|
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: 702.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 1 MALLNVDKLSVHFGDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDFPGRVMAEKLEFNGQDLKRISE 80
Cdd:PRK11022 1 MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 81 KERRSLVGSEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQ 160
Cdd:PRK11022 81 KERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 161 RVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKD 240
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 241 IFRAPRHPYTQALLRALPEFAQDKARLASLPGVVPGKYDRPTGCLLNPRCPYATDKCREQEPELNTVdGGRQSKCHYPLD 320
Cdd:PRK11022 241 IFRAPRHPYTQALLRALPEFAQDKARLASLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPALNML-AGRQSKCHYPLD 319
|
....*..
gi 521291413 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: 521.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKLSVHFGDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDFPGRVmAEKLEFNGQDLKRISEKE 82
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGIT-SGEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 83 RRSLVGSEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQRV 162
Cdd:COG0444 80 LRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 163 MIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDIF 242
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 243 RAPRHPYTQALLRALPEFAQDKARLASLPGVVPGKYDRPTGCLLNPRCPYATDKCREQEPELNTVDGGRQSKCHYPLDDA 322
Cdd:COG0444 240 ENPRHPYTRALLSSIPRLDPDGRRLIPIPGEPPSLLNPPSGCRFHPRCPYAMDRCREEEPPLREVGPGHRVACHLYEEEA 319
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-259 |
3.05e-150 |
|
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: 432.57 E-value: 3.05e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 1 MALLNVDKLSVHFGDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDFPGRVMAEKLEFNGQDLKRISE 80
Cdd:COG4172 4 MPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 81 KERRSLVGSEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQ 160
Cdd:COG4172 84 RELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 161 RVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKD 240
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAE 243
|
250
....*....|....*....
gi 521291413 241 IFRAPRHPYTQALLRALPE 259
Cdd:COG4172 244 LFAAPQHPYTRKLLAAEPR 262
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-319 |
4.59e-133 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 381.56 E-value: 4.59e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 1 MALLNVDKLSVHFGDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDFPGRVMAEKLEFNGQDLKRISE 80
Cdd:COG4170 1 MPLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADRFRWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 81 KERRSLVGSEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNK-----KTRRQRAIDLLNQVGIPDPASRLDVYPHQLS 155
Cdd:COG4170 81 RERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIPSWTFKGKwwqrfKWRKKRAIELLHRVGIKDHKDIMNSYPHELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 156 GGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVET 235
Cdd:COG4170 161 EGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 236 GEAKDIFRAPRHPYTQALLRALPEFAQD---KARLASLPGVVPGKYDRPTGCLLNPRCPYATDKCREQePELNTVDgGRQ 312
Cdd:COG4170 241 GPTEQILKSPHHPYTKALLRSMPDFRQPlphKSRLNTLPGSIPPLQHLPIGCRLGPRCPYAQKKCVET-PRLRKIK-GHE 318
|
....*..
gi 521291413 313 SKCHYPL 319
Cdd:COG4170 319 FACHFPL 325
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-321 |
8.85e-127 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 365.59 E-value: 8.85e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 1 MALLNVDKLSVHFGDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDFPGRVMAEKLeFNGQDLKRISE 80
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSAT-FNGREILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 81 KERRSLVGSEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQ 160
Cdd:PRK09473 89 KELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGGMRQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 161 RVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKD 240
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 241 IFRAPRHPYTQALLRALPEFAQDKARLASLPGVVPGKYDRPTGCLLNPRCPYATDKCREqEPELNTVDGGRQSKCHYPLD 320
Cdd:PRK09473 249 VFYQPSHPYSIGLLNAVPRLDAEGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEICSS-APPLEEFGPGRLRACFKPVE 327
|
.
gi 521291413 321 D 321
Cdd:PRK09473 328 E 328
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-323 |
3.21e-117 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 341.33 E-value: 3.21e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKLSVHFgDVGSEF--------RAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDfP--GRVmaeklEFNG 72
Cdd:COG4608 7 LLEVRDLKKHF-PVRGGLfgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEE-PtsGEI-----LFDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 73 QDLKRISEKERRSLvGSEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGI-PDPASRldvYP 151
Cdd:COG4608 80 QDITGLSGRELRPL-RRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLrPEHADR---YP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 152 HQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQ 231
Cdd:COG4608 156 HEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 232 VVETGEAKDIFRAPRHPYTQALLRA--LPEFAQDKARLAsLPGVVPGKYDRPTGCLLNPRCPYATDKCREQEPELNTVDG 309
Cdd:COG4608 236 IVEIAPRDELYARPLHPYTQALLSAvpVPDPERRRERIV-LEGDVPSPLNPPSGCRFHTRCPYAQDRCATEEPPLREVGP 314
|
330
....*....|....
gi 521291413 310 GRQSKCHYPLDDAG 323
Cdd:COG4608 315 GHQVACHLAEEGSG 328
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-236 |
2.55e-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: 330.24 E-value: 2.55e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKLSVHFGDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLidfpGRVMAEKLEFNGQDLKRISEKE 82
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGL----LKPTSGSIIFDGKDLLKLSRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 83 RRSLvGSEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNqVGIPDPASRLDVYPHQLSGGMSQRV 162
Cdd:cd03257 77 RKIR-RKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLL-VGVGLPEEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521291413 163 MIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-259 |
8.64e-107 |
|
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: 321.08 E-value: 8.64e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKLSVHFG-DVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDfP--GRVmaeklEFNGQDLKRIS 79
Cdd:COG1123 260 LLEVRNLSKRYPvRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR-PtsGSI-----LFDGKDLTKLS 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 80 EKERRSLvGSEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPdpASRLDVYPHQLSGGMS 159
Cdd:COG1123 334 RRSLREL-RRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLP--PDLADRYPHELSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 160 QRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAK 239
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTE 490
|
250 260
....*....|....*....|
gi 521291413 240 DIFRAPRHPYTQALLRALPE 259
Cdd:COG1123 491 EVFANPQHPYTRALLAAVPS 510
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-320 |
1.14e-106 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 314.43 E-value: 1.14e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 1 MALLNVDKLSVHFGDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDFPGRVMAEKLEFNGQDLKRISE 80
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 81 KERRSLVGSEVAMIFQDPMTSLNPCYTVGFQIMEAI-----KVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLS 155
Cdd:PRK15093 81 RERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIpgwtyKGRWWQRFGWRKRRAIELLHRVGIKDHKDAMRSFPYELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 156 GGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVET 235
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 236 GEAKDIFRAPRHPYTQALLRALPEFAQD---KARLASLPGVVPGKYDRPTGCLLNPRCPYATDKCREQePELNTVDgGRQ 312
Cdd:PRK15093 241 APSKELVTTPHHPYTQALIRAIPDFGSAmphKSRLNTLPGAIPLLEHLPIGCRLGPRCPYAQRECIET-PRLTGAK-NHL 318
|
....*...
gi 521291413 313 SKCHYPLD 320
Cdd:PRK15093 319 YACHFPLN 326
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-259 |
7.47e-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: 306.61 E-value: 7.47e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKLSVHF-------GDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDFPGRVMaekleFNGQDL 75
Cdd:COG4172 275 LLEARDLKVWFpikrglfRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEIR-----FDGQDL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 76 KRISEKERRSLvGSEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQ-GGNKKTRRQRAIDLLNQVGIpDPASRlDVYPHQL 154
Cdd:COG4172 350 DGLSRRALRPL-RRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGL-DPAAR-HRYPHEF 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 155 SGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVE 234
Cdd:COG4172 427 SGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVE 506
|
250 260
....*....|....*....|....*
gi 521291413 235 TGEAKDIFRAPRHPYTQALLRALPE 259
Cdd:COG4172 507 QGPTEQVFDAPQHPYTRALLAAAPL 531
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-271 |
2.52e-99 |
|
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: 301.82 E-value: 2.52e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 2 ALLNVDKLSVHFGdvGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDFPGRVmAEKLEFNGQDLKRISEK 81
Cdd:COG1123 3 PLLEVRDLSVRYP--GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRI-SGEVLLDGRDLLELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 82 ERrslvGSEVAMIFQDPMTSLNPcYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQR 161
Cdd:COG1123 80 LR----GRRIGMVFQDPMTQLNP-VTVGDQIAEALEN-LGLSRAEARARVLELLEAVGL---ERRLDRYPHQLSGGQRQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 162 VMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDI 241
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
250 260 270
....*....|....*....|....*....|
gi 521291413 242 FRAPRhpytqaLLRALPEFAQDKARLASLP 271
Cdd:COG1123 231 LAAPQ------ALAAVPRLGAARGRAAPAA 254
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-259 |
2.41e-93 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 286.99 E-value: 2.41e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 1 MALLNVDKLSVHFGDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDFPGRV-MAEKLEFNGQDLKRIS 79
Cdd:PRK15134 3 QPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVyPSGDIRFHGESLLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 80 EKERRSLVGSEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMS 159
Cdd:PRK15134 83 EQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGGER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 160 QRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAK 239
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAA 242
|
250 260
....*....|....*....|
gi 521291413 240 DIFRAPRHPYTQALLRALPE 259
Cdd:PRK15134 243 TLFSAPTHPYTQKLLNSEPS 262
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-259 |
2.08e-91 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 284.83 E-value: 2.08e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKLSVHFGDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDFPG-RVMAEKLEF---NGQ--DLK 76
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGgLVQCDKMLLrrrSRQviELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 77 RISEKERRSLVGSEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSG 156
Cdd:PRK10261 92 EQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 157 GMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
|
250 260
....*....|....*....|...
gi 521291413 237 EAKDIFRAPRHPYTQALLRALPE 259
Cdd:PRK10261 252 SVEQIFHAPQHPYTRALLAAVPQ 274
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
21-326 |
3.71e-91 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 274.92 E-value: 3.71e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 21 RAVDRVSYSVSQGEVVGIVGESGSGKSvsSLAIM-GLIDFPgrvMAEKLEFNGQDLKRISEKERRSLvGSEVAMIFQDPM 99
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKS--TLARLlTMIETP---TGGELYYQGQDLLKADPEAQKLL-RQKIQIVFQNPY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 100 TSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGI-PDPASRldvYPHQLSGGMSQRVMIAMAIACQPKLLIAD 178
Cdd:PRK11308 103 GSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLrPEHYDR---YPHMFSGGQRQRIAIARALMLDPDVVVAD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 179 EPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDIFRAPRHPYTQALLRALP 258
Cdd:PRK11308 180 EPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLSATP 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521291413 259 EFAQDKARLA-SLPGVVPGKYDRPTGCLLNPRCPYATDKCREQEPELNTVDgGRQSKCHYPLDDAGRPT 326
Cdd:PRK11308 260 RLNPDDRRERiKLTGELPSPLNPPPGCAFNARCPRAFGRCRQEQPQLRDYD-GRLVACFAVEQDENPQA 327
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-260 |
1.40e-90 |
|
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: 270.52 E-value: 1.40e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKLSVHFGDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLI-DFPGRVMaekleFNGQDLKRISEK 81
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLErPWSGEVT-----FDGRPVTRRRRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 82 ERRSlvgsEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHqggNKKTRRQRAIDLLNQVGIPdpASRLDVYPHQLSGGMSQR 161
Cdd:COG1124 76 AFRR----RVQMVFQDPYASLHPRHTVDRILAEPLRIH---GLPDREERIAELLEQVGLP--PSFLDRYPHQLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 162 VMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDI 241
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
250
....*....|....*....
gi 521291413 242 FRAPRHPYTQALLRALPEF 260
Cdd:COG1124 227 LAGPKHPYTRELLAASLAF 245
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-305 |
3.82e-84 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 257.33 E-value: 3.82e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKLSVHFgDV----------GSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDFP-GRVMaekleFN 71
Cdd:PRK15079 8 LLEVADLKVHF-DIkdgkqwfwqpPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATdGEVA-----WL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 72 GQDLKRISEKERRSlVGSEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGG-NKKTRRQRAIDLLNQVGI-PDPASRldv 149
Cdd:PRK15079 82 GKDLLGMKDDEWRA-VRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKlSRQEVKDRVKAMMLKVGLlPNLINR--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 150 YPHQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYA 229
Cdd:PRK15079 158 YPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYL 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521291413 230 GQVVETGEAKDIFRAPRHPYTQALLRALPEFAQDKARLAS---LPGVVPGKYDRPTGCLLNPRCPYATDKCREQEPELN 305
Cdd:PRK15079 238 GHAVELGTYDEVYHNPLHPYTKALMSAVPIPDPDLERNKTiqlLEGELPSPINPPSGCVFRTRCPIAGPECAKTRPVLE 316
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
22-256 |
2.24e-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: 238.81 E-value: 2.24e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 22 AVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDFPGRVMAEKLEFNGQDLKRISekerrsLVGSEVAMIFQDPMTS 101
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTQTSGEILLDGRPLLPLS------IRGRHIATIMQNPRTA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 102 LNPCYTVGFQIMEAIKVHqGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQRVMIAMAIACQPKLLIADEPT 181
Cdd:TIGR02770 75 FNPLFTMGNHAIETLRSL-GKLSKQARALILEALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPT 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521291413 182 TALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDIFRAPRHPYTQALLRA 256
Cdd:TIGR02770 154 TDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLSA 228
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-254 |
7.16e-66 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 208.15 E-value: 7.16e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 1 MALLNVDKLSVHFGDVGSEFR-----AVDRVSYSVSQGEVVGIVGESGSGKSvsSLAIM--GLIdfpgRVMAEKLEFNGQ 73
Cdd:COG4167 2 SALLEVRNLSKTFKYRTGLFRrqqfeAVKPVSFTLEAGQTLAIIGENGSGKS--TLAKMlaGII----EPTSGEILINGH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 74 DLKRISEKERRSLVgsevAMIFQDPMTSLNPCYTVGfQIMEA-IKVHQGGNKKTRRQRAIDLLNQVGI-PDPAsrlDVYP 151
Cdd:COG4167 76 KLEYGDYKYRCKHI----RMIFQDPNTSLNPRLNIG-QILEEpLRLNTDLTAEEREERIFATLRLVGLlPEHA---NFYP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 152 HQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQ 231
Cdd:COG4167 148 HMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGE 227
|
250 260
....*....|....*....|...
gi 521291413 232 VVETGEAKDIFRAPRHPYTQALL 254
Cdd:COG4167 228 VVEYGKTAEVFANPQHEVTKRLI 250
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
2-253 |
8.42e-66 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 207.74 E-value: 8.42e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 2 ALLNVDKLSVHFGDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSvSSLAIMGLIDFP--GRVMAEKLEFNGQDLKRIS 79
Cdd:COG4107 7 PLLSVRGLSKRYGPGCGTVVACRDVSFDLYPGEVLGIVGESGSGKS-TLLKCLYFDLAPtsGSVYYRDRDGGPRDLFALS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 80 EKERRSLVGSEVAMIFQDPMTSLNPCYTVGFQIMEaiKVHQGGNK--KTRRQRAIDLLNQVGIPdpASRLDVYPHQLSGG 157
Cdd:COG4107 86 EAERRRLRRTDWGMVYQNPRDGLRMDVSAGGNIAE--RLMAAGERhyGDIRARALEWLERVEIP--LERIDDLPRTFSGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 158 MSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGE 237
Cdd:COG4107 162 MQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKNGRVVESGL 241
|
250
....*....|....*.
