP----NPfPKSIYENIAFGARING--FTGDMDELVESSLRKAALwdeCKDKLNDSGYSLSGGQQQRLCIARTIAIEPE 174
Cdd:PRK15112 94 QDPstslNP-RQRISQILDFPLRLNTdlEPEQREKQIIETLRQVGL---LPDHASYYPHMLAPGQKQRLGLARALILRPK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 175 IILMDEPCSALDPISTLKIEETMHELKMNYTI--IIVTHNMQQALRVSDMTAFFNAveyedgdggkvGYLAEFNSTKKIF 252
Cdd:PRK15112 170 VIIADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHISDQVLVMHQ-----------GEVVERGSTADVL 238
|
250
....*....|....*..
gi 123755092 253 NSPKEKTTQEYISGKFG 269
Cdd:PRK15112 239 ASPLHELTKRLIAGHFG 255
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
14-240 |
2.57e-14 |
|
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: 72.14 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMND-------------LIPNCSLKGTVLFDGT 80
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyeptsgriiyhvaLCEKCGYVERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 81 NI-------------YDKRVDPV--EVRRRIGMVFQQPNPF--PKSIYENIAFGARINGFTGDmdelvESSLRKAALWDE 143
Cdd:TIGR03269 81 PCpvcggtlepeevdFWNLSDKLrrRIRKRIAIMLQRTFALygDDTVLDNVLEALEEIGYEGK-----EAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 144 CK--DKLNDSGYSLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNY--TIIIVTHNMQQALRV 219
Cdd:TIGR03269 156 VQlsHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEVIEDL 235
|
250 260
....*....|....*....|.
gi 123755092 220 SDmtaffNAVEYEDGDGGKVG 240
Cdd:TIGR03269 236 SD-----KAIWLENGEIKEEG 251
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
9-218 |
3.49e-14 |
|
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: 69.77 E-value: 3.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 9 PKNIILSLENVSISYGTFEAVRNVF--CNF--KKGNITSLIGPSGCGKSTVLR---SLNRmndliPNcslKGTVLFDGTN 81
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTILkgISLevEAGESVAIVGASGSGKSTLLGllaGLDR-----PT---SGTVRLAGQD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 82 IY----DKRVdpvEVRRR-IGMVFQQ----PNpfpKSIYENIAFGARINGfTGDMDELVESSLRKAALwdecKDKLNDSG 152
Cdd:COG4181 76 LFaldeDARA---RLRARhVGFVFQSfqllPT---LTALENVMLPLELAG-RRDARARARALLERVGL----GHRLDHYP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 123755092 153 YSLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNY--TIIIVTHNMQQALR 218
Cdd:COG4181 145 AQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgtTLVLVTHDPALAAR 212
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-221 |
3.72e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 70.42 E-value: 3.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNcslKGTVLFDGTNI-YDKRvDPVE 91
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGL--LRPQ---KGAVLWQGKPLdYSKR-GLLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 92 VRRRIGMVFQQPNP--FPKSIYENIAFGARINGFTGD-----MDE---LVESS-LRKAALwdECkdklndsgysLSGGQQ 160
Cdd:PRK13638 75 LRQQVATVFQDPEQqiFYTDIDSDIAFSLRNLGVPEAeitrrVDEaltLVDAQhFRHQPI--QC----------LSHGQK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123755092 161 QRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL-KMNYTIIIVTHNMQQALRVSD 221
Cdd:PRK13638 143 KRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIvAQGNHVIISSHDIDLIYEISD 204
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
27-234 |
3.78e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 69.84 E-value: 3.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 27 EAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDliPNcslKGTVLFDGTNIYD-KRVDPVEVR-RRIGMVFQQPN 104
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDT--PT---SGDVIFNGQPMSKlSSAAKAELRnQKLGFIYQFHH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 105 PFPK-SIYENIAFGARINGF-TGDMDELVESSLRKAALwdecKDKLNDSGYSLSGGQQQRLCIARTIAIEPEIILMDEPC 182
Cdd:PRK11629 98 LLPDfTALENVAMPLLIGKKkPAEINSRALEMLAAVGL----EHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 123755092 183 SALDPISTLKIEETMHELKMNY--TIIIVTHNMQQALRVSdmtaffNAVEYEDG 234
Cdd:PRK11629 174 GNLDARNADSIFQLLGELNRLQgtAFLVVTHDLQLAKRMS------RQLEMRDG 221
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
13-211 |
3.81e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 70.34 E-value: 3.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRmnDLIPNCslkGTVLFDGTniyDKRVDPV-- 90
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSA--RLAPDA---GEVHYRMR---DGQLRDLya 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 91 --EVRRRI------GMVFQQPNPFPK---SIYENI-----AFGARINGftgdmdelvesSLRKAAL-WDE----CKDKLN 149
Cdd:PRK11701 78 lsEAERRRllrtewGFVHQHPRDGLRmqvSAGGNIgerlmAVGARHYG-----------DIRATAGdWLErveiDAARID 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 123755092 150 DSGYSLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTH 211
Cdd:PRK11701 147 DLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvrELGLAVVIVTH 210
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
22-221 |
4.38e-14 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 69.48 E-value: 4.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 22 SYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNcslKGTVLFDGtniydkRVDPVevrrrIGM-VF 100
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGI--YPPD---SGTVTVRG------RVSSL-----LGLgGG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 101 QQPNpfpKSIYENIAFGARINGFTGD-----MDELVESSlrkaalwdECKDKLNDSGYSLSGGQQQRLCIARTIAIEPEI 175
Cdd:cd03220 95 FNPE---LTGRENIYLNGRLLGLSRKeidekIDEIIEFS--------ELGDFIDLPVKTYSSGMKARLAFAIATALEPDI 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 123755092 176 ILMDEPCSALDPISTLKIEETMHELKMNY-TIIIVTHNMQQALRVSD 221
Cdd:cd03220 164 LLIDEVLAVGDAAFQEKCQRRLRELLKQGkTVILVSHDPSSIKRLCD 210
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
13-261 |
6.90e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 70.16 E-value: 6.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYG----TFEAVRNVFCNFKKGNITSLIGPSGCGKStvLRSLNRMNdLI--PNCSLKGTVLFDGTNIydKR 86
Cdd:PRK11022 3 LLNVDKLSVHFGdesaPFRAVDRISYSVKQGEVVGIVGESGSGKS--VSSLAIMG-LIdyPGRVMAEKLEFNGQDL--QR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 87 VDPVEVRRRIG----MVFQQPNpfpKSIYENIAFGARIngftgdMDEL-VESSLRKAALWDECKDKLNDSG--------- 152
Cdd:PRK11022 78 ISEKERRNLVGaevaMIFQDPM---TSLNPCYTVGFQI------MEAIkVHQGGNKKTRRQRAIDLLNQVGipdpasrld 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 153 ---YSLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHNM----QQALRVSDMT 223
Cdd:PRK11022 149 vypHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALVLITHDLalvaEAAHKIIVMY 228
|
250 260 270
....*....|....*....|....*....|....*...
gi 123755092 224 AffnaveyedgdggkvGYLAEFNSTKKIFNSPKEKTTQ 261
Cdd:PRK11022 229 A---------------GQVVETGKAHDIFRAPRHPYTQ 251
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-237 |
1.61e-13 |
|
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: 66.79 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEA-VRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNrmnDLIPncslkgtvLFDGTniydkrvdpVEV 92
Cdd:cd03223 1 IELENLSLATPDGRVlLKDLSFEIKPGDRLLITGPSGTGKSSLFRALA---GLWP--------WGSGR---------IGM 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 93 RRRIGMVF--QQPnpfpksiYeniafgaringftgdmdeLVESSLRKAAL--WDEckdklndsgySLSGGQQQRLCIART 168
Cdd:cd03223 61 PEGEDLLFlpQRP-------Y------------------LPLGTLREQLIypWDD----------VLSGGEQQRLAFARL 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 123755092 169 IAIEPEIILMDEPCSALDPISTLKIEETMHELKMnyTIIIVTHnmQQALRvsdmtAFFNAVEYEDGDGG 237
Cdd:cd03223 106 LLHKPKFVFLDEATSALDEESEDRLYQLLKELGI--TVISVGH--RPSLW-----KFHDRVLDLDGEGG 165
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-221 |
2.57e-13 |
|
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: 69.47 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLnrmNDLIPNCSLKGTVLFDGTNIYDKRVDPVEv 92
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKIL---SGVYPHGTWDGEIYWSGSPLKASNIRDTE- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 93 RRRIGMVFQQPNPFPK-SIYENIAFGARI--NGFTGDMDELVessLRKAALWDECK-DKLNDSGY--SLSGGQQQRLCIA 166
Cdd:TIGR02633 77 RAGIVIIHQELTLVPElSVAENIFLGNEItlPGGRMAYNAMY---LRAKNLLRELQlDADNVTRPvgDYGGGQQQLVEIA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 123755092 167 RTIAIEPEIILMDEPCSALDPISTLKIEETMHELKM-NYTIIIVTHNMQQALRVSD 221
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAhGVACVYISHKLNEVKAVCD 209
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
37-218 |
3.39e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 67.11 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 37 KKGNITSLIGPSGCGKSTVLRSLNRMNDlipncSLKGTVLFDGTNIYdkRVDP---VEVR-RRIGMVFQQPNPFPK-SIY 111
Cdd:PRK10584 34 KRGETIALIGESGSGKSTLLAILAGLDD-----GSSGEVSLVGQPLH--QMDEearAKLRaKHVGFVFQSFMLIPTlNAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 112 ENIAFGARINGFTGDmdelvESSLRKAALWDEC--KDKLNDSGYSLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPIS 189
Cdd:PRK10584 107 ENVELPALLRGESSR-----QSRNGAKALLEQLglGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
|
170 180 190
....*....|....*....|....*....|.
