|
Name |
Accession |
Description |
Interval |
E-value |
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-327 |
0e+00 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 699.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 1 MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLVFNGQDLQRISE 80
Cdd:PRK11022 1 MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 81 KERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKSTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQ 160
Cdd:PRK11022 81 KERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHA 240
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 241 IFHAPRHPYTQALLRALPEFAQDKERLASLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPALNMLAdGRQSKCHYPLD 320
Cdd:PRK11022 241 IFRAPRHPYTQALLRALPEFAQDKARLASLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPALNMLA-GRQSKCHYPLD 319
|
....*..
gi 447119240 321 DAGRPTL 327
Cdd:PRK11022 320 DAGRPTL 326
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-322 |
0e+00 |
|
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: 518.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVmAEKLVFNGQDLQRISEKE 82
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGIT-SGEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 83 RRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKSTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQRV 162
Cdd:COG0444 80 LRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 163 MIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAIF 242
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 243 HAPRHPYTQALLRALPEFAQDKERLASLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPALNMLADGRQSKCHYPLDDA 322
Cdd:COG0444 240 ENPRHPYTRALLSSIPRLDPDGRRLIPIPGEPPSLLNPPSGCRFHPRCPYAMDRCREEEPPLREVGPGHRVACHLYEEEA 319
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-259 |
1.90e-149 |
|
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: 430.65 E-value: 1.90e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 1 MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLVFNGQDLQRISE 80
Cdd:COG4172 4 MPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 81 KERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKSTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQ 160
Cdd:COG4172 84 RELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHA 240
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAE 243
|
250
....*....|....*....
gi 447119240 241 IFHAPRHPYTQALLRALPE 259
Cdd:COG4172 244 LFAAPQHPYTRKLLAAEPR 262
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-321 |
5.34e-129 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 371.36 E-value: 5.34e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 1 MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLvFNGQDLQRISE 80
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSAT-FNGREILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 81 KERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKSTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQ 160
Cdd:PRK09473 89 KELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGGMRQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHA 240
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 241 IFHAPRHPYTQALLRALPEFAQDKERLASLPGVVPGKYDRPNGCLLNPRCPYATDRCRaEEPALNMLADGRQSKCHYPLD 320
Cdd:PRK09473 249 VFYQPSHPYSIGLLNAVPRLDAEGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEICS-SAPPLEEFGPGRLRACFKPVE 327
|
.
gi 447119240 321 D 321
Cdd:PRK09473 328 E 328
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-319 |
3.62e-127 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 366.54 E-value: 3.62e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 1 MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLVFNGQDLQRISE 80
Cdd:COG4170 1 MPLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADRFRWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 81 KERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNK-----STRRQRAIDLLNQVGIPDPASRLDVYPHQLS 155
Cdd:COG4170 81 RERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIPSWTFKGKwwqrfKWRKKRAIELLHRVGIKDHKDIMNSYPHELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVET 235
Cdd:COG4170 161 EGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 236 GDAHAIFHAPRHPYTQALLRALPEFAQD---KERLASLPGVVPGKYDRPNGCLLNPRCPYATDRCrAEEPALNMLaDGRQ 312
Cdd:COG4170 241 GPTEQILKSPHHPYTKALLRSMPDFRQPlphKSRLNTLPGSIPPLQHLPIGCRLGPRCPYAQKKC-VETPRLRKI-KGHE 318
|
....*..
gi 447119240 313 SKCHYPL 319
Cdd:COG4170 319 FACHFPL 325
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-323 |
1.99e-117 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 341.71 E-value: 1.99e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHF-------GDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyP--GRVmaeklVFNGQ 73
Cdd:COG4608 7 LLEVRDLKKHFpvrgglfGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEE-PtsGEI-----LFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 74 DLQRISEKERRNLvGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKSTRRQRAIDLLNQVGI-PDPASRldvYPH 152
Cdd:COG4608 81 DITGLSGRELRPL-RRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLrPEHADR---YPH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
Cdd:COG4608 157 EFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 233 VETGDAHAIFHAPRHPYTQALLRA--LPEFAQDKERLAsLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPALNMLADG 310
Cdd:COG4608 237 VEIAPRDELYARPLHPYTQALLSAvpVPDPERRRERIV-LEGDVPSPLNPPSGCRFHTRCPYAQDRCATEEPPLREVGPG 315
|
330
....*....|...
gi 447119240 311 RQSKCHYPLDDAG 323
Cdd:COG4608 316 HQVACHLAEEGSG 328
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-236 |
5.30e-114 |
|
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: 329.47 E-value: 5.30e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLVFNGQDLQRISEKE 82
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGL----LKPTSGSIIFDGKDLLKLSRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 83 RRNLvGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKSTRRQRAIDLLNqVGIPDPASRLDVYPHQLSGGMSQRV 162
Cdd:cd03257 77 RKIR-RKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLL-VGVGLPEEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447119240 163 MIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-259 |
2.55e-105 |
|
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: 317.23 E-value: 2.55e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHFGDESA-PFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyP--GRVmaeklVFNGQDLQRIS 79
Cdd:COG1123 260 LLEVRNLSKRYPVRGKgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR-PtsGSI-----LFDGKDLTKLS 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 80 EKERRNLvGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKSTRRQRAIDLLNQVGIPdpASRLDVYPHQLSGGMS 159
Cdd:COG1123 334 RRSLREL-RRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLP--PDLADRYPHELSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 160 QRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAH 239
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTE 490
|
250 260
....*....|....*....|
gi 447119240 240 AIFHAPRHPYTQALLRALPE 259
Cdd:COG1123 491 EVFANPQHPYTRALLAAVPS 510
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-320 |
3.04e-102 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 303.26 E-value: 3.04e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 1 MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLVFNGQDLQRISE 80
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 81 KERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAI-----KVHQGGNKSTRRQRAIDLLNQVGIPDPASRLDVYPHQLS 155
Cdd:PRK15093 81 RERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIpgwtyKGRWWQRFGWRKRRAIELLHRVGIKDHKDAMRSFPYELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVET 235
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 236 GDAHAIFHAPRHPYTQALLRALPEFAQD---KERLASLPGVVPGKYDRPNGCLLNPRCPYATDRCrAEEPALnmladgRQ 312
Cdd:PRK15093 241 APSKELVTTPHHPYTQALIRAIPDFGSAmphKSRLNTLPGAIPLLEHLPIGCRLGPRCPYAQREC-IETPRL------TG 313
|
330
....*....|...
gi 447119240 313 SK-----CHYPLD 320
Cdd:PRK15093 314 AKnhlyaCHFPLN 326
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-259 |
2.59e-101 |
|
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: 307.77 E-value: 2.59e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHF-------GDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVmaeklVFNGQDL 75
Cdd:COG4172 275 LLEARDLKVWFpikrglfRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEI-----RFDGQDL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 76 QRISEKERRNLvGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQ-GGNKSTRRQRAIDLLNQVGIpDPASRlDVYPHQL 154
Cdd:COG4172 350 DGLSRRALRPL-RRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGL-DPAAR-HRYPHEF 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVE 234
Cdd:COG4172 427 SGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVE 506
|
250 260
....*....|....*....|....*
gi 447119240 235 TGDAHAIFHAPRHPYTQALLRALPE 259
Cdd:COG4172 507 QGPTEQVFDAPQHPYTRALLAAAPL 531
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-271 |
1.05e-98 |
|
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: 300.28 E-value: 1.05e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 2 ALLNVDKLSVHFGDESAPfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVmAEKLVFNGQDLQRISEK 81
Cdd:COG1123 3 PLLEVRDLSVRYPGGDVP--AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRI-SGEVLLDGRDLLELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 82 ERrnlvGAEVAMIFQDPMTSLNPcYTVGFQIMEAIKVhQGGNKSTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQR 161
Cdd:COG1123 80 LR----GRRIGMVFQDPMTQLNP-VTVGDQIAEALEN-LGLSRAEARARVLELLEAVGL---ERRLDRYPHQLSGGQRQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAI 241
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
250 260 270
....*....|....*....|....*....|
gi 447119240 242 FHAPRhpytqaLLRALPEFAQDKERLASLP 271
Cdd:COG1123 231 LAAPQ------ALAAVPRLGAARGRAAPAA 254
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-259 |
7.91e-95 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 293.69 E-value: 7.91e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPG-RVMAEKLVFNGQDLQRI--- 78
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGgLVQCDKMLLRRRSRQVIels 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 79 --SEKERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKSTRRQRAIDLLNQVGIPDPASRLDVYPHQLSG 156
Cdd:PRK10261 92 eqSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
|
250 260
....*....|....*....|...
gi 447119240 237 DAHAIFHAPRHPYTQALLRALPE 259
Cdd:PRK10261 252 SVEQIFHAPQHPYTRALLAAVPQ 274
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-259 |
8.87e-93 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 285.83 E-value: 8.87e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 1 MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRV-MAEKLVFNGQDLQRIS 79
Cdd:PRK15134 3 QPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVyPSGDIRFHGESLLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 80 EKERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKSTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMS 159
Cdd:PRK15134 83 EQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGGER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 160 QRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAH 239
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAA 242
|
250 260
....*....|....*....|
gi 447119240 240 AIFHAPRHPYTQALLRALPE 259
Cdd:PRK15134 243 TLFSAPTHPYTQKLLNSEPS 262
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
21-326 |
3.05e-91 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 275.30 E-value: 3.05e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 21 RAVDRISYSVKQGEVVGIVGESGSGKSvsSLAIM-GLIDYPgrvMAEKLVFNGQDLQRISEKERRNLvGAEVAMIFQDPM 99
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKS--TLARLlTMIETP---TGGELYYQGQDLLKADPEAQKLL-RQKIQIVFQNPY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 100 TSLNPCYTVGFQIMEAIKVHQGGNKSTRRQRAIDLLNQVGI-PDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIAD 178
Cdd:PRK11308 103 GSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLrPEHYDR---YPHMFSGGQRQRIAIARALMLDPDVVVAD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 179 EPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAIFHAPRHPYTQALLRALP 258
Cdd:PRK11308 180 EPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLSATP 259
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 259 EFAQD--KERLaSLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPALNMLaDGRQSKCHYPLDDAGRPT 326
Cdd:PRK11308 260 RLNPDdrRERI-KLTGELPSPLNPPPGCAFNARCPRAFGRCRQEQPQLRDY-DGRLVACFAVEQDENPQA 327
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-260 |
9.86e-89 |
|
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: 265.90 E-value: 9.86e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLI-DYPGRVMaeklvFNGQDLQRISEK 81
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLErPWSGEVT-----FDGRPVTRRRRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 82 ERRnlvgAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHqggNKSTRRQRAIDLLNQVGIPdpASRLDVYPHQLSGGMSQR 161
Cdd:COG1124 76 AFR----RRVQMVFQDPYASLHPRHTVDRILAEPLRIH---GLPDREERIAELLEQVGLP--PSFLDRYPHQLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAI 241
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
250
....*....|....*....
gi 447119240 242 FHAPRHPYTQALLRALPEF 260
Cdd:COG1124 227 LAGPKHPYTRELLAASLAF 245
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-305 |
1.09e-86 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 263.49 E-value: 1.09e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHF---GDESAPF------RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYP-GRVmaeklVFNG 72
Cdd:PRK15079 8 LLEVADLKVHFdikDGKQWFWqppktlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATdGEV-----AWLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 73 QDLQRISEKERRNlVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGG-NKSTRRQRAIDLLNQVGI-PDPASRldvY 150
Cdd:PRK15079 83 KDLLGMKDDEWRA-VRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKlSRQEVKDRVKAMMLKVGLlPNLINR---Y 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 151 PHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAG 230
Cdd:PRK15079 159 PHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLG 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447119240 231 QVVETGDAHAIFHAPRHPYTQALLRALPEFAQDKERLAS---LPGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPALN 305
Cdd:PRK15079 239 HAVELGTYDEVYHNPLHPYTKALMSAVPIPDPDLERNKTiqlLEGELPSPINPPSGCVFRTRCPIAGPECAKTRPVLE 316
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
22-256 |
6.86e-78 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 237.65 E-value: 6.86e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLVFNGQDLQRISekerrnLVGAEVAMIFQDPMTS 101
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTQTSGEILLDGRPLLPLS------IRGRHIATIMQNPRTA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 102 LNPCYTVGFQIMEAIKVHqGGNKSTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPT 181
Cdd:TIGR02770 75 FNPLFTMGNHAIETLRSL-GKLSKQARALILEALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPT 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447119240 182 TALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAIFHAPRHPYTQALLRA 256
Cdd:TIGR02770 154 TDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLSA 228
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-254 |
3.91e-66 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 208.92 E-value: 3.91e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 1 MALLNVDKLSVHFGDESAPFR-----AVDRISYSVKQGEVVGIVGESGSGKSvsSLAIM--GLIdypgRVMAEKLVFNGQ 73
Cdd:COG4167 2 SALLEVRNLSKTFKYRTGLFRrqqfeAVKPVSFTLEAGQTLAIIGENGSGKS--TLAKMlaGII----EPTSGEILINGH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 74 DLQRISEKERRNLVgaevAMIFQDPMTSLNPCYTVGfQIMEA-IKVHQGGNKSTRRQRAIDLLNQVGI-PDPAsrlDVYP 151
Cdd:COG4167 76 KLEYGDYKYRCKHI----RMIFQDPNTSLNPRLNIG-QILEEpLRLNTDLTAEEREERIFATLRLVGLlPEHA---NFYP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 152 HQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQ 231
Cdd:COG4167 148 HMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGE 227
|
250 260
....*....|....*....|...
gi 447119240 232 VVETGDAHAIFHAPRHPYTQALL 254
Cdd:COG4167 228 VVEYGKTAEVFANPQHEVTKRLI 250
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-255 |
4.63e-64 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 211.10 E-value: 4.63e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHFGDESAPFR-------AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVmaeklVFNGQDL 75
Cdd:PRK15134 275 LLDVEQLQVAFPIRKGILKrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEI-----WFDGQPL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 76 QRISekeRRNL--VGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGG-NKSTRRQRAIDLLNQVGIpDPASRlDVYPH 152
Cdd:PRK15134 350 HNLN---RRQLlpVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTlSAAQREQQVIAVMEEVGL-DPETR-HRYPA 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
Cdd:PRK15134 425 EFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEV 504
|
250 260
....*....|....*....|...
gi 447119240 233 VETGDAHAIFHAPRHPYTQALLR 255
Cdd:PRK15134 505 VEQGDCERVFAAPQQEYTRQLLA 527
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
2-253 |
4.90e-64 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 203.12 E-value: 4.90e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 2 ALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMAEKLVFNGQDLQRIS 79
Cdd:COG4107 7 PLLSVRGLSKRYGPGCGTVVACRDVSFDLYPGEVLGIVGESGSGKS-TLLKCLYFDLAPtsGSVYYRDRDGGPRDLFALS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 80 EKERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEaiKVHQGGNK--STRRQRAIDLLNQVGIPdpASRLDVYPHQLSGG 157
Cdd:COG4107 86 EAERRRLRRTDWGMVYQNPRDGLRMDVSAGGNIAE--RLMAAGERhyGDIRARALEWLERVEIP--LERIDDLPRTFSGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 158 MSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGD 237
Cdd:COG4107 162 MQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKNGRVVESGL 241
|
250
....*....|....*.
gi 447119240 238 AHAIFHAPRHPYTQAL 253
Cdd:COG4107 242 TDQVLEDPQHPYTQLL 257
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-234 |
5.52e-61 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 194.11 E-value: 5.52e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 2 ALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMaeklvFNGQDLQRIS 79
Cdd:COG1136 3 PLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKS-TLLNILGGLDRPtsGEVL-----IDGQDISSLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 80 EKERRNLVGAEVAMIFQDPmtSLNPCYTVGFQIMEAIKVhQGGNKSTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMS 159
Cdd:COG1136 77 ERELARLRRRHIGFVFQFF--NLLPELTALENVALPLLL-AGVSRKERRERARELLERVGLGD---RLDHRPSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447119240 160 QRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALvAEAAHKIIVMYAGQVVE 234
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPEL-AARADRVIRLRDGRIVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-232 |
3.83e-60 |
|
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: 191.93 E-value: 3.83e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVmaeklVFNGQDLQRISEK 81
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS-TLLNILGGLDRPtsGEV-----RVDGTDISKLSEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 82 ERRNLVGAEVAMIFQDPmtSLNPCYTVgFQIMEAIKVHQGGNKSTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMSQR 161
Cdd:cd03255 75 ELAAFRRRHIGFVFQSF--NLLPDLTA-LENVELPLLLAGVPKKERRERAEELLERVGLGD---RLNHYPSELSGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447119240 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLaLVAEAAHKIIVMYAGQV 232
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-277 |
2.64e-59 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 193.37 E-value: 2.64e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 6 VDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvsSLA--IMGLiDYP--GRVmaeklVFNGQDLQRISEK 81
Cdd:COG1135 4 LENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKS--TLIrcINLL-ERPtsGSV-----LVDGVDLTALSER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 82 ERRNL---VGaevaMIFQdpmtslnpcytvGFQIMEAIKV---------HQGGNKSTRRQRAIDLLNQVGIPDpasRLDV 149
Cdd:COG1135 76 ELRAArrkIG----MIFQ------------HFNLLSSRTVaenvalpleIAGVPKAEIRKRVAELLELVGLSD---KADA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 150 YPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYA 229
Cdd:COG1135 137 YPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLEN 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 447119240 230 GQVVETGDAHAIFHAPRHPYTQALLRALPEFAQDKERLASLPGVVPGK 277
Cdd:COG1135 217 GRIVEQGPVLDVFANPQSELTRRFLPTVLNDELPEELLARLREAAGGG 264
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
23-256 |
1.31e-58 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 189.14 E-value: 1.31e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLVFNGQDLQRISekerrnLVGAEVAMIFQDPMTSL 102
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTAGRVLLDGKPVAPCA------LRGRKIATIMQNPRSAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 103 NPCYTVGFQIMEAIKVHqggNKSTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTT 182
Cdd:PRK10418 93 NPLHTMHTHARETCLAL---GKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447119240 183 ALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAIFHAPRHPYTQALLRA 256
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-303 |
1.74e-58 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 198.54 E-value: 1.74e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGrvmaEKLVFNGQDLQRISEKE----RRNlvgaeVAMIFQD 97
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQG----GEIIFNGQRIDTLSPGKlqalRRD-----IQFIFQD 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 98 PMTSLNPCYTVGFQIMEAIKVHQGGNKSTRRQRAIDLLNQVGI-PDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLI 176
Cdd:PRK10261 410 PYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLlPEHAWR---YPHEFSGGQRQRICIARALALNPKVII 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 177 ADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAIFHAPRHPYTQALLRA 256
Cdd:PRK10261 487 ADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAA 566
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 447119240 257 LPefaqdkerlaslpgVVPGKYDRPNGCLLNPRCPYATdRCRAEEPA 303
Cdd:PRK10261 567 VP--------------VADPSRQRPQRVLLSDDLPSNI-HLRGEEVA 598
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-246 |
9.07e-57 |
|
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: 183.55 E-value: 9.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVmaeklVFNGQDLQRISE 80
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKS-TLIRCINGLERPtsGSV-----LVDGTDLTLLSG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 81 KERRNLvGAEVAMIFQ--DPMTSLnpcyTVGFQIMEAIKVHqGGNKSTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGM 158
Cdd:cd03258 75 KELRKA-RRRIGMIFQhfNLLSSR----TVFENVALPLEIA-GVPKAEIEERVLELLELVGLEDKA---DAYPAQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDA 238
Cdd:cd03258 146 KQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTV 225
|
....*...
gi 447119240 239 HAIFHAPR 246
Cdd:cd03258 226 EEVFANPQ 233
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-257 |
6.23e-53 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 174.03 E-value: 6.23e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSvsSL--AIMGL--IDYpGRVmaeklVFNGQDLQrI 78
Cdd:COG1126 1 MIEIENLHKSFGD----LEVLKGISLDVEKGEVVVIIGPSGSGKS--TLlrCINLLeePDS-GTI-----TVDGEDLT-D 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 79 SEKERRNLVgAEVAMIFQdpmtSLN--PCYTVGFQIMEAIKVHQGGNKSTRRQRAIDLLNQVGIPDpasRLDVYPHQLSG 156
Cdd:COG1126 68 SKKDINKLR-RKVGMVFQ----QFNlfPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLAD---KADAYPAQLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:COG1126 140 GQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDL-AKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEG 218
|
250 260
....*....|....*....|.
gi 447119240 237 DAHAIFHAPRHPYTQALLRAL 257
Cdd:COG1126 219 PPEEFFENPQHERTRAFLSKV 239
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-260 |
1.68e-52 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 173.72 E-value: 1.68e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 1 MALLNVDKLSVHFGDES----APFRAV-DRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLiDYP--GRVMaeklvFNGQ 73
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGGlsgkHQHQTVlNNVSLSLKSGETVALLGRSGCGKSTLARLLVGL-ESPsqGNVS-----WRGE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 74 DLQRISEKERRNLVGaEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKSTRRQRAIDLLNQVGIPDpaSRLDVYPHQ 153
Cdd:PRK10419 75 PLAKLNRAQRKAFRR-DIQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDD--SVLDKRPPQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
250 260 270
....*....|....*....|....*....|.
gi 447119240 234 ET---GDAHAIfhapRHPYTQALLRA-LPEF 260
Cdd:PRK10419 232 ETqpvGDKLTF----SSPAGRVLQNAvLPAF 258
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-240 |
4.35e-51 |
|
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: 169.15 E-value: 4.35e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 2 ALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMAeklvfNGQDLQRIS 79
Cdd:COG4181 7 PIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKS-TLLGLLAGLDRPtsGTVRL-----AGQDLFALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 80 EKERRNLVGAEVAMIFQD----P-MTSL-N---PCYTVGFQimEAikvhqggnkstrRQRAIDLLNQVGIpdpASRLDVY 150
Cdd:COG4181 81 EDARARLRARHVGFVFQSfqllPtLTALeNvmlPLELAGRR--DA------------RARARALLERVGL---GHRLDHY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 151 PHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALvAEAAHKIIVMYAG 230
Cdd:COG4181 144 PAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPAL-AARCDRVLRLRAG 222
|
250
....*....|
gi 447119240 231 QVVETGDAHA 240
Cdd:COG4181 223 RLVEDTAATA 232
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-253 |
8.23e-51 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 168.95 E-value: 8.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHFGdesaPFRAVDRISYSVKQGEVVGIVGESGSGKS--VSSLAIM-----GLIDYPGRvmaeklvfNGQ-- 73
Cdd:PRK11701 6 LLSVRGLTKLYG----PRKGCRDVSFDLYPGEVLGIVGESGSGKTtlLNALSARlapdaGEVHYRMR--------DGQlr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 74 DLQRISEKERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIME---AIKVHQGGNKstrRQRAIDLLNQVGIPdpASRLDVY 150
Cdd:PRK11701 74 DLYALSEAERRRLLRTEWGFVHQHPRDGLRMQVSAGGNIGErlmAVGARHYGDI---RATAGDWLERVEID--AARIDDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 151 PHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAG 230
Cdd:PRK11701 149 PTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
250 260
....*....|....*....|...
gi 447119240 231 QVVETGDAHAIFHAPRHPYTQAL 253
Cdd:PRK11701 229 RVVESGLTDQVLDDPQHPYTQLL 251
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2-262 |
8.72e-50 |
|
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: 166.90 E-value: 8.72e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 2 ALLNVDKLSVHFgDESAPFRA------VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLVFNGQDL 75
Cdd:TIGR02769 1 SLLEVRDVTHTY-RTGGLFGAkqrapvLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGL----EKPAQGTVSFRGQDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 76 QRISEKERRNlVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKSTRRQRAIDLLNQVGIPDpaSRLDVYPHQLS 155
Cdd:TIGR02769 76 YQLDRKQRRA-FRRDVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRS--EDADKLPRQLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVET 235
Cdd:TIGR02769 153 GGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEE 232
|
250 260
....*....|....*....|....*...
gi 447119240 236 GDAHAIFhAPRHPYTQALLRA-LPEFAQ 262
Cdd:TIGR02769 233 CDVAQLL-SFKHPAGRNLQSAvLPEHPV 259
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-254 |
2.86e-49 |
|
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: 164.38 E-value: 2.86e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 2 ALLNVDKLSVHFGDesapfRAV-DRISYSVKQGEVVGIVGESGSGKSVssL--AIMGLIdYP--GRVMaeklvFNGQDLQ 76
Cdd:COG1127 4 PMIEVRNLTKSFGD-----RVVlDGVSLDVPRGEILAIIGGSGSGKSV--LlkLIIGLL-RPdsGEIL-----VDGQDIT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 77 RISEKERRNLVgAEVAMIFQ-----DPMTSL-NpcytVGFQIMEaikvHQGGNKSTRRQRAIDLLNQVGIPDPASRldvY 150
Cdd:COG1127 71 GLSEKELYELR-RRIGMLFQggalfDSLTVFeN----VAFPLRE----HTDLSEAEIRELVLEKLELVGLPGAADK---M 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 151 PHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAG 230
Cdd:COG1127 139 PSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADG 218
|
250 260
....*....|....*....|....
gi 447119240 231 QVVETGDAHAIFHAPrHPYTQALL 254
Cdd:COG1127 219 KIIAEGTPEELLASD-DPWVRQFL 241
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-246 |
6.02e-49 |
|
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: 163.27 E-value: 6.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDESapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVmaeklVFNGQDLQRISEKE 82
Cdd:COG1122 1 IELENLSFSYPGGT---PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKpTSGEV-----LVDGKDITKKNLRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 83 RRNLVGaevaMIFQDPMTSL-NPcyTVGFQIMEAIKvHQGGNKSTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQR 161
Cdd:COG1122 73 LRRKVG----LVFQNPDDQLfAP--TVEEDVAFGPE-NLGLPREEIRERVEEALELVGLEHLADR---PPHELSGGQKQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAI 241
Cdd:COG1122 143 VAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNK-EGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
....*
gi 447119240 242 FHAPR 246
Cdd:COG1122 222 FSDYE 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-235 |
9.42e-49 |
|
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: 162.64 E-value: 9.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvsSL--AIMGLIDY-PGRVmaeklVFNGQDLQRise 80
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKS--TLlrIIAGLERPtSGEV-----LVDGEPVTG--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 81 kerrnlVGAEVAMIFQDPmtSLNPCYTVGFQIMEAIKVhQGGNKSTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQ 160
Cdd:cd03293 71 ------PGPDRGYVFQQD--ALLPWLTVLDNVALGLEL-QGVPKAEARERAEELLELVGLSGFENA---YPHQLSGGMRQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDlalVAEA---AHKIIVMYA--GQVVET 235
Cdd:cd03293 139 RVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHD---IDEAvflADRVVVLSArpGRIVAE 215
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-267 |
2.44e-48 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 162.57 E-value: 2.44e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 1 MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvsSL--AIMGLID-YPGRVMaeklvFNGQDLQR 77
Cdd:COG1116 5 APALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKS--TLlrLIAGLEKpTSGEVL-----VDGKPVTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 78 isekerrnlVGAEVAMIFQDPmtSLNPCYTVGFQIMEAIKVhQGGNKSTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGG 157
Cdd:COG1116 78 ---------PGPDRGVVFQEP--ALLPWLTVLDNVALGLEL-RGVPKAERRERARELLELVGL---AGFEDAYPHQLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 158 MSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDlalVAEA---AHKIIVMYA--GQV 232
Cdd:COG1116 143 MRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHD---VDEAvflADRVVVLSArpGRI 219
|
250 260 270
....*....|....*....|....*....|....*.
gi 447119240 233 VETgdaHAI-FHAPRHPytqaLLRALPEFAQDKERL 267
Cdd:COG1116 220 VEE---IDVdLPRPRDR----ELRTSPEFAALRAEI 248
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-249 |
2.78e-48 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 165.27 E-value: 2.78e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 1 MALLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSvsSL--AIMGLIDyP--GRVmaeklVFNGQDLQ 76
Cdd:COG3842 3 MPALELENVSKRYGD----VTALDDVSLSIEPGEFVALLGPSGCGKT--TLlrMIAGFET-PdsGRI-----LLDGRDVT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 77 RISEkERRNlvgaeVAMIFQDP-----MTSL-NpcytVGFqimeAIKVhQGGNKSTRRQRAIDLLNQVGIPDPASRldvY 150
Cdd:COG3842 71 GLPP-EKRN-----VGMVFQDYalfphLTVAeN----VAF----GLRM-RGVPKAEIRARVAELLELVGLEGLADR---Y 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 151 PHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLalvAEA---AHKIIVM 227
Cdd:COG3842 133 PHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQ---EEAlalADRIAVM 209
|
250 260
....*....|....*....|..
gi 447119240 228 YAGQVVETGDAHAIFHAPRHPY 249
Cdd:COG3842 210 NDGRIEQVGTPEEIYERPATRF 231
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
2-257 |
1.56e-47 |
|
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: 160.38 E-value: 1.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 2 ALLNVDKLSVHFGdesaPFRAVDRISYSVKQGEVVGIVGESGSGKS--VSSLAIMGLIDYpGRVMAEKLVFNGQDLQRIS 79
Cdd:TIGR02323 2 PLLQVSGLSKSYG----GGKGCRDVSFDLYPGEVLGIVGESGSGKStlLGCLAGRLAPDH-GTATYIMRSGAELELYQLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 80 EKERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIME---AIKVHQGGNKstrRQRAIDLLNQVGIPdpASRLDVYPHQLSG 156
Cdd:TIGR02323 77 EAERRRLMRTEWGFVHQNPRDGLRMRVSAGANIGErlmAIGARHYGNI---RATAQDWLEEVEID--PTRIDDLPRAFSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:TIGR02323 152 GMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
250 260
....*....|....*....|.