gi 521291413 238 AKDIFRAPRHPYTQAL 253
Cdd:COG4107 242 TDQVLEDPQHPYTQLL 257
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-255 |
3.67e-64 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 211.49 E-value: 3.67e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKLSVHFGDVGSEFR-------AVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDFPGRVmaeklEFNGQDL 75
Cdd:PRK15134 275 LLDVEQLQVAFPIRKGILKrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEI-----WFDGQPL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 76 KRISekeRRSL--VGSEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGG-NKKTRRQRAIDLLNQVGIpDPASRlDVYPH 152
Cdd:PRK15134 350 HNLN---RRQLlpVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTlSAAQREQQVIAVMEEVGL-DPETR-HRYPA 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 153 QLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQV 232
Cdd:PRK15134 425 EFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEV 504
|
250 260
....*....|....*....|...
gi 521291413 233 VETGEAKDIFRAPRHPYTQALLR 255
Cdd:PRK15134 505 VEQGDCERVFAAPQQEYTRQLLA 527
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-234 |
8.51e-61 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 193.72 E-value: 8.51e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 2 ALLNVDKLSVHFGDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSvSSLAIMGLIDFP--GRVMaekleFNGQDLKRIS 79
Cdd:COG1136 3 PLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKS-TLLNILGGLDRPtsGEVL-----IDGQDISSLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 80 EKERRSLVGSEVAMIFQDPmtSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMS 159
Cdd:COG1136 77 ERELARLRRRHIGFVFQFF--NLLPELTALENVALPLLL-AGVSRKERRERARELLERVGLGD---RLDHRPSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521291413 160 QRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALvAEAAHKIIVMYAGQVVE 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 |
2.80e-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: 2.80e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 4 LNVDKLSVHFGDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSvSSLAIMGLIDFP--GRVmaeklEFNGQDLKRISEK 81
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS-TLLNILGGLDRPtsGEV-----RVDGTDISKLSEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 82 ERRSLVGSEVAMIFQDPmtSLNPCYTVgFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMSQR 161
Cdd:cd03255 75 ELAAFRRRHIGFVFQSF--NLLPDLTA-LENVELPLLLAGVPKKERRERAEELLERVGLGD---RLNHYPSELSGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521291413 162 VMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLaLVAEAAHKIIVMYAGQV 232
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
13-258 |
1.21e-59 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 201.62 E-value: 1.21e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 13 FGDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDfpgrVMAEKLEFNGQDLKRISEKERRSLvGSEVA 92
Cdd:PRK10261 330 LNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVE----SQGGEIIFNGQRIDTLSPGKLQAL-RRDIQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 93 MIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGI-PDPASRldvYPHQLSGGMSQRVMIAMAIACQ 171
Cdd:PRK10261 405 FIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLlPEHAWR---YPHEFSGGQRQRICIARALALN 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 172 PKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDIFRAPRHPYTQ 251
Cdd:PRK10261 482 PKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTR 561
|
....*..
gi 521291413 252 ALLRALP 258
Cdd:PRK10261 562 KLMAAVP 568
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-277 |
8.87e-59 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 192.21 E-value: 8.87e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 6 VDKLSVHFGDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSvsSLA--IMGLiDFP--GRVmaeklEFNGQDLKRISEK 81
Cdd:COG1135 4 LENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKS--TLIrcINLL-ERPtsGSV-----LVDGVDLTALSER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 82 ERRSL---VGsevaMIFQdpmtslnpcytvGFQIMEAIKV---------HQGGNKKTRRQRAIDLLNQVGIPDpasRLDV 149
Cdd:COG1135 76 ELRAArrkIG----MIFQ------------HFNLLSSRTVaenvalpleIAGVPKAEIRKRVAELLELVGLSD---KADA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 150 YPHQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYA 229
Cdd:COG1135 137 YPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLEN 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 521291413 230 GQVVETGEAKDIFRAPRHPYTQALLRALPEFAQDKARLASLPGVVPGK 277
Cdd:COG1135 217 GRIVEQGPVLDVFANPQSELTRRFLPTVLNDELPEELLARLREAAGGG 264
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
23-256 |
6.53e-58 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 187.21 E-value: 6.53e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 23 VDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDfPG-RVMAEKLEFNGQDLkrisekERRSLVGSEVAMIFQDPMTS 101
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILP-AGvRQTAGRVLLDGKPV------APCALRGRKIATIMQNPRSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 102 LNPCYTVGFQIMEAIKVHqggNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQRVMIAMAIACQPKLLIADEPT 181
Cdd:PRK10418 92 FNPLHTMHTHARETCLAL---GKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521291413 182 TALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDIFRAPRHPYTQALLRA 256
Cdd:PRK10418 169 TDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-246 |
7.12e-58 |
|
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: 186.63 E-value: 7.12e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKLSVHFGDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSvSSLAIMGLIDFP--GRVmaeklEFNGQDLKRISE 80
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKS-TLIRCINGLERPtsGSV-----LVDGTDLTLLSG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 81 KERRSLvGSEVAMIFQ--DPMTSLnpcyTVGFQIMEAIKVHqGGNKKTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGM 158
Cdd:cd03258 75 KELRKA-RRRIGMIFQhfNLLSSR----TVFENVALPLEIA-GVPKAEIEERVLELLELVGLEDKA---DAYPAQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 159 SQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEA 238
Cdd:cd03258 146 KQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTV 225
|
....*...
gi 521291413 239 KDIFRAPR 246
Cdd:cd03258 226 EEVFANPQ 233
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-257 |
1.49e-52 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 172.87 E-value: 1.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKLSVHFGDvgseFRAVDRVSYSVSQGEVVGIVGESGSGKSvsSL--AIMGLIDF-PGRVmaeklEFNGQDLkRIS 79
Cdd:COG1126 1 MIEIENLHKSFGD----LEVLKGISLDVEKGEVVVIIGPSGSGKS--TLlrCINLLEEPdSGTI-----TVDGEDL-TDS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 80 EKERRSLVgSEVAMIFQdpmtSLN--PCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGG 157
Cdd:COG1126 69 KKDINKLR-RKVGMVFQ----QFNlfPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLAD---KADAYPAQLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 158 MSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGE 237
Cdd:COG1126 141 QQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDL-AKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGP 219
|
250 260
....*....|....*....|
gi 521291413 238 AKDIFRAPRHPYTQALLRAL 257
Cdd:COG1126 220 PEEFFENPQHERTRAFLSKV 239
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-260 |
1.77e-52 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 173.72 E-value: 1.77e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 1 MALLNVDKLSVHFGDVG----SEFRAV-DRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLiDFP--GRVmaeklEFNGQ 73
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGGlsgkHQHQTVlNNVSLSLKSGETVALLGRSGCGKSTLARLLVGL-ESPsqGNV-----SWRGE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 74 DLKRISEKERRSLVGsEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDpaSRLDVYPHQ 153
Cdd:PRK10419 75 PLAKLNRAQRKAFRR-DIQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDD--SVLDKRPPQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 154 LSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVV 233
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
250 260
....*....|....*....|....*...
gi 521291413 234 ETGEAKDIFRApRHPYTQALLRA-LPEF 260
Cdd:PRK10419 232 ETQPVGDKLTF-SSPAGRVLQNAvLPAF 258
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-253 |
5.14e-51 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 169.72 E-value: 5.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKLSVHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKS--VSSLAIM-----GLIDFPGRvmaeklEFNGQDL 75
Cdd:PRK11701 6 LLSVRGLTKLYGPR----KGCRDVSFDLYPGEVLGIVGESGSGKTtlLNALSARlapdaGEVHYRMR------DGQLRDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 76 KRISEKERRSLVGSEVAMIFQDPMTSLNPCYTVGFQIME---AIKVHQGGNKktrRQRAIDLLNQVGIPdpASRLDVYPH 152
Cdd:PRK11701 76 YALSEAERRRLLRTEWGFVHQHPRDGLRMQVSAGGNIGErlmAVGARHYGDI---RATAGDWLERVEID--AARIDDLPT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 153 QLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQV 232
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
250 260
....*....|....*....|.
gi 521291413 233 VETGEAKDIFRAPRHPYTQAL 253
Cdd:PRK11701 231 VESGLTDQVLDDPQHPYTQLL 251
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2-262 |
4.08e-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: 167.67 E-value: 4.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 2 ALLNVDKLSVHF---GDVGSEFRA--VDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLidfpGRVMAEKLEFNGQDLK 76
Cdd:TIGR02769 1 SLLEVRDVTHTYrtgGLFGAKQRApvLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGL----EKPAQGTVSFRGQDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 77 RISEKERRSlVGSEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDpaSRLDVYPHQLSG 156
Cdd:TIGR02769 77 QLDRKQRRA-FRRDVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRS--EDADKLPRQLSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 157 GMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:TIGR02769 154 GQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEEC 233
|
250 260
....*....|....*....|....*..
gi 521291413 237 EAKDIFrAPRHPYTQALLRA-LPEFAQ 262
Cdd:TIGR02769 234 DVAQLL-SFKHPAGRNLQSAvLPEHPV 259
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-246 |
4.25e-50 |
|
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: 166.35 E-value: 4.25e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 4 LNVDKLSVHFGDvgsEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIdFP--GRVmaeklEFNGQDLKRISEK 81
Cdd:COG1122 1 IELENLSFSYPG---GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLL-KPtsGEV-----LVDGKDITKKNLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 82 ERRSLVGsevaMIFQDPMTSL-NPcyTVGFQIMEAIKvHQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQ 160
Cdd:COG1122 72 ELRRKVG----LVFQNPDDQLfAP--TVEEDVAFGPE-NLGLPREEIRERVEEALELVGLEHLADR---PPHELSGGQKQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 161 RVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKD 240
Cdd:COG1122 142 RVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNK-EGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPRE 220
|
....*.
gi 521291413 241 IFRAPR 246
Cdd:COG1122 221 VFSDYE 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-238 |
1.02e-48 |
|
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: 162.99 E-value: 1.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 2 ALLNVDKLSVHFGDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSvSSLAIMGLIDFP--GRVMAeklefNGQDLKRIS 79
Cdd:COG4181 7 PIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKS-TLLGLLAGLDRPtsGTVRL-----AGQDLFALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 80 EKERRSLVGSEVAMIFQD----P-MTSL-N---PCYTVGFQimEAikvhqggnkktrRQRAIDLLNQVGIpdpASRLDVY 150
Cdd:COG4181 81 EDARARLRARHVGFVFQSfqllPtLTALeNvmlPLELAGRR--DA------------RARARALLERVGL---GHRLDHY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 151 PHQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALvAEAAHKIIVMYAG 230
Cdd:COG4181 144 PAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPAL-AARCDRVLRLRAG 222
|
....*...
gi 521291413 231 QVVETGEA 238
Cdd:COG4181 223 RLVEDTAA 230
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-254 |
1.51e-48 |
|
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: 162.46 E-value: 1.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 2 ALLNVDKLSVHFGDvgsefRAV-DRVSYSVSQGEVVGIVGESGSGKSVssL--AIMGLIDfP--GRVmaeklEFNGQDLK 76
Cdd:COG1127 4 PMIEVRNLTKSFGD-----RVVlDGVSLDVPRGEILAIIGGSGSGKSV--LlkLIIGLLR-PdsGEI-----LVDGQDIT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 77 RISEKERRSLVgSEVAMIFQ-----DPMTSL-NpcytVGFQIMEaikvHQGGNKKTRRQRAIDLLNQVGIPDPASRldvY 150
Cdd:COG1127 71 GLSEKELYELR-RRIGMLFQggalfDSLTVFeN----VAFPLRE----HTDLSEAEIRELVLEKLELVGLPGAADK---M 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 151 PHQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAG 230
Cdd:COG1127 139 PSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADG 218
|
250 260
....*....|....*....|....
gi 521291413 231 QVVETGEAKDIFRAPrHPYTQALL 254
Cdd:COG1127 219 KIIAEGTPEELLASD-DPWVRQFL 241
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-267 |
2.78e-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: 2.78e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 1 MALLNVDKLSVHFGDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSvsSL--AIMGLID-FPGRVmaeklEFNGQDLKR 77
Cdd:COG1116 5 APALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKS--TLlrLIAGLEKpTSGEV-----LVDGKPVTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 78 isekerrslVGSEVAMIFQDPmtSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGG 157
Cdd:COG1116 78 ---------PGPDRGVVFQEP--ALLPWLTVLDNVALGLEL-RGVPKAERRERARELLELVGL---AGFEDAYPHQLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 158 MSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDlalVAEA---AHKIIVMYA--GQV 232
Cdd:COG1116 143 MRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHD---VDEAvflADRVVVLSArpGRI 219
|
250 260 270
....*....|....*....|....*....|....*
gi 521291413 233 VETgEAKDIFRaPRHPytqaLLRALPEFAQDKARL 267
Cdd:COG1116 220 VEE-IDVDLPR-PRDR----ELRTSPEFAALRAEI 248
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
2-257 |
4.38e-48 |
|
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: 161.92 E-value: 4.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 2 ALLNVDKLSVHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKS--VSSLAIMGLIDfPGRVMAEKLEFNGQDLKRIS 79
Cdd:TIGR02323 2 PLLQVSGLSKSYGGG----KGCRDVSFDLYPGEVLGIVGESGSGKStlLGCLAGRLAPD-HGTATYIMRSGAELELYQLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 80 EKERRSLVGSEVAMIFQDPMTSLNPCYTVGFQIME---AIKVHQGGNKktrRQRAIDLLNQVGIPdpASRLDVYPHQLSG 156
Cdd:TIGR02323 77 EAERRRLMRTEWGFVHQNPRDGLRMRVSAGANIGErlmAIGARHYGNI---RATAQDWLEEVEID--PTRIDDLPRAFSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 157 GMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:TIGR02323 152 GMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
250 260
....*....|....*....|.
gi 521291413 237 EAKDIFRAPRHPYTQALLRAL 257
Cdd:TIGR02323 232 LTDQVLDDPQHPYTQLLVSSI 252
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-235 |
6.71e-48 |
|
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: 160.33 E-value: 6.71e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 4 LNVDKLSVHFGDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSvSSLAIMGLIDFP--GRVmaeklEFNGQDLKRisek 81
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKS-TLLRIIAGLERPtsGEV-----LVDGEPVTG---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 82 errslVGSEVAMIFQDPmtSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQR 161
Cdd:cd03293 71 -----PGPDRGYVFQQD--ALLPWLTVLDNVALGLEL-QGVPKAEARERAEELLELVGLSGFENA---YPHQLSGGMRQR 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521291413 162 VMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDlalVAEA---AHKIIVMYA--GQVVET 235
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHD---IDEAvflADRVVVLSArpGRIVAE 215
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-249 |
6.47e-47 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 161.80 E-value: 6.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 1 MALLNVDKLSVHFGDvgseFRAVDRVSYSVSQGEVVGIVGESGSGKSvsSL--AIMGLIDfP--GRVMaekleFNGQDLK 76
Cdd:COG3842 3 MPALELENVSKRYGD----VTALDDVSLSIEPGEFVALLGPSGCGKT--TLlrMIAGFET-PdsGRIL-----LDGRDVT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 77 RISEKERRslvgseVAMIFQDP-----MTSL-NpcytVGFqimeAIKVhQGGNKKTRRQRAIDLLNQVGIPDPASRldvY 150
Cdd:COG3842 71 GLPPEKRN------VGMVFQDYalfphLTVAeN----VAF----GLRM-RGVPKAEIRARVAELLELVGLEGLADR---Y 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 151 PHQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLalvAEA---AHKIIVM 227
Cdd:COG3842 133 PHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQ---EEAlalADRIAVM 209
|
250 260
....*....|....*....|..