gi 123755092 190 TLKIEETMHELKMNY--TIIIVTHNMQQALR 218
Cdd:PRK10584 182 GDKIADLLFSLNREHgtTLILVTHDLQLAAR 212
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
16-211 |
3.83e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.55 E-value: 3.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 16 LENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLnrMNDLIPncslkgtvlFDGTNIYDKRVdpvevrrR 95
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKIL--AGELEP---------DSGEVSIPKGL-------R 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 96 IGMVFQQPNPFP-KSIYENIAFG--------ARINGFTGDMDELVESSLRKAALWDECkDKLNdsGY------------- 153
Cdd:COG0488 63 IGYLPQEPPLDDdLTVLDTVLDGdaelraleAELEELEAKLAEPDEDLERLAELQEEF-EALG--GWeaearaeeilsgl 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123755092 154 ------------SLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETmheLKmNY--TIIIVTH 211
Cdd:COG0488 140 gfpeedldrpvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEF---LK-NYpgTVLVVSH 207
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
14-211 |
4.81e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 68.68 E-value: 4.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSI---SYGTFeaVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNrmnDLIPNCSlkGTVLFdgtniydkrvdPV 90
Cdd:COG4178 363 LALEDLTLrtpDGRPL--LEDLSLSLKPGERLLITGPSGSGKSTLLRAIA---GLWPYGS--GRIAR-----------PA 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 91 EVRrrigMVF--QQPnpfpksiY-------ENIAFGARINGFTgdmDELVESSLRKAALwDECKDKLNDS---GYSLSGG 158
Cdd:COG4178 425 GAR----VLFlpQRP-------YlplgtlrEALLYPATAEAFS---DAELREALEAVGL-GHLAERLDEEadwDQVLSLG 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 123755092 159 QQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTH 211
Cdd:COG4178 490 EQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGH 542
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-211 |
5.66e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.17 E-value: 5.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 11 NIILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLnrMNDLIPncsLKGTVLFdGTNIydkrvdpv 90
Cdd:COG0488 313 KKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLL--AGELEP---DSGTVKL-GETV-------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 91 evrrRIGmVFQQ------PNpfpKSIYENIAFGARIN------------GFTGDMdelVESSLRKaalwdeckdklndsg 152
Cdd:COG0488 379 ----KIG-YFDQhqeeldPD---KTVLDELRDGAPGGteqevrgylgrfLFSGDD---AFKPVGV--------------- 432
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 123755092 153 ysLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPistlkieETMHELKM---NY--TIIIVTH 211
Cdd:COG0488 433 --LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDI-------ETLEALEEaldDFpgTVLLVSH 487
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
14-212 |
5.70e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 66.63 E-value: 5.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLnrMNdlIPNCSL-KGTVLFDGTNIYDKRVDpvE- 91
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVL--MG--HPKYEVtSGSILLDGEDILELSPD--Er 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 92 VRRRIGMVFQQPNPFP--------KSIYENIAfGARINGFtgDMDELVESSLRKAALWDECKDK-LNDSgysLSGGQQQR 162
Cdd:COG0396 75 ARAGIFLAFQYPVEIPgvsvsnflRTALNARR-GEELSAR--EFLKLLKEKMKELGLDEDFLDRyVNEG---FSGGEKKR 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 123755092 163 LCIARTIAIEPEIILMDEPCSALDpISTLKI--E--ETMHELKMnyTIIIVTHN 212
Cdd:COG0396 149 NEILQMLLLEPKLAILDETDSGLD-IDALRIvaEgvNKLRSPDR--GILIITHY 199
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
39-222 |
1.24e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.60 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 39 GNITSLIGPSGCGKSTVLrslNRMNDLIPNCSLKGTVLFDGTNIYDkrvdpvEVRRRIGMVFQQPNPFPK-SIYENIAFG 117
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLL---NALAGRIQGNNFTGTILANNRKPTK------QILKRTGFVTQDDILYPHlTVRETLVFC 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 118 ARI---NGFTGDMDELVESSLRKAALWDECKDKLNDSGY--SLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLK 192
Cdd:PLN03211 165 SLLrlpKSLTKQEKILVAESVISELGLTKCENTIIGNSFirGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYR 244
|
170 180 190
....*....|....*....|....*....|
gi 123755092 193 IEETMHELKmNYTIIIVTHNMQQALRVSDM 222
Cdd:PLN03211 245 LVLTLGSLA-QKGKTIVTSMHQPSSRVYQM 273
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
39-217 |
1.43e-12 |
|
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: 67.63 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 39 GNITSLIGPSGCGKSTVLRSLNRMndlipnCSLKGTVLFDGtnIYDKRVDPVEVRRRIGMVFQQPNPFPKSIYENIAFGA 118
Cdd:TIGR01271 1245 GQRVGLLGRTGSGKSTLLSALLRL------LSTEGEIQIDG--VSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYE 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 119 RINgftgdmDELV-----ESSLRkaALWDECKDKLN----DSGYSLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPIS 189
Cdd:TIGR01271 1317 QWS------DEEIwkvaeEVGLK--SVIEQFPDKLDfvlvDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVT 1388
|
170 180
....*....|....*....|....*...
gi 123755092 190 TLKIEETMHELKMNYTIIIVTHNMQQAL 217
Cdd:TIGR01271 1389 LQIIRKTLKQSFSNCTVILSEHRVEALL 1416
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
31-200 |
1.63e-12 |
|
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: 64.57 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 31 NVFCNFKKGNITSLIGPSGCGKSTVLRSL-NRMNDlipnCSLKGTVLFDGtniydkRVDPVEVRRRIGMVFQQPNPFPKS 109
Cdd:cd03232 25 NISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTA----GVITGEILING------RPLDKNFQRSTGYVEQQDVHSPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 110 -IYENIAFGARINGftgdmdelvesslrkaalwdeckdklndsgysLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPI 188
Cdd:cd03232 95 tVREALRFSALLRG--------------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
170
....*....|..
gi 123755092 189 STLKIEETMHEL 200
Cdd:cd03232 143 AAYNIVRFLKKL 154
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
3-231 |
2.32e-12 |
|
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: 66.86 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 3 KTNKKTPKNIILSLENVSIsYGTfEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLnrMNDLIPNcslKGTVLFDGtni 82
Cdd:TIGR01271 418 KARKQPNGDDGLFFSNFSL-YVT-PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMI--MGELEPS---EGKIKHSG--- 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 83 ydkrvdpvevrrRIGMVFQQPNPFPKSIYENIAFGAringftgDMDELVESSLRKAALWDE------CKDK--LNDSGYS 154
Cdd:TIGR01271 488 ------------RISFSPQTSWIMPGTIKDNIIFGL-------SYDEYRYTSVIKACQLEEdialfpEKDKtvLGEGGIT 548
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 123755092 155 LSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKI-EETMHELKMNYTIIIVTHNMQQALRVSDMTAFFNAVEY 231
Cdd:TIGR01271 549 LSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCY 626
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
38-267 |
3.20e-12 |
|
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: 66.51 E-value: 3.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 38 KGNITSLIGPSGCGKSTVLRSL-NRMNDLIPNCSLKGTVLFdgtniydkrvdpvevrrrigmVFQQPNPFPKSIYENIAF 116
Cdd:TIGR00957 663 EGALVAVVGQVGCGKSSLLSALlAEMDKVEGHVHMKGSVAY---------------------VPQQAWIQNDSLRENILF 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 117 GARINgftgdmDELVESSLRKAALWDEC-------KDKLNDSGYSLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPIS 189
Cdd:TIGR00957 722 GKALN------EKYYQQVLEACALLPDLeilpsgdRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHV 795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 190 TLKIEETM---HELKMNYTIIIVTHNMQ-----------QALRVSDMTAFfnaVEYEDGDGGKVGYLAEFNSTKKIFNSP 255
Cdd:TIGR00957 796 GKHIFEHVigpEGVLKNKTRILVTHGISylpqvdviivmSGGKISEMGSY---QELLQRDGAFAEFLRTYAPDEQQGHLE 872
|
250
....*....|..