gi 447119240 237 DAHAIFHAPRHPYTQALLRAL 257
Cdd:TIGR02323 232 LTDQVLDDPQHPYTQLLVSSI 252
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
3-271 |
3.04e-47 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 162.28 E-value: 3.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKlsvHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVmaeklVFNGQDLQRISE 80
Cdd:PRK11153 4 LKNISK---VFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKS-TLIRCINLLERPtsGRV-----LVDGQDLTALSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 81 KE----RRNlvgaeVAMIFQDpmTSLNPCYTVGFQIMEAIKVhQGGNKSTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSG 156
Cdd:PRK11153 75 KElrkaRRQ-----IGMIFQH--FNLLSSRTVFDNVALPLEL-AGTPKAEIKARVTELLELVGLSDKA---DRYPAQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:PRK11153 144 GQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQG 223
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 447119240 237 DAHAIFHAPRHPYTQALLRA-----LPEfaQDKERLASLP 271
Cdd:PRK11153 224 TVSEVFSHPKHPLTREFIQStlhldLPE--DYLARLQAEP 261
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-231 |
5.59e-47 |
|
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: 157.63 E-value: 5.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 6 VDKLSVHFGDESAPfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLI-DYPGRVMaeklvFNGQDLQRISEKERR 84
Cdd:cd03225 2 LKNLSFSYPDGARP--ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLgPTSGEVL-----VDGKDLTKLSLKELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 85 NLVGaevaMIFQDPMTSL-NPcyTVGFQIMEAIKvHQGGNKSTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVM 163
Cdd:cd03225 75 RKVG----LVFQNPDDQFfGP--TVEEEVAFGLE-NLGLPEEEIEERVEEALELVGL---EGLRDRSPFTLSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447119240 164 IAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQ 231
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-249 |
5.75e-47 |
|
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: 158.43 E-value: 5.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 6 VDKLSVHFGDesapfRAV-DRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyP--GRVmaeklVFNGQDLQRISEKE 82
Cdd:cd03261 3 LRGLTKSFGG-----RTVlKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLR-PdsGEV-----LIDGEDISGLSEAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 83 RRNLvGAEVAMIFQDP--MTSLNPCYTVGFQIMEaikvHQGGNKSTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQ 160
Cdd:cd03261 72 LYRL-RRRMGMLFQSGalFDSLTVFENVAFPLRE----HTRLSEEEIREIVLEKLEAVGLRGAE---DLYPAELSGGMKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHA 240
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEE 223
|
....*....
gi 447119240 241 IFHAPrHPY 249
Cdd:cd03261 224 LRASD-DPL 231
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-241 |
2.57e-45 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 154.07 E-value: 2.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyP--GRVMaeklvFNGQDLQRISEK 81
Cdd:COG1131 1 IEVRGLTKRYGD----KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLR-PtsGEVR-----VLGEDVARDPAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 82 ERRNlvgaeVAMIFQDPmtSLNPCYTVGfQIMEAIKVHQGGNKSTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMSQR 161
Cdd:COG1131 71 VRRR-----IGYVPQEP--ALYPDLTVR-ENLRFFARLYGLPRKEARERIDELLELFGLTD---AADRKVGTLSGGMKQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAI 241
Cdd:COG1131 140 LGLALALLHDPELLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-236 |
1.17e-43 |
|
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: 149.21 E-value: 1.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLVFNGQDLQRISEKER 83
Cdd:cd03259 1 LELKGLSKTYGS----VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLE----RPDSGEILIDGRDVTGVPPERR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 84 RnlvgaeVAMIFQDPmtSLNPCYTVGFQIMEAIKVhQGGNKSTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVM 163
Cdd:cd03259 73 N------IGMVFQDY--ALFPHLTVAENIAFGLKL-RGVPKAEIRARVRELLELVGLEGLLNR---YPHELSGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447119240 164 IAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-254 |
5.31e-43 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 149.17 E-value: 5.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHFGDESAPFR-----AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGrvmAEKLVFNGQDLQR 77
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGWFRrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIE-PT---SGELLIDDHPLHF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 78 ISEKERRNlvgaEVAMIFQDPMTSLNPCYTVGfQIMEA-IKVHQGGNKSTRRQRAIDLLNQVGI-PDPASrldVYPHQLS 155
Cdd:PRK15112 80 GDYSYRSQ----RIRMIFQDPSTSLNPRQRIS-QILDFpLRLNTDLEPEQREKQIIETLRQVGLlPDHAS---YYPHMLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVET 235
Cdd:PRK15112 152 PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVER 231
|
250
....*....|....*....
gi 447119240 236 GDAHAIFHAPRHPYTQALL 254
Cdd:PRK15112 232 GSTADVLASPLHELTKRLI 250
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
16-258 |
7.75e-43 |
|
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: 148.56 E-value: 7.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 16 ESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPgrvMAEKLVFNGQDLQRISEKERRNLVGAEVAMIF 95
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIE-P---TSGKVLIDGQDIAAMSRKELRELRRKKISMVF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 96 QDpmTSLNPCYTV------GFQImeaikvhQGGNKSTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMSQRVMIAMAIA 169
Cdd:cd03294 109 QS--FALLPHRTVlenvafGLEV-------QGVPRAEREERAAEALELVGLEG---WEHKYPDELSGGMQQRVGLARALA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 170 CRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAIFHAPRHPY 249
Cdd:cd03294 177 VDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
....*....
gi 447119240 250 TQALLRALP 258
Cdd:cd03294 257 VREFFRGVD 265
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-257 |
1.02e-41 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 145.20 E-value: 1.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 2 ALLNVDKLSVHFGDEsapFRAVDRISYSVKQGEVVGIVGESGSGKSvsSL--AIMGLIDyP--GRVMaeklvFNGQDLQR 77
Cdd:COG3638 1 PMLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKS--TLlrCLNGLVE-PtsGEIL-----VDGQDVTA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 78 ISEKERRNLvGAEVAMIFQDPmtSLNPCYTVgfqiMEAIKV----HQGGNKSTR-------RQRAIDLLNQVGIPDPA-S 145
Cdd:COG3638 70 LRGRALRRL-RRRIGMIFQQF--NLVPRLSV----LTNVLAgrlgRTSTWRSLLglfppedRERALEALERVGLADKAyQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 146 RLDvyphQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKII 225
Cdd:COG3638 143 RAD----QLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRII 218
|
250 260 270
....*....|....*....|....*....|..
gi 447119240 226 VMYAGQVVetgdahaiFHAPRHPYTQALLRAL 257
Cdd:COG3638 219 GLRDGRVV--------FDGPPAELTDAVLREI 242
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-232 |
1.03e-41 |
|
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: 144.21 E-value: 1.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGrvmaEKLVFNGQDLQriSEKER 83
Cdd:cd03262 1 IEIKNLHKSFGD----FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDS----GTIIIDGLKLT--DDKKN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 84 RNLVGAEVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGGNKSTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQRVM 163
Cdd:cd03262 71 INELRQKVGMVFQQ--FNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKA---DAYPAQLSGGQQQRVA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447119240 164 IAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQV 232
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAE-EGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
22-234 |
9.17e-41 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 141.73 E-value: 9.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 22 AVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMaeklvFNGQDLQRISEKE----RRNLvGaevaMIF 95
Cdd:COG2884 17 ALSDVSLEIEKGEFVFLTGPSGAGKS-TLLKLLYGEERPtsGQVL-----VNGQDLSRLKRREipylRRRI-G----VVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 96 QDpmtslnpcytvgFQIME----------AIKVHqGGNKSTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMSQRVMIA 165
Cdd:COG2884 86 QD------------FRLLPdrtvyenvalPLRVT-GKSRKEIRRRVREVLDLVGLSD---KAKALPHELSGGEQQRVAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447119240 166 MAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVE 234
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-257 |
2.18e-40 |
|
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: 141.72 E-value: 2.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSvsSL--AIMGLID-YPGRVMaeklvFNGQDLQRIS 79
Cdd:COG1120 1 MLEAENLSVGYGGR----PVLDDVSLSLPPGEVTALLGPNGSGKS--TLlrALAGLLKpSSGEVL-----LDGRDLASLS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 80 EKERRNLVgaevAMIFQDPMTSLNpcYTVgfqiMEAIKV----HQGGNKSTR---RQRAIDLLNQVGIPDPASRlDVypH 152
Cdd:COG1120 70 RRELARRI----AYVPQEPPAPFG--LTV----RELVALgrypHLGLFGRPSaedREAVEEALERTGLEHLADR-PV--D 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
Cdd:COG1120 137 ELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
250 260
....*....|....*....|....*
gi 447119240 233 VETGDAHAIFhaprhpyTQALLRAL 257
Cdd:COG1120 217 VAQGPPEEVL-------TPELLEEV 234
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-182 |
4.90e-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: 135.08 E-value: 4.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVmaeklVFNGQDLQRISEKERRnlvgAEVAMIFQDPmtS 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSpTEGTI-----LLDGQDLTDDERKSLR----KEIGYVFQDP--Q 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 102 LNPCYTVGFQIMEAIKVhQGGNKSTRRQRAIDLLNQVGIPDPASR-LDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
Cdd:pfam00005 70 LFPRLTVRENLRLGLLL-KGLSKREKDARAEEALEKLGLGDLADRpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
..
gi 447119240 181 TT 182
Cdd:pfam00005 149 TA 150
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-250 |
7.60e-39 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 140.28 E-value: 7.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSvsSL--AIMGLiDYP--GRVmaeklVFNGQDLQ-RI 78
Cdd:COG1118 3 IEVRNISKRFGS----FTLLDDVSLEIASGELVALLGPSGSGKT--TLlrIIAGL-ETPdsGRI-----VLNGRDLFtNL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 79 SEKERRnlvgaeVAMIFQDPMtsLNPCYTVgFQ-IMEAIKVhQGGNKSTRRQRAIDLLNQVGIPDPASRldvYPHQLSGG 157
Cdd:COG1118 71 PPRERR------VGFVFQHYA--LFPHMTV-AEnIAFGLRV-RPPSKAEIRARVEELLELVQLEGLADR---YPSQLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 158 MSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGD 237
Cdd:COG1118 138 QRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGT 217
|
250
....*....|...
gi 447119240 238 AHAIFHAPRHPYT 250
Cdd:COG1118 218 PDEVYDRPATPFV 230
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-241 |
1.41e-38 |
|
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: 136.93 E-value: 1.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDEsapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyP--GRVmaeklVFNGQDLQRISEK 81
Cdd:cd03256 1 IEVENLSKTYPNG---KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVE-PtsGSV-----LIDGTDINKLKGK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 82 ERRNlVGAEVAMIFQDPmtSLNPCYTVgfqiMEAIKVHQGGNKSTRR-----------QRAIDLLNQVGIPDPAS-RLDv 149
Cdd:cd03256 72 ALRQ-LRRQIGMIFQQF--NLIERLSV----LENVLSGRLGRRSTWRslfglfpkeekQRALAALERVGLLDKAYqRAD- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 150 yphQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYA 229
Cdd:cd03256 144 ---QLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKD 220
|
250
....*....|..
gi 447119240 230 GQVVETGDAHAI 241
Cdd:cd03256 221 GRIVFDGPPAEL 232
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
3-234 |
1.70e-38 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 135.94 E-value: 1.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMaeklvFNGQDLQRISE 80
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKS-TLLHLLGGLDNPtsGEVL-----FNGQSLSKLSS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 81 KERRNLVGAEVAMIFQdpMTSLNPCYTVGFQIMEAIKVhqgGNKSTR--RQRAIDLLNQVGIPDpasRLDVYPHQLSGGM 158
Cdd:TIGR02211 75 NERAKLRNKKLGFIYQ--FHHLLPDFTALENVAMPLLI---GKKSVKeaKERAYEMLEKVGLEH---RINHRPSELSGGE 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447119240 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALvAEAAHKIIVMYAGQVVE 234
Cdd:TIGR02211 147 RQRVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLEL-AKKLDRVLEMKDGQLFN 221
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
9-225 |
4.33e-38 |
|
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: 134.28 E-value: 4.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 9 LSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPGRvmaEKLVFNGQDLQRISEKERRNLVG 88
Cdd:TIGR03608 4 ISKKFGDK----VILDDLNLTIEKGKMYAIIGESGSGKS-TLLNIIGLLEKFDS---GQVYLNGQETPPLNSKKASKFRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 89 AEVAMIFQDpmTSLNPCYTVGFQIMEAIKvHQGGNKSTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAI 168
Cdd:TIGR03608 76 EKLGYLFQN--FALIENETVEENLDLGLK-YKKLSKKEKREKKKEALEKVGL---NLKLKQKIYELSGGEQQRVALARAI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447119240 169 ACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLAlVAEAAHKII 225
Cdd:TIGR03608 150 LKPPPLILADEPTGSLDPKNRDEVLDLLLEL-NDEGKTIIIVTHDPE-VAKQADRVI 204
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-270 |
6.36e-38 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 135.76 E-value: 6.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 1 MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvsSL--AIMGLIDYP-GRVMaeklvFNGQDLQR 77
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKT--TLlnLIAGFLAPSsGEIT-----LDGVPVTG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 78 isekerrnlVGAEVAMIFQDpmTSLNPCYTV------GFQImeaikvhQGGNKSTRRQRAIDLLNQVGIPDPASRldvYP 151
Cdd:COG4525 74 ---------PGADRGVVFQK--DALLPWLNVldnvafGLRL-------RGVPKAERRARAEELLALVGLADFARR---RI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 152 HQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDlalVAEA---AHKIIVM- 227
Cdd:COG4525 133 WQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS---VEEAlflATRLVVMs 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 447119240 228 -YAGQVVET------------GDAHAIfhaprhpytqallRALPEFAQDKERLASL 270
Cdd:COG4525 210 pGPGRIVERleldfsrrflagEDARAI-------------KSDPAFIALREELLDI 252
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-242 |
4.70e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 132.91 E-value: 4.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 1 MALLNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSvsSL--AIMGLIdypgRVMAEKLVFNGQDLQRi 78
Cdd:COG1121 4 MPAIELENLTVSYGGR----PVLEDVSLTIPPGEFVAIVGPNGAGKS--TLlkAILGLL----PPTSGTVRLFGKPPRR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 79 sekeRRNLVG-----AEVAMIFqdPMTslnpCYTVgfqIMEAIKVHQG---GNKSTRRQRAIDLLNQVGIPDPASRldvy 150
Cdd:COG1121 73 ----ARRRIGyvpqrAEVDWDF--PIT----VRDV---VLMGRYGRRGlfrRPSRADREAVDEALERVGLEDLADR---- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 151 P-HQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMyA 229
Cdd:COG1121 136 PiGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDLGAVREYFDRVLLL-N 213
|
250
....*....|...
gi 447119240 230 GQVVETGDAHAIF 242
Cdd:COG1121 214 RGLVAHGPPEEVL 226
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-255 |
8.44e-37 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 132.14 E-value: 8.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 5 NVDKlsvHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGL--IDypgrvmAEKLVFNGQDLQRISEKE 82
Cdd:PRK09493 6 NVSK---HFGPTQV----LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLeeIT------SGDLIVDGLKVNDPKVDE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 83 RrnLVGAEVAMIFQD----P-MTSLNpcyTVGFQimeAIKVhQGGNKSTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGG 157
Cdd:PRK09493 73 R--LIRQEAGMVFQQfylfPhLTALE---NVMFG---PLRV-RGASKEEAEKQARELLAKVGL---AERAHHYPSELSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 158 MSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVETGD 237
Cdd:PRK09493 141 QQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAE-EGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGD 219
|
250
....*....|....*...
gi 447119240 238 AHAIFHAPRHPYTQALLR 255
Cdd:PRK09493 220 PQVLIKNPPSQRLQEFLQ 237
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-249 |
8.99e-37 |
|
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: 132.04 E-value: 8.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHFGDESApfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMaeklvFNGQDLQRISEK 81
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQ---ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEpSSGSIL-----LEGTDITKLRGK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 82 ERRNlVGAEVAMIFQD-----PMTSLNPCYTVGFQIMEAIKVHQGGNKSTRRQRAIDLLNQVGIPDPA-SRLDvyphQLS 155
Cdd:TIGR02315 73 KLRK-LRRRIGMIFQHynlieRLTVLENVLHGRLGYKPTWRSLLGRFSEEDKERALSALERVGLADKAyQRAD----QLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVET 235
Cdd:TIGR02315 148 GGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFD 227
|
250
....*....|....*
gi 447119240 236 GDAHAIF-HAPRHPY 249
Cdd:TIGR02315 228 GAPSELDdEVLRHIY 242
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-249 |
2.17e-36 |
|
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: 130.92 E-value: 2.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 6 VDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLiDYP--GRVmaeklVFNGQDLQRISEKER 83
Cdd:cd03296 5 VRNVSKRFGD----FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGL-ERPdsGTI-----LFGGEDATDVPVQER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 84 rnlvgaEVAMIFQD-----PMTSLNpcyTVGFQiMEAIKVHQGGNKSTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGM 158
Cdd:cd03296 75 ------NVGFVFQHyalfrHMTVFD---NVAFG-LRVKPRSERPPEAEIRAKVHELLKLVQLDWLADR---YPAQLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDA 238
Cdd:cd03296 142 RQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTP 221
|
250
....*....|.
gi 447119240 239 HAIFHAPRHPY 249
Cdd:cd03296 222 DEVYDHPASPF 232
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-232 |
7.44e-36 |
|
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: 127.51 E-value: 7.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMaeklvFNGQDLQRISEKE 82
Cdd:cd03230 1 IEVRNLSKRYGK----KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKpDSGEIK-----VLGKDIKKEPEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 83 RRNlvgaeVAMIFQDPmtSLNPCYTVgfqiMEAIKvhqggnkstrrqraidllnqvgipdpasrldvyphqLSGGMSQRV 162
Cdd:cd03230 72 KRR-----IGYLPEEP--SLYENLTV----RENLK------------------------------------LSGGMKQRL 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 163 MIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
Cdd:cd03230 105 ALAQALLHDPELLILDEPTSGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-249 |
8.43e-36 |
|
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: 132.47 E-value: 8.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 1 MALLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLiDYP--GRVMAeklvfNGQDLQRI 78
Cdd:TIGR03265 2 SPYLSIDNIRKRFGA----FTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGL-ERQtaGTIYQ-----GGRDITRL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 79 SEKERrnlvgaEVAMIFQDpmTSLNPCYTVGFQIMEAIKvHQGGNKSTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGM 158
Cdd:TIGR03265 72 PPQKR------DYGIVFQS--YALFPNLTVADNIAYGLK-NRGMGRAEVAERVAELLDLVGLPGSE---RKYPGQLSGGQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDA 238
Cdd:TIGR03265 140 QQRVALARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTP 219
|
250
....*....|.
gi 447119240 239 HAIFHAPRHPY 249
Cdd:TIGR03265 220 QEIYRHPATPF 230
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-241 |
1.09e-35 |
|
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: 128.84 E-value: 1.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMAEKLVFNGQDLQriSEKE 82
Cdd:cd03260 1 IELRDLNVYYGD----KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlIPGAPDEGEVLLDGKDIY--DLDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 83 RRNLVGAEVAMIFQDPmtslNPcytvgFQ--IMEAI----KVHQGGNKSTRRQRAIDLLNQVGIPDPAS-RLDvyPHQLS 155
Cdd:cd03260 75 DVLELRRRVGMVFQKP----NP-----FPgsIYDNVayglRLHGIKLKEELDERVEEALRKAALWDEVKdRLH--ALGLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALVLITHDLALVAEAAHKIIVMYAGQVVET 235
Cdd:cd03260 144 GGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEF 221
|
....*.
gi 447119240 236 GDAHAI 241
Cdd:cd03260 222 GPTEQI 227
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
26-252 |
1.46e-35 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 128.98 E-value: 1.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 26 ISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPG----RVMAEKLVFNgqdlQRISEKERRNLVGaEVAMIFQDpmTS 101
Cdd:COG4161 21 INLECPSGETLVLLGPSGAGKS-SLLRVLNLLETPDsgqlNIAGHQFDFS----QKPSEKAIRLLRQ-KVGMVFQQ--YN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 102 LNPCYTVGFQIMEA-IKVhQGGNKSTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
Cdd:COG4161 93 LWPHLTVMENLIEApCKV-LGLSKEQAREKAMKLLARLRLTDKA---DRFPLHLSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447119240 181 TTALDVTIQAQIIELLLELQQKEnMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAhAIFhapRHPYTQA 252
Cdd:COG4161 169 TAALDPEITAQVVEIIRELSQTG-ITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA-SHF---TQPQTEA 235
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-242 |
2.35e-35 |
|
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: 129.09 E-value: 2.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 6 VDKLSVHFGDESAPfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyP--GRVMaeklvFNGQDLqrISEK-- 81
Cdd:TIGR04520 3 VENVSFSYPESEKP--ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLL-PtsGKVT-----VDGLDT--LDEEnl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 82 -ERRNLVGaevaMIFQDPMTSLnpcytVGFQI-------MEAIKVhqggNKSTRRQRAIDLLNQVGIPDpasRLDVYPHQ 153
Cdd:TIGR04520 73 wEIRKKVG----MVFQNPDNQF-----VGATVeddvafgLENLGV----PREEMRKRVDEALKLVGMED---FRDREPHL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEaAHKIIVMYAGQVV 233
Cdd:TIGR04520 137 LSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIV 215
|
....*....
gi 447119240 234 ETGDAHAIF 242
Cdd:TIGR04520 216 AEGTPREIF 224
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
6-254 |
2.57e-35 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 127.99 E-value: 2.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 6 VDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLiDYP--GRVmaeklVFNGQDLQRISEKER 83
Cdd:TIGR00968 3 IANISKRFGS----FQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGL-EQPdsGRI-----RLNGQDATRVHARDR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 84 rnlvgaEVAMIFQDpmTSLNPCYTVGFQIMEAIKVhQGGNKSTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVM 163
Cdd:TIGR00968 73 ------KIGFVFQH--YALFKHLTVRDNIAFGLEI-RKHPKAKIKARVEELLELVQLEGLGDR---YPNQLSGGQRQRVA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 164 IAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAIFH 243
Cdd:TIGR00968 141 LARALAVEPQVLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYD 220
|
250
....*....|.
gi 447119240 244 APRHPYTQALL 254
Cdd:TIGR00968 221 HPANPFVMSFL 231
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-231 |
2.78e-35 |
|
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: 126.15 E-value: 2.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLVFNGQDLQR---ISE 80
Cdd:cd03229 1 LELKNVSKRYGQK----TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLE----EPDSGSILIDGEDLTDledELP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 81 KERRNlvgaeVAMIFQDPmtSLNPCYTVGFQIMEAikvhqggnkstrrqraidllnqvgipdpasrldvyphqLSGGMSQ 160
Cdd:cd03229 73 PLRRR-----IGMVFQDF--ALFPHLTVLENIALG--------------------------------------LSGGQQQ 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447119240 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQ 231
Cdd:cd03229 108 RVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-246 |
3.78e-35 |
|
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: 127.55 E-value: 3.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSvsSL--AIMGLidYP---GRVmaeklVFNGQDLQRI 78
Cdd:cd03219 1 LEVRGLTKRFGG----LVALDDVSFSVRPGEIHGLIGPNGAGKT--TLfnLISGF--LRptsGSV-----LFDGEDITGL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 79 SEKERRNLvGaeVAMIFQDP-----MTSL-NpcytvgfqIMEAIKVHQGGN---------KSTRRQRAIDLLNQVGIPDp 143
Cdd:cd03219 68 PPHEIARL-G--IGRTFQIPrlfpeLTVLeN--------VMVAAQARTGSGlllararreEREARERAEELLERVGLAD- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 144 asRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHK 223
Cdd:cd03219 136 --LADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADR 212
|
250 260
....*....|....*....|...
gi 447119240 224 IIVMYAGQVVETGDAHAIFHAPR 246
Cdd:cd03219 213 VTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-236 |
3.89e-35 |
|
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: 134.96 E-value: 3.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDESAPfrAVDRISYSVKQGEVVGIVGESGSGKsvSSLA--IMGLID-YPGRVMaeklvFNGQDLQRISE 80
Cdd:COG2274 474 IELENVSFRYPGDSPP--VLDNISLTIKPGERVAIVGRSGSGK--STLLklLLGLYEpTSGRIL-----IDGIDLRQIDP 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 81 KERRNLVGaevaMIFQDPMTslnpcytvgFQ--IMEAIKVhqgGNKSTRRQRAIDLLNQVGIPDPASRLdvyPH------ 152
Cdd:COG2274 545 ASLRRQIG----VVLQDVFL---------FSgtIRENITL---GDPDATDEEIIEAARLAGLHDFIEAL---PMgydtvv 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 153 -----QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALVLITHDLALVAeAAHKIIVM 227
Cdd:COG2274 606 geggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRLSTIR-LADRIIVL 682
|
....*....
gi 447119240 228 YAGQVVETG 236
Cdd:COG2274 683 DKGRIVEDG 691
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-255 |
7.25e-35 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 127.17 E-value: 7.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 1 MALLNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMAEKLVFNGQdlqrI 78
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQ----TVLHGIDLEVKPGEVVAIIGPSGSGKT-TLLRCINLLEQPeaGTIRVGDITIDTA----R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 79 SEKERRNLVGA---EVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGGNKSTRRQRAIDLLNQVGIpdpASRLDVYPHQLS 155
Cdd:PRK11264 72 SLSQQKGLIRQlrqHVGFVFQN--FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGL---AGKETSYPRRLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVET 235
Cdd:PRK11264 147 GGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQ-EKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQ 225
|
250 260
....*....|....*....|
gi 447119240 236 GDAHAIFHAPRHPYTQALLR 255
Cdd:PRK11264 226 GPAKALFADPQQPRTRQFLE 245
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-236 |
8.13e-35 |
|
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: 124.86 E-value: 8.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 6 VDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSvsSL--AIMGLI-DYPGRVMaeklvFNGQDLQRISEKE 82
Cdd:cd03214 2 VENLSVGYGGR----TVLDDLSLSIEAGEIVGILGPNGAGKS--TLlkTLAGLLkPSSGEIL-----LDGKDLASLSPKE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 83 RRNLVGaevamifqdpmtslnpcytVGFQIMEaikvhqggnkstrrqraidllnQVGIPDPASRldvYPHQLSGGMSQRV 162
Cdd:cd03214 71 LARKIA-------------------YVPQALE----------------------LLGLAHLADR---PFNELSGGERQRV 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447119240 163 MIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:cd03214 107 LLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
26-232 |
6.70e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 123.39 E-value: 6.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDY-PGRVMaeklvFNGQDLQRIS-EKERRnlvgaEVAMIFQDPMTSLN 103
Cdd:COG4619 19 VSLTLEAGECVAITGPSGSGKSTLLRALADLDPPtSGEIY-----LDGKPLSAMPpPEWRR-----QVAYVPQEPALWGG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 104 pcyTVGFQIMEAIKVHqggNKSTRRQRAIDLLNQVGIPDpaSRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTA 183
Cdd:COG4619 89 ---TVRDNLPFPFQLR---ERKFDRERALELLERLGLPP--DILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447119240 184 LDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
Cdd:COG4619 161 LDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
26-245 |
1.02e-33 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 123.97 E-value: 1.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 26 ISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMAEKLVFNGQdlQRISEKERRNLvGAEVAMIFQDpmTSLN 103
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKS-SLLRVLNLLEMPrsGTLNIAGNHFDFS--KTPSDKAIREL-RRNVGMVFQQ--YNLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 104 PCYTVGFQIMEA-IKVhQGGNKSTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTT 182
Cdd:PRK11124 95 PHLTVQQNLIEApCRV-LGLSKDQALARAEKLLERLRLKPYADR---FPLHLSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447119240 183 ALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAiFHAP 245
Cdd:PRK11124 171 ALDPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQP 231
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
231-317 |
1.76e-33 |
|
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model represents a domain found in the C-terminal regions of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 213647 [Multi-domain] Cd Length: 87 Bit Score: 118.62 E-value: 1.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 231 QVVETGDAHAIFHAPRHPYTQALLRALPEFAQDKERLASLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPALNMLADG 310
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIKKRDRKLISIPGEVPSLINLPSGCRFYPRCPYAQDECRKEPPALVEIAEG 80
|
....*..