gi 521291413 228 YAGQVVETGEAKDIFRAPRHPY 249
Cdd:COG3842 210 NDGRIEQVGTPEEIYERPATRF 231
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
3-271 |
3.13e-46 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 159.58 E-value: 3.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKlsvHFGDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSvSSLAIMGLIDFP--GRVMAeklefNGQDLKRISE 80
Cdd:PRK11153 4 LKNISK---VFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKS-TLIRCINLLERPtsGRVLV-----DGQDLTALSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 81 KE----RRSlvgseVAMIFQDpmTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSG 156
Cdd:PRK11153 75 KElrkaRRQ-----IGMIFQH--FNLLSSRTVFDNVALPLEL-AGTPKAEIKARVTELLELVGLSDKA---DRYPAQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 157 GMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:PRK11153 144 GQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQG 223
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 521291413 237 EAKDIFRAPRHPYTQALLRA-----LPEfaQDKARLASLP 271
Cdd:PRK11153 224 TVSEVFSHPKHPLTREFIQStlhldLPE--DYLARLQAEP 261
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-249 |
9.91e-46 |
|
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: 155.35 E-value: 9.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 6 VDKLSVHFGDvgsefRAV-DRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDfP--GRVmaeklEFNGQDLKRISEKE 82
Cdd:cd03261 3 LRGLTKSFGG-----RTVlKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLR-PdsGEV-----LIDGEDISGLSEAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 83 RRSLvGSEVAMIFQDP--MTSLNPCYTVGFQIMEaikvHQGGNKKTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQ 160
Cdd:cd03261 72 LYRL-RRRMGMLFQSGalFDSLTVFENVAFPLRE----HTRLSEEEIREIVLEKLEAVGLRGAE---DLYPAELSGGMKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 161 RVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKD 240
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEE 223
|
....*....
gi 521291413 241 IFRAPrHPY 249
Cdd:cd03261 224 LRASD-DPL 231
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-241 |
1.16e-45 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 154.84 E-value: 1.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 4 LNVDKLSVHFGDvgseFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDfP--GRVmaeklEFNGQDLKRISEK 81
Cdd:COG1131 1 IEVRGLTKRYGD----KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLR-PtsGEV-----RVLGEDVARDPAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 82 ERRSlvgseVAMIFQDPmtSLNPCYTVGfQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMSQR 161
Cdd:COG1131 71 VRRR-----IGYVPQEP--ALYPDLTVR-ENLRFFARLYGLPRKEARERIDELLELFGLTD---AADRKVGTLSGGMKQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 162 VMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDI 241
Cdd:COG1131 140 LGLALALLHDPELLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-231 |
2.00e-45 |
|
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: 153.78 E-value: 2.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 6 VDKLSVHFGDVGSEfrAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLI-DFPGRVMaekleFNGQDLKRISEKERR 84
Cdd:cd03225 2 LKNLSFSYPDGARP--ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLgPTSGEVL-----VDGKDLTKLSLKELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 85 SLVGsevaMIFQDPMTSL-NPcyTVGFQIMEAIKvHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVM 163
Cdd:cd03225 75 RKVG----LVFQNPDDQFfGP--TVEEEVAFGLE-NLGLPEEEIEERVEEALELVGL---EGLRDRSPFTLSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521291413 164 IAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALILITHDLALVAEAAHKIIVMYAGQ 231
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-254 |
1.69e-44 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 153.02 E-value: 1.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKLSVHFGDVGSEFR-----AVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLID-FPGRVMAEKLEFNGQDLK 76
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGWFRrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEpTSGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 77 RISEKERrslvgsevaMIFQDPMTSLNPCYTVGfQIMEA-IKVHQGGNKKTRRQRAIDLLNQVGI-PDPASrldVYPHQL 154
Cdd:PRK15112 84 YRSQRIR---------MIFQDPSTSLNPRQRIS-QILDFpLRLNTDLEPEQREKQIIETLRQVGLlPDHAS---YYPHML 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 155 SGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVE 234
Cdd:PRK15112 151 APGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVE 230
|
250 260
....*....|....*....|
gi 521291413 235 TGEAKDIFRAPRHPYTQALL 254
Cdd:PRK15112 231 RGSTADVLASPLHELTKRLI 250
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
22-258 |
1.79e-44 |
|
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: 153.18 E-value: 1.79e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 22 AVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDfPgrvMAEKLEFNGQDLKRISEKERRSLVGSEVAMIFQDpmTS 101
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIE-P---TSGKVLIDGQDIAAMSRKELRELRRKKISMVFQS--FA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 102 LNPCYTV------GFQImeaikvhQGGNKKTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMSQRVMIAMAIACQPKLL 175
Cdd:cd03294 113 LLPHRTVlenvafGLEV-------QGVPRAEREERAAEALELVGLEG---WEHKYPDELSGGMQQRVGLARALAVDPDIL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 176 IADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDIFRAPRHPYTQALLR 255
Cdd:cd03294 183 LMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFR 262
|
...
gi 521291413 256 ALP 258
Cdd:cd03294 263 GVD 265
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-236 |
1.49e-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: 148.82 E-value: 1.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 4 LNVDKLSVHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIdfpgRVMAEKLEFNGQDLKRISEKER 83
Cdd:cd03259 1 LELKGLSKTYGSV----RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLE----RPDSGEILIDGRDVTGVPPERR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 84 RslvgseVAMIFQDPmtSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVM 163
Cdd:cd03259 73 N------IGMVFQDY--ALFPHLTVAENIAFGLKL-RGVPKAEIRARVRELLELVGLEGLLNR---YPHELSGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521291413 164 IAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-257 |
3.72e-42 |
|
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: 146.34 E-value: 3.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKLSVHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSvsSL--AIMGLID-FPGRVmaeklEFNGQDLKRIS 79
Cdd:COG1120 1 MLEAENLSVGYGGR----PVLDDVSLSLPPGEVTALLGPNGSGKS--TLlrALAGLLKpSSGEV-----LLDGRDLASLS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 80 EKERRSLVgsevAMIFQDPMTSLNpcYTVgfqiMEAIKV----HQG---GNKKTRRQRAIDLLNQVGIPDPASRlDVypH 152
Cdd:COG1120 70 RRELARRI----AYVPQEPPAPFG--LTV----RELVALgrypHLGlfgRPSAEDREAVEEALERTGLEHLADR-PV--D 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 153 QLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQV 232
Cdd:COG1120 137 ELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
250 260
....*....|....*....|....*
gi 521291413 233 VETGEAKDIFraprhpyTQALLRAL 257
Cdd:COG1120 217 VAQGPPEEVL-------TPELLEEV 234
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-257 |
1.79e-41 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 144.43 E-value: 1.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 2 ALLNVDKLSVHFGDvgsEFRAVDRVSYSVSQGEVVGIVGESGSGKSvsSL--AIMGLIDfP--GRVmaeklEFNGQDLKR 77
Cdd:COG3638 1 PMLELRNLSKRYPG---GTPALDDVSLEIERGEFVALIGPSGAGKS--TLlrCLNGLVE-PtsGEI-----LVDGQDVTA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 78 ISEKERRSLvGSEVAMIFQDPmtSLNPCYTVgfqiMEAI---KVHQ--------GGNKKTRRQRAIDLLNQVGIPDPA-S 145
Cdd:COG3638 70 LRGRALRRL-RRRIGMIFQQF--NLVPRLSV----LTNVlagRLGRtstwrsllGLFPPEDRERALEALERVGLADKAyQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 146 RLDvyphQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKII 225
Cdd:COG3638 143 RAD----QLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRII 218
|
250 260 270
....*....|....*....|....*....|..
gi 521291413 226 VMYAGQVVetgeakdiFRAPRHPYTQALLRAL 257
Cdd:COG3638 219 GLRDGRVV--------FDGPPAELTDAVLREI 242
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-250 |
5.93e-41 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 146.06 E-value: 5.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 4 LNVDKLSVHFGDvgseFRAVDRVSYSVSQGEVVGIVGESGSGKSvsSL--AIMGLiDFP--GRVmaeklEFNGQDLK-RI 78
Cdd:COG1118 3 IEVRNISKRFGS----FTLLDDVSLEIASGELVALLGPSGSGKT--TLlrIIAGL-ETPdsGRI-----VLNGRDLFtNL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 79 SEKERRslvgseVAMIFQDPMtsLNPCYTVgFQ-IMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGG 157
Cdd:COG1118 71 PPRERR------VGFVFQHYA--LFPHMTV-AEnIAFGLRV-RPPSKAEIRARVEELLELVQLEGLADR---YPSQLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 158 MSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGE 237
Cdd:COG1118 138 QRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGT 217
|
250
....*....|...
gi 521291413 238 AKDIFRAPRHPYT 250
Cdd:COG1118 218 PDEVYDRPATPFV 230
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
22-238 |
1.72e-40 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 141.34 E-value: 1.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 22 AVDRVSYSVSQGEVVGIVGESGSGKSvSSLAIMGLIDFP--GRVMaekleFNGQDLKRISEKE----RRSLvGsevaMIF 95
Cdd:COG2884 17 ALSDVSLEIEKGEFVFLTGPSGAGKS-TLLKLLYGEERPtsGQVL-----VNGQDLSRLKRREipylRRRI-G----VVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 96 QDpmtslnpcytvgFQIME----------AIKVHqGGNKKTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMSQRVMIA 165
Cdd:COG2884 86 QD------------FRLLPdrtvyenvalPLRVT-GKSRKEIRRRVREVLDLVGLSD---KAKALPHELSGGEQQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521291413 166 MAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALILITHDLALVAEAAHKIIVMYAGQVVETGEA 238
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEAR 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-232 |
7.61e-40 |
|
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: 139.20 E-value: 7.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 4 LNVDKLSVHFGDvgseFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGL--IDfpgrvmAEKLEFNGQDLKriSEK 81
Cdd:cd03262 1 IEIKNLHKSFGD----FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLeePD------SGTIIIDGLKLT--DDK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 82 ERRSLVGSEVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQR 161
Cdd:cd03262 69 KNINELRQKVGMVFQQ--FNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKA---DAYPAQLSGGQQQR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521291413 162 VMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALILITHDLALVAEAAHKIIVMYAGQV 232
Cdd:cd03262 144 VAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAE-EGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-241 |
8.33e-40 |
|
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: 140.01 E-value: 8.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 4 LNVDKLSVHFGDvgsEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDfP--GRVmaeklEFNGQDLKRISEK 81
Cdd:cd03256 1 IEVENLSKTYPN---GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVE-PtsGSV-----LIDGTDINKLKGK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 82 ERRSlVGSEVAMIFQDPmtSLNPCYTVGFQI-------MEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPAS-RLDvyphQ 153
Cdd:cd03256 72 ALRQ-LRRQIGMIFQQF--NLIERLSVLENVlsgrlgrRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYqRAD----Q 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 154 LSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVV 233
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
....*...
gi 521291413 234 ETGEAKDI 241
Cdd:cd03256 225 FDGPPAEL 232
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-245 |
2.15e-39 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 139.07 E-value: 2.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 1 MALLNVDKLSVHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSvsSL--AIMGLIdfpgRVMAEKLEFNGQDLKRi 78
Cdd:COG1121 4 MPAIELENLTVSYGGR----PVLEDVSLTIPPGEFVAIVGPNGAGKS--TLlkAILGLL----PPTSGTVRLFGKPPRR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 79 sekeRRSLVG-----SEVAMIFqdPMTslnpCYTVgfqIMEAIKVHQG---GNKKTRRQRAIDLLNQVGIPDPASRldvy 150
Cdd:COG1121 73 ----ARRRIGyvpqrAEVDWDF--PIT----VRDV---VLMGRYGRRGlfrRPSRADREAVDEALERVGLEDLADR---- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 151 P-HQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALILITHDLALVAEAAHKIIVMyA 229
Cdd:COG1121 136 PiGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDLGAVREYFDRVLLL-N 213
|
250
....*....|....*.
gi 521291413 230 GQVVETGEAKDIFRAP 245
Cdd:COG1121 214 RGLVAHGPPEEVLTPE 229
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
3-234 |
2.17e-39 |
|
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: 138.25 E-value: 2.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKLSVHFGDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSvSSLAIMGLIDFP--GRVmaeklEFNGQDLKRISE 80
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKS-TLLHLLGGLDNPtsGEV-----LFNGQSLSKLSS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 81 KERRSLVGSEVAMIFQdpMTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMSQ 160
Cdd:TIGR02211 75 NERAKLRNKKLGFIYQ--FHHLLPDFTALENVAMPLLI-GKKSVKEAKERAYEMLEKVGLEH---RINHRPSELSGGERQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521291413 161 RVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALvAEAAHKIIVMYAGQVVE 234
Cdd:TIGR02211 149 RVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLEL-AKKLDRVLEMKDGQLFN 221
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
24-225 |
4.74e-39 |
|
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: 136.98 E-value: 4.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 24 DRVSYSVSQGEVVGIVGESGSGKSvSSLAIMGLIDFPGRvmaEKLEFNGQDLKRISEKERRSLVGSEVAMIFQDpmTSLN 103
Cdd:TIGR03608 15 DDLNLTIEKGKMYAIIGESGSGKS-TLLNIIGLLEKFDS---GQVYLNGQETPPLNSKKASKFRREKLGYLFQN--FALI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 104 PCYTVGFQIMEAIKvHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACQPKLLIADEPTTA 183
Cdd:TIGR03608 89 ENETVEENLDLGLK-YKKLSKKEKREKKKEALEKVGL---NLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGS 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 521291413 184 LDVTIQAQIIELLLELqQKENMALILITHDLAlVAEAAHKII 225
Cdd:TIGR03608 165 LDPKNRDEVLDLLLEL-NDEGKTIIIVTHDPE-VAKQADRVI 204
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-182 |
5.41e-38 |
|
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: 132.39 E-value: 5.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 23 VDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIdfpgRVMAEKLEFNGQDLKRISEKERRSlvgsEVAMIFQDPmtSL 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLL----SPTEGTILLDGQDLTDDERKSLRK----EIGYVFQDP--QL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 103 NPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPASR-LDVYPHQLSGGMSQRVMIAMAIACQPKLLIADEPT 181
Cdd:pfam00005 71 FPRLTVRENLRLGLLL-KGLSKREKDARAEEALEKLGLGDLADRpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
.
gi 521291413 182 T 182
Cdd:pfam00005 150 A 150
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
11-242 |
8.05e-38 |
|
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: 135.64 E-value: 8.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 11 VHFGDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIdFP--GRVmaeklEFNGQDLKRISE-KERRSLV 87
Cdd:TIGR04520 6 VSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLL-LPtsGKV-----TVDGLDTLDEENlWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 88 GsevaMIFQDPMTSLnpcytVGFQI-------MEAIKVhqggNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQ 160
Cdd:TIGR04520 80 G----MVFQNPDNQF-----VGATVeddvafgLENLGV----PREEMRKRVDEALKLVGM---EDFRDREPHLLSGGQKQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 161 RVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEaAHKIIVMYAGQVVETGEAKD 240
Cdd:TIGR04520 144 RVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPRE 222
|
..