gi 123755092 256 KEKTTQEYISGK 267
Cdd:TIGR00957 873 DSWTALVSGEGK 884
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
14-217 |
4.74e-12 |
|
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: 64.49 E-value: 4.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISY--GTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndlipnCSLKGTVLFDGTNiYDKrVDPVE 91
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL------LNTEGDIQIDGVS-WNS-VPLQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 92 VRRRIGMVFQQPNPFPKSIYENIafgaRINGFTGDmDEL--VESSLRKAALWDECKDKLN----DSGYSLSGGQQQRLCI 165
Cdd:cd03289 75 WRKAFGVIPQKVFIFSGTFRKNL----DPYGKWSD-EEIwkVAEEVGLKSVIEQFPGQLDfvlvDGGCVLSHGHKQLMCL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 123755092 166 ARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTHNMQQAL 217
Cdd:cd03289 150 ARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAML 201
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
36-210 |
4.74e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 65.45 E-value: 4.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 36 FKKGNITSLIGPSGCGKSTVLRSLnrMNDLIPNCSLKGTVLFDGtniydKRVDPVEVRRRIGMVFQQPNPFPK-SIYENI 114
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNAL--AFRSPKGVKGSGSVLLNG-----MPIDAKEMRAISAYVQQDDLFIPTlTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 115 AFGARI---NGFTGD-----MDELVES-SLRKAAlwdecKDKLNDSGY--SLSGGQQQRLCIARTIAIEPEIILMDEPCS 183
Cdd:TIGR00955 121 MFQAHLrmpRRVTKKekrerVDEVLQAlGLRKCA-----NTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180
....*....|....*....|....*..
gi 123755092 184 ALDPISTLKIEETMHELKMNYTIIIVT 210
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQKGKTIICT 222
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
14-211 |
6.40e-12 |
|
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: 61.70 E-value: 6.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLnrMNDLIPNcslKGTVLFDGTNiydkrvdpvevr 93
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLI--AGELEPD---EGIVTWGSTV------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 94 rRIGmVFQQpnpfpksiyeniafgaringftgdmdelvesslrkaalwdeckdklndsgysLSGGQQQRLCIARTIAIEP 173
Cdd:cd03221 64 -KIG-YFEQ----------------------------------------------------LSGGEKMRLALAKLLLENP 89
|
170 180 190
....*....|....*....|....*....|....*...
gi 123755092 174 EIILMDEPCSALDPISTLKIEETMHELKMnyTIIIVTH 211
Cdd:cd03221 90 NLLLLDEPTNHLDLESIEALEEALKEYPG--TVILVSH 125
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
14-221 |
6.41e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.19 E-value: 6.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDliPNcslKGTVLFDGTNiYDKRVDPVEVR 93
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHE--PT---KGTITINNIN-YNKLDHKLAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 94 RRIGMVFQQPNPFPK-SIYENIAFGAR-INGFTG-------DMDELVESSLRKAALwdecKDKLNDSGYSLSGGQQQRLC 164
Cdd:PRK09700 80 LGIGIIYQELSVIDElTVLENLYIGRHlTKKVCGvniidwrEMRVRAAMMLLRVGL----KVDLDEKVANLSISHKQMLE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 123755092 165 IARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNYT-IIIVTHNMQQALRVSD 221
Cdd:PRK09700 156 IAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTaIVYISHKLAEIRRICD 213
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
5-221 |
7.26e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.04 E-value: 7.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 5 NKKTPKNIILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDlipncSLKGTVLFDGTNIYD 84
Cdd:PRK10575 3 EYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQP-----PSEGEILLDAQPLES 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 85 krVDPVEVRRRIGMVFQQ-PNPFPKSIYENIAFG-----ARINGFTGDMDELVESSLRKAALwDECKDKLNDSgysLSGG 158
Cdd:PRK10575 78 --WSSKAFARKVAYLPQQlPAAEGMTVRELVAIGrypwhGALGRFGAADREKVEEAISLVGL-KPLAHRLVDS---LSGG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 123755092 159 QQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHNMQQALRVSD 221
Cdd:PRK10575 152 ERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLsqERGLTVIAVLHDINMAARYCD 216
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
12-221 |
1.11e-11 |
|
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: 62.06 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 12 IILSLENVSISYgtfeAVRNVfcNF--KKGNITSLIGPSGCGKSTVLRSLNRMNDLipncsLKGTVLFDGTNIydkRVDP 89
Cdd:cd03215 3 PVLEVRGLSVKG----AVRDV--SFevRAGEIVGIAGLVGNGQTELAEALFGLRPP-----ASGEITLDGKPV---TRRS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 90 VEVRRRIGMVFqqpnpFPK-----------SIYENIAFGARingftgdmdelvesslrkaalwdeckdklndsgysLSGG 158
Cdd:cd03215 69 PRDAIRAGIAY-----VPEdrkreglvldlSVAENIALSSL-----------------------------------LSGG 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 123755092 159 QQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELK-MNYTIIIVTHNMQQALRVSD 221
Cdd:cd03215 109 NQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAdAGKAVLLISSELDELLGLCD 172
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
14-225 |
1.46e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.20 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNV-FCnFKKGNITSLIGPSGCGKSTVLRSLNRmndLIPncSLKGTVLFDGTNIYDKrvDPVEV 92
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLsFT-LAAGEALVLTGPNGSGKTTLLRLIAG---LLP--PAAGTIKLDGGDIDDP--DVAEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 93 RRRIG----MvfqqpNPFpKSIYENIAFGARINGfTGDMDELvesslrkAALwdeCKDKLND-----SGYsLSGGQQQRL 163
Cdd:PRK13539 75 CHYLGhrnaM-----KPA-LTVAENLEFWAAFLG-GEELDIA-------AAL---EAVGLAPlahlpFGY-LSAGQKRRV 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 123755092 164 CIARTIAIEPEIILMDEPCSALDPISTLKIEETMHE-LKMNYTIIIVTHnmqQAL-----RVSDMTAF 225
Cdd:PRK13539 137 ALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAhLAQGGIVIAATH---IPLglpgaRELDLGPF 201
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
37-213 |
2.80e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.29 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 37 KKGNITSLIGPSGCGKSTVLRSLNrmNDLIPN-CSL-------------KGTVLFDG-TNIYDKRVDPVevrRRIGMVFQ 101
Cdd:PRK13409 97 KEGKVTGILGPNGIGKTTAVKILS--GELIPNlGDYeeepswdevlkrfRGTELQNYfKKLYNGEIKVV---HKPQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 102 QPNPFPKSIYENIAfgaRINGfTGDMDELVESsLRKAALWDEckdKLNDsgysLSGGQQQRLCIARTIAIEPEIILMDEP 181
Cdd:PRK13409 172 IPKVFKGKVRELLK---KVDE-RGKLDEVVER-LGLENILDR---DISE----LSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|..
gi 123755092 182 CSALDPISTLKIEETMHELKMNYTIIIVTHNM 213
Cdd:PRK13409 240 TSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
36-186 |
1.11e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 60.33 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 36 FKKGNITSLIGPSGCGKSTVlrsLNRMNDLIPNcslKGTVLFDGTNIYDkrVDPVEV-RRRIGMVFQQPNPFPKSIYENI 114
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTL---LARMAGLLPG---SGSIQFAGQPLEA--WSAAELaRHRAYLSQQQTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 115 AF----GARINGFTGDMDELVEsSLRKAalwdeckDKLNDSGYSLSGGQQQR-------LCIARTIAIEPEIILMDEPCS 183
Cdd:PRK03695 91 TLhqpdKTRTEAVASALNEVAE-ALGLD-------DKLGRSVNQLSGGEWQRvrlaavvLQVWPDINPAGQLLLLDEPMN 162
|
...
gi 123755092 184 ALD 186
Cdd:PRK03695 163 SLD 165
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-211 |
1.31e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.04 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 4 TNKKTPkniILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndliPNCS-LKGTVLFDGTNI 82
Cdd:CHL00131 1 MNKNKP---ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH----PAYKiLEGDILFKGESI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 83 YDKrvDPvEVRRRIG--MVFQQPnpfpksiyeniafgARINGFTG-DMDELVESSLRKAALWDE---------CKDKLND 150
Cdd:CHL00131 74 LDL--EP-EERAHLGifLAFQYP--------------IEIPGVSNaDFLRLAYNSKRKFQGLPEldplefleiINEKLKL 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 123755092 151 SGYS-----------LSGGQQQRLCIARTIAIEPEIILMDEPCSALDpISTLK-IEETMHELK-MNYTIIIVTH 211
Cdd:CHL00131 137 VGMDpsflsrnvnegFSGGEKKRNEILQMALLDSELAILDETDSGLD-IDALKiIAEGINKLMtSENSIILITH 209
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
29-213 |
1.43e-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: 61.50 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 29 VRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDlipncSLKGTVLFDGTNIYDkrVDPVEVRRRIGMVFQQPNPFPK 108
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINE-----SAEGEIIIDGLNIAK--IGLHDLRFKITIIPQDPVLFSG 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 109 SIYENIafgariNGFTGDMDELVESSLRKAALWD---ECKDKLN----DSGYSLSGGQQQRLCIARTIAIEPEIILMDEP 181
Cdd:TIGR00957 1375 SLRMNL------DPFSQYSDEEVWWALELAHLKTfvsALPDKLDhecaEGGENLSVGQRQLVCLARALLRKTKILVLDEA 1448
|
170 180 190
....*....|....*....|....*....|..
gi 123755092 182 CSALDPISTLKIEETMHELKMNYTIIIVTHNM 213
Cdd:TIGR00957 1449 TAAVDLETDNLIQSTIRTQFEDCTVLTIAHRL 1480
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
37-208 |
1.69e-10 |
|
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: 59.20 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 37 KKGNITSLIGPSGCGKSTVLRSLNrmNDLIPNCSLKGTVLFDGtniYDKRVDPVEVRRRIGMVFQQPNPFPK-SIYENIA 115
Cdd:cd03233 31 KPGEMVLVLGRPGSGCSTLLKALA--NRTEGNVSVEGDIHYNG---IPYKEFAEKYPGEIIYVSEEDVHFPTlTVRETLD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 116 FGARINGftgdmdelvesslrkaalwdeckdklNDSGYSLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTL---- 191
Cdd:cd03233 106 FALRCKG--------------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALeilk 159
|
170
....*....|....*..