gi 447119240 311 RQSKCHY 317
Cdd:TIGR01727 81 HRVACHL 87
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
20-248 |
1.76e-33 |
|
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: 123.56 E-value: 1.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 20 FRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyP--GRVMaeklvFNGQDLQRISEKERRNLVGaevaMIFQD 97
Cdd:cd03295 14 KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIE-PtsGEIF-----IDGEDIREQDPVELRRKIG----YVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 98 pmTSLNPCYTVGFQIMEAIKVhQGGNKSTRRQRAIDLLNQVGIPdPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIA 177
Cdd:cd03295 84 --IGLFPHMTVEENIALVPKL-LKWPKEKIRERADELLALVGLD-PAEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447119240 178 DEPTTALDVTIQAQIIELLLELQQKENMALVLITHDlalVAEA---AHKIIVMYAGQVVETGDAHAIFhapRHP 248
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHD---IDEAfrlADRIAIMKNGEIVQVGTPDEIL---RSP 227
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
4-233 |
2.14e-33 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 122.43 E-value: 2.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDypgRVMAEKLVFNGQDLQRISEKE- 82
Cdd:TIGR02982 2 ISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKT-TLLTLIGGLR---SVQEGSLKVLGQELHGASKKQl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 83 ---RRNLvgaevAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGGNKSTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMS 159
Cdd:TIGR02982 78 vqlRRRI-----GYIFQA--HNLLGFLTARQNVQMALELQPNLSYQEARERARAMLEAVGLGD---HLNYYPHNLSGGQK 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447119240 160 QRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDlALVAEAAHKIIVMYAGQVV 233
Cdd:TIGR02982 148 QRVAIARALVHHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHD-NRILDVADRILQMEDGKLL 220
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-249 |
2.55e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 125.57 E-value: 2.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 1 MALLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSvsSL--AIMGLIDyP--GRVMaeklvFNGQDLQ 76
Cdd:COG3839 1 MASLELENVSKSYGG----VEALKDIDLDIEDGEFLVLLGPSGCGKS--TLlrMIAGLED-PtsGEIL-----IGGRDVT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 77 RISEKERRnlvgaeVAMIFQDPMtsLNPCYTV----GFqimeAIKVhQGGNKSTRRQRAIDLLNQVGIPDpasRLDVYPH 152
Cdd:COG3839 69 DLPPKDRN------IAMVFQSYA--LYPHMTVyeniAF----PLKL-RKVPKAEIDRRVREAAELLGLED---LLDRKPK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLalvAEA---AHKIIVMYA 229
Cdd:COG3839 133 QLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQ---VEAmtlADRIAVMND 209
|
250 260
....*....|....*....|
gi 447119240 230 GQVVETGDAHAIFHAPRHPY 249
Cdd:COG3839 210 GRIQQVGTPEELYDRPANLF 229
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-231 |
2.73e-33 |
|
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: 120.43 E-value: 2.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 6 VDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPgrvmAEKLVFNGQDLQRISEKERRN 85
Cdd:cd00267 2 IENLSFRYGG----RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT----SGEILIDGKDIAKLPLEELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 86 LVGaevamifqdpmtslnpcytvgfqimeaikvhqggnkstrrqraidllnqvgipdpasrldvYPHQLSGGMSQRVMIA 165
Cdd:cd00267 74 RIG-------------------------------------------------------------YVPQLSGGQRQRVALA 92
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447119240 166 MAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQ 231
Cdd:cd00267 93 RALLLNPDLLLLDEPTSGLDPASRERLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-245 |
4.06e-33 |
|
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: 122.35 E-value: 4.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLVFNGQDLQRISEKER 83
Cdd:cd03300 1 IELENVSKFYGG----FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFET----PTSGEILLDGKDITNLPPHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 84 RnlvgaeVAMIFQDpmTSLNPCYTVGFQIMEAIKVhQGGNKSTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVM 163
Cdd:cd03300 73 P------VNTVFQN--YALFPHLTVFENIAFGLRL-KKLPKAEIKERVAEALDLVQLEGYANR---KPSQLSGGQQQRVA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 164 IAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAIFH 243
Cdd:cd03300 141 IARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
..
gi 447119240 244 AP 245
Cdd:cd03300 221 EP 222
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-252 |
4.07e-33 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 122.84 E-value: 4.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSvsSL--AIMGLID-YPGRVMAEKLVFNGQDlqrISE 80
Cdd:COG1117 12 IEVRNLNVYYGD----KQALKDINLDIPENKVTALIGPSGCGKS--TLlrCLNRMNDlIPGARVEGEILLDGED---IYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 81 KE------RRNlvgaeVAMIFQDPmtslNPcytvgF--QIME----AIKVHQGGNKSTRRQRAIDLLNQVGIPDP-ASRL 147
Cdd:COG1117 83 PDvdvvelRRR-----VGMVFQKP----NP-----FpkSIYDnvayGLRLHGIKSKSELDEIVEESLRKAALWDEvKDRL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 148 DVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALVLITHDLALVAEAAHKIIVM 227
Cdd:COG1117 149 KKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL--KKDYTIVIVTHNMQQAARVSDYTAFF 226
|
250 260
....*....|....*....|....*
gi 447119240 228 YAGQVVETGDAHAIFHAPRHPYTQA 252
Cdd:COG1117 227 YLGELVEFGPTEQIFTNPKDKRTED 251
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-245 |
4.50e-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: 4.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDESapfraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyP--GRVMaeklvFNGQDLQRISEK 81
Cdd:cd03299 1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIK-PdsGKIL-----LNGKDITNLPPE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 82 ERRnlvgaeVAMIFQDpmTSLNPCYTVGFQIMEAIKvHQGGNKSTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQR 161
Cdd:cd03299 70 KRD------ISYVPQN--YALFPHMTVYKNIAYGLK-KRKVDKKEIERKVLEIAEMLGI---DHLLNRKPETLSGGEQQR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAI 241
Cdd:cd03299 138 VAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEV 217
|
....
gi 447119240 242 FHAP 245
Cdd:cd03299 218 FKKP 221
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-227 |
4.63e-33 |
|
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: 121.49 E-value: 4.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 6 VDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSvsSL--AIMGLID-YPGRVMaeklvFNGQDLQRiseke 82
Cdd:cd03235 2 VEDLTVSYGGH----PVLEDVSFEVKPGEFLAIVGPNGAGKS--TLlkAILGLLKpTSGSIR-----VFGKPLEK----- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 83 RRNLVGAeVAMIFqdpmtSLNPCY--TVgFQIME----AIKVHQGGNKSTRRQRAIDLLNQVGIPDPASR-LDvyphQLS 155
Cdd:cd03235 66 ERKRIGY-VPQRR-----SIDRDFpiSV-RDVVLmglyGHKGLFRRLSKADKAKVDEALERVGLSELADRqIG----ELS 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447119240 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVM 227
Cdd:cd03235 135 GGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-255 |
5.08e-33 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 122.77 E-value: 5.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSVsslaIMGLIDYPGRVMAEKLVFNGQDLQ------- 76
Cdd:PRK10619 6 LNVIDLHKRYGEH----EVLKGVSLQANAGDVISIIGSSGSGKST----FLRCINFLEKPSEGSIVVNGQTINlvrdkdg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 77 --RISEKERRNLVGAEVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGGNKSTRRQRAIDLLNQVGIPDPASrlDVYPHQL 154
Cdd:PRK10619 78 qlKVADKNQLRLLRTRLTMVFQH--FNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQ--GKYPVHL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVE 234
Cdd:PRK10619 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFARHVSSHVIFLHQGKIEE 232
|
250 260
....*....|....*....|.
gi 447119240 235 TGDAHAIFHAPRHPYTQALLR 255
Cdd:PRK10619 233 EGAPEQLFGNPQSPRLQQFLK 253
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-242 |
6.34e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 122.82 E-value: 6.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHFGDESAPfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyP--------GRVMAEKLVFngqD 74
Cdd:PRK13635 5 IIRVEHISFRYPDAATY--ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLL-PeagtitvgGMVLSEETVW---D 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 75 LQRisekerrnlvgaEVAMIFQDPMTSLnpcytVGFQIMEAIKV---HQGGNKSTRRQRAIDLLNQVGIPDPASRldvYP 151
Cdd:PRK13635 79 VRR------------QVGMVFQNPDNQF-----VGATVQDDVAFgleNIGVPREEMVERVDQALRQVGMEDFLNR---EP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 152 HQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEaAHKIIVMYAGQ 231
Cdd:PRK13635 139 HRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGE 217
|
250
....*....|.
gi 447119240 232 VVETGDAHAIF 242
Cdd:PRK13635 218 ILEEGTPEEIF 228
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
22-249 |
1.33e-32 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 124.45 E-value: 1.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 22 AVDRISYSVKQGEVVGIVGESGSGKSvsSL--AIMGLIDyP--GRVMaeklvFNGQDLQRISEKE----RRNlvgaEVAM 93
Cdd:COG4175 42 GVNDASFDVEEGEIFVIMGLSGSGKS--TLvrCLNRLIE-PtaGEVL-----IDGEDITKLSKKElrelRRK----KMSM 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 94 IFQdpmtS--LNPCYTV------GFQImeaikvhQGGNKSTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIA 165
Cdd:COG4175 110 VFQ----HfaLLPHRTVlenvafGLEI-------QGVPKAERRERAREALELVGL---AGWEDSYPDELSGGMQQRVGLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 166 MAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLalvAEA---AHKIIVMYAGQVVETGDAHAIF 242
Cdd:COG4175 176 RALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDL---DEAlrlGDRIAIMKDGRIVQIGTPEEIL 252
|
....*..
gi 447119240 243 HAPRHPY 249
Cdd:COG4175 253 TNPANDY 259
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-241 |
5.24e-32 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 119.58 E-value: 5.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMaeklvFNGQDLQRISEK 81
Cdd:COG4555 1 MIEVENLSKKYGK----VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKpDSGSIL-----IDGEDVRKEPRE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 82 ERRNLvgaevAMIFQDPMTSLNpcytvgFQIMEAIKVH---QGGNKSTRRQRAIDLLNQVGIPDPasrLDVYPHQLSGGM 158
Cdd:COG4555 72 ARRQI-----GVLPDERGLYDR------LTVRENIRYFaelYGLFDEELKKRIEELIELLGLEEF---LDRRVGELSTGM 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALVLI-THDLALVAEAAHKIIVMYAGQVVETGD 237
Cdd:COG4555 138 KKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRAL--KKEGKTVLFsSHIMQEVEALCDRVVILHKGKVVAQGS 215
|
....
gi 447119240 238 AHAI 241
Cdd:COG4555 216 LDEL 219
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-254 |
3.02e-31 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 117.16 E-value: 3.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDEsaPFRAvdriSYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMaeklvFNGQDLQRISEKE 82
Cdd:COG3840 2 LRLDDLTYRYGDF--PLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPpDSGRIL-----WNGQDLTALPPAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 83 RrnlvgaEVAMIFQDpmTSLNPCYTVGFQImeAIKVHQGGNKS-TRRQRAIDLLNQVGIPDPASRLdvyPHQLSGGMSQR 161
Cdd:COG3840 71 R------PVSMLFQE--NNLFPHLTVAQNI--GLGLRPGLKLTaEQRAQVEQALERVGLAGLLDRL---PGQLSGGQRQR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAI 241
Cdd:COG3840 138 VALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
250
....*....|...
gi 447119240 242 FHAPRHPYTQALL 254
Cdd:COG3840 218 LDGEPPPALAAYL 230
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-233 |
4.36e-31 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 116.20 E-value: 4.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 6 VDKLSVHFGDESapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVmaeklVFNGQDlqrISEKERR 84
Cdd:cd03226 2 IENISFSYKKGT---EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKeSSGSI-----LLNGKP---IKAKERR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 85 NLVGaevaMIFQDPMTSLNPCyTVGFQIMEAIKvhqggNKSTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQRVMI 164
Cdd:cd03226 71 KSIG----YVMQDVDYQLFTD-SVREELLLGLK-----ELDAGNEQAETVLKDLDLYALK---ERHPLSLSGGQKQRLAI 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447119240 165 AMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
Cdd:cd03226 138 AAALLSGKDLLIFDEPTSGLDYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-231 |
5.46e-31 |
|
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: 114.79 E-value: 5.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDESAPfrAVDRISYSVKQGEVVGIVGESGSGKSvsSLA--IMGLID-YPGRVMaeklvFNGQDLQRISE 80
Cdd:cd03228 1 IEFKNVSFSYPGRPKP--VLKDVSLTIKPGEKVAIVGPSGSGKS--TLLklLLRLYDpTSGEIL-----IDGVDLRDLDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 81 KERRNLVgaevAMIFQDP----MTslnpcytvgfqIMEAIkvhqggnkstrrqraidllnqvgipdpasrldvyphqLSG 156
Cdd:cd03228 72 ESLRKNI----AYVPQDPflfsGT-----------IRENI-------------------------------------LSG 99
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447119240 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALVLITHDLALVaEAAHKIIVMYAGQ 231
Cdd:cd03228 100 GQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRAL--AKGKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-218 |
6.06e-31 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 116.42 E-value: 6.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMaeklvFNGQDLQRISEK 81
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDgSSGEVS-----LVGQPLHQMDEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 82 ERRNLVGAEVAMIFQDPM--TSLNPCYTVgfqimEAIKVHQGGNKSTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMS 159
Cdd:PRK10584 81 ARAKLRAKHVGFVFQSFMliPTLNALENV-----ELPALLRGESSRQSRNGAKALLEQLGL---GKRLDHLPAQLSGGEQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447119240 160 QRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVA 218
Cdd:PRK10584 153 QRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAA 211
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-251 |
7.67e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 116.55 E-value: 7.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 1 MALLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMAEKLVFNGQDLQR-- 77
Cdd:PRK14247 1 MNKIEIRDLKVSFGQ----VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElYPEARVSGEVYLDGQDIFKmd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 78 ISEKERRnlvgaeVAMIFQ--DPMTSLNPCYTV--GFQIMEAIKvhqggNKSTRRQRAIDLLNQVGIPDPA-SRLDVYPH 152
Cdd:PRK14247 77 VIELRRR------VQMVFQipNPIPNLSIFENValGLKLNRLVK-----SKKELQERVRWALEKAQLWDEVkDRLDAPAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
Cdd:PRK14247 146 KLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
250
....*....|....*....
gi 447119240 233 VETGDAHAIFHAPRHPYTQ 251
Cdd:PRK14247 224 VEWGPTREVFTNPRHELTE 242
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-236 |
2.70e-30 |
|
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: 114.39 E-value: 2.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 6 VDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLVFNGQDLQRISEKERRN 85
Cdd:cd03265 3 VENLVKKYGD----FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLL----KPTSGRATVAGHDVVREPREVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 86 lvgaeVAMIFQDPmtSLNPCYTvGFQIMEAIKVHQGGNKSTRRQRAIDLLNQVGIPDPASRLDVYphqLSGGMSQRVMIA 165
Cdd:cd03265 75 -----IGIVFQDL--SVDDELT-GWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKT---YSGGMRRRLEIA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447119240 166 MAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:cd03265 144 RSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
18-231 |
3.92e-30 |
|
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: 113.88 E-value: 3.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 18 APFRAVDRISYSVKQGEVVGIVGESGSGKS-VSSLAIMGLIDYPGRVMaeklvFNGQDLQRISEKE----RRnlvgaEVA 92
Cdd:TIGR02673 13 GGVAALHDVSLHIRKGEFLFLTGPSGAGKTtLLKLLYGALTPSRGQVR-----IAGEDVNRLRGRQlpllRR-----RIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 93 MIFQDpmTSLNPCYTVGFQIMEAIKVhQGGNKSTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMSQRVMIAMAIACRP 172
Cdd:TIGR02673 83 VVFQD--FRLLPDRTVYENVALPLEV-RGKKEREIQRRVGAALRQVGLEH---KADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447119240 173 KLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQ 231
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-242 |
5.14e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 116.10 E-value: 5.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHFGD-ESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-----------YPGRVMAEKLVF 70
Cdd:PRK13631 21 ILRVKNLYCVFDEkQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKskygtiqvgdiYIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 71 NGQDLQRISE-KERRNLVGaevaMIFQDPMTSLNPCyTVGFQIM---EAIKVHqggnKSTRRQRAIDLLNQVGIPDPAsr 146
Cdd:PRK13631 101 TNPYSKKIKNfKELRRRVS----MVFQFPEYQLFKD-TIEKDIMfgpVALGVK----KSEAKKLAKFYLNKMGLDDSY-- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 147 LDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLElQQKENMALVLITHDLALVAEAAHKIIV 226
Cdd:PRK13631 170 LERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIV 248
|
250
....*....|....*.
gi 447119240 227 MYAGQVVETGDAHAIF 242
Cdd:PRK13631 249 MDKGKILKTGTPYEIF 264
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
12-242 |
9.21e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 114.76 E-value: 9.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 12 HFGDESAPF--RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLVFNGQDL--QRISEKERRNLV 87
Cdd:PRK13637 10 HIYMEGTPFekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLL----KPTSGKIIIDGVDItdKKVKLSDIRKKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 88 GaevaMIFQDPMTSLnpcytvgFQimEAIK-------VHQGGNKSTRRQRAIDLLNQVGIpDPASRLDVYPHQLSGGMSQ 160
Cdd:PRK13637 86 G----LVFQYPEYQL-------FE--ETIEkdiafgpINLGLSEEEIENRVKRAMNIVGL-DYEDYKDKSPFELSGGQKR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHA 240
Cdd:PRK13637 152 RVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPRE 231
|
..
gi 447119240 241 IF 242
Cdd:PRK13637 232 VF 233
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-251 |
2.29e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 112.83 E-value: 2.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMAE-KLVFNGQDLQRISE 80
Cdd:PRK14246 10 VFNISRLYLYINDKAI----LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiYDSKIKVDgKVLYFGKDIFQIDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 81 KERRNlvgaEVAMIFQDPmtSLNPCYTVGFQIMEAIKVHqgGNKSTRRQRAI--DLLNQVGI-PDPASRLDVYPHQLSGG 157
Cdd:PRK14246 86 IKLRK----EVGMVFQQP--NPFPHLSIYDNIAYPLKSH--GIKEKREIKKIveECLRKVGLwKEVYDRLNSPASQLSGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 158 MSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGD 237
Cdd:PRK14246 158 QQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGS 235
|
250
....*....|....
gi 447119240 238 AHAIFHAPRHPYTQ 251
Cdd:PRK14246 236 SNEIFTSPKNELTE 249
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-257 |
3.32e-29 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 115.52 E-value: 3.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGRvmaEKLVFNGQDLQRISEKERRNLVGAEVAMIFQDpmTS 101
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE-PTR---GQVLIDGVDIAKISDAELREVRRKKIAMVFQS--FA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 102 LNPCYTVGFQIMEAIKVhQGGNKSTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPT 181
Cdd:PRK10070 117 LMPHMTVLDNTAFGMEL-AGINAEERREKALDALRQVGLENYAHS---YPDELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447119240 182 TALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAIFHAPRHPYTQALLRAL 257
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
33-274 |
4.73e-29 |
|
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: 114.43 E-value: 4.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 33 GEVVGIVGESGSGKSvsSL--AIMGLIdypgRVMAEKLVFNGQDLQ----RISEK-ERRNLvgaevAMIFQDPmtSLNPC 105
Cdd:COG4148 25 RGVTALFGPSGSGKT--TLlrAIAGLE----RPDSGRIRLGGEVLQdsarGIFLPpHRRRI-----GYVFQEA--RLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 106 YTVGFQIMEAIKVHQGGNKSTRRQRAIDLLnqvGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALD 185
Cdd:COG4148 92 LSVRGNLLYGRKRAPRAERRISFDEVVELL---GI---GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 186 VTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAIFHAPrhpytqallrALPEFAQDKE 265
Cdd:COG4148 166 LARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP----------DLLPLAGGEE 235
|
....*....
gi 447119240 266 RLASLPGVV 274
Cdd:COG4148 236 AGSVLEATV 244
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
22-232 |
1.47e-28 |
|
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: 109.80 E-value: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 22 AVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLVFNGQDLQRISEKE----RRNLvgaevAMIFQD 97
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKS----TLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylRRKI-----GVVFQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 98 pmTSLNPCYTVGFQIMEAIKVHQGGNKSTRRqRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIA 177
Cdd:cd03292 87 --FRLLPDRNVYENVAFALEVTGVPPREIRK-RVPAALELVGL---SHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447119240 178 DEPTTALDVTIQAQIIELLlelqQKENMA---LVLITHDLALVAEAAHKIIVMYAGQV 232
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLL----KKINKAgttVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
18-242 |
1.61e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 111.00 E-value: 1.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 18 APFrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYP-GRVMAEKLVFNGQDLQRISEkerrnlvgaEVAMIFQ 96
Cdd:PRK13648 21 ASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKsGEIFYNNQAITDDNFEKLRK---------HIGIVFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 97 DPMTSLNPCyTVGFQIMEAIKVHQGGNKSTRRqRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQRVMIAMAIACRPKLLI 176
Cdd:PRK13648 91 NPDNQFVGS-IVKYDVAFGLENHAVPYDEMHR-RVSEALKQVDMLERA---DYEPNALSGGQKQRVAIAGVLALNPSVII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447119240 177 ADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHkIIVMYAGQVVETGDAHAIF 242
Cdd:PRK13648 166 LDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADH-VIVMNKGTVYKEGTPTEIF 230
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-255 |
1.86e-28 |
|
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: 115.25 E-value: 1.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 2 ALLNVDKLSVHFGDESAPfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDY-PGRVMaeklvFNGQDLQRISE 80
Cdd:COG4987 332 PSLELEDVSFRYPGAGRP--VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPqSGSIT-----LGGVDLRDLDE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 81 KERRNLVgaevAMIFQDP---MTSlnpcytvgfqIMEAIKVhqgGNKSTRRQRAIDLLNQVGIPD-----PA---SRLDV 149
Cdd:COG4987 405 DDLRRRI----AVVPQRPhlfDTT----------LRENLRL---ARPDATDEELWAALERVGLGDwlaalPDgldTWLGE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 150 YPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkeNMALVLITHDLALVaEAAHKIIVMYA 229
Cdd:COG4987 468 GGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGL-ERMDRILVLED 544
|
250 260
....*....|....*....|....*.
gi 447119240 230 GQVVETGDAHAIfhAPRHPYTQALLR 255
Cdd:COG4987 545 GRIVEQGTHEEL--LAQNGRYRQLYQ 568
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
6-274 |
3.98e-28 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 112.01 E-value: 3.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 6 VDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGrvMAEKLVFNGQDLQRISeKERRN 85
Cdd:TIGR03258 8 IDHLRVAYGANTV----LDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAG--LTGRIAIADRDLTHAP-PHKRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 86 LvgaevAMIFQDpmTSLNPCYTVGFQIMEAIKVhQGGNKSTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIA 165
Cdd:TIGR03258 81 L-----ALLFQN--YALFPHLKVEDNVAFGLRA-QKMPKADIAERVADALKLVGLGDAAAH---LPAQLSGGMQQRIAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 166 MAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQK-ENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAIFHA 244
Cdd:TIGR03258 150 RAIAIEPDVLLLDEPLSALDANIRANMREEIAALHEElPELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDA 229
|
250 260 270
....*....|....*....|....*....|
gi 447119240 245 PRHPYTQALLRALPEFAQDKERLASLPGVV 274
Cdd:TIGR03258 230 PADGFAAEFLGAANILPAIALGITEAPGLV 259
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-237 |
5.58e-28 |
|
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: 113.70 E-value: 5.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 6 VDKLSVHFGDESApfrAVDRISYSVKQGEVVGIVGESGSGKSvsSLA--IMGLID-YPGRVMaeklvFNGQDLQRISEKE 82
Cdd:COG4988 339 LEDVSFSYPGGRP---ALDGLSLTIPPGERVALVGPSGAGKS--TLLnlLLGFLPpYSGSIL-----INGVDLSDLDPAS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 83 RRNLVgaevAMIFQDPMTslnpcytvgFQ--IMEAIKVhqgGNKSTRRQRAIDLLNQVGIPDPASRLdvyPH-------- 152
Cdd:COG4988 409 WRRQI----AWVPQNPYL---------FAgtIRENLRL---GRPDASDEELEAALEAAGLDEFVAAL---PDgldtplge 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 153 ---QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALVLITHDLALVAEAAHkIIVMYA 229
Cdd:COG4988 470 ggrGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL--AKGRTVILITHRLALLAQADR-ILVLDD 546
|
....*...
gi 447119240 230 GQVVETGD 237
Cdd:COG4988 547 GRIVEQGT 554
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-242 |
5.81e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 109.82 E-value: 5.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 1 MALLNVDKLSVHFGDESAPFrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrvmAE--KLVFNGQDLQRI 78
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEKY-TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLE------AEsgQIIIDGDLLTEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 79 SEKERRNLVGaevaMIFQDPMTSLnpcytVGFQIMEAIKV---HQGGNKSTRRQRAIDLLNQVGIPDPASRldvYPHQLS 155
Cdd:PRK13650 75 NVWDIRHKIG----MVFQNPDNQF-----VGATVEDDVAFgleNKGIPHEEMKERVNEALELVGMQDFKER---EPARLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAeAAHKIIVMYAGQVVET 235
Cdd:PRK13650 143 GGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVEST 221
|
....*..
gi 447119240 236 GDAHAIF 242
Cdd:PRK13650 222 STPRELF 228
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
3-232 |
1.14e-27 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 107.98 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLVFNGQDLQRISEKE 82
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKS-TLLHLLGGLDTP---TSGDVIFNGQPMSKLSSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 83 RRNLVGAEVAMIFQdpMTSLNPCYTVGFQImeAIKVHQGGNKSTR-RQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQR 161
Cdd:PRK11629 81 KAELRNQKLGFIYQ--FHHLLPDFTALENV--AMPLLIGKKKPAEiNSRALEMLAAVGL---EHRANHRPSELSGGERQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447119240 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALvAEAAHKIIVMYAGQV 232
Cdd:PRK11629 154 VAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQL-AKRMSRQLEMRDGRL 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
20-236 |
1.49e-27 |
|
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: 106.96 E-value: 1.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 20 FRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLVFNGQDLQRISEKERrnlvgaEVAMIFQDpm 99
Cdd:cd03301 13 VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEE----PTSGRIYIGGRDVTDLPPKDR------DIAMVFQN-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 100 TSLNPCYTVGFQIMEAIKVHQGGNKSTRRQ--RAIDLLnqvGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIA 177
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERvrEVAELL---QI---EHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447119240 178 DEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-242 |
1.54e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 108.54 E-value: 1.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 2 ALLNVDKLSVHFGDESAPfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLVFNGQDLQRISEK 81
Cdd:PRK13632 6 VMIKVENVSFSYPNSENN--ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLL----KPQSGEIKIDGITISKENLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 82 ERRNLVGaevaMIFQDPMTSLnpcytVGFQIMEAIKVhqgG--NKSTRRQ--RAI--DLLNQVGIPDpasRLDVYPHQLS 155
Cdd:PRK13632 80 EIRKKIG----IIFQNPDNQF-----IGATVEDDIAF---GleNKKVPPKkmKDIidDLAKKVGMED---YLDKEPQNLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLalvAEA--AHKIIVMYAGQVV 233
Cdd:PRK13632 145 GGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDM---DEAilADKVIVFSEGKLI 221
|
....*....
gi 447119240 234 ETGDAHAIF 242
Cdd:PRK13632 222 AQGKPKEIL 230
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-245 |
2.36e-27 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 109.79 E-value: 2.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 6 VDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPgrvmAEKLVFNGQDLQRISEKERRn 85
Cdd:PRK10851 5 IANIKKSFGRT----QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQT----SGHIRFHGTDVSRLHARDRK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 86 lvgaeVAMIFQDpmTSLNPCYTVGFQIMEAIKV---HQGGNKSTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRV 162
Cdd:PRK10851 76 -----VGFVFQH--YALFRHMTVFDNIAFGLTVlprRERPNAAAIKAKVTQLLEMVQLAHLADR---YPAQLSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 163 MIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAIF 242
Cdd:PRK10851 146 ALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVW 225
|
...
gi 447119240 243 HAP 245
Cdd:PRK10851 226 REP 228
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-236 |
6.61e-27 |
|
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: 105.28 E-value: 6.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGdeSAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdYP--GRVMaeklvFNGQDLQRISEK 81
Cdd:cd03263 1 LQIRNLTKTYK--KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGEL-RPtsGTAY-----INGYSIRTDRKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 82 ERRNlvgaeVAMIFQDpmtslNPCYTvGFQIMEAIKVH---QGGNKSTRRQRAIDLLNQVGIPDPASRLdvyPHQLSGGM 158
Cdd:cd03263 73 ARQS-----LGYCPQF-----DALFD-ELTVREHLRFYarlKGLPKSEIKEEVELLLRVLGLTDKANKR---ARTLSGGM 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447119240 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:cd03263 139 KRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-224 |
7.75e-27 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 104.87 E-value: 7.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 2 ALLNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSvsSL--AIMGLI-DYPGRVmaeklVFNGQDLQRI 78
Cdd:COG4133 1 MMLEAENLSCRRGER----LLFSGLSFTLAAGEALALTGPNGSGKT--TLlrILAGLLpPSAGEV-----LWNGEPIRDA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 79 SEKERRNLvgaevAMIFQDPMtsLNPCYTVGfqimEAIKVHQGGNKSTRRQRAID-LLNQVGIpdpASRLDVYPHQLSGG 157
Cdd:COG4133 70 REDYRRRL-----AYLGHADG--LKPELTVR----ENLRFWAALYGLRADREAIDeALEAVGL---AGLADLPVRQLSAG 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447119240 158 MSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMAlVLITHDlALVAEAAHKI 224
Cdd:COG4133 136 QKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAV-LLTTHQ-PLELAAARVL 200
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-227 |
1.31e-26 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 104.49 E-value: 1.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID----YPGRVMaeklvFNGQDLQRIS 79
Cdd:COG4136 2 LSLENLTITLGGR----PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafsASGEVL-----LNGRRLTALP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 80 EKERRnlvgaeVAMIFQDPMtsLNPCYTVGFQIMEAIKvhQGGNKSTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMS 159
Cdd:COG4136 73 AEQRR------IGILFQDDL--LFPHLSVGENLAFALP--PTIGRAQRRARVEQALEEAGLAGFADR---DPATLSGGQR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447119240 160 QRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLAlVAEAAHKIIVM 227
Cdd:COG4136 140 ARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEE-DAPAAGRVLDL 206
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-273 |
1.40e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 106.26 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 19 PF--RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyP--GRVM-AEKLVFNG---QDLQRISEKerrnlvgae 90
Cdd:PRK13634 17 PFerRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQ-PtsGTVTiGERVITAGkknKKLKPLRKK--------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 91 VAMIFQDPMTSLnpcytvgFQimEAIK-------VHQGGNKSTRRQRAIDLLNQVGIPDpaSRLDVYPHQLSGGMSQRVM 163
Cdd:PRK13634 87 VGIVFQFPEHQL-------FE--ETVEkdicfgpMNFGVSEEDAKQKAREMIELVGLPE--ELLARSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 164 IAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAIFh 243
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIF- 234
|
250 260 270
....*....|....*....|....*....|.