gi 521291413 241 IF 242
Cdd:TIGR04520 223 IF 224
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-233 |
1.98e-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: 133.96 E-value: 1.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKLSVHFGDvgsEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDF-PGRVmaeklEFNGQDLKRISEK 81
Cdd:TIGR02315 1 MLEVENLSKVYPN---GKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPsSGSI-----LLEGTDITKLRGK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 82 ERRSlVGSEVAMIFQD-----PMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPA-SRLDvyphQLS 155
Cdd:TIGR02315 73 KLRK-LRRRIGMIFQHynlieRLTVLENVLHGRLGYKPTWRSLLGRFSEEDKERALSALERVGLADKAyQRAD----QLS 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521291413 156 GGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVV 233
Cdd:TIGR02315 148 GGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIV 225
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-249 |
3.72e-37 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 135.93 E-value: 3.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 1 MALLNVDKLSVHFGDvgseFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLiDFP--GRVMAeklefNGQDLKRI 78
Cdd:TIGR03265 2 SPYLSIDNIRKRFGA----FTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGL-ERQtaGTIYQ-----GGRDITRL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 79 SEKERrslvgsEVAMIFQDpmTSLNPCYTVGFQIMEAIKvHQGGNKKTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGM 158
Cdd:TIGR03265 72 PPQKR------DYGIVFQS--YALFPNLTVADNIAYGLK-NRGMGRAEVAERVAELLDLVGLPGSE---RKYPGQLSGGQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 159 SQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEA 238
Cdd:TIGR03265 140 QQRVALARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTP 219
|
250
....*....|.
gi 521291413 239 KDIFRAPRHPY 249
Cdd:TIGR03265 220 QEIYRHPATPF 230
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-235 |
3.50e-36 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 131.14 E-value: 3.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 1 MALLNVDKLSVHFGDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSvsSL--AIMGLIDfP--GRVMaekleFNGQdlk 76
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKT--TLlnLIAGFLA-PssGEIT-----LDGV--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 77 RISEKerrslvGSEVAMIFQDpmTSLNPCYTV------GFQImeaikvhQGGNKKTRRQRAIDLLNQVGIPDPASRldvY 150
Cdd:COG4525 70 PVTGP------GADRGVVFQK--DALLPWLNVldnvafGLRL-------RGVPKAERRARAEELLALVGLADFARR---R 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 151 PHQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDlalVAEA---AHKIIVM 227
Cdd:COG4525 132 IWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS---VEEAlflATRLVVM 208
|
250
....*....|
gi 521291413 228 --YAGQVVET 235
Cdd:COG4525 209 spGPGRIVER 218
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-249 |
4.14e-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: 130.15 E-value: 4.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 6 VDKLSVHFGDvgseFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLiDFP--GRVMaekleFNGQDLKRISEKER 83
Cdd:cd03296 5 VRNVSKRFGD----FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGL-ERPdsGTIL-----FGGEDATDVPVQER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 84 rslvgsEVAMIFQD-----PMTSLNpcyTVGFQiMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGM 158
Cdd:cd03296 75 ------NVGFVFQHyalfrHMTVFD---NVAFG-LRVKPRSERPPEAEIRAKVHELLKLVQLDWLADR---YPAQLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 159 SQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEA 238
Cdd:cd03296 142 RQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTP 221
|
250
....*....|.
gi 521291413 239 KDIFRAPRHPY 249
Cdd:cd03296 222 DEVYDHPASPF 232
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
6-254 |
5.01e-36 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 129.92 E-value: 5.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 6 VDKLSVHFGDvgseFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLiDFP--GRVMaekleFNGQDLKRISEKER 83
Cdd:TIGR00968 3 IANISKRFGS----FQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGL-EQPdsGRIR-----LNGQDATRVHARDR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 84 rslvgsEVAMIFQDpmTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVM 163
Cdd:TIGR00968 73 ------KIGFVFQH--YALFKHLTVRDNIAFGLEI-RKHPKAKIKARVEELLELVQLEGLGDR---YPNQLSGGQRQRVA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 164 IAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDIFR 243
Cdd:TIGR00968 141 LARALAVEPQVLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYD 220
|
250
....*....|.
gi 521291413 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 |
7.06e-36 |
|
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: 127.69 E-value: 7.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 4 LNVDKLSVHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIdfpgRVMAEKLEFNGQDL---KRISE 80
Cdd:cd03229 1 LELKNVSKRYGQK----TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLE----EPDSGSILIDGEDLtdlEDELP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 81 KERRSlvgseVAMIFQDPmtSLNPCYTVGFQIMEAikvhqggnkktrrqraidllnqvgipdpasrldvyphqLSGGMSQ 160
Cdd:cd03229 73 PLRRR-----IGMVFQDF--ALFPHLTVLENIALG--------------------------------------LSGGQQQ 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521291413 161 RVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQ 231
Cdd:cd03229 108 RVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
22-249 |
1.14e-35 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 132.92 E-value: 1.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 22 AVDRVSYSVSQGEVVGIVGESGSGKSvsSL--AIMGLIDfP--GRVmaeklEFNGQDLKRISEKERRSLVGSEVAMIFQd 97
Cdd:COG4175 42 GVNDASFDVEEGEIFVIMGLSGSGKS--TLvrCLNRLIE-PtaGEV-----LIDGEDITKLSKKELRELRRKKMSMVFQ- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 98 pmtS--LNPCYTV------GFQImeaikvhQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIA 169
Cdd:COG4175 113 ---HfaLLPHRTVlenvafGLEI-------QGVPKAERRERAREALELVGL---AGWEDSYPDELSGGMQQRVGLARALA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 170 CQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLalvAEA---AHKIIVMYAGQVVETGEAKDIFRAPR 246
Cdd:COG4175 180 TDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDL---DEAlrlGDRIAIMKDGRIVQIGTPEEILTNPA 256
|
...
gi 521291413 247 HPY 249
Cdd:COG4175 257 NDY 259
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-246 |
1.26e-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: 128.71 E-value: 1.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 4 LNVDKLSVHFGdvgsEFRAVDRVSYSVSQGEVVGIVGESGSGKSvsSL--AIMGLIDfP--GRVMaekleFNGQDLKRIS 79
Cdd:cd03219 1 LEVRGLTKRFG----GLVALDDVSFSVRPGEIHGLIGPNGAGKT--TLfnLISGFLR-PtsGSVL-----FDGEDITGLP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 80 EKERRSLvGseVAMIFQDP-----MTSLNPCYtVGFQIMEAIKVHQGGNKKTR---RQRAIDLLNQVGIPDpasRLDVYP 151
Cdd:cd03219 69 PHEIARL-G--IGRTFQIPrlfpeLTVLENVM-VAAQARTGSGLLLARARREEreaRERAEELLERVGLAD---LADRPA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 152 HQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALILITHDLALVAEAAHKIIVMYAGQ 231
Cdd:cd03219 142 GELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGR 220
|
250
....*....|....*
gi 521291413 232 VVETGEAKDIFRAPR 246
Cdd:cd03219 221 VIAEGTPDEVRNNPR 235
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-232 |
1.33e-35 |
|
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: 126.74 E-value: 1.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 4 LNVDKLSVHFGDvgseFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDfP--GRVmaeklEFNGQDLKRISEK 81
Cdd:cd03230 1 IEVRNLSKRYGK----KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLK-PdsGEI-----KVLGKDIKKEPEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 82 ERRslvgsEVAMIFQDPmtSLNPCYTVgfqiMEAIKvhqggnkktrrqraidllnqvgipdpasrldvyphqLSGGMSQR 161
Cdd:cd03230 71 VKR-----RIGYLPEEP--SLYENLTV----RENLK------------------------------------LSGGMKQR 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521291413 162 VMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALILITHDLALVAEAAHKIIVMYAGQV 232
Cdd:cd03230 104 LALAQALLHDPELLILDEPTSGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
26-252 |
1.80e-35 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 128.59 E-value: 1.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 26 VSYSVSQGEVVGIVGESGSGKSvSSLAIMGLIDFPG----RVMAEKLEFNgqdlKRISEKERRSLVGsEVAMIFQDpmTS 101
Cdd:COG4161 21 INLECPSGETLVLLGPSGAGKS-SLLRVLNLLETPDsgqlNIAGHQFDFS----QKPSEKAIRLLRQ-KVGMVFQQ--YN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 102 LNPCYTVGFQIMEA-IKVhQGGNKKTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQRVMIAMAIACQPKLLIADEP 180
Cdd:COG4161 93 LWPHLTVMENLIEApCKV-LGLSKEQAREKAMKLLARLRLTDKA---DRFPLHLSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521291413 181 TTALDVTIQAQIIELLLELQQKEnMALILITHDLALVAEAAHKIIVMYAGQVVETGEAkDIFrapRHPYTQA 252
Cdd:COG4161 169 TAALDPEITAQVVEIIRELSQTG-ITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA-SHF---TQPQTEA 235
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
17-245 |
2.17e-35 |
|
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: 128.57 E-value: 2.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 17 GSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDfP--GRVMaekleFNGQDLKRISEKERRSLVGsevaMI 94
Cdd:cd03295 11 GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIE-PtsGEIF-----IDGEDIREQDPVELRRKIG----YV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 95 FQDpmTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPdPASRLDVYPHQLSGGMSQRVMIAMAIACQPKL 174
Cdd:cd03295 81 IQQ--IGLFPHMTVEENIALVPKL-LKWPKEKIRERADELLALVGLD-PAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521291413 175 LIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDlalVAEA---AHKIIVMYAGQVVETGEAKDIFRAP 245
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHD---IDEAfrlADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-241 |
2.98e-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: 127.68 E-value: 2.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 4 LNVDKLSVHFGDvgseFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDFPGRVMAE-KLEFNGQDLKriSEKE 82
Cdd:cd03260 1 IELRDLNVYYGD----KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEgEVLLDGKDIY--DLDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 83 RRSLVGSEVAMIFQDPmtslNPcytvgFQ--IMEAI----KVHQGGNKKTRRQRAIDLLNQVGIPDPAS-RLDvyPHQLS 155
Cdd:cd03260 75 DVLELRRRVGMVFQKP----NP-----FPgsIYDNVayglRLHGIKLKEELDERVEEALRKAALWDEVKdRLH--ALGLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 156 GGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALILITHDLALVAEAAHKIIVMYAGQVVET 235
Cdd:cd03260 144 GGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEF 221
|
....*.
gi 521291413 236 GEAKDI 241
Cdd:cd03260 222 GPTEQI 227
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-255 |
3.98e-35 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 127.90 E-value: 3.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 5 NVDKlsvHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDFPGrvmaEKLEFNGQDLKRISEKERr 84
Cdd:PRK09493 6 NVSK---HFGPT----QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITS----GDLIVDGLKVNDPKVDER- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 85 sLVGSEVAMIFQD----P-MTSLNpcyTVGFQimeAIKVhQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMS 159
Cdd:PRK09493 74 -LIRQEAGMVFQQfylfPhLTALE---NVMFG---PLRV-RGASKEEAEKQARELLAKVGL---AERAHHYPSELSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 160 QRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAK 239
Cdd:PRK09493 143 QRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAE-EGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQ 221
|
250
....*....|....*.
gi 521291413 240 DIFRAPRHPYTQALLR 255
Cdd:PRK09493 222 VLIKNPPSQRLQEFLQ 237
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-236 |
5.10e-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: 125.63 E-value: 5.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 6 VDKLSVHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSvsSL--AIMGLIDF-PGRVMaekleFNGQDLKRISEKE 82
Cdd:cd03214 2 VENLSVGYGGR----TVLDDLSLSIEAGEIVGILGPNGAGKS--TLlkTLAGLLKPsSGEIL-----LDGKDLASLSPKE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 83 RRSLVGsevamifqdpmtslnpcYtvgfqimeaikVHQggnkktrrqraidLLNQVGIPDPASRldvYPHQLSGGMSQRV 162
Cdd:cd03214 71 LARKIA-----------------Y-----------VPQ-------------ALELLGLAHLADR---PFNELSGGERQRV 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521291413 163 MIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:cd03214 107 LLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-245 |
2.92e-34 |
|
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: 125.14 E-value: 2.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 4 LNVDKLSVHFGdvgsEFRaVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDfP--GRVMaekleFNGQDLKRISEK 81
Cdd:cd03299 1 LKVENLSKDWK----EFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIK-PdsGKIL-----LNGKDITNLPPE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 82 ERRslvgseVAMIFQDpmTSLNPCYTVGFQIMEAIKvHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQR 161
Cdd:cd03299 70 KRD------ISYVPQN--YALFPHMTVYKNIAYGLK-KRKVDKKEIERKVLEIAEMLGI---DHLLNRKPETLSGGEQQR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 162 VMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDI 241
Cdd:cd03299 138 VAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEV 217
|
....
gi 521291413 242 FRAP 245
Cdd:cd03299 218 FKKP 221
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
26-232 |
3.95e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 124.16 E-value: 3.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 26 VSYSVSQGEVVGIVGESGSGKSVssL--AIMGLIDF-PGRVMaekleFNGQDLKRISEKERRSlvgsEVAMIFQDPMTSL 102
Cdd:COG4619 19 VSLTLEAGECVAITGPSGSGKST--LlrALADLDPPtSGEIY-----LDGKPLSAMPPPEWRR----QVAYVPQEPALWG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 103 NpcyTVGFQIMEAIKVHqggNKKTRRQRAIDLLNQVGIPDpaSRLDVYPHQLSGGMSQRVMIAMAIACQPKLLIADEPTT 182
Cdd:COG4619 88 G---TVRDNLPFPFQLR---ERKFDRERALELLERLGLPP--DILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 521291413 183 ALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQV 232
Cdd:COG4619 160 ALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-278 |
6.10e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 125.51 E-value: 6.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKLSVHFGDvgSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDFPgrvmAEKLEFNGQDLKRISEKE 82
Cdd:PRK13635 5 IIRVEHISFRYPD--AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPE----AGTITVGGMVLSEETVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 83 RRSLVGsevaMIFQDPMTSLnpcytVGFQIMEAIKV---HQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMS 159
Cdd:PRK13635 79 VRRQVG----MVFQNPDNQF-----VGATVQDDVAFgleNIGVPREEMVERVDQALRQVGMEDFLNR---EPHRLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 160 QRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEaAHKIIVMYAGQVVETGEAK 239
Cdd:PRK13635 147 QRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPE 225
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 521291413 240 DIFRaprhpYTQALLRA---LPEFAQDKARLASLPGVVPGKY 278
Cdd:PRK13635 226 EIFK-----SGHMLQEIgldVPFSVKLKELLKRNGILLPNTY 262
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
26-233 |
7.00e-34 |
|
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: 123.98 E-value: 7.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 26 VSYSVSQGEVVGIVGESGSGKSvSSLAIMGLIDfpgRVMAEKLEFNGQDLKRISEKERRSLVGSeVAMIFQDpmTSLNPC 105
Cdd:TIGR02982 24 INLEINPGEIVILTGPSGSGKT-TLLTLIGGLR---SVQEGSLKVLGQELHGASKKQLVQLRRR-IGYIFQA--HNLLGF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 106 YTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMSQRVMIAMAIACQPKLLIADEPTTALD 185
Cdd:TIGR02982 97 LTARQNVQMALELQPNLSYQEARERARAMLEAVGLGD---HLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 521291413 186 VTIQAQIIELLLELQQKENMALILITHDlALVAEAAHKIIVMYAGQVV 233
Cdd:TIGR02982 174 SKSGRDVVELMQKLAKEQGCTILMVTHD-NRILDVADRILQMEDGKLL 220
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
11-236 |
7.40e-34 |
|
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: 131.49 E-value: 7.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 11 VHFGDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKsvSSLA--IMGLIDfP--GRVMaekleFNGQDLKRISEKERRSL 86
Cdd:COG2274 479 VSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGK--STLLklLLGLYE-PtsGRIL-----IDGIDLRQIDPASLRRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 87 VGsevaMIFQDPMTslnpcytvgFQ--IMEAIKVhqgGNKKTRRQRAIDLLNQVGIPDPASRLdvyPH-----------Q 153
Cdd:COG2274 551 IG----VVLQDVFL---------FSgtIRENITL---GDPDATDEEIIEAARLAGLHDFIEAL---PMgydtvvgeggsN 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 154 LSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALILITHDLALVAeAAHKIIVMYAGQVV 233
Cdd:COG2274 612 LSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRLSTIR-LADRIIVLDKGRIV 688
|
...