gi 123755092 192 KIEETMHELKMnyTIII 208
Cdd:cd03233 160 CIRTMADVLKT--TTFV 174
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
23-224 |
1.85e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.91 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 23 YGTFEAVRNVfcNF--KKGNITSLIGPSGCGKSTVLRSLnrmNDLIPNCSlkGTV-LFdgtniyDKRVDP--VEVRRRIG 97
Cdd:NF033858 276 FGDFTAVDHV--SFriRRGEIFGFLGSNGCGKSTTMKML---TGLLPASE--GEAwLF------GQPVDAgdIATRRRVG 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 98 MVFQQpnpFpkSIYE------NIAFGARINGFTGD-MDELVESSLRKAALwDECKDKLNDsgySLSGGQQQRLCIArtIA 170
Cdd:NF033858 343 YMSQA---F--SLYGeltvrqNLELHARLFHLPAAeIAARVAEMLERFDL-ADVADALPD---SLPLGIRQRLSLA--VA 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123755092 171 I--EPEIILMDEPCSALDPISTLKIEETMHEL--KMNYTIIIVTHNMQQAL---RVSDMTA 224
Cdd:NF033858 412 VihKPELLILDEPTSGVDPVARDMFWRLLIELsrEDGVTIFISTHFMNEAErcdRISLMHA 472
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
14-211 |
2.19e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 60.50 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAV-RNVFCNFKKGNITSLIGPSGCGKSTvLRSLnRMNDLIPNcslKGTVLFDGTNI--YDKRVdpv 90
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVlQNINLSVPSRGFVALVGHTGSGKST-LASL-LMGYYPLT---EGEIRLDGRPLssLSHSV--- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 91 eVRRRIGMVFQQPNPFPKSIYENIAFGARINgftgdmDELVESSLRKAALWDECKD-------KLNDSGYSLSGGQQQRL 163
Cdd:PRK10790 413 -LRQGVAMVQQDPVVLADTFLANVTLGRDIS------EEQVWQALETVQLAELARSlpdglytPLGEQGNNLSVGQKQLL 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 123755092 164 CIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTH 211
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAH 533
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
13-213 |
2.29e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 59.36 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRslnrmndlipncslkgTVLfdGTNIYDKRVDPVEV 92
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVR----------------VVL--GLVAPDEGVIKRNG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 93 RRRIGMVfqqpnpfPKSIYENIAFGARINGF------TGDMDELVESSLRKAA-LWDECKDKlndsgysLSGGQQQRLCI 165
Cdd:PRK09544 66 KLRIGYV-------PQKLYLDTTLPLTVNRFlrlrpgTKKEDILPALKRVQAGhLIDAPMQK-------LSGGETQRVLL 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 123755092 166 ARTIAIEPEIILMDEPCSALDPISTLKIEETMHELK--MNYTIIIVTHNM 213
Cdd:PRK09544 132 ARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRreLDCAVLMVSHDL 181
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
39-224 |
3.23e-10 |
|
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: 58.27 E-value: 3.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 39 GNITSLIGPSGCGKSTVLRSLNrmnDLIPncSLKGTVLFDGTNIYDKRVDPVEvrrriGMVFQQPNPFPK---SIYENIA 115
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILA---GLSP--PLAGRVLLNGGPLDFQRDSIAR-----GLLYLGHAPGIKttlSVLENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 116 FGARINGftgdmDELVESSLrkaalwdeckDKLNDSGY------SLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPIS 189
Cdd:cd03231 96 FWHADHS-----DEQVEEAL----------ARVGLNGFedrpvaQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 123755092 190 TLKIEETM-HELKMNYTIIIVTH---NMQQA-LRVSDMTA 224
Cdd:cd03231 161 VARFAEAMaGHCARGGMVVLTTHqdlGLSEAgARELDLGF 200
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
37-213 |
3.77e-10 |
|
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: 59.80 E-value: 3.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 37 KKGNITSLIGPSGCGKSTVLRSLNrmNDLIPNCS--------------LKGTVLFDG-TNIYDKRVDPVevrRRIGMVFQ 101
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILS--GELKPNLGdydeepswdevlkrFRGTELQDYfKKLANGEIKVA---HKPQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 102 qpnpFPKSiyeniafgaringFTGDMDELvessLRKA---ALWDECKDKLNDSGY------SLSGGQQQRLCIARTIAIE 172
Cdd:COG1245 172 ----IPKV-------------FKGTVREL----LEKVderGKLDELAEKLGLENIldrdisELSGGELQRVAIAAALLRD 230
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 123755092 173 PEIILMDEPCSALDPISTLKIEETMHEL-KMNYTIIIVTHNM 213
Cdd:COG1245 231 ADFYFFDEPSSYLDIYQRLNVARLIRELaEEGKYVLVVEHDL 272
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
29-221 |
7.09e-10 |
|
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: 58.33 E-value: 7.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 29 VRNVFCNFKKGNITSLIGPSGCGKSTVLRSLnrMNDLIPNcslKGTVLFDGtniydkrvdpvevrrRIGMVFQQPNPFPK 108
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLI--LGELEPS---EGKIKHSG---------------RISFSSQFSWIMPG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 109 SIYENIAFGAringftgDMDELVESSLRKAALWDEC------KDK--LNDSGYSLSGGQQQRLCIARTIAIEPEIILMDE 180
Cdd:cd03291 113 TIKENIIFGV-------SYDEYRYKSVVKACQLEEDitkfpeKDNtvLGEGGITLSGGQRARISLARAVYKDADLYLLDS 185
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 123755092 181 PCSALDPISTLKI-EETMHELKMNYTIIIVTHNMQQaLRVSD 221
Cdd:cd03291 186 PFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEH-LKKAD 226
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
37-231 |
8.35e-10 |
|
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: 57.76 E-value: 8.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 37 KKGNITSLIGPSGCGKSTVLRSLNrmNDLIPNCSLKG------TVL--FDGT--NIYDKRV--DPVEVRRRIGMVFQQPN 104
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILA--GKLKPNLGKFDdppdwdEILdeFRGSelQNYFTKLleGDVKVIVKPQYVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 105 PFPKSIYENIAFGARingfTGDMDELVESSlrkaalwdECKDKLNDSGYSLSGGQQQRLCIARTIAIEPEIILMDEPCSA 184
Cdd:cd03236 102 AVKGKVGELLKKKDE----RGKLDELVDQL--------ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 123755092 185 LDPISTLKIEETMHEL-KMNYTIIIVTHNmqqaLRVSDMTAFFNAVEY 231
Cdd:cd03236 170 LDIKQRLNAARLIRELaEDDNYVLVVEHD----LAVLDYLSDYIHCLY 213
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
12-214 |
1.61e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.04 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 12 IILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLnrMNDLIPNC-SLK-GTVL----FDGtniYDK 85
Cdd:PRK11147 318 IVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLM--LGQLQADSgRIHcGTKLevayFDQ---HRA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 86 RVDPvevrrrigmvfqqpnpfPKSIYENIAFGAR---INGFT----GDMDELVESSLR-----KAalwdeckdklndsgy 153
Cdd:PRK11147 393 ELDP-----------------EKTVMDNLAEGKQevmVNGRPrhvlGYLQDFLFHPKRamtpvKA--------------- 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 123755092 154 sLSGGQQQRLCIARTIAIEPEIILMDEPCSALDpISTLkieETMHELKMNY--TIIIVTHNMQ 214
Cdd:PRK11147 441 -LSGGERNRLLLARLFLKPSNLLILDEPTNDLD-VETL---ELLEELLDSYqgTVLLVSHDRQ 498
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
13-221 |
1.62e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.02 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLnrmNDLIPNCSLKGTVLFDGTNIYDKRVDPVEv 92
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVL---SGVYPHGTYEGEIIFEGEELQASNIRDTE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 93 RRRIGMVFQQPNPFPK-SIYENIAFGARI--NGFTgDMDELVessLRKAALWDECKDKLNDSG--YSLSGGQQQRLCIAR 167
Cdd:PRK13549 81 RAGIAIIHQELALVKElSVLENIFLGNEItpGGIM-DYDAMY---LRAQKLLAQLKLDINPATpvGNLGLGQQQLVEIAK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 123755092 168 TIAIEPEIILMDEPCSALDPISTLKIEETMHELK-MNYTIIIVTHNMQQALRVSD 221
Cdd:PRK13549 157 ALNKQARLLILDEPTASLTESETAVLLDIIRDLKaHGIACIYISHKLNEVKAISD 211
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-214 |
2.29e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 57.02 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 3 KTNKKTP--KNIILSLenVSISYGTFEAVRNVfcNF--KKGNITSLIGPSGCGKSTVLRSLNRMndLIPNcslKGTVLFD 78
Cdd:COG4586 12 RVYEKEPglKGALKGL--FRREYREVEAVDDI--SFtiEPGEIVGFIGPNGAGKSTTIKMLTGI--LVPT---SGEVRVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 79 GTNIYDKRvdpVEVRRRIGMVFQQPN------P----FP--KSIYE--NIAFGARINGFTG--DMDELVESSLRKaalwd 142
Cdd:COG4586 83 GYVPFKRR---KEFARRIGVVFGQRSqlwwdlPaidsFRllKAIYRipDAEYKKRLDELVEllDLGELLDTPVRQ----- 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 123755092 143 eckdklndsgysLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNY--TIIIVTHNMQ 214
Cdd:COG4586 155 ------------LSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMD 216
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-222 |
2.45e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.37 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 1 MIKTNKKTPKniILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSlnrMNDLIPNCSlkGTVLFDGT 80
Cdd:PRK15439 1 MQTSDTTAPP--LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKI---IAGIVPPDS--GTLEIGGN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 81 NIYdkRVDPVEVRRR-IGMVFQQPNPFPK-SIYENIAFG-ARINGFTGDMDELVesslrkAALwdECKDKLNDSGYSLSG 157
Cdd:PRK15439 74 PCA--RLTPAKAHQLgIYLVPQEPLLFPNlSVKENILFGlPKRQASMQKMKQLL------AAL--GCQLDLDSSAGSLEV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 158 GQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL-KMNYTIIIVTHNM----QQALRVSDM 222
Cdd:PRK15439 144 ADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELlAQGVGIVFISHKLpeirQLADRISVM 213
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
44-213 |
2.48e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.68 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 44 LIGPSGCGKSTVLRSLNRMNDLipncsLKGTVLFDGTNIydKRVDPVEVRRRIGMVFQQPNPFPKSIYENIafgariNGF 123
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVEL-----EKGRIMIDDCDV--AKFGLTDLRRVLSIIPQSPVLFSGTVRFNI------DPF 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 124 TGDMDELVESSLRKAALWDECKD-------KLNDSGYSLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEET 196
Cdd:PLN03232 1334 SEHNDADLWEALERAHIKDVIDRnpfgldaEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRT 1413
|
170
....*....|....*..