gi 447119240 244 apRHP-YTQALLRALPEFAQDKERLASLPGV 273
Cdd:PRK13634 235 --ADPdELEAIGLDLPETVKFKRALEEKFGI 263
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
12-236 |
1.79e-26 |
|
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: 106.32 E-value: 1.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 12 HFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLVFNGQDLQRISEKERRnlvgaEV 91
Cdd:TIGR01188 2 VYGD----FKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLL----RPTSGTARVAGYDVVREPRKVRR-----SI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 92 AMIFQDPmtSLNPCYTvGFQIMEAIKVHQGGNKSTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACR 171
Cdd:TIGR01188 69 GIVPQYA--SVDEDLT-GRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADR---PVGTYSGGMRRRLDIAASLIHQ 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447119240 172 PKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:TIGR01188 143 PDVLFLDEPTTGLDPRTRRAIWDYIRAL-KEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEG 206
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
33-236 |
1.92e-26 |
|
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: 103.91 E-value: 1.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 33 GEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLVFNGQDLQR------ISEKERRnlvgaeVAMIFQDpmTSLNPCY 106
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLE----KPDGGTIVLNGTVLFDsrkkinLPPQQRK------IGLVFQQ--YALFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 107 TVGFQIMEAIKVHQggnKSTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDV 186
Cdd:cd03297 91 NVRENLAFGLKRKR---NREDRISVDELLDLLGL---DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447119240 187 TIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:cd03297 165 ALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
6-245 |
3.47e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 104.88 E-value: 3.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 6 VDKLSVHFGDESAPfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdYPGRVMAEKLVFNGQDLQRISEKERRN 85
Cdd:PRK13640 8 FKHVSFTYPDSKKP--ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLL-LPDDNPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 86 LVGaevaMIFQDPMTSLNPCyTVGFQIMEAIKvhqggNKSTRRQRAI----DLLNQVGIPDPAsrlDVYPHQLSGGMSQR 161
Cdd:PRK13640 85 KVG----IVFQNPDNQFVGA-TVGDDVAFGLE-----NRAVPRPEMIkivrDVLADVGMLDYI---DSEPANLSGGQKQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLAlVAEAAHKIIVMYAGQVVETGDAHAI 241
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDID-EANMADQVLVLDDGKLLAQGSPVEI 230
|
....
gi 447119240 242 FHAP 245
Cdd:PRK13640 231 FSKV 234
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
20-242 |
5.55e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 104.48 E-value: 5.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 20 FRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMAEKLVFNgqdlQRISEKERRNlVGAEVAMIFQDP 98
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKpTTGTVTVDDITIT----HKTKDKYIRP-VRKRIGMVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 99 MTSLNPcYTVGFQIMEAIKvHQGGNKSTRRQRAIDLLNQVGIPdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIAD 178
Cdd:PRK13646 95 ESQLFE-DTVEREIIFGPK-NFKMNLDEVKNYAHRLLMDLGFS--RDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447119240 179 EPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAIF 242
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
14-242 |
1.80e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 102.86 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 14 GDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGL-IDYPGRVMAEKL-VFNGQDLQRIsekerRNLVGaev 91
Cdd:PRK13633 17 NEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALlIPSEGKVYVDGLdTSDEENLWDI-----RNKAG--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 92 aMIFQDPMTslnpcytvgfQIMEAIkVHQ---------GGNKSTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQRV 162
Cdd:PRK13633 89 -MVFQNPDN----------QIVATI-VEEdvafgpenlGIPPEEIRERVDESLKKVGMYEYR---RHAPHLLSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 163 MIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEaAHKIIVMYAGQVVETGDAHAIF 242
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
38-254 |
1.94e-25 |
|
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: 103.73 E-value: 1.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 38 IVGESGSGKSVSSLAIMGLIdypgRVMAEKLVFNGQDLQRISEKERrnlvgaEVAMIFQDpmTSLNPCYTVGFQIMEAIK 117
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFE----QPDSGSIMLDGEDVTNVPPHLR------HINMVFQS--YALFPHMTVEENVAFGLK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 118 VhQGGNKSTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLL 197
Cdd:TIGR01187 69 M-RKVPRAEIKPRVLEALRLVQLEEFADR---KPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELK 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447119240 198 ELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAIFHAPRHPYTQALL 254
Cdd:TIGR01187 145 TIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFI 201
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
11-236 |
2.71e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 106.02 E-value: 2.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 11 VHFG-DESAPfrAVDRISYSVKQGEVVGIVGESGSGKSvsSLA--IMGLIDyP--GRVMaeklvFNGQDLQRISEKERRN 85
Cdd:COG1132 345 VSFSyPGDRP--VLKDISLTIPPGETVALVGPSGSGKS--TLVnlLLRFYD-PtsGRIL-----IDGVDIRDLTLESLRR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 86 LVGaevaMIFQDP----MTslnpcytvgfqIMEAIKVhqgGNKSTRRQRAIDLLNQVGIPDPASRLdvyPH--------- 152
Cdd:COG1132 415 QIG----VVPQDTflfsGT-----------IRENIRY---GRPDATDEEVEEAAKAAQAHEFIEAL---PDgydtvvger 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 153 --QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkeNMALVLITHDLALVAeAAHKIIVMYAG 230
Cdd:COG1132 474 gvNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIR-NADRILVLDDG 550
|
....*.
gi 447119240 231 QVVETG 236
Cdd:COG1132 551 RIVEQG 556
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
22-242 |
3.04e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 102.46 E-value: 3.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVM--AEKLVFNGQDLQRISEKerrnlvgaeVAMIFQDP 98
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKpTSGEVLikGEPIKYDKKSLLEVRKT---------VGIVFQNP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 99 MTSL-NPCYT--VGFQIMeaikvHQGGNKSTRRQRAIDLLNQVGIPDPASRLdvyPHQLSGGMSQRVMIAMAIACRPKLL 175
Cdd:PRK13639 88 DDQLfAPTVEedVAFGPL-----NLGLSKEEVEKRVKEALKAVGMEGFENKP---PHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447119240 176 IADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAIF 242
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYDL-NKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVF 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-265 |
3.26e-25 |
|
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: 105.65 E-value: 3.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYP---GRVM-----------AEKLV 69
Cdd:TIGR03269 1 IEVKNLTKKFDG----KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptsGRIIyhvalcekcgyVERPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 70 FNGQ--------------DLQRISEKERRNLVgAEVAMIFQDPMtSLNPCYTVGFQIMEAIkvHQGGNKSTRR-QRAIDL 134
Cdd:TIGR03269 77 KVGEpcpvcggtlepeevDFWNLSDKLRRRIR-KRIAIMLQRTF-ALYGDDTVLDNVLEAL--EEIGYEGKEAvGRAVDL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 135 LNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDL 214
Cdd:TIGR03269 153 IEMVQL---SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWP 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 447119240 215 ALVAEAAHKIIVMYAGQVVETGDAHAIfhaprhpyTQALLRALPEFAQDKE 265
Cdd:TIGR03269 230 EVIEDLSDKAIWLENGEIKEEGTPDEV--------VAVFMEGVSEVEKECE 272
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-241 |
4.16e-25 |
|
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: 100.59 E-value: 4.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLVFNGQDLQRISEKER 83
Cdd:cd03224 1 LEVENLNAGYGK----SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLL----PPRSGSIRFDGRDITGLPPHER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 84 rnlVGAEVAMIFQDPM--TSLnpcyTVGFQIMEAIKVHQGGNKSTRRQRAIDLLnqvgiPDPASRLDVYPHQLSGGMSQR 161
Cdd:cd03224 73 ---ARAGIGYVPEGRRifPEL----TVEENLLLGAYARRRAKRKARLERVYELF-----PRLKERRKQLAGTLSGGEQQM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKEnMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAI 241
Cdd:cd03224 141 LAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEG-VTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-247 |
5.13e-25 |
|
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: 100.62 E-value: 5.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLiDYPGrvmAEKLVFNGQDLQRisekerrnlVGAEVAMIFQDpmTSL 102
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGL-AQPT---SGGVILEGKQITE---------PGPDRMVVFQN--YSL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 103 NPCYTVGFQIMEAIK-VHQGGNKSTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPT 181
Cdd:TIGR01184 66 LPWLTVRENIALAVDrVLPDLSKSERRAIVEEHIALVGLTEAA---DKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447119240 182 TALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAI-FHAPRH 247
Cdd:TIGR01184 143 GALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRD 209
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-235 |
5.44e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 101.31 E-value: 5.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYP-GRVMAEKLVFNGQdlqrisek 81
Cdd:PRK11248 1 MLQISHLYADYGGK----PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQhGSITLDGKPVEGP-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 82 errnlvGAEVAMIFQD----PMTSLNPCYTVGFQImeaikvhQGGNKSTRRQRAIDLLNQVGIPDPASRldvYPHQLSGG 157
Cdd:PRK11248 69 ------GAERGVVFQNegllPWRNVQDNVAFGLQL-------AGVEKMQRLEIAHQMLKKVGLEGAEKR---YIWQLSGG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 158 MSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMY--AGQVVET 235
Cdd:PRK11248 133 QRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVER 212
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-251 |
1.83e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 99.53 E-value: 1.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 9 LSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDY--PGRVMAEKLVFnGQDLqrISEKERRNL 86
Cdd:PRK14267 10 LRVYYGSN----HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELneEARVEGEVRLF-GRNI--YSPDVDPIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 87 VGAEVAMIFQDPmtslNPcyTVGFQIMEAIKVHQGGNKSTRRQRAIDLLNQVGIPDPA------SRLDVYPHQLSGGMSQ 160
Cdd:PRK14267 83 VRREVGMVFQYP----NP--FPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAAlwdevkDRLNDYPSNLSGGQRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHA 240
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRK 234
|
250
....*....|.
gi 447119240 241 IFHAPRHPYTQ 251
Cdd:PRK14267 235 VFENPEHELTE 245
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-232 |
2.22e-24 |
|
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: 97.50 E-value: 2.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 2 ALLNVDKLSVHfgdesapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLVFNGQDLQRISEK 81
Cdd:cd03215 3 PVLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLR----PPASGEITLDGKPVTRRSPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 82 ERRNlvgAEVAMIFQDpmtslnpcytvgfqimeaikvhqggnkstRRQRAIdllnqvgIPDpasrLDVY-----PHQLSG 156
Cdd:cd03215 71 DAIR---AGIAYVPED-----------------------------RKREGL-------VLD----LSVAenialSSLLSG 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447119240 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQV 232
Cdd:cd03215 108 GNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAD-AGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-242 |
2.30e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 100.17 E-value: 2.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHFGDESaPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMAeklvfngqDLQRISEK 81
Cdd:PRK13642 4 ILEVENLVFKYEKES-DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEeFEGKVKI--------DGELLTAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 82 ERRNLvGAEVAMIFQDPMTSLnpcytVGFQIMEAIKV---HQGGNKSTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGM 158
Cdd:PRK13642 75 NVWNL-RRKIGMVFQNPDNQF-----VGATVEDDVAFgmeNQGIPREEMIKRVDEALLAVNMLDFKTR---EPARLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAeAAHKIIVMYAGQVVETGDA 238
Cdd:PRK13642 146 KQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAA-SSDRILVMKAGEIIKEAAP 224
|
....
gi 447119240 239 HAIF 242
Cdd:PRK13642 225 SELF 228
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
20-242 |
4.24e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 99.70 E-value: 4.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 20 FRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGL-IDYPGRVMAEKLVFNGqDLQRISEKERrnlVGAEVAMIFQDP 98
Cdd:PRK13645 24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiISETGQTIVGDYAIPA-NLKKIKEVKR---LRKEIGLVFQFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 99 MTSLnpcytvgFQimEAIK-------VHQGGNKSTRRQRAIDLLNQVGIP-DPASRldvYPHQLSGGMSQRVMIAMAIAC 170
Cdd:PRK13645 100 EYQL-------FQ--ETIEkdiafgpVNLGENKQEAYKKVPELLKLVQLPeDYVKR---SPFELSGGQKRRVALAGIIAM 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447119240 171 RPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAIF 242
Cdd:PRK13645 168 DGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
21-236 |
5.80e-24 |
|
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: 97.29 E-value: 5.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLVFNGQDLQRISEKERRnlVGAEV-AMIFQDPM 99
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLI----KPDSGEITFDGKSYQKNIEALRR--IGALIeAPGFYPNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 100 TSlnpcytvgfqiMEAIKVHQGGnKSTRRQRAIDLLNQVGipdpasrLDVYPH----QLSGGMSQRVMIAMAIACRPKLL 175
Cdd:cd03268 88 TA-----------RENLRLLARL-LGIRKKRIDEVLDVVG-------LKDSAKkkvkGFSLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447119240 176 IADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
14-233 |
6.23e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 102.11 E-value: 6.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 14 GDESApfRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPG----RVMAEKLV-FNGQDLQRIsekeRRNLVG 88
Cdd:PRK10535 17 GEEQV--EVLKGISLDIYAGEMVAIVGASGSGKS-TLMNILGCLDKPTsgtyRVAGQDVAtLDADALAQL----RREHFG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 89 aevaMIFQ--DPMTSLNPCYTVgfqimEAIKVHQGGNKSTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMSQRVMIAM 166
Cdd:PRK10535 90 ----FIFQryHLLSHLTAAQNV-----EVPAVYAGLERKQRLLRAQELLQRLGLED---RVEYQPSQLSGGQQQRVSIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447119240 167 AIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENmALVLITHDlALVAEAAHKIIVMYAGQVV 233
Cdd:PRK10535 158 ALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGH-TVIIVTHD-PQVAAQAERVIEIRDGEIV 222
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-256 |
1.19e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 97.53 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 2 ALLNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSvsSL--AIMG-LIDYPGRVMaeklvFNGQDLQRI 78
Cdd:PRK13548 1 AMLEARNLSVRLGGR----TLLDDVSLTLRPGEVVAILGPNGAGKS--TLlrALSGeLSPDSGEVR-----LNGRPLADW 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 79 SEKE---RRnlvgaevAMIFQDPmtslnpcyTVGFqimeAIKVHQ--------GGNKSTRRQRAID-LLNQVGIPDPASR 146
Cdd:PRK13548 70 SPAElarRR-------AVLPQHS--------SLSF----PFTVEEvvamgrapHGLSRAEDDALVAaALAQVDLAHLAGR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 147 LdvYPhQLSGGMSQRVMIAMAIA------CRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEA 220
Cdd:PRK13548 131 D--YP-QLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARY 207
|
250 260 270
....*....|....*....|....*....|....*.
gi 447119240 221 AHKIIVMYAGQVVETGdahaifhAPRHPYTQALLRA 256
Cdd:PRK13548 208 ADRIVLLHQGRLVADG-------TPAEVLTPETLRR 236
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-241 |
2.56e-23 |
|
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: 100.26 E-value: 2.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGRvmAEKLVFNGQDLQRISEK--ERRNLVGAEVAMIFQDp 98
Cdd:TIGR03269 298 KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLE-PTS--GEVNVRVGDEWVDMTKPgpDGRGRAKRYIGILHQE- 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 99 mTSLNPCYTVGFQIMEAIKVHQggNKSTRRQRAIDLLNQVGIPDPASR--LDVYPHQLSGGMSQRVMIAMAIACRPKLLI 176
Cdd:TIGR03269 374 -YDLYPHRTVLDNLTEAIGLEL--PDELARMKAVITLKMVGFDEEKAEeiLDKYPDELSEGERHRVALAQVLIKEPRIVI 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447119240 177 ADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAI 241
Cdd:TIGR03269 451 LDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-274 |
3.07e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 97.10 E-value: 3.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyP--GRVMaeklvFNGQDLQRisek 81
Cdd:COG4152 2 LELKGLTKRFGD----KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILA-PdsGEVL-----WDGEPLDP---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 82 ERRNLVG---AEvamifqdpmTSLNPCYTVGFQI--MEAIKvhqGGNKSTRRQRAIDLLNQVGIPDpasRLDVYPHQLSG 156
Cdd:COG4152 68 EDRRRIGylpEE---------RGLYPKMKVGEQLvyLARLK---GLSKAEAKRRADEWLERLGLGD---RANKKVEELSK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:COG4152 133 GNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSG 211
|
250 260 270
....*....|....*....|....*....|....*...
gi 447119240 237 DAHAIfhapRHPYTQALLRAlpEFAQDKERLASLPGVV 274
Cdd:COG4152 212 SVDEI----RRQFGRNTLRL--EADGDAGWLRALPGVT 243
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
22-227 |
3.79e-23 |
|
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: 95.58 E-value: 3.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 22 AVDRISYSVKQGEVVGIVGESGSGKS-----------VSSLAImgLIDYPGRVMaeklvfngqDLQRISEKE----RRNL 86
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKStllkciygnylPDSGSI--LVRHDGGWV---------DLAQASPREilalRRRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 87 VGaevamifqdpMTS--LN-----PCYTVgfqIMEAIkVHQGGNKSTRRQRAIDLLNQVGIPdpaSRL-DVYPHQLSGGM 158
Cdd:COG4778 95 IG----------YVSqfLRviprvSALDV---VAEPL-LERGVDREEARARARELLARLNLP---ERLwDLPPATFSGGE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447119240 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVM 227
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKA-RGTAIIGIFHDEEVREAVADRVVDV 225
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-251 |
4.13e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 96.00 E-value: 4.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 2 ALLNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKS--VSSLAIMGLIDyPGRVMAEKLVFNGQDL--QR 77
Cdd:PRK14239 4 PILQVSDLSVYYNKK----KALNSVSLDFYPNEITALIGPSGSGKStlLRSINRMNDLN-PEVTITGSIVYNGHNIysPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 78 ISEKERRNlvgaEVAMIFQDPmtslNPC-YTVGFQIMEAIKVHQGGNKSTRRQRAIDLLNQVGIPDPAS-RLDVYPHQLS 155
Cdd:PRK14239 79 TDTVDLRK----EIGMVFQQP----NPFpMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKdRLHDSALGLS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVliTHDLALVAEAAHKIIVMYAGQVVET 235
Cdd:PRK14239 151 GGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLV--TRSMQQASRISDRTGFFLDGDLIEY 228
|
250
....*....|....*.
gi 447119240 236 GDAHAIFHAPRHPYTQ 251
Cdd:PRK14239 229 NDTKQMFMNPKHKETE 244
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-245 |
9.54e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 96.71 E-value: 9.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKlsvHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLiDYPgrvMAEKLVFNGQDLQRISEKE 82
Cdd:PRK11432 9 LKNITK---RFGSN----TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGL-EKP---TEGQIFIDGEDVTHRSIQQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 83 RrnlvgaEVAMIFQDpmTSLNPCYTVGFQIMEAIKVhQGGNKSTRRQRAIDLLNQVgipDPASRLDVYPHQLSGGMSQRV 162
Cdd:PRK11432 78 R------DICMVFQS--YALFPHMSLGENVGYGLKM-LGVPKEERKQRVKEALELV---DLAGFEDRYVDQISGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 163 MIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAIF 242
Cdd:PRK11432 146 ALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELY 225
|
...
gi 447119240 243 HAP 245
Cdd:PRK11432 226 RQP 228
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
22-250 |
9.57e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 97.21 E-value: 9.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 22 AVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLVFNGQDLQRISEKERrnlvgaEVAMIFQDpmTS 101
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKS-TLLRMLAGFEQP---TAGQIMLDGVDLSHVPPYQR------PINMMFQS--YA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 102 LNPCYTVGFQIMEAIKvHQGGNKSTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPT 181
Cdd:PRK11607 102 LFPHMTVEQNIAFGLK-QDKLPKAEIASRVNEMLGLVHMQEFAKR---KPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447119240 182 TALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAIFHAPRHPYT 250
Cdd:PRK11607 178 GALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
26-249 |
1.08e-22 |
|
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: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLVFNGQDLQRISEK-----ERRnlvgaEVAMIFQDpmT 100
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLT----RPDEGEIVLNGRTLFDSRKGiflppEKR-----RIGYVFQE--A 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 101 SLNPCYTVGFQIMEAIKVHQGGNKSTRRQRAIDLLnqvGIpDPAsrLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
Cdd:TIGR02142 85 RLFPHLSVRGNLRYGMKRARPSERRISFERVIELL---GI-GHL--LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447119240 181 TTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAIFHAPRHPY 249
Cdd:TIGR02142 159 LAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-235 |
1.16e-22 |
|
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: 92.49 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGdesaPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyP--GRVmaeklVFNGQDLQRISEK 81
Cdd:cd03216 1 LELRGITKRFG----GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYK-PdsGEI-----LVDGKEVSFASPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 82 ERRNLvGaeVAMIfqdpmtslnpcytvgfqimeaikvhqggnkstrrqraidllnqvgipdpasrldvypHQLSGGMSQR 161
Cdd:cd03216 71 DARRA-G--IAMV---------------------------------------------------------YQLSVGERQM 90
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447119240 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQVVET 235
Cdd:cd03216 91 VEIARALARNARLLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-238 |
1.42e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 97.69 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidYPGRVMAEKLVFNGQDLQ--RISEKERrnlvgAEVAMIFQDP 98
Cdd:PRK13549 19 KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV--YPHGTYEGEIIFEGEELQasNIRDTER-----AGIAIIHQEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 99 MtsLNPCYTVGFQIMEAIKVHQGG--NKSTRRQRAIDLLNQVGIP-DPASRLdvypHQLSGGMSQRVMIAMAIACRPKLL 175
Cdd:PRK13549 92 A--LVKELSVLENIFLGNEITPGGimDYDAMYLRAQKLLAQLKLDiNPATPV----GNLGLGQQQLVEIAKALNKQARLL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447119240 176 IADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVETGDA 238
Cdd:PRK13549 166 ILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGRHIGTRPA 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-241 |
1.49e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.78 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 1 MALLNVDKLSVHFGdesaPFRAVDRISYSVKQGEVVGIVGESGSGKsvSSL--AIMGLidYP---GRVmaeklVFNGQDL 75
Cdd:COG1129 2 EPLLEMRGISKSFG----GVKALDGVSLELRPGEVHALLGENGAGK--STLmkILSGV--YQpdsGEI-----LLDGEPV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 76 QRISEKERRNLvGaeVAMIFQDPmtSLNPCYTVgfqiMEAI----KVHQGG--NKSTRRQRAIDLLNQVGIP-DPASRLD 148
Cdd:COG1129 69 RFRSPRDAQAA-G--IAIIHQEL--NLVPNLSV----AENIflgrEPRRGGliDWRAMRRRARELLARLGLDiDPDTPVG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 149 vyphQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMY 228
Cdd:COG1129 140 ----DLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLR 214
|
250
....*....|...
gi 447119240 229 AGQVVETGDAHAI 241
Cdd:COG1129 215 DGRLVGTGPVAEL 227
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
21-264 |
1.90e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 94.80 E-value: 1.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGlIDYP--GRVMaeklVFnGQDLQRISEKERRNLVGaevaMIFQDP 98
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNG-IYLPqrGRVK----VM-GREVNAENEKWVRSKVG----LVFQDP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 99 ---MTSLNPCYTVGFQimeaiKVHQGGNKSTRRQRAIDLLNQVGIPDPASRLdvyPHQLSGGMSQRVMIAMAIACRPKLL 175
Cdd:PRK13647 89 ddqVFSSTVWDDVAFG-----PVNMGLDKDEVERRVEEALKAVRMWDFRDKP---PYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 176 IADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAH-----AIFHAP--RHP 248
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLHN-QGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSlltdeDIVEQAglRLP 239
|
250
....*....|....*.
gi 447119240 249 YTQALLRALPEFAQDK 264
Cdd:PRK13647 240 LVAQIFEDLPELGQSK 255
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-236 |
2.01e-22 |
|
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: 93.03 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDEsapfRAVDRISYSVKQGeVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLVFNGQDLQRISEKER 83
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLT----PPSSGTIRIDGQDVLKQPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 84 RnLVGaevaMIFQDPMTSlnPCYTVgFQIMEAIKVHQGGNKSTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVM 163
Cdd:cd03264 72 R-RIG----YLPQEFGVY--PNFTV-REFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKK---KIGSLSGGMRRRVG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447119240 164 IAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:cd03264 141 IAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSEL--GEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-266 |
2.03e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 94.78 E-value: 2.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID------YPGRVM-AEKLVFNGQDlqrISEKERRnlvgaeVAMIF 95
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkvsgyrYSGDVLlGGRSIFNYRD---VLEFRRR------VGMLF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 96 QDPmtslNPC-YTVGFQIMEAIKVHQGGNKSTRRQRAIDLLNQVGIPDPAS-RLDVYPHQLSGGMSQRVMIAMAIACRPK 173
Cdd:PRK14271 108 QRP----NPFpMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKdRLSDSPFRLSGGQQQLLCLARTLAVNPE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 174 LLIADEPTTALDVTIQAQIIELLLELQQKenMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAIFHAPRHPYTQAL 253
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARY 261
|
250
....*....|...
gi 447119240 254 LRALPEFAQDKER 266
Cdd:PRK14271 262 VAGLSGDVKDAKR 274
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-236 |
2.29e-22 |
|
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: 92.73 E-value: 2.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdYPGrvmAEKLVFNGQDLQrISEKER 83
Cdd:cd03269 1 LEVENVTKRFGRV----TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGII-LPD---SGEVLFDGKPLD-IAARNR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 84 RNLVGAEvamifqdpmTSLNPCYTVGFQIMEAIKVHqGGNKSTRRQRAIDLLNQVGIPDPAS-RLDvyphQLSGGMSQRV 162
Cdd:cd03269 72 IGYLPEE---------RGLYPKMKVIDQLVYLAQLK-GLKKEEARRRIDEWLERLELSEYANkRVE----ELSKGNQQKV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447119240 163 MIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:cd03269 138 QFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-239 |
2.31e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 97.02 E-value: 2.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHfgdESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLVFNGQDLQRISEKE 82
Cdd:COG3845 257 VLEVENLSVR---DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLR----PPASGSIRLDGEDITGLSPRE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 83 RRNLvGaeVAMIFQDPM-TSLNPCYTVGFQIM----EAIKVHQGG--NKSTRRQRAIDLLNQVGI--PDPASRLDvyphQ 153
Cdd:COG3845 330 RRRL-G--VAYIPEDRLgRGLVPDMSVAENLIlgryRRPPFSRGGflDRKAIRAFAEELIEEFDVrtPGPDTPAR----S 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
Cdd:COG3845 403 LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
....*.
gi 447119240 234 ETGDAH 239
Cdd:COG3845 482 GEVPAA 487
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
20-241 |
4.23e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 94.38 E-value: 4.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 20 FRAVDRISYSVKQGEVVGIVGESGSGKS-----VSSLAI--MGLIDY------------PGRVMAEKLVFNGQDLQRISE 80
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTtfiehLNALLLpdTGTIEWifkdeknkkktkEKEKVLEKLVIQKTRFKKIKK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 81 -KERRNLVGaevaMIFQdpmtslnpcyTVGFQIMEAI--------KVHQGGNKSTRRQRAIDLLNQVGIPDpaSRLDVYP 151
Cdd:PRK13651 100 iKEIRRRVG----VVFQ----------FAEYQLFEQTiekdiifgPVSMGVSKEEAKKRAAKYIELVGLDE--SYLQRSP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 152 HQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQ 231
Cdd:PRK13651 164 FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNL-NKQGKTIILVTHDLDNVLEWTKRTIFFKDGK 242
|
250
....*....|
gi 447119240 232 VVETGDAHAI 241
Cdd:PRK13651 243 IIKDGDTYDI 252
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-242 |
4.68e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 93.76 E-value: 4.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHFGDESapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLVFNGQ--DLQRISE 80
Cdd:PRK13636 5 ILKVEELNYNYSDGT---HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGIL----KPSSGRILFDGKpiDYSRKGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 81 KERRNLVGaevaMIFQDPMTSLNPCYTvgFQIMEAIKVHQGGNKSTRRQRAIDLLNQVGIpdpaSRLDVYP-HQLSGGMS 159
Cdd:PRK13636 78 MKLRESVG----MVFQDPDNQLFSASV--YQDVSFGAVNLKLPEDEVRKRVDNALKRTGI----EHLKDKPtHCLSFGQK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 160 QRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAH 239
Cdd:PRK13636 148 KRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPK 227
|
...
gi 447119240 240 AIF 242
Cdd:PRK13636 228 EVF 230
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-236 |
1.15e-21 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 92.10 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSvsSL--AIMGLID-YPGRVMaeklvFNGQDLQRIS 79
Cdd:COG4559 1 MLEAENLSVRLGGR----TLLDDVSLTLRPGELTAIIGPNGAGKS--TLlkLLTGELTpSSGEVR-----LNGRPLAAWS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 80 EKE---RRnlvgaevAMIFQDpmTSLNPCYTVgFQIMEAIKVHQGGNKSTRRQRAIDLLNQVGIPDPASRLdvYPhQLSG 156
Cdd:COG4559 70 PWElarRR-------AVLPQH--SSLAFPFTV-EEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRS--YQ-TLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 157 GMSQRVMIAMAIA-------CRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYA 229
Cdd:COG4559 137 GEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLAR-RGGGVVAVLHDLNLAAQYADRILLLHQ 215
|
....*..
gi 447119240 230 GQVVETG 236
Cdd:COG4559 216 GRLVAQG 222
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
21-233 |
1.47e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 91.09 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGlIDYPGrvmAEKLVFNGQDLQRISEKE----RRnlvgaEVAMIFQ 96
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICG-IERPS---AGKIWFSGHDITRLKNREvpflRR-----QIGMIFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 97 DPMTSLNPCYTVGFQIMEAIKvhqGGNKSTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLI 176
Cdd:PRK10908 87 DHHLLMDRTVYDNVAIPLIIA---GASGDDIRRRVSAALDKVGLLDKAKN---FPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447119240 177 ADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-227 |
1.95e-21 |
|
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: 94.66 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDESApfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGRvmaEKLVFNGQDLQRISEKER 83
Cdd:TIGR02857 322 LEFSGVSVAYPGRRP---ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVD-PTE---GSIAVNGVPLADADADSW 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 84 RnlvgAEVAMIFQDPmtslnpcYTVGFQIMEAIKVHQGGNKSTRRQRAIDL--LNQV--GIPDP-ASRLDVYPHQLSGGM 158
Cdd:TIGR02857 395 R----DQIAWVPQHP-------FLFAGTIAENIRLARPDASDAEIREALERagLDEFvaALPQGlDTPIGEGGAGLSGGQ 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447119240 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkeNMALVLITHDLALvAEAAHKIIVM 227
Cdd:TIGR02857 464 AQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLAL-AALADRIVVL 529
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-246 |
2.26e-21 |
|
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: 90.81 E-value: 2.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 1 MALLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSvsSL--AIMGLIdypgRVMAEKLVFNGQDLQRI 78
Cdd:COG0410 1 MPMLEVENLHAGYGG----IHVLHGVSLEVEEGEIVALLGRNGAGKT--TLlkAISGLL----PPRSGSIRFDGEDITGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 79 SEKERrnlVGAEVAM------IFQDpMTslnpcytvgfqIME-----AIKVHQGGNKSTRRQRAIDLLnqvgiPDPASRL 147
Cdd:COG0410 71 PPHRI---ARLGIGYvpegrrIFPS-LT-----------VEEnlllgAYARRDRAEVRADLERVYELF-----PRLKERR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 148 DVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVM 227
Cdd:COG0410 131 RQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVL 209
|
250
....*....|....*....
gi 447119240 228 YAGQVVETGDAHAIFHAPR 246
Cdd:COG0410 210 ERGRIVLEGTAAELLADPE 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-238 |
2.39e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 94.32 E-value: 2.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKlsvHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKS--VSslAIMGLidYP---GRVmaeklVFNGQDLQR 77
Cdd:COG3845 8 LRGITK---RFGG----VVANDDVSLTVRPGEIHALLGENGAGKStlMK--ILYGL--YQpdsGEI-----LIDGKPVRI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 78 ISEKERRNLvGaeVAMIFQDPMtsLNPCYTVGFQIMEAIKVHQGG--NKSTRRQRAIDLLNQVGIP-DPasrlDVYPHQL 154
Cdd:COG3845 72 RSPRDAIAL-G--IGMVHQHFM--LVPNLTVAENIVLGLEPTKGGrlDRKAARARIRELSERYGLDvDP----DAKVEDL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALdvTIQaQIIELLLELQQ--KENMALVLITHDLALVAEAAHKIIVMYAGQV 232
Cdd:COG3845 143 SVGEQQRVEILKALYRGARILILDEPTAVL--TPQ-EADELFEILRRlaAEGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
....*.
gi 447119240 233 VETGDA 238
Cdd:COG3845 220 VGTVDT 225
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
11-236 |
2.66e-21 |
|
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: 90.36 E-value: 2.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 11 VHFG-DESAPfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLVFNGQDLQRISEKERRNLVGa 89
Cdd:cd03254 8 VNFSyDEKKP--VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYD----PQKGQILIDGIDIRDISRKSLRSMIG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 90 evaMIFQDPMTslnpcytvgFQ--IMEAIKVhqgGNKSTRRQRAIDLLNQVGIPDPASRL-DVYPHQ-------LSGGMS 159
Cdd:cd03254 81 ---VVLQDTFL---------FSgtIMENIRL---GRPNATDEEVIEAAKEAGAHDFIMKLpNGYDTVlgenggnLSQGER 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447119240 160 QRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQqkENMALVLITHDLALVAEaAHKIIVMYAGQVVETG 236
Cdd:cd03254 146 QLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLM--KGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEG 219
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
233-297 |
3.63e-21 |
|
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid.
Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 85.15 E-value: 3.63e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447119240 233 VETGDAHAIFHAPRHPYTQALLRALPEFAQDKERLASLPGVVPGKYDRPNGCLLNPRCPYATDRC 297
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPKRPLYTIPGNVPSLLELPEGCPFAPRCPFATEEC 65
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-236 |
1.21e-20 |
|
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: 88.58 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLVFNGQDLQRISEKE 82
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLL----EPDAGFATVDGFDVVKEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 83 RRNLVGAEVAMIFQDPMTSL-NPCYTVGFQimeaikvhqGGNKSTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMSQR 161
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTAReNLEYFAGLY---------GLKGDELTARLEELADRLGMEE---LLDRRVGGFSTGMRQK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447119240 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:cd03266 145 VAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRA-LGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-246 |
2.59e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 90.67 E-value: 2.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 1 MALLNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGrvmAEKLVFNGQDLQRISE 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGDT----TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLT-PT---AGTVLVAGDDVEALSA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 81 KErrnlVGAEVAMIFQDpmTSLNPCYTVGfQIMEAIKV-HQG--GNKSTRRQRAID-LLNQVGIPDPASRlDVypHQLSG 156
Cdd:PRK09536 73 RA----ASRRVASVPQD--TSLSFEFDVR-QVVEMGRTpHRSrfDTWTETDRAAVErAMERTGVAQFADR-PV--TSLSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLItHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:PRK09536 143 GERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAG 221
|
250
....*....|
gi 447119240 237 DAHAIFHAPR 246
Cdd:PRK09536 222 PPADVLTADT 231
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-236 |
2.59e-20 |
|
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: 87.08 E-value: 2.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDESAPfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLVFNGQDLQRIS-EKE 82
Cdd:cd03369 7 IEVENLSVRYAPDLPP--VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLE----AEEGKIEIDGIDISTIPlEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 83 RRNLvgaevAMIFQDPM-------TSLNPC--YTvGFQIMEAIKVHQGGNkstrrqraidllnqvgipdpasrldvyphQ 153
Cdd:cd03369 81 RSSL-----TIIPQDPTlfsgtirSNLDPFdeYS-DEEIYGALRVSEGGL-----------------------------N 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkeNMALVLITHDLALVAEAAhKIIVMYAGQVV 233
Cdd:cd03369 126 LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIIDYD-KILVMDAGEVK 202
|
...
gi 447119240 234 ETG 236
Cdd:cd03369 203 EYD 205
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
27-237 |
3.03e-20 |
|
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: 87.60 E-value: 3.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 27 SYSVKQGEVVGIVGESGSGKSvsslAIMGLID--Y-P--GRVMaeklvFNGQDLQRISEKERRNLVGaevaMIFQDPMts 101
Cdd:cd03249 23 SLTIPPGKTVALVGSSGCGKS----TVVSLLErfYdPtsGEIL-----LDGVDIRDLNLRWLRSQIG----LVSQEPV-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 102 LNPCytvgfQIMEAIKVHQGGNKSTRRQRAIDLLNQ----VGIPDpasRLD--VYPH--QLSGGMSQRVMIAMAIACRPK 173
Cdd:cd03249 88 LFDG-----TIAENIRYGKPDATDEEVEEAAKKANIhdfiMSLPD---GYDtlVGERgsQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447119240 174 LLIADEPTTALDVTIQAQIIELLLELqqKENMALVLITHDLALVaEAAHKIIVMYAGQVVETGD 237
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRA--MKGRTTIVIAHRLSTI-RNADLIAVLQNGQVVEQGT 220
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-241 |
3.07e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 87.72 E-value: 3.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 25 RISYSVKQGEVVGIVGESGSGKSvsslAIMGLIdyPGRVMAEK--LVFNGQDLQRISEKERrnlvgaEVAMIFQDpmTSL 102
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKS----TLLNLI--AGFLTPASgsLTLNGQDHTTTPPSRR------PVSMLFQE--NNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 103 NPCYTVGFQImeAIKVHQGG--NKSTRRQRAiDLLNQVGIPDPASRLdvyPHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
Cdd:PRK10771 83 FSHLTVAQNI--GLGLNPGLklNAAQREKLH-AIARQMGIEDLLARL---PGQLSGGQRQRVALARCLVREQPILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447119240 181 TTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAI 241
Cdd:PRK10771 157 FSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
22-236 |
5.29e-20 |
|
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: 87.16 E-value: 5.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidYP---GRVmaeklVFNGQDLQRISEKERRnlvgAEVAMIFQDP 98
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRF--YVpenGRV-----LVDGHDLALADPAWLR----RQVGVVLQEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 99 mTSLNPcytvgfQIMEAIKVhqgGNKSTRRQRAIDLLNQVGIPDPASRLDVYPHQ--------LSGGMSQRVMIAMAIAC 170
Cdd:cd03252 86 -VLFNR------SIRDNIAL---ADPGMSMERVIEAAKLAGAHDFISELPEGYDTivgeqgagLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447119240 171 RPKLLIADEPTTALDVTIQAQIIELLLELQqkENMALVLITHDLALVaEAAHKIIVMYAGQVVETG 236
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDIC--AGRTVIIIAHRLSTV-KNADRIIVMEKGRIVEQG 218
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
11-236 |
6.39e-20 |
|
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: 86.90 E-value: 6.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 11 VHFGDEsaPFRAVDR-ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLVFNGQDLQRISEKERRNLVGa 89
Cdd:cd03253 6 VTFAYD--PGRPVLKdVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYD----VSSGSILIDGQDIREVTLDSLRRAIG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 90 evaMIFQDpmtslnpcyTVGFQ--IMEAIKVhqgGNKSTRRQRAIDLLNQVGIPDPASRL-DVYPHQ-------LSGGMS 159
Cdd:cd03253 79 ---VVPQD---------TVLFNdtIGYNIRY---GRPDATDEEVIEAAKAAQIHDKIMRFpDGYDTIvgerglkLSGGEK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447119240 160 QRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALVLITHDLALVAEaAHKIIVMYAGQVVETG 236
Cdd:cd03253 144 QRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDV--SKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERG 217
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-240 |
7.20e-20 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 89.85 E-value: 7.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 21 RAVDRISYSVKQGEVVGIVGESGSGKS----VSSlaimGLidYPGRVMAEKLVFNGQDLQ--RISEKERRNLV--GAEVA 92
Cdd:NF040905 15 KALDDVNLSVREGEIHALCGENGAGKStlmkVLS----GV--YPHGSYEGEILFDGEVCRfkDIRDSEALGIViiHQELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 93 MIfqdPMTSlnpcytvgfqIMEAIKVhqgGNKSTRR---------QRAIDLLNQVGIP-DPASRLDvyphQLSGGMSQRV 162
Cdd:NF040905 89 LI---PYLS----------IAENIFL---GNERAKRgvidwnetnRRARELLAKVGLDeSPDTLVT----DIGVGKQQLV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447119240 163 MIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHA 240
Cdd:NF040905 149 EIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCRA 225
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-236 |
8.55e-20 |
|
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: 86.01 E-value: 8.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 25 RISYSVKQGEVVGIVGESGSGKSVSSLAIMGLiDYP--GRVmaeklVFNGQDLQRISEKERrnlvgaEVAMIFQDpmTSL 102
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGF-ETPqsGRV-----LINGVDVTAAPPADR------PVSMLFQE--NNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 103 NPCYTVGFQImeAIKVHQGGNKSTRRQRAID-LLNQVGIPDPASRLdvyPHQLSGGMSQRVMIAMAIACRPKLLIADEPT 181
Cdd:cd03298 82 FAHLTVEQNV--GLGLSPGLKLTAEDRQAIEvALARVGLAGLEKRL---PGELSGGERQRVALARVLVRDKPVLLLDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447119240 182 TALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:cd03298 157 AALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-233 |
1.02e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 86.68 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 21 RAVDRISYSVKQGEVVGIVGESGSGKSvsSL--AIMGLIdypgRVMAEKLVFNGQDLQRISEKERRNLVGaevaMIFQDP 98
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKS--TLlnAIAGSL----PPDSGSILIDGKDVTKLPEYKRAKYIG----RVFQDP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 99 M--TSLNpcytvgFQIME--AIKVHQG-------GNKSTRRQRAIDLLNQV--GIPDpasRLDVYPHQLSGGMSQRVMIA 165
Cdd:COG1101 90 MmgTAPS------MTIEEnlALAYRRGkrrglrrGLTKKRRELFRELLATLglGLEN---RLDTKVGLLSGGQRQALSLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 166 MAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDL--ALvaEAAHKIIVMYAGQVV 233
Cdd:COG1101 161 MATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMeqAL--DYGNRLIMMHEGRII 228
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-275 |
1.28e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 86.96 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHFGDESApfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLVFNGQDLQRISE-K 81
Cdd:PRK13644 1 MIRLENVSYSYPDGTP---ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLL----RPQKGKVLVSGIDTGDFSKlQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 82 ERRNLVGaevaMIFQDPMTSLnpcytVGFQIMEAIKVhqgGNKS------TRRQRAIDLLNQVGIPDPASRldvYPHQLS 155
Cdd:PRK13644 74 GIRKLVG----IVFQNPETQF-----VGRTVEEDLAF---GPENlclppiEIRKRVDRALAEIGLEKYRHR---SPKTLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVaEAAHKIIVMYAGQVVET 235
Cdd:PRK13644 139 GGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEEL-HDADRIIVMDRGKIVLE 216
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 447119240 236 GDAHAIFHAPRhpyTQALLRALPEFAQDKERLASLPGVVP 275
Cdd:PRK13644 217 GEPENVLSDVS---LQTLGLTPPSLIELAENLKMHGVVIP 253
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-242 |
1.37e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 87.19 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 21 RAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDypGRVMAEKLVFNGQDLQRISEKERRNL--VGAEVAMIFQDP 98
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKS----TLMQHFN--ALLKPSSGTITIAGYHITPETGNKNLkkLRKKVSLVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 99 MTSLNPcYTVGFQIMEAIKvHQGGNKSTRRQRAIDLLNQVGIPDpaSRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIAD 178
Cdd:PRK13641 95 EAQLFE-NTVLKDVEFGPK-NFGFSEDEAKEKALKWLKKVGLSE--DLISKSPFELSGGQMRRVAIAGVMAYEPEILCLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447119240 179 EPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAIF 242
Cdd:PRK13641 171 EPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIF 233
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
26-238 |
2.01e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 85.50 E-value: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYpgRVMAEKLVFNGQDLQRISEKERrnlVGAEVAMIFQDPMTSlnPC 105
Cdd:COG0396 19 VNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKY--EVTSGSILLDGEDILELSPDER---ARAGIFLAFQYPVEI--PG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 106 YTVGFQIMEAIKVHQGGNKSTR--RQRAIDLLNQVGI-PDPASR-LDVyphQLSGGMSQRVMIAMAIACRPKLLIADEPT 181
Cdd:COG0396 92 VSVSNFLRTALNARRGEELSARefLKLLKEKMKELGLdEDFLDRyVNE---GFSGGEKKRNEILQMLLLEPKLAILDETD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447119240 182 TALDV---TIQAQIIELLlelqQKENMALVLITHDLALVAE-AAHKIIVMYAGQVVETGDA 238
Cdd:COG0396 169 SGLDIdalRIVAEGVNKL----RSPDRGILIITHYQRILDYiKPDFVHVLVDGRIVKSGGK 225
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
10-240 |
2.95e-19 |
|
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: 84.97 E-value: 2.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 10 SVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLVFNGQDLQRISEKERRNLVGa 89
Cdd:cd03251 5 NVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKS----TLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 90 evaMIFQDpmtslnpcyTVGFQ--IMEAIKVhqgGNKSTRRQRAIDLLNQVGIPDPASRLDVYPH--------QLSGGMS 159
Cdd:cd03251 80 ---LVSQD---------VFLFNdtVAENIAY---GRPGATREEVEEAARAANAHEFIMELPEGYDtvigergvKLSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 160 QRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQqkENMALVLITHDLALVaEAAHKIIVMYAGQVVETGDaH 239
Cdd:cd03251 145 QRIAIARALLKDPPILILDEATSALDTESERLVQAALERLM--KNRTTFVIAHRLSTI-ENADRIVVLEDGKIVERGT-H 220
|
.
gi 447119240 240 A 240
Cdd:cd03251 221 E 221
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-241 |
3.29e-19 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 87.96 E-value: 3.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidYPGRVMAEKLVFNGQDL--QRISE 80
Cdd:TIGR02633 1 LLEMKGIVKTFGG----VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV--YPHGTWDGEIYWSGSPLkaSNIRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 81 KERrnlvgAEVAMIFQDPMtsLNPCYTVGFQIMEAIKV-HQGG--NKSTRRQRAIDLLNQVGIPDPASRLDVypHQLSGG 157
Cdd:TIGR02633 75 TER-----AGIVIIHQELT--LVPELSVAENIFLGNEItLPGGrmAYNAMYLRAKNLLRELQLDADNVTRPV--GDYGGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 158 MSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVETGD 237
Cdd:TIGR02633 146 QQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVATKD 224
|
....
gi 447119240 238 AHAI 241
Cdd:TIGR02633 225 MSTM 228
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
21-242 |
3.85e-19 |
|
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: 84.52 E-value: 3.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLVFNGQDLQRISEKERRNL-VG--AEVAMIFQD 97
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLV----KPDSGKILLDGQDITKLPMHKRARLgIGylPQEASIFRK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 98 pmtslnpcYTVGFQIMEAIKVHqGGNKSTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIA 177
Cdd:cd03218 90 --------LTVEENILAVLEIR-GLSKKEREEKLEELLEEFHI---THLRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447119240 178 DEPTTALDVTIQAQIIELLLELQQKeNMAlVLIT-HDLALVAEAAHKIIVMYAGQVVETGDAHAIF 242
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKILKDR-GIG-VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
22-245 |
5.83e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 85.24 E-value: 5.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLVFNGQDLQRISEKERRNLVGaevaMIFQDPMTS 101
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGIL----KPTSGSVLIRGEPITKENIREVRKFVG----LVFQNPDDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 102 L-NPcyTVGfQIMEAIKVHQGGNKSTRRQRAIDLLNQVGIPDPASRLdvyPHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
Cdd:PRK13652 91 IfSP--TVE-QDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRV---PHHLSGGEKKRVAIAGVIAMEPQVLVLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447119240 181 TTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAIFHAP 245
Cdd:PRK13652 165 TAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-242 |
7.05e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 84.12 E-value: 7.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 26 ISYSVKQGEVVGIVGESGSGKSvSSLAIM-GLIDYPGRVMaeklvFNGQDLQRISEKE---RRnlvgaevAMIFQDPMTS 101
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKS-TLLARMaGLLPGQGEIL-----LNGRPLSDWSAAElarHR-------AYLSQQQSPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 102 LnpcytvgfqimeAIKVHQ----GGNKSTRRQRAIDLLNQVgipdpASRL---DVYP---HQLSGGMSQRVMIAMAI--- 168
Cdd:COG4138 82 F------------AMPVFQylalHQPAGASSEAVEQLLAQL-----AEALgleDKLSrplTQLSGGEWQRVRLAAVLlqv 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447119240 169 --ACRP--KLLIADEPTTALDVTIQAQIIELLLELQQKENmALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAIF 242
Cdd:COG4138 145 wpTINPegQLLLLDEPMNSLDVAQQAALDRLLRELCQQGI-TVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
25-236 |
1.22e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 86.64 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 25 RISYSVKQGEVVGIVGESGSGKS--VSSLA--IMGLIDYPGRVMAEKLVFNGQDLQRISekerrnlvgaevAMIFQDPMt 100
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTtlMNALAfrSPKGVKGSGSVLLNGMPIDAKEMRAIS------------AYVQQDDL- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 101 sLNPCYTV--GFQIMEAIKVHQGGNKSTRRQRAIDLLNQVGIPDPASRLDVYPHQ---LSGGMSQRVMIAMAIACRPKLL 175
Cdd:TIGR00955 110 -FIPTLTVreHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRvkgLSGGERKRLAFASELLTDPPLL 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447119240 176 IADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLG 249
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-241 |
1.37e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 83.15 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 1 MALLNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLI--DYpGRVMaeklvFNGQDLQRI 78
Cdd:COG1137 1 MMTLEAENLVKSYGKR----TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVkpDS-GRIF-----LDGEDITHL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 79 SEKER-RNLVG--AEVAMIFQDpmtsLnpcyTVGFQIMeAIKVHQGGNKSTRRQRAIDLLNQVGIpdpASRLDVYPHQLS 155
Cdd:COG1137 71 PMHKRaRLGIGylPQEASIFRK----L----TVEDNIL-AVLELRKLSKKEREERLEELLEEFGI---THLRKSKAYSLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 156 GGMSQRVMIAMAIACRPKLLIADEPTTALD-VTIqAQIIELLLELQQKeNMAlVLIT-HD----LALVAEAAhkiiVMYA 229
Cdd:COG1137 139 GGERRRVEIARALATNPKFILLDEPFAGVDpIAV-ADIQKIIRHLKER-GIG-VLITdHNvretLGICDRAY----IISE 211
|
250
....*....|..
gi 447119240 230 GQVVETGDAHAI 241
Cdd:COG1137 212 GKVLAEGTPEEI 223
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-242 |
3.54e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 82.87 E-value: 3.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 19 PF--RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGL-IDYPGRVMAEKLVFNGQDlqriSEKERRNlVGAEVAMIF 95
Cdd:PRK13649 17 PFegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLhVPTQGSVRVDDTLITSTS----KNKDIKQ-IRKKVGLVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 96 QDPMTslnpcytvgfQIMEAIKVHQ--------GGNKSTRRQRAIDLLNQVGIPDpaSRLDVYPHQLSGGMSQRVMIAMA 167
Cdd:PRK13649 92 QFPES----------QLFEETVLKDvafgpqnfGVSQEEAEALAREKLALVGISE--SLFEKNPFELSGGQMRRVAIAGI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447119240 168 IACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAIF 242
Cdd:PRK13649 160 LAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-255 |
3.57e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 82.37 E-value: 3.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLVFNGQDLQRISEKEr 83
Cdd:PRK11231 3 LRTENLTVGYGTK----RILNDLSLSLPTGKITALIGPNGCGKS-TLLKCFARLLTP---QSGTVFLGDKPISMLSSRQ- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 84 rnlVGAEVAMIFQDPMTSlnpcytvgfqimEAIKVHQ------------GGNKSTRRQRAIDL-LNQVGIPDPASRLdvy 150
Cdd:PRK11231 74 ---LARRLALLPQHHLTP------------EGITVRElvaygrspwlslWGRLSAEDNARVNQaMEQTRINHLADRR--- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 151 PHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAG 230
Cdd:PRK11231 136 LTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNT-QGKTVVTVLHDLNQASRYCDHLVVLANG 214
|
250 260
....*....|....*....|....*
gi 447119240 231 QVVETGdahaifhAPRHPYTQALLR 255
Cdd:PRK11231 215 HVMAQG-------TPEEVMTPGLLR 232
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-232 |
4.40e-18 |
|
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: 80.34 E-value: 4.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDESAPfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLVFNGQDLQRISEKER 83
Cdd:cd03246 1 LEVENVSFRYPGAEPP--VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLL----RPTSGRVRLDGADISQWDPNEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 84 RNLVG--AEVAMIFQDpmtslnpcytvgfQIMEAIkvhqggnkstrrqraidllnqvgipdpasrldvyphqLSGGMSQR 161
Cdd:cd03246 75 GDHVGylPQDDELFSG-------------SIAENI-------------------------------------LSGGQRQR 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447119240 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAeAAHKIIVMYAGQV 232
Cdd:cd03246 105 LGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
9-245 |
5.68e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 83.46 E-value: 5.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 9 LSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDY-PGRVMaeklvFNGQDLQRISeKERRNlv 87
Cdd:PRK09452 20 ISKSFDGKEV----ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPdSGRIM-----LDGQDITHVP-AENRH-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 88 gaeVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGGNKSTRRqRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMA 167
Cdd:PRK09452 88 ---VNTVFQS--YALFPHMTVFENVAFGLRMQKTPAAEITP-RVMEALRMVQLEEFAQR---KPHQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 168 IACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLalvAEA---AHKIIVMYAGQVVETGDAHAIFHA 244
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQ---EEAltmSDRIVVMRDGRIEQDGTPREIYEE 235
|
.
gi 447119240 245 P 245
Cdd:PRK09452 236 P 236
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-242 |
5.73e-18 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 81.67 E-value: 5.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 1 MALLNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSvsSLaiMGLI---DYPG-----RVMAEKlvFNG 72
Cdd:COG1119 1 DPLLELRNVTVRRGGK----TILDDISWTVKPGEHWAILGPNGAGKS--TL--LSLItgdLPPTygndvRLFGER--RGG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 73 QDLQRIsekeRRN--LVGAEVAMIFQDPMTSLNpcyTV--GF----QIMEAIKVHQggnkstrRQRAIDLLNQVGIpdpA 144
Cdd:COG1119 71 EDVWEL----RKRigLVSPALQLRFPRDETVLD---VVlsGFfdsiGLYREPTDEQ-------RERARELLELLGL---A 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 145 SRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKI 224
Cdd:COG1119 134 HLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHV 213
|
250
....*....|....*...
gi 447119240 225 IVMYAGQVVETGDAHAIF 242
Cdd:COG1119 214 LLLKDGRVVAAGPKEEVL 231
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
22-236 |
6.02e-18 |
|
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: 81.10 E-value: 6.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyP--GRVMaeklvFNGQDLQRISEKE-RRNL--VGAEVAMIF- 95
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYK-PtsGSVL-----LDGTDIRQLDPADlRRNIgyVPQDVTLFYg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 96 --QDPMTSLNPcYTVGFQIMEAIKVhQGGNKSTRRQ-RAIDLlnQVGipdpaSRLDvyphQLSGGMSQRVMIAMAIACRP 172
Cdd:cd03245 93 tlRDNITLGAP-LADDERILRAAEL-AGVTDFVNKHpNGLDL--QIG-----ERGR----GLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447119240 173 KLLIADEPTTALDVTIQAQIIELLLELqqKENMALVLITHDLALVaEAAHKIIVMYAGQVVETG 236
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQL--LGDKTLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
23-238 |
7.89e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 80.26 E-value: 7.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYpgRVMAEKLVFNGQDLQRISEKERrnlVGAEVAMIFQDPMTsl 102
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKY--EVTEGEILFKGEDITDLPPEER---ARLGIFLAFQYPPE-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 103 npcytvgfqiMEAIKVhqggnkstrrqraIDLLNQVGIpdpasrldvyphQLSGGMSQRVMIAMAIACRPKLLIADEPTT 182
Cdd:cd03217 89 ----------IPGVKN-------------ADFLRYVNE------------GFSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447119240 183 ALDVT---IQAQIIELLLElqqkENMALVLITH--DLA--LVAEAAHkiiVMYAGQVVETGDA 238
Cdd:cd03217 134 GLDIDalrLVAEVINKLRE----EGKSVLIITHyqRLLdyIKPDRVH---VLYDGRIVKSGDK 189
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
26-246 |
8.43e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 83.16 E-value: 8.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLVFNGQDLQRISEKERrnlvgaEVAMIFQDpmTSLNPC 105
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLED----ITSGDLFIGEKRMNDVPPAER------GVGMVFQS--YALYPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 106 YTVGFQIMEAIKVhQGGNKSTRRQRaidlLNQVG-IPDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTAL 184
Cdd:PRK11000 90 LSVAENMSFGLKL-AGAKKEEINQR----VNQVAeVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447119240 185 DVTIQAQI-IElLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAIFHAPR 246
Cdd:PRK11000 165 DAALRVQMrIE-ISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-237 |
8.65e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 82.44 E-value: 8.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 21 RAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIM-GLIdYP--GRVMaeklvFNGQDlqrISEKERRNLvgAEVAMIFqd 97
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKS-TTIKMLtGIL-VPtsGEVR-----VLGYV---PFKRRKEFA--RRIGVVF-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 98 pmtslnpcytvgfqimeaikvhqgGNKStrrQRAIDL-------LNQV--GIPDPA--SRLDVY------------P-HQ 153
Cdd:COG4586 102 ------------------------GQRS---QLWWDLpaidsfrLLKAiyRIPDAEykKRLDELvelldlgelldtPvRQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 154 LSGGmsQRvM---IAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAG 230
Cdd:COG4586 155 LSLG--QR-MrceLAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHG 231
|
....*..