gi 521291413 234 ETG 236
Cdd:COG2274 689 EDG 691
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-252 |
9.77e-34 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 124.38 E-value: 9.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 4 LNVDKLSVHFGDvgseFRAVDRVSYSVSQGEVVGIVGESGSGKSvsSL--AIMGLIDF-PGRVMAEKLEFNGQDL--KRI 78
Cdd:COG1117 12 IEVRNLNVYYGD----KQALKDINLDIPENKVTALIGPSGCGKS--TLlrCLNRMNDLiPGARVEGEILLDGEDIydPDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 79 SEKERRSLVGsevaMIFQDPmtslNPcytvgF--QIME----AIKVHQGGNKKTRRQRAIDLLNQVGIPDP-ASRLDVYP 151
Cdd:COG1117 86 DVVELRRRVG----MVFQKP----NP-----FpkSIYDnvayGLRLHGIKSKSELDEIVEESLRKAALWDEvKDRLKKSA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 152 HQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALILITHDLALVAEAAHKIIVMYAGQ 231
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL--KKDYTIVIVTHNMQQAARVSDYTAFFYLGE 230
|
250 260
....*....|....*....|.
gi 521291413 232 VVETGEAKDIFRAPRHPYTQA 252
Cdd:COG1117 231 LVEFGPTEQIFTNPKDKRTED 251
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-245 |
1.38e-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: 123.50 E-value: 1.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 4 LNVDKLSVHFGDvgseFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDfpgrVMAEKLEFNGQDLKRISEKER 83
Cdd:cd03300 1 IELENVSKFYGG----FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFET----PTSGEILLDGKDITNLPPHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 84 RslvgseVAMIFQDpmTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVM 163
Cdd:cd03300 73 P------VNTVFQN--YALFPHLTVFENIAFGLRL-KKLPKAEIKERVAEALDLVQLEGYANR---KPSQLSGGQQQRVA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 164 IAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDIFR 243
Cdd:cd03300 141 IARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
..
gi 521291413 244 AP 245
Cdd:cd03300 221 EP 222
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-227 |
1.52e-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: 122.64 E-value: 1.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 6 VDKLSVHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSvsSL--AIMGLID-FPGRVmaeklEFNGQDLKRiseke 82
Cdd:cd03235 2 VEDLTVSYGGH----PVLEDVSFEVKPGEFLAIVGPNGAGKS--TLlkAILGLLKpTSGSI-----RVFGKPLEK----- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 83 RRSLVGSeVAMIFqdpmtSLNPCY--TVgFQIME----AIKVHQGGNKKTRRQRAIDLLNQVGIPDPASR-LDvyphQLS 155
Cdd:cd03235 66 ERKRIGY-VPQRR-----SIDRDFpiSV-RDVVLmglyGHKGLFRRLSKADKAKVDEALERVGLSELADRqIG----ELS 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521291413 156 GGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALILITHDLALVAEAAHKIIVM 227
Cdd:cd03235 135 GGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-231 |
1.94e-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: 120.81 E-value: 1.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 6 VDKLSVHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDFPgrvmAEKLEFNGQDLKRISEKERRS 85
Cdd:cd00267 2 IENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT----SGEILIDGKDIAKLPLEELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 86 LVGsevamifqdpmtslnpcytvgfqimeaikvhqggnkktrrqraidllnqvgipdpasrldvYPHQLSGGMSQRVMIA 165
Cdd:cd00267 74 RIG-------------------------------------------------------------YVPQLSGGQRQRVALA 92
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521291413 166 MAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALILITHDLALVAEAAHKIIVMYAGQ 231
Cdd:cd00267 93 RALLLNPDLLLLDEPTSGLDPASRERLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
30-255 |
1.95e-33 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 123.71 E-value: 1.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 30 VSQGEVVGIVGESGSGKSvSSLAIMGLIDFP--GRVMAEKLEFNGQdlKRISEKER--RSLvGSEVAMIFQDpmTSLNPC 105
Cdd:PRK11264 26 VKPGEVVAIIGPSGSGKT-TLLRCINLLEQPeaGTIRVGDITIDTA--RSLSQQKGliRQL-RQHVGFVFQN--FNLFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 106 YTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACQPKLLIADEPTTALD 185
Cdd:PRK11264 100 RTVLENIIEGPVIVKGEPKEEATARARELLAKVGL---AGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 186 VTIQAQIIELLLELQQkENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDIFRAPRHPYTQALLR 255
Cdd:PRK11264 177 PELVGEVLNTIRQLAQ-EKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFLE 245
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-247 |
4.50e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 125.19 E-value: 4.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 1 MALLNVDKLSVHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSvsSL--AIMGLIDfP--GRVmaeklEFNGQDLK 76
Cdd:COG3839 1 MASLELENVSKSYGGV----EALKDIDLDIEDGEFLVLLGPSGCGKS--TLlrMIAGLED-PtsGEI-----LIGGRDVT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 77 RISEKERRslvgseVAMIFQDPmtSLNPCYTV----GFqimeAIKVhQGGNKKTRRQRAIDLLNQVGIPDpasRLDVYPH 152
Cdd:COG3839 69 DLPPKDRN------IAMVFQSY--ALYPHMTVyeniAF----PLKL-RKVPKAEIDRRVREAAELLGLED---LLDRKPK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 153 QLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLalvAEA---AHKIIVMYA 229
Cdd:COG3839 133 QLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQ---VEAmtlADRIAVMND 209
|
250
....*....|....*...
gi 521291413 230 GQVVETGEAKDIFRAPRH 247
Cdd:COG3839 210 GRIQQVGTPEELYDRPAN 227
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-255 |
5.64e-33 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 122.77 E-value: 5.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 4 LNVDKLSVHFGdvgsEFRAVDRVSYSVSQGEVVGIVGESGSGKSVsslaIMGLIDFPGRVMAEKLEFNGQDLK------- 76
Cdd:PRK10619 6 LNVIDLHKRYG----EHEVLKGVSLQANAGDVISIIGSSGSGKST----FLRCINFLEKPSEGSIVVNGQTINlvrdkdg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 77 --RISEKERRSLVGSEVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASrlDVYPHQL 154
Cdd:PRK10619 78 qlKVADKNQLRLLRTRLTMVFQH--FNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQ--GKYPVHL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 155 SGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALILITHDLALVAEAAHKIIVMYAGQVVE 234
Cdd:PRK10619 154 SGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFARHVSSHVIFLHQGKIEE 232
|
250 260
....*....|....*....|.
gi 521291413 235 TGEAKDIFRAPRHPYTQALLR 255
Cdd:PRK10619 233 EGAPEQLFGNPQSPRLQQFLK 253
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-251 |
8.55e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 121.94 E-value: 8.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 1 MALLNVDKLSVHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLID-FPGRVMAEKLEFNGQDLKR-- 77
Cdd:PRK14247 1 MNKIEIRDLKVSFGQV----EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElYPEARVSGEVYLDGQDIFKmd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 78 ISEKERRslvgseVAMIFQ--DPMTSLNPCYTV--GFQIMEAIKvhqggNKKTRRQRAIDLLNQVGIPDPA-SRLDVYPH 152
Cdd:PRK14247 77 VIELRRR------VQMVFQipNPIPNLSIFENValGLKLNRLVK-----SKKELQERVRWALEKAQLWDEVkDRLDAPAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 153 QLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALILITHDLALVAEAAHKIIVMYAGQV 232
Cdd:PRK14247 146 KLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
250
....*....|....*....
gi 521291413 233 VETGEAKDIFRAPRHPYTQ 251
Cdd:PRK14247 224 VEWGPTREVFTNPRHELTE 242
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
26-245 |
1.40e-32 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 120.89 E-value: 1.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 26 VSYSVSQGEVVGIVGESGSGKSvSSLAIMGLIDFP--GRVMAEKLEFNGQdlKRISEKERRSLvGSEVAMIFQDpmTSLN 103
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKS-SLLRVLNLLEMPrsGTLNIAGNHFDFS--KTPSDKAIREL-RRNVGMVFQQ--YNLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 104 PCYTVGFQIMEA-IKVhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACQPKLLIADEPTT 182
Cdd:PRK11124 95 PHLTVQQNLIEApCRV-LGLSKDQALARAEKLLERLRLKPYADR---FPLHLSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521291413 183 ALDVTIQAQIIELLLELQQKeNMALILITHDLALVAEAAHKIIVMYAGQVVETGEAkDIFRAP 245
Cdd:PRK11124 171 ALDPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVEQGDA-SCFTQP 231
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-241 |
1.21e-31 |
|
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: 118.42 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKLSVHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDF-PGRVMaekleFNGQDLKRISEK 81
Cdd:COG4555 1 MIEVENLSKKYGKV----PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPdSGSIL-----IDGEDVRKEPRE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 82 ERRSLVGSEVAMIFQDPMTslnpcytvgfqIMEAIKVH---QGGNKKTRRQRAIDLLNQVGIPDPasrLDVYPHQLSGGM 158
Cdd:COG4555 72 ARRQIGVLPDERGLYDRLT-----------VRENIRYFaelYGLFDEELKKRIEELIELLGLEEF---LDRRVGELSTGM 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 159 SQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEA 238
Cdd:COG4555 138 KKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSL 216
|
...
gi 521291413 239 KDI 241
Cdd:COG4555 217 DEL 219
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-233 |
2.18e-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: 116.97 E-value: 2.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 6 VDKLSVHFGDVGsefRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIdfpgRVMAEKLEFNGqdlKRISEKERRS 85
Cdd:cd03226 2 IENISFSYKKGT---EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLI----KESSGSILLNG---KPIKAKERRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 86 LVGsevaMIFQDPMTSLNPCyTVGFQIMEAIKVHQGGNKKTRrqraiDLLNQVGIPDPAsrlDVYPHQLSGGMSQRVMIA 165
Cdd:cd03226 72 SIG----YVMQDVDYQLFTD-SVREELLLGLKELDAGNEQAE-----TVLKDLDLYALK---ERHPLSLSGGQKQRLAIA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521291413 166 MAIACQPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALILITHDLALVAEAAHKIIVMYAGQVV 233
Cdd:cd03226 139 AALLSGKDLLIFDEPTSGLDYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-254 |
2.25e-31 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 117.55 E-value: 2.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 4 LNVDKLSVHFGDVgsEFRAvdrvSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIdFP--GRVMaekleFNGQDLKRISEK 81
Cdd:COG3840 2 LRLDDLTYRYGDF--PLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFL-PPdsGRIL-----WNGQDLTALPPA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 82 ERrslvgsEVAMIFQDpmTSLNPCYTVGFQImeAIKVHQGGN-KKTRRQRAIDLLNQVGIPDPASRLdvyPHQLSGGMSQ 160
Cdd:COG3840 70 ER------PVSMLFQE--NNLFPHLTVAQNI--GLGLRPGLKlTAEQRAQVEQALERVGLAGLLDRL---PGQLSGGQRQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 161 RVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKD 240
Cdd:COG3840 137 RVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAA 216
|
250
....*....|....
gi 521291413 241 IFRAPRHPYTQALL 254
Cdd:COG3840 217 LLDGEPPPALAAYL 230
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
20-231 |
2.36e-31 |
|
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: 116.96 E-value: 2.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 20 FRAVDRVSYSVSQGEVVGIVGESGSGKSvsslAIMGLIdfpgrVMAEKL-----EFNGQDLKRISEKE----RRSlvgse 90
Cdd:TIGR02673 15 VAALHDVSLHIRKGEFLFLTGPSGAGKT----TLLKLL-----YGALTPsrgqvRIAGEDVNRLRGRQlpllRRR----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 91 VAMIFQDpmTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMSQRVMIAMAIAC 170
Cdd:TIGR02673 81 IGVVFQD--FRLLPDRTVYENVALPLEV-RGKKEREIQRRVGAALRQVGLEH---KADAFPEQLSGGEQQRVAIARAIVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521291413 171 QPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALILITHDLALVAEAAHKIIVMYAGQ 231
Cdd:TIGR02673 155 SPPLLLADEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-218 |
2.82e-31 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 117.19 E-value: 2.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKLSVHFGDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLID-FPGRVMaekleFNGQDLKRISEK 81
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDgSSGEVS-----LVGQPLHQMDEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 82 ERRSLVGSEVAMIFQDPM--TSLNPCYTVgfqimEAIKVHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMS 159
Cdd:PRK10584 81 ARAKLRAKHVGFVFQSFMliPTLNALENV-----ELPALLRGESSRQSRNGAKALLEQLGL---GKRLDHLPAQLSGGEQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 521291413 160 QRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVA 218
Cdd:PRK10584 153 QRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAA 211
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
231-317 |
2.65e-30 |
|
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: 110.14 E-value: 2.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 231 QVVETGEAKDIFRAPRHPYTQALLRALPEFAQDKARLASLPGVVPGKYDRPTGCLLNPRCPYATDKCREQEPELNTVDGG 310
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIKKRDRKLISIPGEVPSLINLPSGCRFYPRCPYAQDECRKEPPALVEIAEG 80
|
....*..