gi 123755092 197 MHELKMNYTIIIVTHNM 213
Cdd:PLN03232 1414 IREEFKSCTMLVIAHRL 1430
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
13-214 |
3.33e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 56.73 E-value: 3.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGTFE----AVRNVFCNFKKGNITSLIGPSGCGKSTVLRSL---NRMNDLIPNCSLKgtvlFDGTNIYdk 85
Cdd:PRK15093 3 LLDIRNLTIEFKTSDgwvkAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAIcgvTKDNWRVTADRMR----FDDIDLL-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 86 RVDPVEVRRRIG----MVFQQP----NPfPKSIYENIAfgARINGFT--GDMDELVESSLRKA-------ALWDEcKDKL 148
Cdd:PRK15093 77 RLSPRERRKLVGhnvsMIFQEPqsclDP-SERVGRQLM--QNIPGWTykGRWWQRFGWRKRRAiellhrvGIKDH-KDAM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 123755092 149 NDSGYSLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMN--YTIIIVTHNMQ 214
Cdd:PRK15093 153 RSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnnTTILLISHDLQ 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-181 |
5.46e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.18 E-value: 5.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 6 KKTPKNIILSLENVSISygtfEAVRNVfcNF--KKGNITSLIGPSGCGKSTVLRSL---NRMndlipncsLKGTVLFDGT 80
Cdd:COG1129 249 AAAPGEVVLEVEGLSVG----GVVRDV--SFsvRAGEILGIAGLVGAGRTELARALfgaDPA--------DSGEIRLDGK 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 81 NIydKRVDPVE-VRRRIGMV---------FQqpnpfPKSIYENIAFGA----RINGF--TGDMDELVESSLRK-----AA 139
Cdd:COG1129 315 PV--RIRSPRDaIRAGIAYVpedrkgeglVL-----DLSIRENITLASldrlSRGGLldRRRERALAEEYIKRlriktPS 387
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 123755092 140 LWDECKdklndsgySLSGGQQQRLCIARTIAIEPEIILMDEP 181
Cdd:COG1129 388 PEQPVG--------NLSGGNQQKVVLAKWLATDPKVLILDEP 421
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
29-224 |
8.30e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.83 E-value: 8.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 29 VRNVFCNFKKGNITSLIGPSGCGKSTVLRSLnrMNDL----IPN-CSLKGTVLFDGTNIydKRVDPVEVRRRIGMVFQQP 103
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKAL--AGDLtgggAPRgARVTGDVTLNGEPL--AAIDAPRLARLRAVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 104 NP-FPKSIYENIAFG----ARINGFTGDMD-ELVESSLRKAAlwdecKDKLNDSGY-SLSGGQQQRLCIARTIA------ 170
Cdd:PRK13547 93 QPaFAFSAREIVLLGryphARRAGALTHRDgEIAWQALALAG-----ATALVGRDVtTLSGGELARVQFARVLAqlwpph 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 123755092 171 ---IEPEIILMDEPCSALDPISTLKIEETMHELKMNYTI--IIVTHNMQQALRVSDMTA 224
Cdd:PRK13547 168 daaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgvLAIVHDPNLAARHADRIA 226
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
13-211 |
9.35e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.80 E-value: 9.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDLIPNcslKGTVLFDGTNIYDkrVDPVEv 92
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVT---GGTVEFKGKDLLE--LSPED- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 93 rrRIG----MVFQQPNPFP---KSIYENIAFGArINGFTG-------DMDELVESslrKAALWDECKDKLNDS-GYSLSG 157
Cdd:PRK09580 75 --RAGegifMAFQYPVEIPgvsNQFFLQTALNA-VRSYRGqepldrfDFQDLMEE---KIALLKMPEDLLTRSvNVGFSG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 123755092 158 GQQQRLCIARTIAIEPEIILMDEPCSALDpISTLKI-EETMHELK-MNYTIIIVTH 211
Cdd:PRK09580 149 GEKKRNDILQMAVLEPELCILDESDSGLD-IDALKIvADGVNSLRdGKRSFIIVTH 203
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
13-221 |
1.47e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.01 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLnrmndlipncslkgtvlfdgTNIYDKRVDPVEV 92
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVL--------------------TGIYTRDAGSILY 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 93 RRR--------------IGMVFQQPNPFPK-SIYENIAFGARingFTGDMDELVESSLRKAAlwDECKDKLNDSGYS--- 154
Cdd:PRK10762 64 LGKevtfngpkssqeagIGIIHQELNLIPQlTIAENIFLGRE---FVNRFGRIDWKKMYAEA--DKLLARLNLRFSSdkl 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123755092 155 ---LSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELK-MNYTIIIVTHNMQQALRVSD 221
Cdd:PRK10762 139 vgeLSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKsQGRGIVYISHRLKEIFEICD 209
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
28-223 |
4.34e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 52.96 E-value: 4.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 28 AVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDLIpncslKGTVLFDGTniydkrvdPVEVRRRIGMVFQQPNP-- 105
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLA-----SGKISILGQ--------PTRQALQKNLVAYVPQSee 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 106 ----FPkSIYENIAFGARIngftGDMDELVESSLRKAALWDECKDKLNDSGY------SLSGGQQQRLCIARTIAIEPEI 175
Cdd:PRK15056 89 vdwsFP-VLVEDVVMMGRY----GHMGWLRRAKKRDRQIVTAALARVDMVEFrhrqigELSGGQKKRVFLARAIAQQGQV 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 123755092 176 ILMDEPCSALDPISTLKIEETMHELK-MNYTIIIVTHNMQQALRVSDMT 223
Cdd:PRK15056 164 ILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYT 212
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
3-221 |
4.68e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.58 E-value: 4.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 3 KTNkkTPKNIILSLENVSISYGTfeAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDLIpncslKGTVLFDGTNI 82
Cdd:PRK10982 242 KEN--KPGEVILEVRNLTSLRQP--SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKS-----AGTITLHGKKI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 83 YDKRVDP---------VEVRRRIGmvfqqpnpfpksIYENIAFG-----ARINGFTGDMDELVESSLRKAALWDECKDKL 148
Cdd:PRK10982 313 NNHNANEainhgfalvTEERRSTG------------IYAYLDIGfnsliSNIRNYKNKVGLLDNSRMKSDTQWVIDSMRV 380
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 123755092 149 NDSGY-----SLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL-KMNYTIIIVTHNMQQALRVSD 221
Cdd:PRK10982 381 KTPGHrtqigSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEMPELLGITD 459
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
44-211 |
4.94e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 53.63 E-value: 4.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 44 LIGPSGCGKSTVLRSLNRMNDLipnCSlkGTVLFDGTNI--YDKRvdpvEVRRRIGMVFQQPNPFPKSIYENI-----AF 116
Cdd:PTZ00243 1341 IVGRTGSGKSTLLLTFMRMVEV---CG--GEIRVNGREIgaYGLR----ELRRQFSMIPQDPVLFDGTVRQNVdpfleAS 1411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 117 GARINGFTgdmdELVESSLRKAALWDECKDKLNDSGYSLSGGQQQRLCIARTIAIEPE-IILMDEPCSALDPISTLKIEE 195
Cdd:PTZ00243 1412 SAEVWAAL----ELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSgFILMDEATANIDPALDRQIQA 1487
|
170
....*....|....*.