gi 447119240 231 QVVETGD 237
Cdd:COG4586 232 RIIYDGS 238
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-233 |
1.04e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.53 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHfgdesapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLiDYP--GRVmaeklVFNGQDLQRISE 80
Cdd:COG1129 256 VLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGA-DPAdsGEI-----RLDGKPVRIRSP 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 81 KERrnlVGAEVAMIFQDPMTS-LNPCYTVGFQIMEAI--KVHQGGNKSTRRQRAI--DLLNQVGI--PDPASRLDvyphQ 153
Cdd:COG1129 322 RDA---IRAGIAYVPEDRKGEgLVLDLSIRENITLASldRLSRGGLLDRRRERALaeEYIKRLRIktPSPEQPVG----N 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
Cdd:COG1129 395 LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIREL-AAEGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
11-236 |
2.58e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 82.85 E-value: 2.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 11 VHFGDESAPFRAVDR-ISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLVFNGQDLQRISEKERRNlvga 89
Cdd:TIGR00958 484 VSFSYPNRPDVPVLKgLTFTLHPGEVVALVGPSGSGKS----TVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHR---- 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 90 EVAMIFQDPM-----TSLNPCYTVGF----QIMEAIKVHQGGNKSTRRQRAIDLlnqvgipdpasrlDVYPH--QLSGGM 158
Cdd:TIGR00958 556 QVALVGQEPVlfsgsVRENIAYGLTDtpdeEIMAAAKAANAHDFIMEFPNGYDT-------------EVGEKgsQLSGGQ 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447119240 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAqiieLLLELQQKENMALVLITHDLALVaEAAHKIIVMYAGQVVETG 236
Cdd:TIGR00958 623 KQRIAIARALVRKPRVLILDEATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTV-ERADQILVLKKGSVVEMG 695
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
23-232 |
1.47e-16 |
|
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: 80.25 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidYPGRVMAEKLVfngqDLQRISEKERRNLVGAEVAMIFQD-PMTS 101
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGA--YPGKFEGNVFI----NGKPVDIRNPAQAIRAGIAMVPEDrKRHG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 102 LNPCYTVGFQIMEAIKvhqggNKSTRRQRAIDLLNQVGIPDPASRLDV---YPH----QLSGGMSQRVMIAMAIACRPKL 174
Cdd:TIGR02633 350 IVPILGVGKNITLSVL-----KSFCFKMRIDAAAELQIIGSAIQRLKVktaSPFlpigRLSGGNQQKAVLAKMLLTNPRV 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 447119240 175 LIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQV 232
Cdd:TIGR02633 425 LILDEPTRGVDVGAKYEIYKLINQLAQ-EGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-232 |
1.72e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 77.80 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDesapfRAV-DRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPGrvmAEKLVFNGQDLQRISEKE 82
Cdd:PRK11247 13 LLLNAVSKRYGE-----RTVlNQLDLHIPAGQFVAVVGRSGCGKS-TLLRLLAGLETPS---AGELLAGTAPLAEAREDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 83 RrnlvgaevaMIFQDpmTSLNPCYTVgfqimeaIKVHQGGNKSTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRV 162
Cdd:PRK11247 84 R---------LMFQD--ARLLPWKKV-------IDNVGLGLKGQWRDAALQALAAVGL---ADRANEWPAALSGGQKQRV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447119240 163 MIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDlalVAEA---AHKIIVMYAGQV 232
Cdd:PRK11247 143 ALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHD---VSEAvamADRVLLIEEGKI 212
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-251 |
2.17e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 77.77 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAE-KLVFNGQDLQrisekE 82
Cdd:PRK14258 8 IKVNNLSFYYDTQ----KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEgRVEFFNQNIY-----E 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 83 RR---NLVGAEVAMIFQDPmtSLNPcYTVGFQIMEAIKVhqggnKSTRRQRAIDLLNQVGIPDpASRLDVYPHQ------ 153
Cdd:PRK14258 79 RRvnlNRLRRQVSMVHPKP--NLFP-MSVYDNVAYGVKI-----VGWRPKLEIDDIVESALKD-ADLWDEIKHKihksal 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 154 -LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYA--- 229
Cdd:PRK14258 150 dLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnen 229
|
250 260
....*....|....*....|....
gi 447119240 230 --GQVVETGDAHAIFHAPRHPYTQ 251
Cdd:PRK14258 230 riGQLVEFGLTKKIFNSPHDSRTR 253
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
21-236 |
2.30e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 79.62 E-value: 2.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 21 RAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMaeklvFNGQDLQRISEKE-RRNLvgaevAMIFQD 97
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKS-TLINLLQRVFDPqsGRIL-----IDGTDIRTVTRASlRRNI-----AVVFQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 98 PMTsLNPcytvgfQIMEAIKVHQGG------NKSTRRQRAIDLLnqvgipdpASRLDVYP-------HQLSGGMSQRVMI 164
Cdd:PRK13657 418 AGL-FNR------SIEDNIRVGRPDatdeemRAAAERAQAHDFI--------ERKPDGYDtvvgergRQLSGGERQRLAI 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447119240 165 AMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkeNMALVLITHDLALVAEAAhKIIVMYAGQVVETG 236
Cdd:PRK13657 483 ARALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRNAD-RILVFDNGRVVESG 551
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-252 |
3.39e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 77.13 E-value: 3.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDY-PGRVMAEKLVFNGQDL--QRIS 79
Cdd:PRK14243 10 VLRTENLNVYYGS----FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLiPGFRVEGKVTFHGKNLyaPDVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 80 EKERRNLVGaevaMIFQDPmtslNPC-YTVGFQIMEAIKV--HQGGN----KSTRRQRAI-----DLLNQVGIpdpasrl 147
Cdd:PRK14243 86 PVEVRRRIG----MVFQKP----NPFpKSIYDNIAYGARIngYKGDMdelvERSLRQAALwdevkDKLKQSGL------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 148 dvyphQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALVLITHDLALVAEAAHKIIVM 227
Cdd:PRK14243 151 -----SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL--KEQYTIIIVTHNMQQAARVSDMTAFF 223
|
250 260 270
....*....|....*....|....*....|....
gi 447119240 228 YA---------GQVVETGDAHAIFHAPRHPYTQA 252
Cdd:PRK14243 224 NVeltegggryGYLVEFDRTEKIFNSPQQQATRD 257
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
21-236 |
1.01e-15 |
|
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: 75.06 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdYP--GRVmaeklvfngQDLQRISEKERRNLVgAEVAMIF-QD 97
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLL-QPtsGEV---------RVAGLVPWKRRKKFL-RRIGVVFgQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 98 PMTSLNPCYTVGFQIMEAIKVHQGGNKSTRRQRAIDLLnqvgipDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIA 177
Cdd:cd03267 104 TQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELL------DLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447119240 178 DEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:cd03267 178 DEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
17-243 |
1.46e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 75.54 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 17 SAPF--RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMAEKLVFNGQDLQRISEKERRnlvgaEVAM 93
Cdd:PRK13643 14 NSPFasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQpTEGKVTVGDIVVSSTSKQKEIKPVRK-----KVGV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 94 IFQDPMTSLnpcytvgFQ--IMEAIKV---HQGGNKSTRRQRAIDLLNQVGIPDpaSRLDVYPHQLSGGMSQRVMIAMAI 168
Cdd:PRK13643 89 VFQFPESQL-------FEetVLKDVAFgpqNFGIPKEKAEKIAAEKLEMVGLAD--EFWEKSPFELSGGQMRRVAIAGIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447119240 169 ACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAIFH 243
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-236 |
1.64e-15 |
|
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: 74.07 E-value: 1.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 6 VDKLSVHFGDESAPfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLVFNGQDLQRIS-EKERR 84
Cdd:cd03244 5 FKNVSLRYRPNLPP--VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVE----LSSGSILIDGVDISKIGlHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 85 NLvgaevAMIFQDPMT-------SLNPC--YTVGfQIMEAIKvhQGGNKSTrrqraidLLNQVGIPDpaSRLDVYPHQLS 155
Cdd:cd03244 79 RI-----SIIPQDPVLfsgtirsNLDPFgeYSDE-ELWQALE--RVGLKEF-------VESLPGGLD--TVVEEGGENLS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLlelqqKENMA---LVLITHDLALVAEaAHKIIVMYAGQV 232
Cdd:cd03244 142 VGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTI-----REAFKdctVLTIAHRLDTIID-SDRILVLDKGRV 215
|
....
gi 447119240 233 VETG 236
Cdd:cd03244 216 VEFD 219
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-238 |
1.74e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 74.58 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVmaeklVFNGQDLQRISEKE---RRNLVGAEVAMIFQDPMtsl 102
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSI-----QFAGQPLEAWSAAElarHRAYLSQQQTPPFAMPV--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 103 npcytvgFQiMEAIKVHQGGNKSTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAI-----ACRP--KLL 175
Cdd:PRK03695 87 -------FQ-YLTLHQPDKTRTEAVASALNEVAEALGLDDKLGR---SVNQLSGGEWQRVRLAAVVlqvwpDINPagQLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447119240 176 IADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVETGDA 238
Cdd:PRK03695 156 LLDEPMNSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRR 217
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-245 |
2.07e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 76.81 E-value: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 26 ISYSVKQGEVVGIVGESGSGKSvsSL--AIMGLIDYPGrvmaeKLVFNGQDLQRISEKE-RRNL--VGaevamifQDPMT 100
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKT--SLlnALLGFLPYQG-----SLKINGIELRELDPESwRKHLswVG-------QNPQL 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 101 slnPCYTvgfqIMEAIKVhqgGNKSTRRQRAIDLLNQVGIPDPASRLDV---YPHQ-----LSGGMSQRVMIAMAIACRP 172
Cdd:PRK11174 435 ---PHGT----LRDNVLL---GNPDASDEQLQQALENAWVSEFLPLLPQgldTPIGdqaagLSVGQAQRLALARALLQPC 504
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447119240 173 KLLIADEPTTALDVTIQAQIIELLLELQQKEnmALVLITHDLALVAEaAHKIIVMYAGQVVETGDAHAIFHAP 245
Cdd:PRK11174 505 QLLLLDEPTASLDAHSEQLVMQALNAASRRQ--TTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
11-267 |
2.85e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 76.40 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 11 VHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLVFNGQDLQRISEKERRNLvgae 90
Cdd:PRK11160 344 VSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKS----TLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQA---- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 91 vamifqdpMTSLNpcytvgfQimeaiKVH----------QGGNKSTRRQRAIDLLNQVGIP---DPASRLDVY----PHQ 153
Cdd:PRK11160 416 --------ISVVS-------Q-----RVHlfsatlrdnlLLAAPNASDEALIEVLQQVGLEkllEDDKGLNAWlgegGRQ 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkeNMALVLITHDLALVaEAAHKIIVMYAGQVV 233
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGL-EQFDRICVMDNGQII 552
|
250 260 270
....*....|....*....|....*....|....
gi 447119240 234 ETGDaHaifhaprhpytQALLRALPEFAQDKERL 267
Cdd:PRK11160 553 EQGT-H-----------QELLAQQGRYYQLKQRL 574
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-240 |
3.47e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 74.28 E-value: 3.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHFGDESApFRAVDrisYSVKQGEVVGIVGESGSGKSVSSLAIMGLI--DYPGRVMAEKLVFNGQDLQRISE 80
Cdd:PRK09984 4 IIRVEKLAKTFNQHQA-LHAVD---LNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGSHIELLGRTVQREGRLAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 81 KERRNLvgAEVAMIFQDpMTSLNPcytvgFQIMEAIKVHQGGN-----------KSTRRQRAIDLLNQVGIPDpasrldv 149
Cdd:PRK09984 80 DIRKSR--ANTGYIFQQ-FNLVNR-----LSVLENVLIGALGStpfwrtcfswfTREQKQRALQALTRVGMVH------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 150 YPHQ----LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKII 225
Cdd:PRK09984 145 FAHQrvstLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIV 224
|
250
....*....|....*
gi 447119240 226 VMYAGQVVETGDAHA 240
Cdd:PRK09984 225 ALRQGHVFYDGSSQQ 239
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-236 |
3.56e-15 |
|
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: 72.35 E-value: 3.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDESAPfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLVFNGQDLQrISEKER 83
Cdd:cd03247 1 LSINNVSFSYPEQEQQ--VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLK----PQQGEITLDGVPVS-DLEKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 84 RNLVGaevaMIFQDPMTslnpcytvgFqimeaikvhqggnkstrrqrAIDLLNQVGIpdpasrldvyphQLSGGMSQRVM 163
Cdd:cd03247 74 SSLIS----VLNQRPYL---------F--------------------DTTLRNNLGR------------RFSGGERQRLA 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447119240 164 IAMAIACRPKLLIADEPTTALDVTIQAQIIELLLElqQKENMALVLITHDLALVaEAAHKIIVMYAGQVVETG 236
Cdd:cd03247 109 LARILLQDAPIVLLDEPTVGLDPITERQLLSLIFE--VLKDKTLIWITHHLTGI-EHMDKILFLENGKIIMQG 178
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
13-245 |
4.10e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.05 E-value: 4.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 13 FGDESAPFRAVDR-----ISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPGrvmAEKLVFNGQDLQRISEKerrnLV 87
Cdd:PRK10575 12 FALRNVSFRVPGRtllhpLSLTFPAGKVTGLIGHNGSGKS-TLLKMLGRHQPPS---EGEILLDAQPLESWSSK----AF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 88 GAEVAMIFQD-PMTSlnpcytvGFQIMEAIKVHQ-------GGNKSTRRQRAIDLLNQVGIPDPASRLdvyPHQLSGGMS 159
Cdd:PRK10575 84 ARKVAYLPQQlPAAE-------GMTVRELVAIGRypwhgalGRFGAADREKVEEAISLVGLKPLAHRL---VDSLSGGER 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 160 QRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAH 239
Cdd:PRK10575 154 QRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPA 233
|
....*.
gi 447119240 240 AIFHAP 245
Cdd:PRK10575 234 ELMRGE 239
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-254 |
4.38e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 73.87 E-value: 4.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 2 ALLNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVsslaimgLIDYPGRVM--AEKLVF-NGQDLQRI 78
Cdd:PRK10253 6 ARLRGEQLTLGYGKYTV----AENLTVEIPDGHFTAIIGPNGCGKST-------LLRTLSRLMtpAHGHVWlDGEHIQHY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 79 SEKErrnlVGAEVAMIFQDPMTSLNpcYTVGFQIMEAIKVHQGGNKSTRRQRAIDL---LNQVGIPDPASR-LDVyphqL 154
Cdd:PRK10253 75 ASKE----VARRIGLLAQNATTPGD--ITVQELVARGRYPHQPLFTRWRKEDEEAVtkaMQATGITHLADQsVDT----L 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVE 234
Cdd:PRK10253 145 SGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVA 224
|
250 260
....*....|....*....|
gi 447119240 235 TGdahaifhAPRHPYTQALL 254
Cdd:PRK10253 225 QG-------APKEIVTAELI 237
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
26-236 |
5.00e-15 |
|
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: 73.07 E-value: 5.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEkLVFNGQDLqrisekeRRNLVGAEVAMIFQDpmTSLNPC 105
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQ-ILFNGQPR-------KPDQFQKCVAYVRQD--DILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 106 YTVG----FQIMEAIKVHQggNKSTRRQRAID-LLNQVGIPDPAsrlDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
Cdd:cd03234 96 LTVRetltYTAILRLPRKS--SDAIRKKRVEDvLLRDLALTRIG---GNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447119240 181 TTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
26-241 |
5.51e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.47 E-value: 5.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLVFNGQDLQRISEKER--RNLV----GAEVAMIFQDPM 99
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGL----RPARGGRIMLNGKEINALSTAQRlaRGLVylpeDRQSSGLYLDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 100 TSLNPCytvgfqimeAIKVHQGGN-KSTRRQRAI--DLLNQVGI----PDPASRldvyphQLSGGMSQRVMIAMAIACRP 172
Cdd:PRK15439 358 LAWNVC---------ALTHNRRGFwIKPARENAVleRYRRALNIkfnhAEQAAR------TLSGGNQQKVLIAKCLEASP 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447119240 173 KLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAI 241
Cdd:PRK15439 423 QLLIVDEPTRGVDVSARNDIYQLIRSI-AAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAI 490
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
35-242 |
7.27e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.50 E-value: 7.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 35 VVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLVFNGQDLqrisEKERRNLVG--AEVAMIFQDPMTSLnpCYT-VGFQ 111
Cdd:PRK13638 29 VTGLVGANGCGKSTLFMNLSGLL----RPQKGAVLWQGKPL----DYSKRGLLAlrQQVATVFQDPEQQI--FYTdIDSD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 112 IMEAIKvHQGGNKSTRRQRAIDLLNQVGipdpASRLDVYPHQ-LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQA 190
Cdd:PRK13638 99 IAFSLR-NLGVPEAEITRRVDEALTLVD----AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447119240 191 QIIELLLELQQKENMaLVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAIF 242
Cdd:PRK13638 174 QMIAIIRRIVAQGNH-VIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
27-244 |
1.40e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.61 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 27 SYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLVFNGQDLQRiseKERRNLVgaevAMIFQDPMTSLNPCY 106
Cdd:PRK15056 27 SFTVPGGSIAALVGVNGSGKSTLFKALMGFV----RLASGKISILGQPTRQ---ALQKNLV----AYVPQSEEVDWSFPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 107 TVGFQIMEAIKVHQG---GNKSTRRQRAIDLLNQVGIPDpasrldvYPH----QLSGGMSQRVMIAMAIACRPKLLIADE 179
Cdd:PRK15056 96 LVEDVVMMGRYGHMGwlrRAKKRDRQIVTAALARVDMVE-------FRHrqigELSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447119240 180 PTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAhKIIVMYAGQVVETGDAHAIFHA 244
Cdd:PRK15056 169 PFTGVDVKTEARIISLLRELRD-EGKTMLVSTHNLGSVTEFC-DYTVMVKGTVLASGPTETTFTA 231
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
11-214 |
1.51e-14 |
|
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: 73.93 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 11 VHFGDESAPfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYP-GRVmaeklVFNGQDLQRISEKERRNLVG- 88
Cdd:TIGR02868 340 LSAGYPGAP-PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLqGEV-----TLDGVPVSSLDQDEVRRRVSv 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 89 -AEVAMIFQdpmTSlnpcytvgfqIMEAIKVhqgGNKSTRRQRAIDLLNQVGIPDPASRL------DVYPH--QLSGGMS 159
Cdd:TIGR02868 414 cAQDAHLFD---TT----------VRENLRL---ARPDATDEELWAALERVGLADWLRALpdgldtVLGEGgaRLSGGER 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447119240 160 QRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLleLQQKENMALVLITHDL 214
Cdd:TIGR02868 478 QRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-232 |
3.60e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 73.04 E-value: 3.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidYPGRVMAEKLVfNGQdlqRISEKERRNLVGAEVAMIFQD-PM 99
Cdd:PRK13549 276 KRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGA--YPGRWEGEIFI-DGK---PVKIRNPQQAIAQGIAMVPEDrKR 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 100 TSLNPCYTVGFQIMEAIKvhqggNKSTRRQRAIDLLNQVGIPDPASRLDV---YPHQ----LSGGMSQRVMIAMAIACRP 172
Cdd:PRK13549 350 DGIVPVMGVGKNITLAAL-----DRFTGGSRIDDAAELKTILESIQRLKVktaSPELaiarLSGGNQQKAVLAKCLLLNP 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 173 KLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQV 232
Cdd:PRK13549 425 KILILDEPTRGIDVGAKYEIYKLINQLVQ-QGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
133-227 |
4.66e-14 |
|
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: 68.24 E-value: 4.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 133 DLLNQVGIPDPASRLDV-YPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkenmALVLIT 211
Cdd:cd03221 49 ELEPDEGIVTWGSTVKIgYFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG----TVILVS 124
|
90
....*....|....*.
gi 447119240 212 HDLALVAEAAHKIIVM 227
Cdd:cd03221 125 HDRYFLDQVATKIIEL 140
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
16-236 |
9.28e-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: 9.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 16 ESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVmaeklvfngqdlqrisekERRNLVGAEVAM 93
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKS-TLLRLLAGIYPPdsGTV------------------TVRGRVSSLLGL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 94 ifqdpMTSLNPCYTVgfqiMEAIKVH---QGGNKSTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMSQRVMIAMAIAC 170
Cdd:cd03220 92 -----GGGFNPELTG----RENIYLNgrlLGLSRKEIDEKIDEIIEFSELGD---FIDLPVKTYSSGMKARLAFAIATAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447119240 171 RPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:cd03220 160 EPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
128-225 |
9.71e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 68.80 E-value: 9.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 128 RQRAIDLLNQVGIPDPASR-LDvyphQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMA 206
Cdd:NF040873 97 RAAVDDALERVGLADLAGRqLG----ELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEE-HARGAT 171
|
90
....*....|....*....
gi 447119240 207 LVLITHDLALVAEAAHKII 225
Cdd:NF040873 172 VVVVTHDLELVRRADPCVL 190
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
3-246 |
1.81e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 69.25 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidYpgRVMAEKLVFNGQDLQRISEKE 82
Cdd:PRK11300 5 LLSVSGLMMRFGG----LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGF--Y--KPTGGTILLRGQHIEGLPGHQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 83 --RRNLVgaevaMIFQDpmTSLNPCYTVGFQIMEAIKVHQGGN--------KSTRR------QRAIDLLNQVGIPDPASR 146
Cdd:PRK11300 77 iaRMGVV-----RTFQH--VRLFREMTVIENLLVAQHQQLKTGlfsgllktPAFRRaesealDRAATWLERVGLLEHANR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 147 ldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIV 226
Cdd:PRK11300 150 ---QAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYV 226
|
250 260
....*....|....*....|
gi 447119240 227 MYAGQVVETGDAHAIFHAPR 246
Cdd:PRK11300 227 VNQGTPLANGTPEEIRNNPD 246
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-217 |
1.93e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.99 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgrvmaeklvfngQDLQRISEKE 82
Cdd:PRK09544 4 LVSLENVSVSFGQR----RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLV---------------APDEGVIKRN 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 83 RRNLVGAEVAMIFQDPmtslnpcyTVGFQIMEAIKVHQGgnksTRRQRAIDLLNQVgipdPASRLDVYPHQ-LSGGMSQR 161
Cdd:PRK09544 65 GKLRIGYVPQKLYLDT--------TLPLTVNRFLRLRPG----TKKEDILPALKRV----QAGHLIDAPMQkLSGGETQR 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447119240 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALV 217
Cdd:PRK09544 129 VLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLV 184
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
4-242 |
2.03e-13 |
|
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: 70.55 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDESAPfrAVDRISYSVKQGEVVGIVGESGSGKSvsSLA--IMGLIdypgRVMAEKLVFNGQDLQRISEK 81
Cdd:COG4618 331 LSVENLTVVPPGSKRP--ILRGVSFSLEPGEVLGVIGPSGSGKS--TLArlLVGVW----PPTAGSVRLDGADLSQWDRE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 82 ERRNLVG-------------AE-VAMiFQDPMTSlnpcytvgfQIMEAIK---VHQggnkstrrqrAIDLLNQvGIpdpA 144
Cdd:COG4618 403 ELGRHIGylpqdvelfdgtiAEnIAR-FGDADPE---------KVVAAAKlagVHE----------MILRLPD-GY---D 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 145 SRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAeAAHKI 224
Cdd:COG4618 459 TRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKA-RGATVVVITHRPSLLA-AVDKL 536
|
250
....*....|....*...
gi 447119240 225 IVMYAGQVVETGDAHAIF 242
Cdd:COG4618 537 LVLRDGRVQAFGPRDEVL 554
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
23-248 |
2.15e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 70.61 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 23 VDRISYSVKQGEVVGIVGESGSGKSvsSL--AIMGL-------IDYPGrvmaeklvfngqdlqrisekerrnlvGAEVAM 93
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKS--TLlrAIAGLwpygsgrIARPA--------------------------GARVLF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 94 IFQDP---MTSLnpcytvgfqiMEAIkVHQGGNKSTRRQRAIDLLNQVGIPDPASRLDV---YPHQLSGGMSQRVMIAMA 167
Cdd:COG4178 431 LPQRPylpLGTL----------REAL-LYPATAEAFSDAELREALEAVGLGHLAERLDEeadWDQVLSLGEQQRLAFARL 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 168 IACRPKLLIADEPTTALDVTIQAQIIELLLElqQKENMALVLITHDLALVAeaahkiivmYAGQVVE-TGDAHAIFHAPR 246
Cdd:COG4178 500 LLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGHRSTLAA---------FHDRVLElTGDGSWQLLPAE 568
|
..
gi 447119240 247 HP 248
Cdd:COG4178 569 AP 570
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
26-232 |
3.99e-13 |
|
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: 67.50 E-value: 3.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidYP---GRVMAeklvfngqDLQRISEKERRNLvGAEVAMIFQDPMT-- 100
Cdd:cd03248 33 VSFTLHPGEVTALVGPSGSGKSTVVALLENF--YQpqgGQVLL--------DGKPISQYEHKYL-HSKVSLVGQEPVLfa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 101 -SLNPCYTVGFQ------IMEA-IKVHQGGNkstrrqraIDLLNQvgipDPASRLDVYPHQLSGGMSQRVMIAMAIACRP 172
Cdd:cd03248 102 rSLQDNIAYGLQscsfecVKEAaQKAHAHSF--------ISELAS----GYDTEVGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 173 KLLIADEPTTALDVTIQAQIIELLleLQQKENMALVLITHDLALVaEAAHKIIVMYAGQV 232
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQAL--YDWPERRTVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-242 |
4.20e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 68.00 E-value: 4.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 1 MALLNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPgrvmAEKLVFNGQDLQRISE 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGR----RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRD----AGNIIIDDEDISLLPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 81 KER-RNLVG--AEVAMIFQDpmtslnpcYTVGFQIMEAIKVHQGGNKSTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGG 157
Cdd:PRK10895 73 HARaRRGIGylPQEASIFRR--------LSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHI---EHLRDSMGQSLSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 158 MSQRVMIAMAIACRPKLLIADEPTTALDvTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGD 237
Cdd:PRK10895 142 ERRRVEIARALAANPKFILLDEPFAGVD-PISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
....*
gi 447119240 238 AHAIF 242
Cdd:PRK10895 221 PTEIL 225
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-249 |
4.65e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.60 E-value: 4.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 1 MALLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLVFNGQDlqrISE 80
Cdd:PRK11614 3 KVMLSFDKVSAHYGK----IQALHEVSLHINQGEIVTLIGANGAGKT----TLLGTLCGDPRATSGRIVFDGKD---ITD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 81 KERRNLVGAEVAMIFQdpmtslnpcytvGFQIMEAIKVHQ----GGNKSTRRQ------RAIDLLnqvgiPDPASRLDVY 150
Cdd:PRK11614 72 WQTAKIMREAVAIVPE------------GRRVFSRMTVEEnlamGGFFAERDQfqerikWVYELF-----PRLHERRIQR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 151 PHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAG 230
Cdd:PRK11614 135 AGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLRE-QGMTIFLVEQNANQALKLADRGYVLENG 213
|
250 260
....*....|....*....|.
gi 447119240 231 QVV--ETGDAHAIFHAPRHPY 249
Cdd:PRK11614 214 HVVleDTGDALLANEAVRSAY 234
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-213 |
6.05e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 67.05 E-value: 6.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 2 ALLNVDKlsVHFGDESAPFraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGRvmaEKLVFNGQDLQRISEK 81
Cdd:PRK10247 6 PLLQLQN--VGYLAGDAKI--LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLIS-PTS---GTLLFEGEDISTLKPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 82 ERRNlvgaEVAMIFQDPMTSLNPCYTvgfqimEAIKVHQGGNKSTRRQRAIDLLNQVGIPDpaSRLDVYPHQLSGGMSQR 161
Cdd:PRK10247 78 IYRQ----QVSYCAQTPTLFGDTVYD------NLIFPWQIRNQQPDPAIFLDDLERFALPD--TILTKNIAELSGGEKQR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447119240 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHD 213
Cdd:PRK10247 146 ISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
35-245 |
6.12e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 68.75 E-value: 6.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 35 VVGIVGESGSGKSvsSL--AIMGLIDyP--GRVmaeklVFNGQDLQRISEK-----ERRNlvgaeVAMIFQDpmTSLNPC 105
Cdd:PRK11144 26 ITAIFGRSGAGKT--SLinAISGLTR-PqkGRI-----VLNGRVLFDAEKGiclppEKRR-----IGYVFQD--ARLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 106 YTVgfqimeaikvhQG----GNKSTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPT 181
Cdd:PRK11144 91 YKV-----------RGnlryGMAKSMVAQFDKIVALLGI---EPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447119240 182 TALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAIFHAP 245
Cdd:PRK11144 157 ASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
24-241 |
6.50e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 67.87 E-value: 6.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 24 DRISYSVKQGEVVGIVGESGSGKSvSSLAIMGlidypGRVMAEK--LVFNGQDLQRISekeRRNLVGA--EVAMIFQDP- 98
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKT-TLLRLIG-----GQIAPDHgeILFDGENIPAMS---RSRLYTVrkRMSMLFQSGa 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 99 -MTSLNPCYTVGFQIMEAIKVHQGGNKSTRRQRaidlLNQVGIPDPAsrlDVYPHQLSGGMSQRVMIAMAIACRPKLLIA 177
Cdd:PRK11831 95 lFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMK----LEAVGLRGAA---KLMPSELSGGMARRAALARAIALEPDLIMF 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447119240 178 DEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAI 241
Cdd:PRK11831 168 DEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
9-233 |
6.92e-13 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 66.42 E-value: 6.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 9 LSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvsSL--AIMGLIDYPGrvMAEKLVFNGQDLqrisekeRRNL 86
Cdd:cd03213 11 VTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKS--TLlnALAGRRTGLG--VSGEVLINGRPL-------DKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 87 VGAEVAMIFQDPMtsLNPCYTVgfqiMEAIKVhqggnkstrrqraidllnqvgipdpASRLdvypHQLSGGMSQRVMIAM 166
Cdd:cd03213 80 FRKIIGYVPQDDI--LHPTLTV----RETLMF-------------------------AAKL----RGLSGGERKRVSIAL 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447119240 167 AIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDL-ALVAEAAHKIIVMYAGQVV 233
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAD-TGRTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
22-251 |
7.93e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 68.89 E-value: 7.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 22 AVDRISYSVKQGEVVGIVGESGSGKSVsslaIMGLIDYPGRVMAEKLVFNGQDLQRISEKERRN---LVGAEVAMiFQDp 98
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKST----IANLLTRFYDIDEGEILLDGHDLRDYTLASLRNqvaLVSQNVHL-FND- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 99 mtslnpcyTVGFQIMEAIKvhqggNKSTRRQ--------RAIDLLNQVgipdpASRLDVYPHQ----LSGGMSQRVMIAM 166
Cdd:PRK11176 432 --------TIANNIAYART-----EQYSREQieeaarmaYAMDFINKM-----DNGLDTVIGEngvlLSGGQRQRIAIAR 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 167 AIACRPKLLIADEPTTALDV----TIQAQIIELllelqQKENMALVlITHDLALVaEAAHKIIVMYAGQVVETGdAHAIF 242
Cdd:PRK11176 494 ALLRDSPILILDEATSALDTeserAIQAALDEL-----QKNRTSLV-IAHRLSTI-EKADEILVVEDGEIVERG-THAEL 565
|
....*....