gi 521291413 311 RQSKCHY 317
Cdd:TIGR01727 81 HRVACHL 87
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-243 |
3.45e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 115.92 E-value: 3.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 19 EFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDfP--GRVMaekleFNGQDL--KRISEKERRSLVGsevaMI 94
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLK-PtsGKII-----IDGVDItdKKVKLSDIRKKVG----LV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 95 FQDPMTSLnpcytvgFQimEAIK-------VHQGGNKKTRRQRAIDLLNQVGIpDPASRLDVYPHQLSGGMSQRVMIAMA 167
Cdd:PRK13637 89 FQYPEYQL-------FE--ETIEkdiafgpINLGLSEEEIENRVKRAMNIVGL-DYEDYKDKSPFELSGGQKRRVAIAGV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521291413 168 IACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDIFR 243
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
11-242 |
8.49e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 114.46 E-value: 8.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 11 VHFGDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGlIDFP--GRVMAEKLEFNGQDLKRISEkerrslvg 88
Cdd:PRK13648 13 VSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIG-IEKVksGEIFYNNQAITDDNFEKLRK-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 89 sEVAMIFQDPMTSLNPCyTVGFQIMEAIKVHQGGNKKTRRqRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQRVMIAMAI 168
Cdd:PRK13648 84 -HIGIVFQNPDNQFVGS-IVKYDVAFGLENHAVPYDEMHR-RVSEALKQVDMLERA---DYEPNALSGGQKQRVAIAGVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521291413 169 ACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHkIIVMYAGQVVETGEAKDIF 242
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADH-VIVMNKGTVYKEGTPTEIF 230
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
11-242 |
1.02e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 114.32 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 11 VHFGDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIdfpgRVMAEKLEFNGQDLKRISEKERRSLVGse 90
Cdd:PRK13632 13 VSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLL----KPQSGEIKIDGITISKENLKEIRKKIG-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 91 vaMIFQDPMTSLnpcytVGFQIMEAIKVhqgG--NKKTRRQ--RAI--DLLNQVGIPDpasRLDVYPHQLSGGMSQRVMI 164
Cdd:PRK13632 87 --IIFQNPDNQF-----IGATVEDDIAF---GleNKKVPPKkmKDIidDLAKKVGMED---YLDKEPQNLSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 165 AMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLalvAEA--AHKIIVMYAGQVVETGEAKDIF 242
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDM---DEAilADKVIVFSEGKLIAQGKPKEIL 230
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-242 |
2.72e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 114.18 E-value: 2.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKLSVHFGDVGS-EFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLI----------DF-PGRVMAEKLEF 70
Cdd:PRK13631 21 ILRVKNLYCVFDEKQEnELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIkskygtiqvgDIyIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 71 NGQDLKRISE-KERRSLVGsevaMIFQDPMTSLNPCyTVGFQIM---EAIKVHqggnKKTRRQRAIDLLNQVGIPDPAsr 146
Cdd:PRK13631 101 TNPYSKKIKNfKELRRRVS----MVFQFPEYQLFKD-TIEKDIMfgpVALGVK----KSEAKKLAKFYLNKMGLDDSY-- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 147 LDVYPHQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLElQQKENMALILITHDLALVAEAAHKIIV 226
Cdd:PRK13631 170 LERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIV 248
|
250
....*....|....*.
gi 521291413 227 MYAGQVVETGEAKDIF 242
Cdd:PRK13631 249 MDKGKILKTGTPYEIF 264
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-236 |
2.78e-29 |
|
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: 111.69 E-value: 2.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 6 VDKLSVHFGDvgseFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIdfpgRVMAEKLEFNGQDLKRISEKERRS 85
Cdd:cd03265 3 VENLVKKYGD----FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLL----KPTSGRATVAGHDVVREPREVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 86 lvgseVAMIFQDPmtSLNPCYTvGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYphqLSGGMSQRVMIA 165
Cdd:cd03265 75 -----IGIVFQDL--SVDDELT-GWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKT---YSGGMRRRLEIA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521291413 166 MAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:cd03265 144 RSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
11-231 |
5.14e-29 |
|
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: 109.39 E-value: 5.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 11 VHFGDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSvsSLA--IMGLID-FPGRVmaeklEFNGQDLKRISEKERRSLV 87
Cdd:cd03228 6 VSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKS--TLLklLLRLYDpTSGEI-----LIDGVDLRDLDLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 88 gsevAMIFQDP----MTslnpcytvgfqIMEAIkvhqggnkktrrqraidllnqvgipdpasrldvyphqLSGGMSQRVM 163
Cdd:cd03228 79 ----AYVPQDPflfsGT-----------IRENI-------------------------------------LSGGQRQRIA 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521291413 164 IAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALILITHDLALVaEAAHKIIVMYAGQ 231
Cdd:cd03228 107 IARALLRDPPILILDEATSALDPETEALILEALRAL--AKGKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
9-243 |
5.29e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 112.57 E-value: 5.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 9 LSVHFGDV------GS--EFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIdfpgRVMAEKLEFNGQDL-KRIS 79
Cdd:PRK13646 1 MTIRFDNVsytyqkGTpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALL----KPTTGTVTVDDITItHKTK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 80 EKERRSlVGSEVAMIFQDPMTSLNPcYTVGFQIMEAIKvHQGGNKKTRRQRAIDLLNQVGIPdpASRLDVYPHQLSGGMS 159
Cdd:PRK13646 77 DKYIRP-VRKRIGMVFQFPESQLFE-DTVEREIIFGPK-NFKMNLDEVKNYAHRLLMDLGFS--RDVMSQSPFQMSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 160 QRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAK 239
Cdd:PRK13646 152 RKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPK 231
|
....
gi 521291413 240 DIFR 243
Cdd:PRK13646 232 ELFK 235
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
26-274 |
5.74e-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: 114.04 E-value: 5.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 26 VSYSVSQGEVVGIVGESGSGKSvsSL--AIMGLIDFP-GRVmaeklEFNGQDL----KRISEK-ERRSLvgsevAMIFQD 97
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKT--TLlrAIAGLERPDsGRI-----RLGGEVLqdsaRGIFLPpHRRRI-----GYVFQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 98 PmtSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLnqvGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACQPKLLIA 177
Cdd:COG4148 86 A--RLFPHLSVRGNLLYGRKRAPRAERRISFDEVVELL---GI---GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 178 DEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDIFRAPrhpytqallrAL 257
Cdd:COG4148 158 DEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP----------DL 227
|
250
....*....|....*..
gi 521291413 258 PEFAQDKARLASLPGVV 274
Cdd:COG4148 228 LPLAGGEEAGSVLEATV 244
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-257 |
7.89e-29 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 114.36 E-value: 7.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 22 AVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDfPGRvmaEKLEFNGQDLKRISEKERRSLVGSEVAMIFQDpmTS 101
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE-PTR---GQVLIDGVDIAKISDAELREVRRKKIAMVFQS--FA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 102 LNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACQPKLLIADEPT 181
Cdd:PRK10070 117 LMPHMTVLDNTAFGMEL-AGINAEERREKALDALRQVGLENYAHS---YPDELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521291413 182 TALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDIFRAPRHPYTQALLRAL 257
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
22-232 |
1.64e-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: 109.42 E-value: 1.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 22 AVDRVSYSVSQGEVVGIVGESGSGKSvsslAIMGLIDFPGRVMAEKLEFNGQDLKRISEKE----RRSLvgsevAMIFQD 97
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKS----TLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylRRKI-----GVVFQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 98 pmTSLNPCYTVGFQIMEAIKVHQGGNKKTRRqRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACQPKLLIA 177
Cdd:cd03292 87 --FRLLPDRNVYENVAFALEVTGVPPREIRK-RVPAALELVGL---SHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 521291413 178 DEPTTALDVTIQAQIIELLlelqQKENMA---LILITHDLALVAEAAHKIIVMYAGQV 232
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLL----KKINKAgttVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-245 |
2.07e-28 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 112.48 E-value: 2.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 6 VDKLSVHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLidfpGRVMAEKLEFNGQDLKRISEKERRs 85
Cdd:PRK10851 5 IANIKKSFGRT----QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGL----EHQTSGHIRFHGTDVSRLHARDRK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 86 lvgseVAMIFQDpmTSLNPCYTVGFQIMEAIKV---HQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRV 162
Cdd:PRK10851 76 -----VGFVFQH--YALFRHMTVFDNIAFGLTVlprRERPNAAAIKAKVTQLLEMVQLAHLADR---YPAQLSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 163 MIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDIF 242
Cdd:PRK10851 146 ALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVW 225
|
...
gi 521291413 243 RAP 245
Cdd:PRK10851 226 REP 228
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
26-232 |
5.91e-28 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 108.75 E-value: 5.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 26 VSYSVSQGEVVGIVGESGSGKSvSSLAIMGLIDFP--GRVMaekleFNGQDLKRISEKERRSLVGSEVAMIFQdpMTSLN 103
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKS-TLLHLLGGLDTPtsGDVI-----FNGQPMSKLSSAAKAELRNQKLGFIYQ--FHHLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 104 PCYTVGFQImeAIKVHQGGNKKTR-RQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACQPKLLIADEPTT 182
Cdd:PRK11629 100 PDFTALENV--AMPLLIGKKKPAEiNSRALEMLAAVGL---EHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 521291413 183 ALDVTIQAQIIELLLELQQKENMALILITHDLALvAEAAHKIIVMYAGQV 232
Cdd:PRK11629 175 NLDARNADSIFQLLGELNRLQGTAFLVVTHDLQL-AKRMSRQLEMRDGRL 223
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-224 |
6.85e-28 |
|
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: 107.56 E-value: 6.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 2 ALLNVDKLSVHFGDvgsefRAV-DRVSYSVSQGEVVGIVGESGSGKSvsSL--AIMGLI-DFPGRVmaeklEFNGQDLKR 77
Cdd:COG4133 1 MMLEAENLSCRRGE-----RLLfSGLSFTLAAGEALALTGPNGSGKT--TLlrILAGLLpPSAGEV-----LWNGEPIRD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 78 isekeRRSLVGSEVAMIFQDPMtsLNPCYTVGfqimEAIKVHQGGNKKTRRQRAID-LLNQVGIpdpASRLDVYPHQLSG 156
Cdd:COG4133 69 -----AREDYRRRLAYLGHADG--LKPELTVR----ENLRFWAALYGLRADREAIDeALEAVGL---AGLADLPVRQLSA 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521291413 157 GMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMAlILITHDlALVAEAAHKI 224
Cdd:COG4133 135 GQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAV-LLTTHQ-PLELAAARVL 200
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
19-236 |
6.91e-28 |
|
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: 107.73 E-value: 6.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 19 EFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDFP-GRVMaekleFNGQDLKRISEKERrslvgsEVAMIFQD 97
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTsGRIY-----IGGRDVTDLPPKDR------DIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 98 pmTSLNPCYTVGFQIMEAIKVHqGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACQPKLLIA 177
Cdd:cd03301 81 --YALYPHMTVYDNIAFGLKLR-KVPKDEIDERVREVAELLQI---EHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 521291413 178 DEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-251 |
8.62e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 108.98 E-value: 8.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKLSVHFGDvgsefRAVDR-VSYSVSQGEVVGIVGESGSGKSVSSLAIMGLID-FPGRVMAE-KLEFNGQDLKRIS 79
Cdd:PRK14246 10 VFNISRLYLYIND-----KAILKdITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiYDSKIKVDgKVLYFGKDIFQID 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 80 EKERRSlvgsEVAMIFQDPmtSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGI-PDPASRLDVYPHQLSGGM 158
Cdd:PRK14246 85 AIKLRK----EVGMVFQQP--NPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLNSPASQLSGGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 159 SQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEA 238
Cdd:PRK14246 159 QQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSS 236
|
250
....*....|...
gi 521291413 239 KDIFRAPRHPYTQ 251
Cdd:PRK14246 237 NEIFTSPKNELTE 249
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-236 |
1.03e-27 |
|
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: 112.93 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 6 VDKLSVHFGDvgsEFRAVDRVSYSVSQGEVVGIVGESGSGKSvsSLA--IMGLIDfP--GRVMaekleFNGQDLKRISEK 81
Cdd:COG4988 339 LEDVSFSYPG---GRPALDGLSLTIPPGERVALVGPSGAGKS--TLLnlLLGFLP-PysGSIL-----INGVDLSDLDPA 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 82 ERRSLVgsevAMIFQDPMTslnpcytvgFQ--IMEAIKVhqgGNKKTRRQRAIDLLNQVGIPDPASRLdvyPH------- 152
Cdd:COG4988 408 SWRRQI----AWVPQNPYL---------FAgtIRENLRL---GRPDASDEELEAALEAAGLDEFVAAL---PDgldtplg 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 153 ----QLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALILITHDLALVAEAAHkIIVMY 228
Cdd:COG4988 469 eggrGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL--AKGRTVILITHRLALLAQADR-ILVLD 545
|
....*...
gi 521291413 229 AGQVVETG 236
Cdd:COG4988 546 DGRIVEQG 553
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
33-236 |
1.91e-27 |
|
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: 106.61 E-value: 1.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 33 GEVVGIVGESGSGKSVSSLAIMGLIdfpgRVMAEKLEFNGQDL----KRI--SEKERRslvgseVAMIFQDpmTSLNPCY 106
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLE----KPDGGTIVLNGTVLfdsrKKInlPPQQRK------IGLVFQQ--YALFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 107 TVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIpdpasrLDVYPHQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDV 186
Cdd:cd03297 91 NVRENLAFGLKRKRNREDRISVDELLDLLGLDHL------LNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 521291413 187 TIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:cd03297 165 ALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
12-241 |
1.95e-27 |
|
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: 109.02 E-value: 1.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 12 HFGDvgseFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIdfpgRVMAEKLEFNGQDLKRISEKERRSlvgseV 91
Cdd:TIGR01188 2 VYGD----FKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLL----RPTSGTARVAGYDVVREPRKVRRS-----I 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 92 AMIFQDPmtSLNPCYTvGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACQ 171
Cdd:TIGR01188 69 GIVPQYA--SVDEDLT-GRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADR---PVGTYSGGMRRRLDIAASLIHQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 172 PKLLIADEPTTALDVTIQAQIIELLLELqQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDI 241
Cdd:TIGR01188 143 PDVLFLDEPTTGLDPRTRRAIWDYIRAL-KEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-282 |
3.00e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 108.18 E-value: 3.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 19 EFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDfP--GRVM-------AEKlefNGQDLKRISEKerrslvgs 89
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQ-PtsGTVTigervitAGK---KNKKLKPLRKK-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 90 eVAMIFQDPMTSLnpcytvgFQimEAIK-------VHQGGNKKTRRQRAIDLLNQVGIPDpaSRLDVYPHQLSGGMSQRV 162
Cdd:PRK13634 87 -VGIVFQFPEHQL-------FE--ETVEkdicfgpMNFGVSEEDAKQKAREMIELVGLPE--ELLARSPFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 163 MIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDIF 242
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIF 234
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 521291413 243 RAPRhpYTQALLRALPEFAQDKARLASLPGVvpgKYDRPT 282
Cdd:PRK13634 235 ADPD--ELEAIGLDLPETVKFKRALEEKFGI---SFPKPC 269
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-255 |
5.68e-27 |
|
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: 111.01 E-value: 5.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 2 ALLNVDKLSVHFGdvGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDfP--GRVMaekleFNGQDLKRIS 79
Cdd:COG4987 332 PSLELEDVSFRYP--GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD-PqsGSIT-----LGGVDLRDLD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 80 EKERRSLVgsevAMIFQDP---MTSlnpcytvgfqIMEAIKVhqgGNKKTRRQRAIDLLNQVGIPD-----PA---SRLD 148
Cdd:COG4987 404 EDDLRRRI----AVVPQRPhlfDTT----------LRENLRL---ARPDATDEELWAALERVGLGDwlaalPDgldTWLG 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 149 VYPHQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQkeNMALILITHDLALVaEAAHKIIVMY 228
Cdd:COG4987 467 EGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGL-ERMDRILVLE 543
|
250 260
....*....|....*....|....*..