gi 123755092 196 TMHELKMNYTIIIVTH 211
Cdd:PTZ00243 1488 TVMSAFSAYTVITIAH 1503
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
9-211 |
7.95e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.94 E-value: 7.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 9 PKNIilSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLR--SLNRMNDLIPNCSL---KGTVLFDGTN-- 81
Cdd:PLN03073 175 IKDI--HMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymAMHAIDGIPKNCQIlhvEQEVVGDDTTal 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 82 --IYDKRVDPVEVRRRIGMVFQQPNPFPKSIYENIAFGARINGFTGD-MDELVESSLRKAALWD----ECKDKLNDSGYS 154
Cdd:PLN03073 253 qcVLNTDIERTQLLEEEAQLVAQQRELEFETETGKGKGANKDGVDKDaVSQRLEEIYKRLELIDaytaEARAASILAGLS 332
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 123755092 155 L------------SGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMheLKMNYTIIIVTH 211
Cdd:PLN03073 333 FtpemqvkatktfSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSH 399
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
26-226 |
2.40e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 51.32 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 26 FEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDLIpncslKGTVLFDGTNIYDKrvDPVEVRRRiGMVFQQPNP 105
Cdd:PRK09700 276 RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRA-----GGEIRLNGKDISPR--SPLDAVKK-GMAYITESR 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 106 -----FPK-SIYENIAFGARIN--GFTGDMDELVESSLRKAAlwDECKDKLNDSGYS-------LSGGQQQRLCIARTIA 170
Cdd:PRK09700 348 rdngfFPNfSIAQNMAISRSLKdgGYKGAMGLFHEVDEQRTA--ENQRELLALKCHSvnqniteLSGGNQQKVLISKWLC 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 123755092 171 IEPEIILMDEPCSALDPISTLKIEETMHEL-KMNYTIIIVTHNMQQALRVSDMTAFF 226
Cdd:PRK09700 426 CCPEVIIFDEPTRGIDVGAKAEIYKVMRQLaDDGKVILMVSSELPEIITVCDRIAVF 482
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
13-189 |
2.45e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.66 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVL------RSLNRmndlipncslkGTVLFDGTNIYDKR 86
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLsliagaRKIQQ-----------GRVEVLGGDMADAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 87 vdpveVRRRIG-----MvfqqP-----NPFPK-SIYENIAFGARINGFTGD-----MDELVESS-L-----RKAAlwdec 144
Cdd:NF033858 70 -----HRRAVCpriayM----PqglgkNLYPTlSVFENLDFFGRLFGQDAAerrrrIDELLRATgLapfadRPAG----- 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 123755092 145 KdklndsgysLSGGQQQR--LCIArtiAI-EPEIILMDEPCSALDPIS 189
Cdd:NF033858 136 K---------LSGGMKQKlgLCCA---LIhDPDLLILDEPTTGVDPLS 171
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
16-221 |
2.64e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.27 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 16 LENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDliPNcslKGTVLFDGTNIyDKRVDPVEVRRR 95
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQ--KD---SGSILFQGKEI-DFKSSKEALENG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 96 IGMVFQQPNPF-PKSIYENIAFGAR-INGFTGDMDELVESSlrkAALWDECKDKLN--DSGYSLSGGQQQRLCIARTIAI 171
Cdd:PRK10982 75 ISMVHQELNLVlQRSVMDNMWLGRYpTKGMFVDQDKMYRDT---KAIFDELDIDIDprAKVATLSVSQMQMIEIAKAFSY 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 123755092 172 EPEIILMDEPCSALDPISTLKIEETMHELK-MNYTIIIVTHNMQQALRVSD 221
Cdd:PRK10982 152 NAKIVIMDEPTSSLTEKEVNHLFTIIRKLKeRGCGIVYISHKMEEIFQLCD 202
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
147-222 |
3.28e-07 |
|
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: 49.24 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 147 KLNDSGYSLSGGQQQRLCIARTIAIEPE--IILMDEPCSALDPISTLKIEETMHEL-KMNYTIIIVTHN---MQQALRVS 220
Cdd:cd03238 80 TLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLiDLGNTVILIEHNldvLSSADWII 159
|
..
gi 123755092 221 DM 222
Cdd:cd03238 160 DF 161
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
29-186 |
5.75e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.55 E-value: 5.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 29 VRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDLIpncslKGTVLfdgtniydkrvdpveVRRRIGMVFQQPNPFPK 108
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEIS-----EGRVW---------------AERSIAYVPQQAWIMNA 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 109 SIYENIAF-----------GARINGFTGDMDELvesslrKAALWDECKDKlndsGYSLSGGQQQRLCIARTIAIEPEIIL 177
Cdd:PTZ00243 736 TVRGNILFfdeedaarladAVRVSQLEADLAQL------GGGLETEIGEK----GVNLSGGQKARVSLARAVYANRDVYL 805
|
....*....
gi 123755092 178 MDEPCSALD 186
Cdd:PTZ00243 806 LDDPLSALD 814
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
36-200 |
5.95e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.49 E-value: 5.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 36 FKKGNITSLIGPSGCGKSTVLRSL-NRMNdlipncslkGTVLFDGTNIYDKRVDPVEVRRRIGMVFQQPNPFPKS-IYEN 113
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLaERVT---------TGVITGGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTStVRES 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 114 IAFGARI---NGFT-GDMDELVESSLRKAALwDECKDKL-NDSGYSLSGGQQQRLCIARTIAIEPEIIL-MDEPCSALDP 187
Cdd:TIGR00956 857 LRFSAYLrqpKSVSkSEKMEYVEEVIKLLEM-ESYADAVvGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDS 935
|
170
....*....|...
gi 123755092 188 ISTLKIEETMHEL 200
Cdd:TIGR00956 936 QTAWSICKLMRKL 948
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
14-225 |
9.38e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.52 E-value: 9.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNrmNDLIPNcslKGTVLFDGtniydkrvdpVEVR 93
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILS--GNYQPD---AGSILIDG----------QEMR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 94 RR---------IGMVFQQPNPFPK-SIYENIAFGARINGFtgdmdelveSSLRKAALWDECKDKLNDSGY---------S 154
Cdd:PRK11288 70 FAsttaalaagVAIIYQELHLVPEmTVAENLYLGQLPHKG---------GIVNRRLLNYEAREQLEHLGVdidpdtplkY 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 123755092 155 LSGGQQQRLCIARTIAIEPEIILMDEPCSALdpiSTLKIEETM---HELKMNYTIII-VTHNMQQALRVSD-MTAF 225
Cdd:PRK11288 141 LSIGQRQMVEIAKALARNARVIAFDEPTSSL---SAREIEQLFrviRELRAEGRVILyVSHRMEEIFALCDaITVF 213
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
14-187 |
9.49e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 49.59 E-value: 9.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGT--FeAVRNVFCNFKKGNITSLIGPSGCGKST---VLRSLNRmndlipncSLKGTVLFDGTNIYDKrvD 88
Cdd:PRK10522 323 LELRNVTFAYQDngF-SVGPINLTIKRGELLFLIGGNGSGKSTlamLLTGLYQ--------PQSGEILLDGKPVTAE--Q 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 89 PVEVRRRIGMVFQQPNPFPKSIYENiafgarinGFTGDmDELVESSLRKAALwdecKDKLNDSGY-----SLSGGQQQRL 163
Cdd:PRK10522 392 PEDYRKLFSAVFTDFHLFDQLLGPE--------GKPAN-PALVEKWLERLKM----AHKLELEDGrisnlKLSKGQKKRL 458
|
170 180
....*....|....*....|....
gi 123755092 164 CIARTIAIEPEIILMDEPCSALDP 187
Cdd:PRK10522 459 ALLLALAEERDILLLDEWAADQDP 482
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1-211 |
1.42e-06 |
|
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: 49.16 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 1 MIKTNKKTP--KNIilsLENVSISYgtfeavrnvFCNFKKGnitsLIGPSGCGKSTVLRSlnrMNDLIPNcslkgtvlFD 78
Cdd:TIGR03719 7 MNRVSKVVPpkKEI---LKDISLSF---------FPGAKIG----VLGLNGAGKSTLLRI---MAGVDKD--------FN 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 79 GtniyDKRVDPvevRRRIGMVFQQPNPFP-KSIYENIAFG--------ARINGFT-------GDMDEL------VESSLR 136
Cdd:TIGR03719 60 G----EARPQP---GIKVGYLPQEPQLDPtKTVRENVEEGvaeikdalDRFNEISakyaepdADFDKLaaeqaeLQEIID 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 137 KAALWD-ECK-----DKL----NDSGYS-LSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMnyT 205
Cdd:TIGR03719 133 AADAWDlDSQleiamDALrcppWDADVTkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG--T 210
|
....*.
gi 123755092 206 IIIVTH 211
Cdd:TIGR03719 211 VVAVTH 216
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
14-252 |
2.24e-06 |
|
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: 47.60 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTF--EAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMNDLipncsLKGTVLFDGTNIydKRVDPVE 91
Cdd:cd03288 20 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDI-----FDGKIVIDGIDI--SKLPLHT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 92 VRRRIGMVFQQPNPFPKSIYENIAFGARINgftgdmDELVESSLRKAALWDECKD-------KLNDSGYSLSGGQQQRLC 164
Cdd:cd03288 93 LRSRLSIILQDPILFSGSIRFNLDPECKCT------DDRLWEALEIAQLKNMVKSlpggldaVVTEGGENFSVGQRQLFC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 165 IARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTHNMQQALRVSDMTAFfnaveyedgdggKVGYLAE 244
Cdd:cd03288 167 LARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVL------------SRGILVE 234
|
....*...