gi 447119240 243 HAPRHPYTQ 251
Cdd:PRK11176 566 LAQNGVYAQ 574
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
11-240 |
9.92e-13 |
|
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: 68.69 E-value: 9.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 11 VHFGDESapfravDR-----ISYSVKQGEVVGIVGESGSGKS-----------VSSLAImgLIDypgrvmaeklvfnGQD 74
Cdd:COG5265 363 VSFGYDP------ERpilkgVSFEVPAGKTVAIVGPSGAGKStlarllfrfydVTSGRI--LID-------------GQD 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 75 LQRISEKERRNLVGaevaMIFQDpmTSL-NPcyTVGFQI--------MEAIkvhqggnkstrrQRAIDLLNqvgIPDPAS 145
Cdd:COG5265 422 IRDVTQASLRAAIG----IVPQD--TVLfND--TIAYNIaygrpdasEEEV------------EAAARAAQ---IHDFIE 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 146 RL-DVYPHQ-------LSGGMSQRVMIAMAIACRPKLLIADEPTTALDV----TIQAQIIELllelqQKENMALVlITHD 213
Cdd:COG5265 479 SLpDGYDTRvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSrterAIQAALREV-----ARGRTTLV-IAHR 552
|
250 260
....*....|....*....|....*..
gi 447119240 214 LALVAEaAHKIIVMYAGQVVETGdAHA 240
Cdd:COG5265 553 LSTIVD-ADEILVLEAGRIVERG-THA 577
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
20-212 |
1.89e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 65.75 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 20 FRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGlidypgrvmaeklvfngqdlqrisekERRNLVGAEVAMIFQDPM 99
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG--------------------------ALKGTPVAGCVDVPDNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 100 TSLNPcytvgfqIMEAIkvHQGGNKSTrrqrAIDLLNQVGIPDPASRLDVYPHqLSGGMSQRVMIAMAIACRPKLLIADE 179
Cdd:COG2401 97 GREAS-------LIDAI--GRKGDFKD----AVELLNAVGLSDAVLWLRRFKE-LSTGQKFRFRLALLLAERPKLLVIDE 162
|
170 180 190
....*....|....*....|....*....|....
gi 447119240 180 PTTALDVTiQAQIIEL-LLELQQKENMALVLITH 212
Cdd:COG2401 163 FCSHLDRQ-TAKRVARnLQKLARRAGITLVVATH 195
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-225 |
2.31e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.40 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 6 VDKLSVHFGDesapfRAV-DRISYSVKQGEVVGIVGESGSGKSvsSL--AIMGLID-YPGRVMAEKlvfngqdlqrisek 81
Cdd:COG0488 1 LENLSKSFGG-----RPLlDDVSLSINPGDRIGLVGRNGAGKS--TLlkILAGELEpDSGEVSIPK-------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 82 errnlvGAEVAMIFQDPmtSLNPCYTV------GFQ-IMEAIK-----VHQGGNKS-------------------TRRQR 130
Cdd:COG0488 60 ------GLRIGYLPQEP--PLDDDLTVldtvldGDAeLRALEAeleelEAKLAEPDedlerlaelqeefealggwEAEAR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 131 AIDLLNQVGIPDPASRLDVypHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDvtIQAqiIELLLELQQKENMALVLI 210
Cdd:COG0488 132 AEEILSGLGFPEEDLDRPV--SELSGGWRRRVALARALLSEPDLLLLDEPTNHLD--LES--IEWLEEFLKNYPGTVLVV 205
|
250
....*....|....*
gi 447119240 211 THDLALVAEAAHKII 225
Cdd:COG0488 206 SHDRYFLDRVATRIL 220
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
24-224 |
2.82e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.83 E-value: 2.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 24 DRISYSVKQGEVVGIVGESGSGKSvSSLAIM-GLID-YPGRVMaeklvFNGQDLQRISEKERRNLvgaevamifqdpmts 101
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKT-SLLRILaGLARpDAGEVL-----WQGEPIRRQRDEYHQDL--------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 102 lnpCYtVGfqimeaikvHQGGNKS-----------------TRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMI 164
Cdd:PRK13538 77 ---LY-LG---------HQPGIKTeltalenlrfyqrlhgpGDDEALWEALAQVGL---AGFEDVPVRQLSAGQQRRVAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447119240 165 AMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMAlVLITH-DLALVAEAAHKI 224
Cdd:PRK13538 141 ARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMV-ILTTHqDLPVASDKVRKL 200
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
20-244 |
2.85e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 65.49 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 20 FRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVmaeklvfngqdlqrisekERRNLVGA--EVAMIF 95
Cdd:COG1134 39 FWALKDVSFEVERGESVGIIGRNGAGKS-TLLKLIAGILEPtsGRV------------------EVNGRVSAllELGAGF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 96 QDPMTSLNPCYTVGfQIM----EAIKvhqggnkstRRQRAI-------DLLNQvgipdpasrldvyP-HQLSGGMSQRVM 163
Cdd:COG1134 100 HPELTGRENIYLNG-RLLglsrKEID---------EKFDEIvefaelgDFIDQ-------------PvKTYSSGMRARLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 164 IAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAIFH 243
Cdd:COG1134 157 FAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIA 235
|
.
gi 447119240 244 A 244
Cdd:COG1134 236 A 236
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
18-245 |
9.01e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 65.25 E-value: 9.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 18 APFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLVFNGQDLQRISEKERrnlvgaEVAMIFQD 97
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGL----ERITSGEIWIGGRVVNELEPADR------DIAMVFQN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 98 pmTSLNPCYTVgFQIME-AIKVhQGGNKSTRRQRaidLLNQVGIPDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLI 176
Cdd:PRK11650 85 --YALYPHMSV-RENMAyGLKI-RGMPKAEIEER---VAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447119240 177 ADEPTTALDVTIQAQI-IElLLELQQKENMALVLITHDLalvAEA---AHKIIVMYAGQVVETGDAHAIFHAP 245
Cdd:PRK11650 158 FDEPLSNLDAKLRVQMrLE-IQRLHRRLKTTSLYVTHDQ---VEAmtlADRVVVMNGGVAEQIGTPVEVYEKP 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-232 |
9.40e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.41 E-value: 9.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 23 VDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLI--DYP---GRVMaeklvFNGQDLQR-------------ISEKERR 84
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRT----ELMKVLygALPrtsGYVT-----LDGHEVVTrspqdglangivyISEDRKR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 85 NlvGAEVAMIFQDPM--TSLNPCYTVGFQImeaikvhqggNKSTRRQRAIDLLNQVGIPDPAsrLDVYPHQLSGGMSQRV 162
Cdd:PRK10762 339 D--GLVLGMSVKENMslTALRYFSRAGGSL----------KHADEQQAVSDFIRLFNIKTPS--MEQAIGLLSGGNQQKV 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 163 MIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQV 232
Cdd:PRK10762 405 AIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKA-EGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
26-251 |
2.20e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 64.74 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidYPgrVMAEKLVFNGQDLQRISEKERRNlvgaEVAMIFQDPMT---SL 102
Cdd:PRK10790 360 INLSVPSRGFVALVGHTGSGKSTLASLLMGY--YP--LTEGEIRLDGRPLSSLSHSVLRQ----GVAMVQQDPVVladTF 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 103 NPCYTVGFQIMEAiKVHQGgnkstrrQRAIDLLNQV-GIPDPA-SRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
Cdd:PRK10790 432 LANVTLGRDISEE-QVWQA-------LETVQLAELArSLPDGLyTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEA 503
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447119240 181 TTALDVTIQAQIIELLLELqqKENMALVLITHDLALVAEAAHkIIVMYAGQVVETGdAHAIFHAPRHPYTQ 251
Cdd:PRK10790 504 TANIDSGTEQAIQQALAAV--REHTTLVVIAHRLSTIVEADT-ILVLHRGQAVEQG-THQQLLAAQGRYWQ 570
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-241 |
2.90e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 63.29 E-value: 2.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 2 ALLNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdYPgrvMAEKLVFNGQDLQRISEK 81
Cdd:PRK13537 6 APIDFRNVEKRYGDKLV----VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLT-HP---DAGSISLCGEPVPSRARH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 82 ERrnlvgAEVAMIFQdpMTSLNPCYTVgfqiMEAIKV---HQGGNKSTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGM 158
Cdd:PRK13537 78 AR-----QRVGVVPQ--FDNLDPDFTV----RENLLVfgrYFGLSAAAARALVPPLLEFAKL---ENKADAKVGELSGGM 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALvLITHDLALVAEAAHKIIVMYAGQVVETGDA 238
Cdd:PRK13537 144 KRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTIL-LTTHFMEEAERLCDRLCVIEEGRKIAEGAP 222
|
...
gi 447119240 239 HAI 241
Cdd:PRK13537 223 HAL 225
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-240 |
3.48e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.78 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 1 MALLNVDKLSVHFgdesaP-FRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPGrvmAEKLVFNGQDLQRIS 79
Cdd:PRK11288 2 SPYLSFDGIGKTF-----PgVKALDDISFDCRAGQVHALMGENGAGKS-TLLKILSGNYQPD---AGSILIDGQEMRFAS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 80 EKERRNlvgAEVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGG--NKSTRRQRAIDLLNQVGIP-DPASRLdvypHQLSG 156
Cdd:PRK11288 73 TTAALA---AGVAIIYQE--LHLVPEMTVAENLYLGQLPHKGGivNRRLLNYEAREQLEHLGVDiDPDTPL----KYLSI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:PRK11288 144 GQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATF 222
|
....
gi 447119240 237 DAHA 240
Cdd:PRK11288 223 DDMA 226
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-241 |
4.30e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.50 E-value: 4.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 27 SYSVKQGEVVGIVGESGSGKSVSSLAIMG-LIDYPGRvmaekLVFNGQDLQRISEKERRNLVGAEvamiFQDPMTSL--- 102
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGeLPLLSGE-----RQSQFSHITRLSFEQLQKLVSDE----WQRNNTDMlsp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 103 ---NPCYTVGFQIMEAIKvhqggnkstRRQRAIDLLNQVGIPDPASRLDVYphqLSGGMSQRVMIAMAIACRPKLLIADE 179
Cdd:PRK10938 94 gedDTGRTTAEIIQDEVK---------DPARCEQLAQQFGITALLDRRFKY---LSTGETRKTLLCQALMSEPDLLILDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447119240 180 PTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAI 241
Cdd:PRK10938 162 PFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-241 |
4.75e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 62.02 E-value: 4.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 6 VDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMG-LIDY-PGRVMaeklvFNGQDLQRISEKE- 82
Cdd:COG4604 4 IKNVSKRYGGK----VVLDDVSLTIPKGGITALIGPNGAGKS-TLLSMISrLLPPdSGEVL-----VDGLDVATTPSREl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 83 -RRnlvgaeVAMIFQDPMTSLNpcytvgfqimeaIKV----------HQGGNKSTRRQRAID-LLNQVGIPDPASR-LDv 149
Cdd:COG4604 74 aKR------LAILRQENHINSR------------LTVrelvafgrfpYSKGRLTAEDREIIDeAIAYLDLEDLADRyLD- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 150 yphQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYA 229
Cdd:COG4604 135 ---ELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKD 211
|
250
....*....|..
gi 447119240 230 GQVVETGDAHAI 241
Cdd:COG4604 212 GRVVAQGTPEEI 223
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-233 |
9.54e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.66 E-value: 9.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 1 MALLNVDKLSVHFGDesAPFraVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMG---LIDyPGRVMAEklvfngQDL-- 75
Cdd:PRK11147 1 MSLISIHGAWLSFSD--APL--LDNAELHIEDNERVCLVGRNGAGKS-TLMKILNgevLLD-DGRIIYE------QDLiv 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 76 QRISEKERRNLVG----------AEVA-----------MIFQDPMTS-LNPCYtvgfQIMEAIKVHQGGNKSTRRQraiD 133
Cdd:PRK11147 69 ARLQQDPPRNVEGtvydfvaegiEEQAeylkryhdishLVETDPSEKnLNELA----KLQEQLDHHNLWQLENRIN---E 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 134 LLNQVGIpDPASRLDvyphQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTiqaqIIELLLELQQKENMALVLITHD 213
Cdd:PRK11147 142 VLAQLGL-DPDAALS----SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIE----TIEWLEGFLKTFQGSIIFISHD 212
|
250 260
....*....|....*....|
gi 447119240 214 LALVAEAAHKIIVMYAGQVV 233
Cdd:PRK11147 213 RSFIRNMATRIVDLDRGKLV 232
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
23-241 |
1.45e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 61.39 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGrvmAEKLVFNGqdlqrISEKERRNLVGAEVAMIFQdpMTSL 102
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTS-PD---AGKITVLG-----VPVPARARLARARIGVVPQ--FDNL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 103 NPCYTVgfqiMEAIKVH-QGGNKSTRRQRAI--DLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADE 179
Cdd:PRK13536 126 DLEFTV----RENLLVFgRYFGMSTREIEAVipSLLEFARL---ESKADARVSDLSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447119240 180 PTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAI 241
Cdd:PRK13536 199 PTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-234 |
2.40e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.34 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 20 FRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGlIDypgRVMAEKLVFNGQDLQRISEKERrnlVGAEVAMIFQDPM 99
Cdd:PRK09700 276 RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFG-VD---KRAGGEIRLNGKDISPRSPLDA---VKKGMAYITESRR 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 100 -TSLNPCYTVGFQIMEAIKVHQGG--------NKSTRRQRAIDLLNQVGIPdpASRLDVYPHQLSGGMSQRVMIAMAIAC 170
Cdd:PRK09700 349 dNGFFPNFSIAQNMAISRSLKDGGykgamglfHEVDEQRTAENQRELLALK--CHSVNQNITELSGGNQQKVLISKWLCC 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447119240 171 RPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVE 234
Cdd:PRK09700 427 CPEVIIFDEPTRGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-234 |
3.20e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 60.85 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSvsSLA--IMGLIDyP--GRVmaeklvfngqdlqRI 78
Cdd:COG0488 315 VLELEGLSKSYGDK----TLLDDLSLRIDRGDRIGLIGPNGAGKS--TLLklLAGELE-PdsGTV-------------KL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 79 SEKerrnlvgAEVAMIFQDpMTSLNPCYTVgfqiMEAIkvhQGGNKSTRRQRAIDLLNQVGIPdpASRLDVYPHQLSGGM 158
Cdd:COG0488 375 GET-------VKIGYFDQH-QEELDPDKTV----LDEL---RDGAPGGTEQEVRGYLGRFLFS--GDDAFKPVGVLSGGE 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447119240 159 SQRVMIAMAIACRPKLLIADEPTTALDV-TIQAqIIELLLELQQkenmALVLITHDLALVAEAAHKIIVMYAGQVVE 234
Cdd:COG0488 438 KARLALAKLLLSPPNVLLLDEPTNHLDIeTLEA-LEEALDDFPG----TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-237 |
4.60e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.57 E-value: 4.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHFGdesaPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPGrvmAEKLVFNGQDLQRISEKE 82
Cdd:PRK09700 5 YISMAGIGKSFG----PVHALKSVNLTVYPGEIHALLGENGAGKS-TLMKVLSGIHEPT---KGTITINNINYNKLDHKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 83 RRNLvgaEVAMIFQ-----DPMTSLNPCY--------TVGFQIMEAIKVhqggnkstrRQRAIDLLNQVGIpdpASRLDV 149
Cdd:PRK09700 77 AAQL---GIGIIYQelsviDELTVLENLYigrhltkkVCGVNIIDWREM---------RVRAAMMLLRVGL---KVDLDE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 150 YPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALdvtIQAQIIELLLELQQ--KENMALVLITHDLALVAEAAHKIIVM 227
Cdd:PRK09700 142 KVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL---TNKEVDYLFLIMNQlrKEGTAIVYISHKLAEIRRICDRYTVM 218
|
250
....*....|
gi 447119240 228 YAGQVVETGD 237
Cdd:PRK09700 219 KDGSSVCSGM 228
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-233 |
9.77e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.54 E-value: 9.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 26 ISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLVFNGQdlqRISEKERRNLVGAEVAMIFQD-PMTSLNP 104
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRS----ELMKLLYGATRRTAGQVYLDGK---PIDIRSPRDAIRAGIMLCPEDrKAEGIIP 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 105 CYTVGFQImeaikvhqggNKSTRRQ--RAIDLLNQVGIPDPASR----LDV---YPHQ----LSGGMSQRVMIAMAIACR 171
Cdd:PRK11288 345 VHSVADNI----------NISARRHhlRAGCLINNRWEAENADRfirsLNIktpSREQlimnLSGGNQQKAILGRWLSED 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447119240 172 PKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVV 233
Cdd:PRK11288 415 MKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
30-237 |
9.94e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 58.26 E-value: 9.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 30 VKQGEVVGIVGESGSGKSVSSLAIMGLIDYpgRVMAEKLVFNGQDLQRISEKERrnlVGAEVAMIFQDPMTSlnPCYTVG 109
Cdd:PRK09580 24 VRPGEVHAIMGPNGSGKSTLSATLAGREDY--EVTGGTVEFKGKDLLELSPEDR---AGEGIFMAFQYPVEI--PGVSNQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 110 FQIMEAIKvhqgGNKSTRRQRAIDLLN-QVGIPDPASRLDVYPHQL--------SGGMSQRVMIAMAIACRPKLLIADEP 180
Cdd:PRK09580 97 FFLQTALN----AVRSYRGQEPLDRFDfQDLMEEKIALLKMPEDLLtrsvnvgfSGGEKKRNDILQMAVLEPELCILDES 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447119240 181 TTALDV---TIQAQIIELLlelqQKENMALVLITHDLALVAEAAHKII-VMYAGQVVETGD 237
Cdd:PRK09580 173 DSGLDIdalKIVADGVNSL----RDGKRSFIIVTHYQRILDYIKPDYVhVLYQGRIVKSGD 229
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-241 |
1.22e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 58.30 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGliDYPGRVMAE------KLVFNGQDLQRISEKE--RRNLV---GA 89
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTGGGAPRgarvtgDVTLNGEPLAAIDAPRlaRLRAVlpqAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 90 EVAMIFQDPMTSLNPCYTvgfqimeaiKVHQGGNKSTRRQRAIDLLNQVGIPDPASRLDVYphQLSGGMSQRVMIAMAIA 169
Cdd:PRK13547 93 QPAFAFSAREIVLLGRYP---------HARRAGALTHRDGEIAWQALALAGATALVGRDVT--TLSGGELARVQFARVLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 170 ---------CRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHA 240
Cdd:PRK13547 162 qlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPAD 241
|
.
gi 447119240 241 I 241
Cdd:PRK13547 242 V 242
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
26-230 |
2.63e-09 |
|
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: 56.57 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLVFNGQDLQRISEKERRNLVGAEVAMIFQDPmtslnpc 105
Cdd:cd03290 20 INIRIPTGQLTMIVGQVGCGKSSLLLAILGEM----QTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKP------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 106 YTVGFQIMEAIKVHQGGNKStRRQRAIDLLNQVgiPDpasrLDVYPH-----------QLSGGMSQRVMIAMAIACRPKL 174
Cdd:cd03290 89 WLLNATVEENITFGSPFNKQ-RYKAVTDACSLQ--PD----IDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447119240 175 LIADEPTTALDVTIQAQII-ELLLELQQKENMALVLITHDLALVAEaAHKIIVMYAG 230
Cdd:cd03290 162 VFLDDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
26-227 |
3.53e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.12 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyP-------------------------GRVMAEKLVFNG-------- 72
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYD-PtegdiiindshnlkdinlkwwrskiGVVSQDPLLFSNsiknniky 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 73 -----QDLQRISE------------KERRNLVGAEVAMIFQDPMTSlnpcyTVGFQIMEAIKVHQggnkSTRRQRAIDLL 135
Cdd:PTZ00265 483 slyslKDLEALSNyynedgndsqenKNKRNSCRAKCAGDLNDMSNT-----TDSNELIEMRKNYQ----TIKDSEVVDVS 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 136 NQVGIPDPASRL-DVY-------PHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMAL 207
Cdd:PTZ00265 554 KKVLIHDFVSALpDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRIT 633
|
250 260
....*....|....*....|
gi 447119240 208 VLITHDLALVaEAAHKIIVM 227
Cdd:PTZ00265 634 IIIAHRLSTI-RYANTIFVL 652
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
112-226 |
4.71e-09 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 54.67 E-value: 4.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 112 IMEAIKVHQGGNKSTRRQRaidLLNQVGIPDPASRLDVYP--HQLSGGMSQRVMIAMAIA----CRPKLLIADEPTTALD 185
Cdd:cd03227 37 ILDAIGLALGGAQSATRRR---SGVKAGCIVAAVSAELIFtrLQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLD 113
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 447119240 186 VTIQAQIIELLLELQQKENMALVlITHDLALVAEAAHKIIV 226
Cdd:cd03227 114 PRDGQALAEAILEHLVKGAQVIV-ITHLPELAELADKLIHI 153
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-221 |
1.29e-08 |
|
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: 53.15 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 32 QGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMaekLVFNGQDLQRISEKERRNLVGAEvamifqdpmtslnpcytvgfq 111
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV---IYIDGEDILEEVLDQLLLIIVGG--------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 112 imeaikvhqggnkstrrqraidllnqvgipdpasrldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQ 191
Cdd:smart00382 57 --------------------------------------KKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEAL 98
|
170 180 190
....*....|....*....|....*....|....*
gi 447119240 192 IIEL-----LLELQQKENMALVLITHDLALVAEAA 221
Cdd:smart00382 99 LLLLeelrlLLLLKSEKNLTVILTTNDEKDLGPAL 133
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-288 |
1.30e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.51 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLVF--NGQDLQRISEK 81
Cdd:NF000106 14 VEVRGLVKHFGE----VKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*TWcaNRRALRRTIG* 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 82 ERRNLVGAevamifQDPMTSLNPCYTVGFQImeaikvhqGGNKSTRRQRAIDLLNQVGIPDPASRLDVyphQLSGGMSQR 161
Cdd:NF000106 90 HRPVR*GR------RESFSGRENLYMIGR*L--------DLSRKDARARADELLERFSLTEAAGRAAA---KYSGGMRRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAHAI 241
Cdd:NF000106 153 LDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSM-VRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 447119240 242 fhapRHPYTQALLRALPEFAQDKERL------ASLPGVVPGKYDRPNGCLLNP 288
Cdd:NF000106 232 ----KTKVGGRTLQIRPAHAAELDRMvgaiaqAGLDGIAGATADHEDGVVNVP 280
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
26-238 |
2.22e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.26 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYpgRVMAEKLVFNGQDLQRISEKERRNLvGAEVAmiFQDPMTslnpc 105
Cdd:CHL00131 26 LNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAY--KILEGDILFKGESILDLEPEERAHL-GIFLA--FQYPIE----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 106 yTVGFQIMEAIKVHQGGNKSTRRQRAIDLLNQVGIPDPASRL-DVYPHQL--------SGGMSQRVMIAMAIACRPKLLI 176
Cdd:CHL00131 96 -IPGVSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLKLvGMDPSFLsrnvnegfSGGEKKRNEILQMALLDSELAI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447119240 177 ADEPTTALDVTIQAQIIELLLELQQKENmALVLITHDLAL----VAEAAHkiiVMYAGQVVETGDA 238
Cdd:CHL00131 175 LDETDSGLDIDALKIIAEGINKLMTSEN-SIILITHYQRLldyiKPDYVH---VMQNGKIIKTGDA 236
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
21-224 |
2.58e-08 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 53.27 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 21 RAV-DRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLVFNGQDLQRISEKERRNL--VGAEVAMifqd 97
Cdd:cd03231 13 RALfSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLS----PPLAGRVLLNGGPLDFQRDSIARGLlyLGHAPGI---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 98 pMTSLNPCYTVGFqimeaikVHQGGNKSTrrqrAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIA 177
Cdd:cd03231 85 -KTTLSVLENLRF-------WHADHSDEQ----VEEALARVGL---NGFEDRPVAQLSAGQQRRVALARLLLSGRPLWIL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447119240 178 DEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKI 224
Cdd:cd03231 150 DEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-228 |
2.59e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 53.91 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 29 SVKQGEVVGIVGESGSGKSvSSLAIM--------GLIDYPGR---VMAEklvFNGQDLQRISEKerrnLVGAEVAMIFQD 97
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKS-TALKILagklkpnlGKFDDPPDwdeILDE---FRGSELQNYFTK----LLEGDVKVIVKP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 98 PMTSLNPCYTVGFQIMEAIKVHQGGNKSTrrqrAIDLLNQVGIpdpasrLDVYPHQLSGGMSQRVMIAMAIACRPKLLIA 177
Cdd:cd03236 94 QYVDLIPKAVKGKVGELLKKKDERGKLDE----LVDQLELRHV------LDRNIDQLSGGELQRVAIAAALARDADFYFF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447119240 178 DEPTTALDVTIQAQIIELLLELQQKENMALVlITHDLALVAEAAHKIIVMY 228
Cdd:cd03236 164 DEPSSYLDIKQRLNAARLIRELAEDDNYVLV-VEHDLAVLDYLSDYIHCLY 213
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
26-235 |
2.60e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.12 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGL-------IDYPGRVM----AEKLVFNGQDLqrISEKERRNLVGAEVAMI 94
Cdd:PRK10982 267 VSFDLHKGEILGIAGLVGAKRTDIVETLFGIreksagtITLHGKKInnhnANEAINHGFAL--VTEERRSTGIYAYLDIG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 95 FQDPMTSLNPcYTVGFQIMEAIKVhqggnkSTRRQRAIDLLNqvgIPDPASRLDVypHQLSGGMSQRVMIAMAIACRPKL 174
Cdd:PRK10982 345 FNSLISNIRN-YKNKVGLLDNSRM------KSDTQWVIDSMR---VKTPGHRTQI--GSLSGGNQQKVIIGRWLLTQPEI 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447119240 175 LIADEPTTALDVTIQAQIIELLLELQQKENmALVLITHDLALVAEAAHKIIVMYAGQV---VET 235
Cdd:PRK10982 413 LMLDEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEMPELLGITDRILVMSNGLVagiVDT 475
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
38-226 |
2.83e-08 |
|
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: 52.99 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 38 IVGESGSGKSVSSLAI-MGLidYPGRVMAEKLVFNGQDLqrISEKERRnlvgAEVAMIFQDPMTSLnpcYTV--GFQIME 114
Cdd:cd03240 27 IVGQNGAGKTTIIEALkYAL--TGELPPNSKGGAHDPKL--IREGEVR----AQVKLAFENANGKK---YTItrSLAILE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 115 -AIKVHQGGnkstrrqraIDLLnqvgIPDPASRLdvyphqlSGGmsQRVMIAMAIAC--------RPKLLIADEPTTALD 185
Cdd:cd03240 96 nVIFCHQGE---------SNWP----LLDMRGRC-------SGG--EKVLASLIIRLalaetfgsNCGILALDEPTTNLD 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 447119240 186 V-TIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIV 226
Cdd:cd03240 154 EeNIEESLAEIIEERKSQKNFQLIVITHDEELVDAADHIYRV 195
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
67-226 |
3.13e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.04 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 67 KLVFNGQDLQRISEKERRNLVgaevAMIFQDPMTslnpcytVGFQIMEAIKVhqGGNKSTRRQ-------RAIDLLNQvG 139
Cdd:PTZ00265 1278 KILLDGVDICDYNLKDLRNLF----SIVSQEPML-------FNMSIYENIKF--GKEDATREDvkrackfAAIDEFIE-S 1343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 140 IPDP-ASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVa 218
Cdd:PTZ00265 1344 LPNKyDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI- 1422
|
....*...
gi 447119240 219 EAAHKIIV 226
Cdd:PTZ00265 1423 KRSDKIVV 1430
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
15-231 |
6.96e-08 |
|
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: 52.09 E-value: 6.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 15 DESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvsSL--AIMGLIdypgRVMAEKLVFNGQD--------LQRISEKErr 84
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKS--SLlsALLGEL----EKLSGSVSVPGSIayvsqepwIQNGTIRE-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 85 NLvgaevamIFQDPMtslnpcytvgfqimeaikvhqggnKSTRRQRAIDL--LNqvgiPDpasrLDVYPHQ--------- 153
Cdd:cd03250 85 NI-------LFGKPF------------------------DEERYEKVIKAcaLE----PD----LEILPDGdlteigekg 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 154 --LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHkIIVMYAGQ 231
Cdd:cd03250 126 inLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPHADQ-IVVLDNGR 204
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
149-212 |
9.81e-08 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 51.00 E-value: 9.81e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447119240 149 VYP--HQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLlelqQKENMALVLITH 212
Cdd:cd03223 85 IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL----KELGITVISVGH 146
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
26-233 |
1.09e-07 |
|
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: 51.49 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAeKLVFNGQDLQRISEKERRnlvgaEVAMIFQDpmTSLNPC 105
Cdd:cd03233 26 FSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEG-DIHYNGIPYKEFAEKYPG-----EIIYVSEE--DVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 106 YTVGfQIME-AIKVHqgGNKSTRrqraidllnqvGIpdpasrldvyphqlSGGMSQRVMIAMAIACRPKLLIADEPTTAL 184
Cdd:cd03233 98 LTVR-ETLDfALRCK--GNEFVR-----------GI--------------SGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 447119240 185 DVTIQAQIIELLLELQQKENMALVLIThdLALVAEAAH---KIIVMYAGQVV 233
Cdd:cd03233 150 DSSTALEILKCIRTMADVLKTTTFVSL--YQASDEIYDlfdKVLVLYEGRQI 199
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-236 |
1.28e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.20 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 6 VDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSvsSLaiMGLID-----YPGRVMaeklVFNGQdlqrISE 80
Cdd:NF033858 4 LEGVSHRYGKT----VALDDVSLDIPAGCMVGLIGPDGVGKS--SL--LSLIAgarkiQQGRVE----VLGGD----MAD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 81 KERRNLVGAEVAMIFQDPMTSLNPCYTVgfqiMEAIKVHQ---GGNKSTRRQRAIDLLNQVGI---PD-PASrldvyphQ 153
Cdd:NF033858 68 ARHRRAVCPRIAYMPQGLGKNLYPTLSV----FENLDFFGrlfGQDAAERRRRIDELLRATGLapfADrPAG-------K 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLEL-QQKENMALVLIThdlALVAEAAH--KIIVMYAG 230
Cdd:NF033858 137 LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIrAERPGMSVLVAT---AYMEEAERfdWLVAMDAG 213
|
....*.