gi 521291413 229 AGQVVETGEAKDIfrAPRHPYTQALLR 255
Cdd:COG4987 544 DGRIVEQGTHEEL--LAQNGRYRQLYQ 568
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-227 |
6.81e-27 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 104.87 E-value: 6.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 4 LNVDKLSVHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLID----FPGRVMaekleFNGQDLKRIS 79
Cdd:COG4136 2 LSLENLTITLGGR----PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafsASGEVL-----LNGRRLTALP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 80 EKERRslvgseVAMIFQDPMtsLNPCYTVGFQIMEAIKvhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMS 159
Cdd:COG4136 73 AEQRR------IGILFQDDL--LFPHLSVGENLAFALP--PTIGRAQRRARVEQALEEAGLAGFADR---DPATLSGGQR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521291413 160 QRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLAlVAEAAHKIIVM 227
Cdd:COG4136 140 ARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEE-DAPAAGRVLDL 206
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
22-245 |
6.86e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 106.70 E-value: 6.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 22 AVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDfP--GRVM--AEKLEFNGQDLKRISEKerrslvgseVAMIFQD 97
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILK-PtsGEVLikGEPIKYDKKSLLEVRKT---------VGIVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 98 PMTSL-NPCYT--VGFQIMeaikvHQGGNKKTRRQRAIDLLNQVGIPDPASRLdvyPHQLSGGMSQRVMIAMAIACQPKL 174
Cdd:PRK13639 87 PDDQLfAPTVEedVAFGPL-----NLGLSKEEVEKRVKEALKAVGMEGFENKP---PHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521291413 175 LIADEPTTALDVTIQAQIIELLLELqQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDIFRAP 245
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDL-NKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
6-274 |
7.70e-27 |
|
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: 108.54 E-value: 7.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 6 VDKLSVHFGDvgsefRAV-DRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDFPGrvMAEKLEFNGQDLKRISEKERr 84
Cdd:TIGR03258 8 IDHLRVAYGA-----NTVlDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAG--LTGRIAIADRDLTHAPPHKR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 85 slvgsEVAMIFQDpmTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMI 164
Cdd:TIGR03258 80 -----GLALLFQN--YALFPHLKVEDNVAFGLRA-QKMPKADIAERVADALKLVGLGDAAAH---LPAQLSGGMQQRIAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 165 AMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQK-ENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDIFR 243
Cdd:TIGR03258 149 ARAIAIEPDVLLLDEPLSALDANIRANMREEIAALHEElPELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYD 228
|
250 260 270
....*....|....*....|....*....|.
gi 521291413 244 APRHPYTQALLRALPEFAQDKARLASLPGVV 274
Cdd:TIGR03258 229 APADGFAAEFLGAANILPAIALGITEAPGLV 259
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-242 |
1.80e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 105.86 E-value: 1.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 19 EFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGL-IDFPGRVMAEKLEFNGqDLKRISEKERrslVGSEVAMIFQD 97
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiISETGQTIVGDYAIPA-NLKKIKEVKR---LRKEIGLVFQF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 98 PMTSLnpcytvgFQimEAIK-------VHQGGNKKTRRQRAIDLLNQVGIP-DPASRldvYPHQLSGGMSQRVMIAMAIA 169
Cdd:PRK13645 99 PEYQL-------FQ--ETIEkdiafgpVNLGENKQEAYKKVPELLKLVQLPeDYVKR---SPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521291413 170 CQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDIF 242
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-242 |
1.84e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 105.58 E-value: 1.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 1 MALLNVDKLSVHFgDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDfpgrvmAEKLEF--NGQDLKRI 78
Cdd:PRK13650 2 SNIIEVKNLTFKY-KEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLE------AESGQIiiDGDLLTEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 79 SEKERRSLVGsevaMIFQDPMTSLnpcytVGFQIMEAIKV---HQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLS 155
Cdd:PRK13650 75 NVWDIRHKIG----MVFQNPDNQF-----VGATVEDDVAFgleNKGIPHEEMKERVNEALELVGMQDFKER---EPARLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 156 GGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAeAAHKIIVMYAGQVVET 235
Cdd:PRK13650 143 GGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVEST 221
|
....*..
gi 521291413 236 GEAKDIF 242
Cdd:PRK13650 222 STPRELF 228
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-236 |
2.07e-26 |
|
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: 104.12 E-value: 2.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 4 LNVDKLSVHFGdvGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIdFP--GRVMaekleFNGQDLKRisek 81
Cdd:cd03263 1 LQIRNLTKTYK--KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGEL-RPtsGTAY-----INGYSIRT---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 82 eRRSLVGSEVAMIFQDpmtslNPCYTvGFQIMEAIKVH---QGGNKKTRRQRAIDLLNQVGIPDPASRLdvyPHQLSGGM 158
Cdd:cd03263 69 -DRKAARQSLGYCPQF-----DALFD-ELTVREHLRFYarlKGLPKSEIKEEVELLLRVLGLTDKANKR---ARTLSGGM 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521291413 159 SQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALILITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:cd03263 139 KRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
14-242 |
2.23e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 105.55 E-value: 2.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 14 GDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIdFP--GRVMAEKLEfnGQDLKRISEKERRSlvgsev 91
Cdd:PRK13633 17 NEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALL-IPseGKVYVDGLD--TSDEENLWDIRNKA------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 92 AMIFQDPMTslnpcytvgfQIMEAIkVHQ---------GGNKKTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQRV 162
Cdd:PRK13633 88 GMVFQNPDN----------QIVATI-VEEdvafgpenlGIPPEEIRERVDESLKKVGMYEYR---RHAPHLLSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 163 MIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEaAHKIIVMYAGQVVETGEAKDIF 242
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
6-245 |
3.14e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 105.27 E-value: 3.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 6 VDKLSVHFGDvgSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIdFPGRVMAEKLEFNGQDLKRISEKERRS 85
Cdd:PRK13640 8 FKHVSFTYPD--SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLL-LPDDNPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 86 LVGsevaMIFQDPMTSLNPCyTVGFQIMEAIKvhqggNKKTRRQRAI----DLLNQVGIPDPAsrlDVYPHQLSGGMSQR 161
Cdd:PRK13640 85 KVG----IVFQNPDNQFVGA-TVGDDVAFGLE-----NRAVPRPEMIkivrDVLADVGMLDYI---DSEPANLSGGQKQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 162 VMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLAlVAEAAHKIIVMYAGQVVETGEAKDI 241
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDID-EANMADQVLVLDDGKLLAQGSPVEI 230
|
....
gi 521291413 242 FRAP 245
Cdd:PRK13640 231 FSKV 234
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-236 |
1.68e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 106.79 E-value: 1.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 4 LNVDKLSVHFGDV----GSEFRAVDRVSYSVSQGEVVGIVGESGSGKSvsSLA--IMGLIDfP--GRVmaeklEFNGQDL 75
Cdd:COG1132 333 LPPVRGEIEFENVsfsyPGDRPVLKDISLTIPPGETVALVGPSGSGKS--TLVnlLLRFYD-PtsGRI-----LIDGVDI 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 76 KRISEKERRSLVGsevaMIFQDP----MTslnpcytvgfqIMEAIKVhqgGNKKTRRQRAIDLLNQVGIPDPASRLdvyP 151
Cdd:COG1132 405 RDLTLESLRRQIG----VVPQDTflfsGT-----------IRENIRY---GRPDATDEEVEEAAKAAQAHEFIEAL---P 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 152 HQ-----------LSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQkeNMALILITHDLALVAeA 220
Cdd:COG1132 464 DGydtvvgergvnLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIR-N 540
|
250
....*....|....*.
gi 521291413 221 AHKIIVMYAGQVVETG 236
Cdd:COG1132 541 ADRILVLDDGRIVEQG 556
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-241 |
2.31e-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: 101.36 E-value: 2.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 4 LNVDKLSVHFGdvgsEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIdfpgRVMAEKLEFNGQDLKRISEkER 83
Cdd:cd03224 1 LEVENLNAGYG----KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLL----PPRSGSIRFDGRDITGLPP-HE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 84 RSLVGseVAMIFQDPM--TSLnpcyTVGFQIMEAIKVHQGGNKKTRRQRAIDLLnqvgiPDPASRLDVYPHQLSGGMSQR 161
Cdd:cd03224 72 RARAG--IGYVPEGRRifPEL----TVEENLLLGAYARRRAKRKARLERVYELF-----PRLKERRKQLAGTLSGGEQQM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 162 VMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKEnMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDI 241
Cdd:cd03224 141 LAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEG-VTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
24-233 |
4.03e-25 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 105.96 E-value: 4.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 24 DRVSYSVSQGEVVGIVGESGSGKSvSSLAIMGLIDFPG----RVMAEKL-EFNGQDLKRIsekeRRSLVGsevaMIFQ-- 96
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKS-TLMNILGCLDKPTsgtyRVAGQDVaTLDADALAQL----RREHFG----FIFQry 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 97 DPMTSLNPCYTVgfqimEAIKVHQGGNKKTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMSQRVMIAMAIACQPKLLI 176
Cdd:PRK10535 96 HLLSHLTAAQNV-----EVPAVYAGLERKQRLLRAQELLQRLGLED---RVEYQPSQLSGGQQQRVSIARALMNGGQVIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 521291413 177 ADEPTTALDVTIQAQIIELLLELQQKENmALILITHDlALVAEAAHKIIVMYAGQVV 233
Cdd:PRK10535 168 ADEPTGALDSHSGEEVMAILHQLRDRGH-TVIIVTHD-PQVAAQAERVIEIRDGEIV 222
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
18-242 |
8.06e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 101.32 E-value: 8.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 18 SEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLID-FPGRVMAEKLEFNGQDLKRISEKerrslvgseVAMIFQ 96
Cdd:PRK13642 18 SDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEeFEGKVKIDGELLTAENVWNLRRK---------IGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 97 DPMTSLnpcytVGFQIMEAIKV---HQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACQPK 173
Cdd:PRK13642 89 NPDNQF-----VGATVEDDVAFgmeNQGIPREEMIKRVDEALLAVNMLDFKTR---EPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521291413 174 LLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAeAAHKIIVMYAGQVVETGEAKDIF 242
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAA-SSDRILVMKAGEIIKEAAPSELF 228
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
38-254 |
9.01e-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: 102.19 E-value: 9.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 38 IVGESGSGKSVSSLAIMGLIdfpgRVMAEKLEFNGQDLKRISeKERRSlvgseVAMIFQDpmTSLNPCYTVGFQIMEAIK 117
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFE----QPDSGSIMLDGEDVTNVP-PHLRH-----INMVFQS--YALFPHMTVEENVAFGLK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 118 VhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLL 197
Cdd:TIGR01187 69 M-RKVPRAEIKPRVLEALRLVQLEEFADR---KPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELK 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 521291413 198 ELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDIFRAPRHPYTQALL 254
Cdd:TIGR01187 145 TIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFI 201
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
18-243 |
9.28e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 101.70 E-value: 9.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 18 SEFRAVDRVSYSVSQGEVVGIVGESGSGKS-----VSSLAI--MGLIDF----------PGRVMAEKLEFNGQ-----DL 75
Cdd:PRK13651 18 TELKALDNVSVEINQGEFIAIIGQTGSGKTtfiehLNALLLpdTGTIEWifkdeknkkkTKEKEKVLEKLVIQktrfkKI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 76 KRISEKERRslvgseVAMIFQdpmtslnpcyTVGFQIMEAI--------KVHQGGNKKTRRQRAIDLLNQVGIPDpaSRL 147
Cdd:PRK13651 98 KKIKEIRRR------VGVVFQ----------FAEYQLFEQTiekdiifgPVSMGVSKEEAKKRAAKYIELVGLDE--SYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 148 DVYPHQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALILITHDLALVAEAAHKIIVM 227
Cdd:PRK13651 160 QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNL-NKQGKTIILVTHDLDNVLEWTKRTIFF 238
|
250
....*....|....*.
gi 521291413 228 YAGQVVETGEAKDIFR 243
Cdd:PRK13651 239 KDGKIIKDGDTYDILS 254
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-274 |
1.16e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 101.34 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 4 LNVDKLSVHFGDvgseFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDfP--GRVmaeklEFNGQ-----DLK 76
Cdd:COG4152 2 LELKGLTKRFGD----KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILA-PdsGEV-----LWDGEpldpeDRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 77 RIS---EkERrslvgsevamifqdpmtSLNPCYTVGFQI--MEAIKvhqGGNKKTRRQRAIDLLNQVGIPDpasRLDVYP 151
Cdd:COG4152 72 RIGylpE-ER-----------------GLYPKMKVGEQLvyLARLK---GLSKAEAKRRADEWLERLGLGD---RANKKV 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 152 HQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALILITHDLALVAEAAHKIIVMYAGQ 231
Cdd:COG4152 128 EELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGR 206
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 521291413 232 VVETGEAKDIfRApRHPYTQALLralpEFAQDKARLASLPGVV 274
Cdd:COG4152 207 KVLSGSVDEI-RR-QFGRNTLRL----EADGDAGWLRALPGVT 243
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-241 |
1.82e-24 |
|
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: 103.34 E-value: 1.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 4 LNVDKLSVHFGDvgseFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDFP---GRVM-----------AEKLE 69
Cdd:TIGR03269 1 IEVKNLTKKFDG----KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptsGRIIyhvalcekcgyVERPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 70 FNGQ--------------DLKRISEKERRSLVgSEVAMIFQDPMtSLNPCYTVGFQIMEAIkvHQGGNK-KTRRQRAIDL 134
Cdd:TIGR03269 77 KVGEpcpvcggtlepeevDFWNLSDKLRRRIR-KRIAIMLQRTF-ALYGDDTVLDNVLEAL--EEIGYEgKEAVGRAVDL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 135 LNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDL 214
Cdd:TIGR03269 153 IEMVQL---SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWP 229
|
250 260
....*....|....*....|....*..