gi 123755092 245 FNSTKKIF 252
Cdd:cd03288 235 CDTPENLL 242
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
44-211 |
2.36e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.58 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 44 LIGPSGCGKSTVLRSLNRMNDLipncsLKGTVLFDGTNIydKRVDPVEVRRRIGMVFQQPNPFPKSIYENIafgariNGF 123
Cdd:PLN03130 1270 IVGRTGAGKSSMLNALFRIVEL-----ERGRILIDGCDI--SKFGLMDLRKVLGIIPQAPVLFSGTVRFNL------DPF 1336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 124 TGDMDELVESSLRKAALWDECKD-------KLNDSGYSLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEET 196
Cdd:PLN03130 1337 NEHNDADLWESLERAHLKDVIRRnslgldaEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKT 1416
|
170
....*....|....*
gi 123755092 197 MHELKMNYTIIIVTH 211
Cdd:PLN03130 1417 IREEFKSCTMLIIAH 1431
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
148-222 |
5.66e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 46.10 E-value: 5.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 148 LNDSGYSLSGGQQQRLCIARTIAIEPEIIL--MDEPCSALDPISTLKIEETMHELK-MNYTIIIVTHN---MQQALRVSD 221
Cdd:cd03270 131 LSRSAPTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRdLGNTVLVVEHDedtIRAADHVID 210
|
.
gi 123755092 222 M 222
Cdd:cd03270 211 I 211
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-186 |
6.92e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.28 E-value: 6.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 19 VSISYGTFE--------AVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLnrMNDLIPncslkgtvlfdgtniydKRVDPV 90
Cdd:PLN03232 615 ISIKNGYFSwdsktskpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAM--LGELSH-----------------AETSSV 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 91 EVRRRIGMVFQQPNPFPKSIYENIAFGAR-----------INGFTGDMDELVESSLrkaalwdeckDKLNDSGYSLSGGQ 159
Cdd:PLN03232 676 VIRGSVAYVPQVSWIFNATVRENILFGSDfeserywraidVTALQHDLDLLPGRDL----------TEIGERGVNISGGQ 745
|
170 180
....*....|....*....|....*..
gi 123755092 160 QQRLCIARTIAIEPEIILMDEPCSALD 186
Cdd:PLN03232 746 KQRVSMARAVYSNSDIYIFDDPLSALD 772
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-186 |
6.93e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 46.94 E-value: 6.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 6 KKTPKNIILSLENVSI-SYGTFEAVRNVfcNF--KKGNITSLIGPSGCGKSTVLRSLNRmndLIPncSLKGTVLFDGTNI 82
Cdd:COG3845 250 PAEPGEVVLEVENLSVrDDRGVPALKDV--SLevRAGEILGIAGVAGNGQSELAEALAG---LRP--PASGSIRLDGEDI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 83 ydKRVDPVEVRR-----------RIGMVfqqPNpFpkSIYENIAFG---------------ARINGFTgdmDELVES-SL 135
Cdd:COG3845 323 --TGLSPRERRRlgvayipedrlGRGLV---PD-M--SVAENLILGryrrppfsrggfldrKAIRAFA---EELIEEfDV 391
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 123755092 136 RKAALWDECKdklndsgySLSGGQQQRLCIARTIAIEPEIILMDEPCSALD 186
Cdd:COG3845 392 RTPGPDTPAR--------SLSGGNQQKVILARELSRDPKLLIAAQPTRGLD 434
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
14-212 |
8.04e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 45.39 E-value: 8.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSiSYGTFEAVrnvfcNFKKGnITSLIGPSGCGKSTVLRSL------------NRMNDLIPNCSLKGTVLFD--- 78
Cdd:COG0419 5 LRLENFR-SYRDTETI-----DFDDG-LNLIVGPNGAGKSTILEAIryalygkarsrsKLRSDLINVGSEEASVELEfeh 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 79 GTNIYdkrvdpvEVRRRIGMVFQQPNPFPKSIYENIA--FGA-RINGFTGDMDELVESSLRKAALWDECKDKLND----- 150
Cdd:COG0419 78 GGKRY-------RIERRQGEFAEFLEAKPSERKEALKrlLGLeIYEELKERLKELEEALESALEELAELQKLKQEilaql 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 123755092 151 SGY----SLSGGQQQRLCIARTIAiepeiILMDEpcSALDPISTLKIEETMHELKmnytiiIVTHN 212
Cdd:COG0419 151 SGLdpieTLSGGERLRLALADLLS-----LILDF--GSLDEERLERLLDALEELA------IITHV 203
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
8-237 |
2.93e-05 |
|
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: 45.12 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 8 TPKNIILslenvsISYGTFEavrnvfcnFKKGNITSLIGPSGCGKSTVLRSLNrmnDLIPncslkgtvLFDGTNIYDKRV 87
Cdd:TIGR00954 461 TPNGDVL------IESLSFE--------VPSGNNLLICGPNGCGKSSLFRILG---ELWP--------VYGGRLTKPAKG 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 88 DPVEVRRRIGM---VFQQPNPFPKSIYENIAFGARINGFTGDMDEL-VESSLRKAALWDECKDKLNdsgySLSGGQQQRL 163
Cdd:TIGR00954 516 KLFYVPQRPYMtlgTLRDQIIYPDSSEDMKRRGLSDKDLEQILDNVqLTHILEREGGWSAVQDWMD----VLSGGEKQRI 591
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 123755092 164 CIARTIAIEPEIILMDEPCSALDPistlKIEETMHEL--KMNYTIIIVTHnmqqalRVSdMTAFFNAVEYEDGDGG 237
Cdd:TIGR00954 592 AMARLFYHKPQFAILDECTSAVSV----DVEGYMYRLcrEFGITLFSVSH------RKS-LWKYHEYLLYMDGRGG 656
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
14-224 |
4.89e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.11 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 14 LSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLnrMNDLIPNcslKGTVLF-DGTNI-Ydkrvdpve 91
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL--VGELEPD---SGTVKWsENANIgY-------- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 92 vrrrigmvfqqpnpFPKSIYENiaFGARINGF--------TGDMDELVESSLRKaALWDEckDKLNDSGYSLSGGQQQRL 163
Cdd:PRK15064 387 --------------YAQDHAYD--FENDLTLFdwmsqwrqEGDDEQAVRGTLGR-LLFSQ--DDIKKSVKVLSGGEKGRM 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 123755092 164 CIARTIAIEPEIILMDEPCSALDPIStlkIEETMHELKmNY--TIIIVTHNMQ----QALRVSDMTA 224
Cdd:PRK15064 448 LFGKLMMQKPNVLVMDEPTNHMDMES---IESLNMALE-KYegTLIFVSHDREfvssLATRIIEITP 510
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
154-221 |
6.24e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 44.05 E-value: 6.24e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 123755092 154 SLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL-KMNYTIIIVTHNMQQALRVSD 221
Cdd:TIGR02633 403 RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLaQEGVAIIVVSSELAEVLGLSD 471
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-186 |
6.50e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.34 E-value: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 16 LENVSISYGTFE--------AVRNVFCNFKKGNITSLIGPSGCGK----STVLRSLNRMNDliPNCSLKGTVLFdgtniy 83
Cdd:PLN03130 612 LPAISIKNGYFSwdskaerpTLSNINLDVPVGSLVAIVGSTGEGKtsliSAMLGELPPRSD--ASVVIRGTVAY------ 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 84 dkrvdpvevrrrigmVFQQPNPFPKSIYENIAFGA-----------RINGFTGDMDELVESSLrkaalwdeckDKLNDSG 152
Cdd:PLN03130 684 ---------------VPQVSWIFNATVRDNILFGSpfdperyeraiDVTALQHDLDLLPGGDL----------TEIGERG 738
|
170 180 190
....*....|....*....|....*....|....
gi 123755092 153 YSLSGGQQQRLCIARTIAIEPEIILMDEPCSALD 186
Cdd:PLN03130 739 VNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
153-266 |
8.96e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 8.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 153 YSLSGGQQQRLCIARTI---AIEPEIILMDEPCSALdpiSTLKIEETMHELK----MNYTIIIVTHNMqQALRVSDMTaf 225
Cdd:PRK00635 808 SSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGL---HTHDIKALIYVLQslthQGHTVVIIEHNM-HVVKVADYV-- 881
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 123755092 226 fnaVEYEDGDGGKVGYLAEFNSTKKIF--NSPKEKTTQEYISG 266
Cdd:PRK00635 882 ---LELGPEGGNLGGYLLASCSPEELIhlHTPTAKALRPYLSS 921
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
154-221 |
1.52e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.61 E-value: 1.52e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 123755092 154 SLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHEL-KMNYTIIIVTHNMQQALRVSD 221
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLvQQGVAIIVISSELPEVLGLSD 473
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
13-221 |
1.79e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 41.47 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 13 ILSLENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLRSLNRMndLIPNcslKGTVLFDGTNIyDKrvDPVEV 92
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGL--LNPE---KGEILFERQSI-KK--DLCTY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 93 RRRIGMVFQQP--NPFpKSIYENIAFGARINGFTGDMDELVESSLRKAALWDECKdklndsgySLSGGQQQRLCIARTIA 170
Cdd:PRK13540 73 QKQLCFVGHRSgiNPY-LTLRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCG--------LLSSGQKRQVALLRLWM 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 123755092 171 IEPEIILMDEPCSALDPISTLKIEETMHELKMNYTIIIVTHNMQQALRVSD 221
Cdd:PRK13540 144 SKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
155-221 |
1.87e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 42.30 E-value: 1.87e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 123755092 155 LSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMN-YTIIIVTHNMQQALRVSD 221
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEgLSIILVSSEMPEVLGMSD 463
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
124-186 |
2.04e-04 |
|
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: 42.46 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 124 TGDMDELVESSLRKAAlwdecKDKLNDSGY-------------------SLSGGQQQRLCIARTIAIEPEIILMDEPCSA 184
Cdd:COG1245 411 SPDYDGTVEEFLRSAN-----TDDFGSSYYkteiikplgleklldknvkDLSGGELQRVAIAACLSRDADLYLLDEPSAH 485
|
..