gi 447119240 231 QVVETG 236
Cdd:NF033858 214 RVLATG 219
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
33-239 |
1.52e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 52.96 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 33 GEVVGIVGESGSGKSVSSLAIMGLI---DYPGRVMAEKLVFNGQDLQRIsekerrnlvgaevAMIFQDPMtsLNPCYTVG 109
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIqgnNFTGTILANNRKPTKQILKRT-------------GFVTQDDI--LYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 110 FQIM--EAIKVHQGGNKSTRRQRAIDLLNQVGIPDPASRL--DVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALD 185
Cdd:PLN03211 159 ETLVfcSLLRLPKSLTKQEKILVAESVISELGLTKCENTIigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447119240 186 VTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGDAH 239
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGS 292
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-228 |
2.68e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 30 VKQGEVVGIVGESGSGKSvSSLAIM-GLI-----DYPGRVMAEKLV--FNGQDLQ----RISEKERRnlvgaevamifqd 97
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKT-TAVKILsGELipnlgDYEEEPSWDEVLkrFRGTELQnyfkKLYNGEIK------------- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 98 pmTSLNPcytvgfQIMEAI-KVHQGgnkstrrqRAIDLLNQV---GIPDP-ASRLDVYP------HQLSGGMSQRVMIAM 166
Cdd:PRK13409 162 --VVHKP------QYVDLIpKVFKG--------KVRELLKKVderGKLDEvVERLGLENildrdiSELSGGELQRVAIAA 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447119240 167 AIACRPKLLIADEPTTALDVTIQAQIIELLLELQqkENMALVLITHDLALVAEAAHKIIVMY 228
Cdd:PRK13409 226 ALLRDADFYFFDEPTSYLDIRQRLNVARLIRELA--EGKYVLVVEHDLAVLDYLADNVHIAY 285
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
9-236 |
3.88e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.66 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 9 LSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrvmaeklvfngqdlqrISEKERRnLVG 88
Cdd:NF033858 272 LTMRFGD----FTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLP-------------------ASEGEAW-LFG 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 89 AEVamifqDP-----------MT---SLnpcY---TVG---------FQIMEAikvhqggnksTRRQRAIDLLNQVGIpd 142
Cdd:NF033858 328 QPV-----DAgdiatrrrvgyMSqafSL---YgelTVRqnlelharlFHLPAA----------EIAARVAEMLERFDL-- 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 143 pASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHdlaLVAEAAH 222
Cdd:NF033858 388 -ADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTH---FMNEAER 463
|
250
....*....|....*.
gi 447119240 223 --KIIVMYAGQVVETG 236
Cdd:NF033858 464 cdRISLMHAGRVLASD 479
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
4-256 |
4.92e-07 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 50.29 E-value: 4.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 4 LNVDKLSVHFGDESAPfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLVFNGQDLQRISEKER 83
Cdd:cd03288 20 IKIHDLCVRYENNLKP--VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVD----IFDGKIVIDGIDISKLPLHTL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 84 RnlvgAEVAMIFQDPMT-------SLNP-CYTVGFQIMEAIKVHQGGNKSTRRQRAIDLLNQVGipdpasrldvyPHQLS 155
Cdd:cd03288 94 R----SRLSIILQDPILfsgsirfNLDPeCKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEG-----------GENFS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQaQIIELLLeLQQKENMALVLITHDLALVAEaAHKIIVMYAGQVVET 235
Cdd:cd03288 159 VGQRQLFCLARAFVRKSSILIMDEATASIDMATE-NILQKVV-MTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVEC 235
|
250 260
....*....|....*....|.
gi 447119240 236 GDAHAIFHAPRHPYTqALLRA 256
Cdd:cd03288 236 DTPENLLAQEDGVFA-SLVRT 255
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-237 |
5.92e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 51.04 E-value: 5.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGL-------IDYPGR--VMAEKLVFNGQdLQRISEKERRNLVGAeva 92
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVtmpnkgtVDIKGSaaLIAISSGLNGQ-LTGIENIELKGLMMG--- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 93 mIFQDPMTSLNPcytvgfQIMEAIKVHQggnkstrrqraidLLNQvgipdPASrldvyphQLSGGMSQRVMIAMAIACRP 172
Cdd:PRK13545 115 -LTKEKIKEIIP------EIIEFADIGK-------------FIYQ-----PVK-------TYSSGMKSRLGFAISVHINP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447119240 173 KLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVETGD 237
Cdd:PRK13545 163 DILVIDEALSVGDQTFTKKCLDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGD 226
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
26-269 |
7.59e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 50.71 E-value: 7.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRV-MAEKLVFNGQDLQRISEKERRNLvgaevamIFQDPmtsLN 103
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDkVEGHVhMKGSVAYVPQQAWIQNDSLRENI-------LFGKA---LN 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 104 PCYTVgfQIMEA------IKVHQGGNKSTRRQRAIDLlnqvgipdpasrldvyphqlSGGMSQRVMIAMAIACRPKLLIA 177
Cdd:TIGR00957 727 EKYYQ--QVLEAcallpdLEILPSGDRTEIGEKGVNL--------------------SGGQKQRVSLARAVYSNADIYLF 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 178 DEPTTALDVTIQAQIIELLL-ELQQKENMALVLITHDLALVAEaAHKIIVMYAGQVVETGdahaifhaprhPYTQALLR- 255
Cdd:TIGR00957 785 DDPLSAVDAHVGKHIFEHVIgPEGVLKNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMG-----------SYQELLQRd 852
|
250
....*....|....*....
gi 447119240 256 -ALPEF----AQDKERLAS 269
Cdd:TIGR00957 853 gAFAEFlrtyAPDEQQGHL 871
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
26-243 |
8.25e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.93 E-value: 8.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLVFNGQDLQRISEKERRNlvgaEVAMIFQDPM------ 99
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVE----VCGGEIRVNGREIGAYGLRELRR----QFSMIPQDPVlfdgtv 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 100 -TSLNPcytvgfqIMEAikvhqggnKSTRRQRAIDLlnqVGIPDPA--------SRLdvyphqLSGG----MSQRVMIAM 166
Cdd:PTZ00243 1401 rQNVDP-------FLEA--------SSAEVWAALEL---VGLRERVasesegidSRV------LEGGsnysVGQRQLMCM 1456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 167 AIACRPK---LLIADEPTT----ALDVTIQAQIIELLlelqqkENMALVLITHDLALVAEaAHKIIVMYAGQVVETG--- 236
Cdd:PTZ00243 1457 ARALLKKgsgFILMDEATAnidpALDRQIQATVMSAF------SAYTVITIAHRLHTVAQ-YDKIIVMDHGAVAEMGspr 1529
|
250
....*....|.
gi 447119240 237 ----DAHAIFH 243
Cdd:PTZ00243 1530 elvmNRQSIFH 1540
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
21-217 |
8.32e-07 |
|
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: 48.89 E-value: 8.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLVFNGQDLQRISEKERRNLvgaevAMIFQDPmt 100
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLL----RPDSGEVRWNGTPLAEQRDEPHENI-----LYLGHLP-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 101 SLNPCYTV--GFQIMEAIkvHQGgnkstrRQRAI-DLLNQVGIPDPAsrlDVYPHQLSGGMSQRVMIAMAIACRPKLLIA 177
Cdd:TIGR01189 83 GLKPELSAleNLHFWAAI--HGG------AQRTIeDALAAVGLTGFE---DLPAAQLSAGQQRRLALARLWLSRRPLWIL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 447119240 178 DEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALV 217
Cdd:TIGR01189 152 DEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-228 |
8.67e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.17 E-value: 8.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 31 KQGEVVGIVGESGSGKSvSSLAIM-GLI-----DYPGRVMAEKLV--FNGQDLQ----RISEKERRnlvgaevamifqdp 98
Cdd:COG1245 97 KKGKVTGILGPNGIGKS-TALKILsGELkpnlgDYDEEPSWDEVLkrFRGTELQdyfkKLANGEIK-------------- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 99 mTSLNPcytvgfQIMEAI-KVHQGgnkstrrqRAIDLLNQV---GIPDP-ASRLDVYP------HQLSGGMSQRVMIAMA 167
Cdd:COG1245 162 -VAHKP------QYVDLIpKVFKG--------TVRELLEKVderGKLDElAEKLGLENildrdiSELSGGELQRVAIAAA 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447119240 168 IACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLAL---VAEAAHkiiVMY 228
Cdd:COG1245 227 LLRDADFYFFDEPSSYLDIYQRLNVARLIREL-AEEGKYVLVVEHDLAIldyLADYVH---ILY 286
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
15-231 |
1.08e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.00 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 15 DESAP-FRAVDRISYSVKQGEVVGIVGESGSGKSvsslAIM-----------GLIDYPGrvmaEKLVFNGQdlqRISEKe 82
Cdd:PRK10762 11 DKAFPgVKALSGAALNVYPGRVMALVGENGAGKS----TMMkvltgiytrdaGSILYLG----KEVTFNGP---KSSQE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 83 rrnlvgAEVAMIFQDpmtsLN--PCYTvgfqIMEAIKVhqgGNKSTRRQRAID----------LLNQVGIPDPASRLdvy 150
Cdd:PRK10762 79 ------AGIGIIHQE----LNliPQLT----IAENIFL---GREFVNRFGRIDwkkmyaeadkLLARLNLRFSSDKL--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 151 PHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAG 230
Cdd:PRK10762 139 VGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKS-QGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
.
gi 447119240 231 Q 231
Cdd:PRK10762 218 Q 218
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
154-236 |
1.53e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 47.70 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 154 LSGGMSQRVMIAMAIACRPK--LLIADEPTTALDVTIQAQIIELLLELQQKENmALVLITHDLAlVAEAAHKIIVM---- 227
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGN-TVILIEHNLD-VLSSADWIIDFgpgs 165
|
90
....*....|.
gi 447119240 228 --YAGQVVETG 236
Cdd:cd03238 166 gkSGGKVVFSG 176
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
26-234 |
1.66e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.97 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYP-GRVMaeklvFNGQDLQRISEKERRNLVgaevAMIFQDPMTSLNp 104
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEkGRIM-----IDDCDVAKFGLTDLRRVL----SIIPQSPVLFSG- 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 105 cyTVGFQImEAIKVHQGGN--KSTRRQRAIDLL--NQVGIPDPASRLDvypHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
Cdd:PLN03232 1325 --TVRFNI-DPFSEHNDADlwEALERAHIKDVIdrNPFGLDAEVSEGG---ENFSVGQRQLLSLARALLRRSKILVLDEA 1398
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447119240 181 TTALDVTIQAQIIELLLElqQKENMALVLITHDLALVAEaAHKIIVMYAGQVVE 234
Cdd:PLN03232 1399 TASVDVRTDSLIQRTIRE--EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLE 1449
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
155-239 |
1.92e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.72 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLElqqkenmaLVLITHDLALVA---------EAAHKII 225
Cdd:TIGR00956 211 SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKT--------SANILDTTPLVAiyqcsqdayELFDKVI 282
|
90
....*....|....
gi 447119240 226 VMYAGQVVETGDAH 239
Cdd:TIGR00956 283 VLYEGYQIYFGPAD 296
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
26-213 |
1.94e-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: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 26 ISYSVKQGEVVGIVGESGSGKSvSSLAIMGLID--YPGRVMAEKLVFNG---QDLQRISEKERRNLVGA----------- 89
Cdd:TIGR03719 24 ISLSFFPGAKIGVLGLNGAGKS-TLLRIMAGVDkdFNGEARPQPGIKVGylpQEPQLDPTKTVRENVEEgvaeikdaldr 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 90 --EVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKSTRRQRAIDLLNQvgipdPASRLDVypHQLSGGMSQRVMIAMA 167
Cdd:TIGR03719 103 fnEISAKYAEPDADFDKLAAEQAELQEIIDAADAWDLDSQLEIAMDALRC-----PPWDADV--TKLSGGERRRVALCRL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447119240 168 IACRPKLLIADEPTTALDvtiqAQIIELLLELQQKENMALVLITHD 213
Cdd:TIGR03719 176 LLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHD 217
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-240 |
4.58e-06 |
|
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: 47.02 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 29 SVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGRVMAEKlvfngqDLQRISEKERRnlVGAEVAMifqdpmtslnpcyTV 108
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLK-PDEGDIEI------ELDTVSYKPQY--IKADYEG-------------TV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 109 GFQIMEAIKvhqggNKSTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDV-- 186
Cdd:cd03237 79 RDLLSSITK-----DFYTHPYFKTEIAKPLQI---EQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeq 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447119240 187 -TIQAQIIELLLElqQKENMALVlITHDLALVAEAAHKIIVmYAGQVVETGDAHA 240
Cdd:cd03237 151 rLMASKVIRRFAE--NNEKTAFV-VEHDIIMIDYLADRLIV-FEGEPSVNGVANP 201
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
26-236 |
6.56e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 47.35 E-value: 6.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 26 ISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPGrvmAEKLVFNGQDLQRISEKERRNLvgaEVAMIFQDPMtsLNPC 105
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKS-TLMKIIAGIVPPD---SGTLEIGGNPCARLTPAKAHQL---GIYLVPQEPL--LFPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 106 YTVGFQIMEAIKVHQGgnkstRRQRAIDLLNQVGI---PD-PASRLDVYPHQLsggmsqrVMIAMAIACRPKLLIADEPT 181
Cdd:PRK15439 101 LSVKENILFGLPKRQA-----SMQKMKQLLAALGCqldLDsSAGSLEVADRQI-------VEILRGLMRDSRILILDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447119240 182 TALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:PRK15439 169 ASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIALSG 222
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
3-237 |
7.27e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 47.40 E-value: 7.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 3 LLNVDKLSVHFGDESAPfrAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLVFNGQDLQRISEKE 82
Cdd:PRK10789 313 ELDVNIRQFTYPQTDHP--ALENVNFTLKPGQMLGICGPTGSGKS----TLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 83 RRnlvgAEVAMIFQDPMTslnpcytvgFQIMEAIKVHQGGNKSTRRQ--RAIDLLNqvgIPDPASRL-DVYPHQ------ 153
Cdd:PRK10789 387 WR----SRLAVVSQTPFL---------FSDTVANNIALGRPDATQQEieHVARLAS---VHDDILRLpQGYDTEvgergv 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 154 -LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLleLQQKENMALVLITHDLALVAEAAhKIIVMYAGQV 232
Cdd:PRK10789 451 mLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNL--RQWGEGRTVIISAHRLSALTEAS-EILVMQHGHI 527
|
....*
gi 447119240 233 VETGD 237
Cdd:PRK10789 528 AQRGN 532
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
153-232 |
7.40e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.47 E-value: 7.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkenmALVLITHDLALVAEAAHKIIVMYAGQV 232
Cdd:PRK10636 430 RFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEG----ALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
126-225 |
2.55e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.93 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 126 TRRQRAIDLLNQVGIPDPasRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDvtIQAQIielLLELQQKE-N 204
Cdd:PRK10636 124 TIRSRAASLLHGLGFSNE--QLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD--LDAVI---WLEKWLKSyQ 196
|
90 100
....*....|....*....|.
gi 447119240 205 MALVLITHDLALVAEAAHKII 225
Cdd:PRK10636 197 GTLILISHDRDFLDPIVDKII 217
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
154-236 |
2.96e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 44.91 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 154 LSGGMSQRVMIAMAIACR---PKLLIADEPTTAL---DVtiqAQIIELLLELQQKENMALVlITHDLALVAEAAHkIIVM 227
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLhfhDV---KKLLEVLQRLVDKGNTVVV-IEHNLDVIKCADW-IIDL 244
|
90
....*....|....*
gi 447119240 228 ------YAGQVVETG 236
Cdd:cd03271 245 gpeggdGGGQVVASG 259
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
154-236 |
3.17e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.88 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLL--ELQQKENmalVLITHDLALVAEaAHKIIVMYAGQ 231
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIkdELRGKTR---VLVTNQLHFLSQ-VDRIILVHEGM 816
|
....*
gi 447119240 232 VVETG 236
Cdd:PLN03130 817 IKEEG 821
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-226 |
1.47e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.26 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 30 VKQGEVVGIVGESGSGKS--VSSLAimGLIDyP--GRVMAEklvfngqdlQRISEKERRnlVGAEVAMifqdpmtslnpc 105
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTtfAKLLA--GVLK-PdeGEVDPE---------LKISYKPQY--IKPDYDG------------ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 106 yTVGfQIMEAIKVHQGGN--KStrrqraiDLLNQVGIPDpasRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTA 183
Cdd:PRK13409 416 -TVE-DLLRSITDDLGSSyyKS-------EIIKPLQLER---LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAH 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447119240 184 LDV---TIQAQIIELLLElqQKENMALVlITHDLALVAEAAHKIIV 226
Cdd:PRK13409 484 LDVeqrLAVAKAIRRIAE--EREATALV-VDHDIYMIDYISDRLMV 526
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-236 |
1.67e-04 |
|
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: 43.46 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 22 AVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLVFNGQDLQRISEKERRNLvgaevamifqdpmtS 101
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKT-TTLSILTGLLPP---TSGTVLVGGKDIETNLDAVRQSL--------------G 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 102 LNPCYTVGFQ---IMEAIKVH---QGGNKSTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLL 175
Cdd:TIGR01257 1007 MCPQHNILFHhltVAEHILFYaqlKGRSWEEAQLEMEAMLEDTGL---HHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVV 1083
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447119240 176 IADEPTTALDVTIQAQIIELLleLQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:TIGR01257 1084 VLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
26-245 |
2.45e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.84 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYP-GRVMAEK-LVFNGQDLQRISEKERRNLvgaevamIFQDPMTSLN 103
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISeGRVWAERsIAYVPQQAWIMNATVRGNI-------LFFDEEDAAR 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 104 PCYTVGFQIMEAIKVHQGGNKSTRrqraidlLNQVGIpdpasrldvyphQLSGGMSQRVMIAMAIACRPKLLIADEPTTA 183
Cdd:PTZ00243 752 LADAVRVSQLEADLAQLGGGLETE-------IGEKGV------------NLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447119240 184 LDVTIQAQIIE--LLLELQQKENmalVLITHDLALVAEAAHkIIVMYAGQVVETGDAHAIFHAP 245
Cdd:PTZ00243 813 LDAHVGERVVEecFLGALAGKTR---VLATHQVHVVPRADY-VVALGDGRVEFSGSSADFMRTS 872
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
130-213 |
3.40e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.19 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 130 RAIDLLNQVGIPDpasrldvypHQLSGGMSQ-------RVMIAMAIACRPKLLIADEPTTALDV-TIQaqiieLLLELQQ 201
Cdd:PRK15064 134 RAGELLLGVGIPE---------EQHYGLMSEvapgwklRVLLAQALFSNPDILLLDEPTNNLDInTIR-----WLEDVLN 199
|
90
....*....|..
gi 447119240 202 KENMALVLITHD 213
Cdd:PRK15064 200 ERNSTMIIISHD 211
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
154-236 |
3.40e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.31 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 154 LSGGMSQRVMIAMAIACR---PKLLIADEPTTAL---DVtiqAQIIELLLELQQKENmALVLITHDLALVAEAAHKIIV- 226
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdDI---KKLLEVLQRLVDKGN-TVVVIEHNLDVIKTADYIIDLg 905
|
90
....*....|....
gi 447119240 227 ----MYAGQVVETG 236
Cdd:TIGR00630 906 peggDGGGTVVASG 919
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-237 |
3.80e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 41.34 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 20 FRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGRVMAEKlvfNGQ-DLQRISEKERRNLVGAEvAMIFQdp 98
Cdd:PRK13546 37 FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLS-PTVGKVDR---NGEvSVIAISAGLSGQLTGIE-NIEFK-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 99 mtslnpCYTVGFqimeaikvhqggnkstRRQRAIDLLNQVgipDPASRLDVYPHQ----LSGGMSQRVMIAMAIACRPKL 174
Cdd:PRK13546 110 ------MLCMGF----------------KRKEIKAMTPKI---IEFSELGEFIYQpvkkYSSGMRAKLGFSINITVNPDI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447119240 175 LIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVETGD 237
Cdd:PRK13546 165 LVIDEALSVGDQTFAQKCLDKIYEFKE-QNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGE 226
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
154-236 |
4.09e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 42.27 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLL--ELQQKENmalVLITHDLALVAEaAHKIIVMYAGQ 231
Cdd:PLN03232 741 ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMkdELKGKTR---VLVTNQLHFLPL-MDRIILVSEGM 816
|
....*
gi 447119240 232 VVETG 236
Cdd:PLN03232 817 IKEEG 821
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-226 |
4.23e-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: 42.08 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 29 SVKQGEVVGIVGESGSGKS--VSSLAimGLIDYPGRVMAEKLvfngqdlqRISEKERRnlVGAEVAMifqdpmtslnpcy 106
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTtfAKILA--GVLKPDEGEVDEDL--------KISYKPQY--ISPDYDG------------- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 107 TVGFQIMEAIKVHQGGNKstrrqraidLLNQVGIPDPASRL-DVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALD 185
Cdd:COG1245 417 TVEEFLRSANTDDFGSSY---------YKTEIIKPLGLEKLlDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 447119240 186 V---TIQAQIIELLLElqQKENMALVlITHDLALVAEAAHKIIV 226
Cdd:COG1245 488 VeqrLAVAKAIRRFAE--NRGKTAMV-VDHDIYLIDYISDRLMV 528
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
122-228 |
4.39e-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: 40.63 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 122 GNKSTRRQRAIDLLNQVGIPD------PASRLDVYPH--QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQII 193
Cdd:cd03222 32 GPNGTGKTTAVKILAGQLIPNgdndewDGITPVYKPQyiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAA 111
|
90 100 110
....*....|....*....|....*....|....*
gi 447119240 194 ELLLELQQKENMALVLITHDLALVAEAAHKIIVMY 228
Cdd:cd03222 112 RAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
26-224 |
6.05e-04 |
|
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: 40.70 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 26 ISYSVKQGEVVGIVGESGSGKSvsSLAIMGLIDYPGRVMAEKL-VFNGQDLQRISEKERRNLVGAEVAMIFQDPMTSLNP 104
Cdd:cd03270 14 VDVDIPRNKLVVITGVSGSGKS--SLAFDTIYAEGQRRYVESLsAYARQFLGQMDKPDVDSIEGLSPAIAIDQKTTSRNP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 105 CYTVGfQIMEAikvhqggNKSTR--------RQRaIDLLNQVGIPdpASRLDVYPHQLSGGMSQRVMIAMAIACRPK--L 174
Cdd:cd03270 92 RSTVG-TVTEI-------YDYLRllfarvgiRER-LGFLVDVGLG--YLTLSRSAPTLSGGEAQRIRLATQIGSGLTgvL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447119240 175 LIADEPTTALDVTIQAQIIELLLELQQKENmALVLITHDLALVAEAAHKI 224
Cdd:cd03270 161 YVLDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVVEHDEDTIRAADHVI 209
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
146-224 |
6.65e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 6.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 146 RLDVYP-----HQLSGGMSQRVMIA---MAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALV 217
Cdd:PRK00635 797 GLDYLPlgrplSSLSGGEIQRLKLAyelLAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTH-QGHTVVIIEHNMHVV 875
|
....*..
gi 447119240 218 AEAAHKI 224
Cdd:PRK00635 876 KVADYVL 882
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
26-234 |
9.28e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 41.26 E-value: 9.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYP-GRVMaeklvFNGQDLQRISEKERRNLVGaevaMIFQDPMTSLNp 104
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELErGRIL-----IDGCDISKFGLMDLRKVLG----IIPQAPVLFSG- 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 105 cyTVGFQiMEAIKVHQGGN--KSTRRQRAIDLL--NQVGIPDPASRLDvypHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
Cdd:PLN03130 1328 --TVRFN-LDPFNEHNDADlwESLERAHLKDVIrrNSLGLDAEVSEAG---ENFSVGQRQLLSLARALLRRSKILVLDEA 1401
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447119240 181 TTALDVTIQAQIIELLLELQQKENMalVLITHDLALVAEaAHKIIVMYAGQVVE 234
Cdd:PLN03130 1402 TAAVDVRTDALIQKTIREEFKSCTM--LIIAHRLNTIID-CDRILVLDAGRVVE 1452
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
23-212 |
1.19e-03 |
|
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: 40.50 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 23 VDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIdYPgrvmaeklVFNGqdlqRISEKERRNLVgaevaMIFQDPMTSL 102
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKS-SLFRILGEL-WP--------VYGG----RLTKPAKGKLF-----YVPQRPYMTL 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 103 NpcyTVGFQIMEAIKVHQGGNKSTRRQRAIDLLNQVGIPDPASR----------LDVyphqLSGGMSQRVMIAMAIACRP 172
Cdd:TIGR00954 529 G---TLRDQIIYPDSSEDMKRRGLSDKDLEQILDNVQLTHILEReggwsavqdwMDV----LSGGEKQRIAMARLFYHKP 601
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 447119240 173 KLLIADEPTTALDVTIQAQIIELLlelqQKENMALVLITH 212
Cdd:TIGR00954 602 QFAILDECTSAVSVDVEGYMYRLC----REFGITLFSVSH 637
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
154-217 |
1.76e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 39.93 E-value: 1.76e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447119240 154 LSGGMSQRVMIAmAIACRP-KLLIADEPTTALDVtiqaQIIELLLELQQKENMALVLITHDLALV 217
Cdd:PRK11147 441 LSGGERNRLLLA-RLFLKPsNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHDRQFV 500
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
26-216 |
2.34e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 38.70 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 26 ISYSVKQGEVVGIVGESGSGKSvsSL--AIMGLIdypgRVMAEKLVFNGQDLQRISEKERRNLVGAEVAMifqdpmtslN 103
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKT--TLlrLIAGLL----PPAAGTIKLDGGDIDDPDVAEACHYLGHRNAM---------K 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 104 PCYTVgfqiMEAIKVHQGgNKSTRRQRAIDLLNQVGIPDPASRLDVYphqLSGGMSQRVMIA-MAIACRPkLLIADEPTT 182
Cdd:PRK13539 86 PALTV----AENLEFWAA-FLGGEELDIAAALEAVGLAPLAHLPFGY---LSAGQKRRVALArLLVSNRP-IWILDEPTA 156
|
170 180 190
....*....|....*....|....*....|....*
gi 447119240 183 ALDVTIQAQIIELLLElQQKENMALVLITH-DLAL 216
Cdd:PRK13539 157 ALDAAAVALFAELIRA-HLAQGGIVIAATHiPLGL 190
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
23-233 |
2.91e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.39 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLiDYpGRVMAEKLVFNGQ--DLQRISEKerrnlVGAEVAMIFQDPMT 100
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGR-SY-GRNISGTVFKDGKevDVSTVSDA-----IDAGLAYVTEDRKG 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 101 S-LNPCYTVGFQIMEAI--KVHQGG--NKSTRRQRAIDLLNQVGIPDPasrlDVYPH--QLSGGMSQRVMIAMAIACRPK 173
Cdd:NF040905 349 YgLNLIDDIKRNITLANlgKVSRRGviDENEEIKVAEEYRKKMNIKTP----SVFQKvgNLSGGNQQKVVLSKWLFTDPD 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 174 LLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
Cdd:NF040905 425 VLILDEPTRGIDVGAKYEIYTIINEL-AAEGKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
154-233 |
3.93e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 38.72 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVtiqaQIIELLlelqqkeNMAL-------VLITHDLALVAEAAHKIIV 226
Cdd:PRK15064 439 LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDM----ESIESL-------NMALekyegtlIFVSHDREFVSSLATRIIE 507
|
....*..
gi 447119240 227 MYAGQVV 233
Cdd:PRK15064 508 ITPDGVV 514
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
152-253 |
4.70e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 38.69 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 152 HQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkenmALVLITHDLALVAEAAHKIIVMYAGQ 231
Cdd:PLN03073 626 YTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQG----GVLMVSHDEHLISGSVDELWVVSEGK 701
|
90 100
....*....|....*....|..
gi 447119240 232 VvetgdahAIFHAPRHPYTQAL 253
Cdd:PLN03073 702 V-------TPFHGTFHDYKKTL 716
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
152-216 |
7.98e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 37.72 E-value: 7.98e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447119240 152 HQLSGGMsQRVM-IAMAIA---CRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLAL 216
Cdd:COG1106 201 SEESDGT-KRLLaLAGALLdalAKGGVLLIDEIEASLHPSLLRKLLKLFLDLANKNNAQLIFTTHSTEL 268
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
15-97 |
8.04e-03 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 37.86 E-value: 8.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447119240 15 DESAPFrAVDRISYSVKQGEVVGIVGESGSGKsvSSLA--IMGLidYP---GRVMaeklvFNGqdlQRISEKER---RNL 86
Cdd:COG4615 341 DGDEGF-TLGPIDLTIRRGELVFIVGGNGSGK--STLAklLTGL--YRpesGEIL-----LDG---QPVTADNReayRQL 407
|
90
....*....|.
gi 447119240 87 VGAevamIFQD 97
Cdd:COG4615 408 FSA----VFSD 414
|
|
| |