gi 123755092 185 LD 186
Cdd:COG1245 486 LD 487
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
38-235 |
4.38e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 39.66 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 38 KGNITSLIGPSGCGKSTVLRSLnrMNDLIPNCslKGTVLFDGTNIydkrvdpvevrrrigmvfqqpnpfpksiyeniafg 117
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARAL--ARELGPPG--GGVIYIDGEDI----------------------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 118 aringftgdmdelvesslRKAALWDECKDKLNDSGYSLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETM 197
Cdd:smart00382 42 ------------------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLE 103
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 123755092 198 HELKM-------NYTIIIVTHNMQQALRVSDMTAFFNAVEYEDGD 235
Cdd:smart00382 104 ELRLLlllksekNLTVILTTNDEKDLGPALLRRRFDRRIVLLLIL 148
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
154-226 |
4.56e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 40.25 E-value: 4.56e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 123755092 154 SLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMN--YTIIIVTHNMQQALRVSDMTAFF 226
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEgkKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
153-186 |
4.80e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.38 E-value: 4.80e-04
10 20 30
....*....|....*....|....*....|....
gi 123755092 153 YSLSGGQQQRLCIARTIAIEPEIILMDEPCSALD 186
Cdd:PLN03073 626 YTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
16-188 |
5.73e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.77 E-value: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 16 LENVSISYGTFEAVRNVFCNFKKGNITSLIGPSGCGKSTVLrSL-------NRMNDLipncslkgtVLF-----DGTNIY 83
Cdd:PRK10938 263 LNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLL-SLitgdhpqGYSNDL---------TLFgrrrgSGETIW 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 84 DkrvdpveVRRRIGMVFQQpnpfpksiyenIAFGARING------FTGDMDEL-----VESSLRKAAlwDECKDKLNDSG 152
Cdd:PRK10938 333 D-------IKKHIGYVSSS-----------LHLDYRVSTsvrnviLSGFFDSIgiyqaVSDRQQKLA--QQWLDILGIDK 392
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 123755092 153 -------YSLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPI 188
Cdd:PRK10938 393 rtadapfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPL 435
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-211 |
5.97e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.87 E-value: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 1 MIKTNKKTP--KNIilsLENVSISYgtfeavrnvFCNFKKGnitsLIGPSGCGKSTVLRSlnrMNDLIPNcslkgtvlFD 78
Cdd:PRK11819 9 MNRVSKVVPpkKQI---LKDISLSF---------FPGAKIG----VLGLNGAGKSTLLRI---MAGVDKE--------FE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 79 GtniydkrvdpvEVRR----RIGMVFQQP--NPfPKSIYENIAFG--------ARINGFT-------GDMDEL------- 130
Cdd:PRK11819 62 G-----------EARPapgiKVGYLPQEPqlDP-EKTVRENVEEGvaevkaalDRFNEIYaayaepdADFDALaaeqgel 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 131 -----------VESSLRKA--AL----WDECKDKLndsgyslSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKI 193
Cdd:PRK11819 130 qeiidaadawdLDSQLEIAmdALrcppWDAKVTKL-------SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWL 202
|
250 260
....*....|....*....|
gi 123755092 194 EETMHElkmnY--TIIIVTH 211
Cdd:PRK11819 203 EQFLHD----YpgTVVAVTH 218
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
36-211 |
8.52e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.51 E-value: 8.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 36 FKKGnITSLIGPSGCGKSTVLRSLNR--MNDLIPNCSL---KGTVLFDGTNIYDKRV-------DPVEVRRRIgmvfqqp 103
Cdd:cd03240 20 FFSP-LTLIVGQNGAGKTTIIEALKYalTGELPPNSKGgahDPKLIREGEVRAQVKLafenangKKYTITRSL------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 104 npfpkSIYENIAFGARingftGDMDELVEsslrkaalwDECKdklndsgySLSGGQQQ------RLCIARTIAIEPEIIL 177
Cdd:cd03240 92 -----AILENVIFCHQ-----GESNWPLL---------DMRG--------RCSGGEKVlasliiRLALAETFGSNCGILA 144
|
170 180 190
....*....|....*....|....*....|....*...
gi 123755092 178 MDEPCSALDP----ISTLKIEEtMHELKMNYTIIIVTH 211
Cdd:cd03240 145 LDEPTTNLDEenieESLAEIIE-ERKSQKNFQLIVITH 181
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
154-222 |
9.77e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 40.32 E-value: 9.77e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 123755092 154 SLSGGQQQRLCIARTIAIEPEIILMDEPCSALDpISTLkieETMHELKMNY--TIIIVTH------NMqqALRVSDM 222
Cdd:PRK11147 156 SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD-IETI---EWLEGFLKTFqgSIIFISHdrsfirNM--ATRIVDL 226
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
128-220 |
1.09e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 39.72 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 128 DELVES-SLRKAAlwdeckdklNDSGYSLSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKI-EETMHELKMNYT 205
Cdd:NF000106 126 DELLERfSLTEAA---------GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVwDEVRSMVRDGAT 196
|
90
....*....|....*
gi 123755092 206 IIIVTHNMQQALRVS 220
Cdd:NF000106 197 VLLTTQYMEEAEQLA 211
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
148-268 |
1.63e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.61 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 148 LNDSGYSLSGGQQQRLCIARTIAIEPEIIL--MDEPCSALDPISTLKIEETMHELK-MNYTIIIVTHNmQQALRVSDMTa 224
Cdd:TIGR00630 482 LSRAAGTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHQRDNRRLINTLKRLRdLGNTLIVVEHD-EDTIRAADYV- 559
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 123755092 225 ffnaVEYEDGDGGKVGYLAEFNSTKKIFNSPKEKTTQeYISGKF 268
Cdd:TIGR00630 560 ----IDIGPGAGEHGGEVVASGTPEEILANPDSLTGQ-YLSGRK 598
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
155-186 |
1.72e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 39.83 E-value: 1.72e-03
10 20 30
....*....|....*....|....*....|..
gi 123755092 155 LSGGQQQRLCIARTIAIEPEIILMDEPCSALD 186
Cdd:PLN03140 1020 LSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
156-215 |
1.99e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 38.64 E-value: 1.99e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123755092 156 SGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELK-MNYTIIIVTHNMQQ 215
Cdd:PRK13546 145 SSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKeQNKTIFFVSHNLGQ 205
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
155-240 |
2.16e-03 |
|
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: 38.54 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 155 LSGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMNY--TIIIVTHNMQQALRVSDMTAFFnaveye 232
Cdd:cd03237 116 LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNekTAFVVEHDIIMIDYLADRLIVF------ 189
|
....*...
gi 123755092 233 DGDGGKVG 240
Cdd:cd03237 190 EGEPSVNG 197
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
37-221 |
2.99e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 38.74 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 37 KKGNITSLIGPSGCGKSTVLRSL---NRMNDlipncslkGTVLFDGtniydKRVDPVEVRRRI--GMVF-----QQPNPF 106
Cdd:PRK11288 277 RAGEIVGLFGLVGAGRSELMKLLygaTRRTA--------GQVYLDG-----KPIDIRSPRDAIraGIMLcpedrKAEGII 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123755092 107 P-KSIYENIAFGARINGFTGDMdelVESSLRKAALWDECKDKLNDSGYS-------LSGGQQQRLCIARTIAIEPEIILM 178
Cdd:PRK11288 344 PvHSVADNINISARRHHLRAGC---LINNRWEAENADRFIRSLNIKTPSreqlimnLSGGNQQKAILGRWLSEDMKVILL 420
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 123755092 179 DEPCSALDPISTLKIEETMHEL-KMNYTIIIVTHNMQQALRVSD 221
Cdd:PRK11288 421 DEPTRGIDVGAKHEIYNVIYELaAQGVAVLFVSSDLPEVLGVAD 464
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
156-215 |
4.11e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 38.33 E-value: 4.11e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 123755092 156 SGGQQQRLCIARTIAIEPEIILMDEPCSALDPISTLKIEETMHELKMN-YTIIIVTHNMQQ 215
Cdd:PRK13545 145 SSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQgKTIFFISHSLSQ 205
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
155-186 |
9.11e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 37.10 E-value: 9.11e-03
10 20 30
....*....|....*....|....*....|..
gi 123755092 155 LSGGQQQRLCIARTIAIEPEIILMDEPCSALD 186
Cdd:PRK13409 454 LSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| |