gi 521291413 215 ALVAEAAHKIIVMYAGQVVETGEAKDI 241
Cdd:TIGR03269 230 EVIEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-236 |
1.99e-24 |
|
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: 98.42 E-value: 1.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 4 LNVDKLSVHFGDVgsefRAVDRVSYSVSQGeVVGIVGESGSGKSvSSLAIMGLIDFPGrvmAEKLEFNGQDLKRiSEKER 83
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKT-TLMRILATLTPPS---SGTIRIDGQDVLK-QPQKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 84 RSLVGsevaMIFQDPMTSlnPCYTVgFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVM 163
Cdd:cd03264 71 RRRIG----YLPQEFGVY--PNFTV-REFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKK---KIGSLSGGMRRRVG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521291413 164 IAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALILITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:cd03264 141 IAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSEL--GEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-256 |
2.04e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 99.46 E-value: 2.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 2 ALLNVDKLSVHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSvsSL--AIMGLIDfP--GRVmaeklEFNGQDLKR 77
Cdd:PRK13548 1 AMLEARNLSVRLGGR----TLLDDVSLTLRPGEVVAILGPNGAGKS--TLlrALSGELS-PdsGEV-----RLNGRPLAD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 78 ISEKER-RSLvgsevAMIFQDPmtslnpcyTVGFqimeAIKVHQ--------GGNKKTRRQRAID-LLNQVGIPDPASRL 147
Cdd:PRK13548 69 WSPAELaRRR-----AVLPQHS--------SLSF----PFTVEEvvamgrapHGLSRAEDDALVAaALAQVDLAHLAGRD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 148 dvYPhQLSGGMSQRVMIAMAIA------CQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAA 221
Cdd:PRK13548 132 --YP-QLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYA 208
|
250 260 270
....*....|....*....|....*....|....*
gi 521291413 222 HKIIVMYAGQVVETGeakdifrAPRHPYTQALLRA 256
Cdd:PRK13548 209 DRIVLLHQGRLVADG-------TPAEVLTPETLRR 236
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
26-249 |
2.33e-24 |
|
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: 101.34 E-value: 2.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 26 VSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIdfpgRVMAEKLEFNGQDLKRISEK-----ERRSlvgseVAMIFQDpmT 100
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLT----RPDEGEIVLNGRTLFDSRKGiflppEKRR-----IGYVFQE--A 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 101 SLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLnqvGIpDPAsrLDVYPHQLSGGMSQRVMIAMAIACQPKLLIADEP 180
Cdd:TIGR02142 85 RLFPHLSVRGNLRYGMKRARPSERRISFERVIELL---GI-GHL--LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521291413 181 TTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDIFRAPRHPY 249
Cdd:TIGR02142 159 LAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-251 |
2.64e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 99.15 E-value: 2.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 26 VSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDFPGRVMAE-KLEFNGQDLkrISEKERRSLVGSEVAMIFQDPmtslNP 104
Cdd:PRK14267 23 VDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEgEVRLFGRNI--YSPDVDPIEVRREVGMVFQYP----NP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 105 cyTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPA------SRLDVYPHQLSGGMSQRVMIAMAIACQPKLLIAD 178
Cdd:PRK14267 97 --FPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAAlwdevkDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521291413 179 EPTTALDVTIQAQIIELLLELqqKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDIFRAPRHPYTQ 251
Cdd:PRK14267 175 EPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTE 245
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-247 |
3.69e-24 |
|
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: 98.31 E-value: 3.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 23 VDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLiDFP--GRVMAEKlefngqdlKRISEKerrslvGSEVAMIFQDpmT 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGL-AQPtsGGVILEG--------KQITEP------GPDRMVVFQN--Y 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 101 SLNPCYTVGFQIMEAIK-VHQGGNKKTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQRVMIAMAIACQPKLLIADE 179
Cdd:TIGR01184 64 SLLPWLTVRENIALAVDrVLPDLSKSERRAIVEEHIALVGLTEAA---DKRPGQLSGGMKQRVAIARALSIRPKVLLLDE 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521291413 180 PTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDI-FRAPRH 247
Cdd:TIGR01184 141 PFGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRD 209
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-227 |
3.89e-24 |
|
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: 98.28 E-value: 3.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 2 ALLNVDKLSVHF-----GdvGSEFRAVDRVSYSVSQGEVVGIVGESGSGKS-----------VSSLAImgLIDFPGRVMa 65
Cdd:COG4778 3 TLLEVENLSKTFtlhlqG--GKRLPVLDGVSFSVAAGECVALTGPSGAGKStllkciygnylPDSGSI--LVRHDGGWV- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 66 eklefngqDLKRISEKE----RRSLVG--SEvamiFqdpmtsLN-----PCYTVgfqIMEAIkVHQGGNKKTRRQRAIDL 134
Cdd:COG4778 78 --------DLAQASPREilalRRRTIGyvSQ----F------LRviprvSALDV---VAEPL-LERGVDREEARARAREL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 135 LNQVGIPdpaSRL-DVYPHQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALILITHD 213
Cdd:COG4778 136 LARLNLP---ERLwDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKA-RGTAIIGIFHD 211
|
250
....*....|....
gi 521291413 214 LALVAEAAHKIIVM 227
Cdd:COG4778 212 EEVREAVADRVVDV 225
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-232 |
5.18e-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: 96.35 E-value: 5.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 2 ALLNVDKLSVHfgdvgsefRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIdfpgRVMAEKLEFNGQDLKRISEK 81
Cdd:cd03215 3 PVLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLR----PPASGEITLDGKPVTRRSPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 82 ERRSLvgsEVAMIFQDpmtslnpcytvgfqimeaikvhqggnkktRRQRAIdllnqvgIPDpasrLDVY-----PHQLSG 156
Cdd:cd03215 71 DAIRA---GIAYVPED-----------------------------RKREGL-------VLD----LSVAenialSSLLSG 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521291413 157 GMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALILITHDLALVAEAAHKIIVMYAGQV 232
Cdd:cd03215 108 GNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAD-AGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-241 |
6.55e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 101.63 E-value: 6.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 1 MALLNVDKLSVHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSVsslaimgLIdfpgRVMA-------EKLEFNGQ 73
Cdd:COG1129 2 EPLLEMRGISKSFGGV----KALDGVSLELRPGEVHALLGENGAGKST-------LM----KILSgvyqpdsGEILLDGE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 74 DLKRISEKERRSLvGseVAMIFQDPmtSLNPCYTVgfqiMEAI----KVHQGG--NKKTRRQRAIDLLNQVGIP-DPASR 146
Cdd:COG1129 67 PVRFRSPRDAQAA-G--IAIIHQEL--NLVPNLSV----AENIflgrEPRRGGliDWRAMRRRARELLARLGLDiDPDTP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 147 LDvyphQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALILITHDLALVAEAAHKIIV 226
Cdd:COG1129 138 VG----DLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTV 212
|
250
....*....|....*
gi 521291413 227 MYAGQVVETGEAKDI 241
Cdd:COG1129 213 LRDGRLVGTGPVAEL 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-243 |
3.10e-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: 99.88 E-value: 3.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 21 RAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDfPgrvMAEKLEFN-GQDLKRISEK--ERRSLVGSEVAMIFQD 97
Cdd:TIGR03269 298 KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLE-P---TSGEVNVRvGDEWVDMTKPgpDGRGRAKRYIGILHQE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 98 pmTSLNPCYTVGFQIMEAIKVHQggNKKTRRQRAIDLLNQVGIPDPASR--LDVYPHQLSGGMSQRVMIAMAIACQPKLL 175
Cdd:TIGR03269 374 --YDLYPHRTVLDNLTEAIGLEL--PDELARMKAVITLKMVGFDEEKAEeiLDKYPDELSEGERHRVALAQVLIKEPRIV 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521291413 176 IADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDIFR 243
Cdd:TIGR03269 450 ILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-251 |
3.81e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 96.00 E-value: 3.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 2 ALLNVDKLSVHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDF-PGRVMAEKLEFNGQDL--KRI 78
Cdd:PRK14239 4 PILQVSDLSVYYNKK----KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnPEVTITGSIVYNGHNIysPRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 79 SEKERRSlvgsEVAMIFQDPmtslNPcytVGFQIMEAIkVH----QGGNKKTRRQRAIDL-LNQVGIPDPAS-RLDVYPH 152
Cdd:PRK14239 80 DTVDLRK----EIGMVFQQP----NP---FPMSIYENV-VYglrlKGIKDKQVLDEAVEKsLKGASIWDEVKdRLHDSAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 153 QLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMalILITHDLALVAEAAHKIIVMYAGQV 232
Cdd:PRK14239 148 GLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTM--LLVTRSMQQASRISDRTGFFLDGDL 225
|
250
....*....|....*....
gi 521291413 233 VETGEAKDIFRAPRHPYTQ 251
Cdd:PRK14239 226 IEYNDTKQMFMNPKHKETE 244
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-246 |
6.39e-23 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 95.57 E-value: 6.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKLSVHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSvsSL--AIMGLID-FPGRVMaekleFNGQDLKRIS 79
Cdd:COG4559 1 MLEAENLSVRLGGR----TLLDDVSLTLRPGELTAIIGPNGAGKS--TLlkLLTGELTpSSGEVR-----LNGRPLAAWS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 80 EKE---RRslvgsevAMIFQDpmTSLNPCYTVgFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLdvYPhQLSG 156
Cdd:COG4559 70 PWElarRR-------AVLPQH--SSLAFPFTV-EEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRS--YQ-TLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 157 GMSQRVMIAMAIA-------CQPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALILITHDLALVAEAAHKIIVMYA 229
Cdd:COG4559 137 GEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLAR-RGGGVVAVLHDLNLAAQYADRILLLHQ 215
|
250
....*....|....*..
gi 521291413 230 GQVVETGEAKDIFRAPR 246
Cdd:COG4559 216 GRLVAQGTPEEVLTDEL 232
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-245 |
7.37e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 97.10 E-value: 7.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKlsvHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLiDFP--GRVMaekleFNGQDLKRISE 80
Cdd:PRK11432 9 LKNITK---RFGSN----TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGL-EKPteGQIF-----IDGEDVTHRSI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 81 KERrslvgsEVAMIFQDpmTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVgipDPASRLDVYPHQLSGGMSQ 160
Cdd:PRK11432 76 QQR------DICMVFQS--YALFPHMSLGENVGYGLKM-LGVPKEERKQRVKEALELV---DLAGFEDRYVDQISGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 161 RVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKD 240
Cdd:PRK11432 144 RVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQE 223
|
....*
gi 521291413 241 IFRAP 245
Cdd:PRK11432 224 LYRQP 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-242 |
8.10e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 96.07 E-value: 8.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKLSVHFGDvGSEfrAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLID-FPGRVMaekleFNGQ--DLKRIS 79
Cdd:PRK13636 5 ILKVEELNYNYSD-GTH--ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKpSSGRIL-----FDGKpiDYSRKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 80 EKERRSLVGsevaMIFQDPMTSLNPCYTvgFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIpdpaSRLDVYP-HQLSGGM 158
Cdd:PRK13636 77 LMKLRESVG----MVFQDPDNQLFSASV--YQDVSFGAVNLKLPEDEVRKRVDNALKRTGI----EHLKDKPtHCLSFGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 159 SQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEA 238
Cdd:PRK13636 147 KKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNP 226
|
....
gi 521291413 239 KDIF 242
Cdd:PRK13636 227 KEVF 230
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-235 |
1.03e-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: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 4 LNVDKLSVHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDfP--GRVMaekleFNGQDLKRISEK 81
Cdd:cd03216 1 LELRGITKRFGGV----KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYK-PdsGEIL-----VDGKEVSFASPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 82 ERRSLvGseVAMIfqdpmtslnpcytvgfqimeaikvhqggnkktrrqraidllnqvgipdpasrldvypHQLSGGMSQR 161
Cdd:cd03216 71 DARRA-G--IAMV---------------------------------------------------------YQLSVGERQM 90
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521291413 162 VMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALILITHDLALVAEAAHKIIVMYAGQVVET 235
Cdd:cd03216 91 VEIARALARNARLLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
233-297 |
1.10e-22 |
|
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: 89.38 E-value: 1.10e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521291413 233 VETGEAKDIFRAPRHPYTQALLRALPEFAQDKARLASLPGVVPGKYDRPTGCLLNPRCPYATDKC 297
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPKRPLYTIPGNVPSLLELPEGCPFAPRCPFATEEC 65
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-245 |
1.11e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 95.67 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 19 EFRAVDRVSYSVSQGEVVGIVGESGSGKSvsslAIM-----------GLIDFPGRVMAekLEFNGQDLKRISEKerrslv 87
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKS----TLMqhfnallkpssGTITIAGYHIT--PETGNKNLKKLRKK------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 88 gseVAMIFQDPMTSLNPcYTVGFQIMEAIKvHQGGNKKTRRQRAIDLLNQVGIPDpaSRLDVYPHQLSGGMSQRVMIAMA 167
Cdd:PRK13641 87 ---VSLVFQFPEAQLFE-NTVLKDVEFGPK-NFGFSEDEAKEKALKWLKKVGLSE--DLISKSPFELSGGQMRRVAIAGV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521291413 168 IACQPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDIFRAP 245
Cdd:PRK13641 160 MAYEPEILCLDEPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-235 |
1.15e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 94.77 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKLSVHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDFP-GRVMAEKLEFNGQdlkrisek 81
Cdd:PRK11248 1 MLQISHLYADYGGK----PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQhGSITLDGKPVEGP-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 82 errslvGSEVAMIFQD----PMTSLNPCYTVGFQImeaikvhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGG 157
Cdd:PRK11248 69 ------GAERGVVFQNegllPWRNVQDNVAFGLQL-------AGVEKMQRLEIAHQMLKKVGLEGAEKR---YIWQLSGG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 158 MSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMY--AGQVVET 235
Cdd:PRK11248 133 QRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVER 212
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
21-264 |
1.18e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 95.19 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 21 RAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGlIDFPGRvmaEKLEFNGQDLKRISEKERRSLVGsevaMIFQDP-- 98
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNG-IYLPQR---GRVKVMGREVNAENEKWVRSKVG----LVFQDPdd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 99 -MTSLNPCYTVGFQimeaiKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLdvyPHQLSGGMSQRVMIAMAIACQPKLLIA 177
Cdd:PRK13647 91 qVFSSTVWDDVAFG-----PVNMGLDKDEVERRVEEALKAVRMWDFRDKP---PYHLSYGQKKRVAIAGVLAMDPDVIVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 178 DEPTTALDVTIQAQIIELLLELQQkENMALILITHDLALVAEAAHKIIVMYAGQVVETGEA-----KDIFRAP--RHPYT 250
Cdd:PRK13647 163 DEPMAYLDPRGQETLMEILDRLHN-QGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKslltdEDIVEQAglRLPLV 241
|
250
....*....|....
gi 521291413 251 QALLRALPEFAQDK 264
Cdd:PRK13647 242 AQIFEDLPELGQSK 255
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
21-236 |
1.31e-22 |
|
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: 93.44 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 21 RAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIdfpgRVMAEKLEFNGQDLKRISEKERRslVGSEV-AMIFQDPM 99
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLI----KPDSGEITFDGKSYQKNIEALRR--IGALIeAPGFYPNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 100 TSlnpcytvgfqiMEAIKVHqgGNKKTRRQRAID-LLNQVGipdpasrLDVYPH----QLSGGMSQRVMIAMAIACQPKL 174
Cdd:cd03268 88 TA-----------RENLRLL--ARLLGIRKKRIDeVLDVVG-------LKDSAKkkvkGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521291413 175 LIADEPTTALDVTIQAQIIELLLELqQKENMALILITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-240 |
1.40e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 97.79 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKlsvHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKS--VSslAIMGLIdFP--GRVmaeklEFNGQDLKRI 78
Cdd:COG3845 8 LRGITK---RFGGV----VANDDVSLTVRPGEIHALLGENGAGKStlMK--ILYGLY-QPdsGEI-----LIDGKPVRIR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 79 SEKERRSLvGseVAMIFQDPMtsLNPCYTVGFQIMEAIKVHQGG--NKKTRRQRAIDLLNQVGIP-DPasrlDVYPHQLS 155
Cdd:COG3845 73 SPRDAIAL-G--IGMVHQHFM--LVPNLTVAENIVLGLEPTKGGrlDRKAARARIRELSERYGLDvDP----DAKVEDLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 156 GGMSQRVMIAMAIACQPKLLIADEPTTALdvTIQaQIIELLLELQQ--KENMALILITHDLALVAEAAHKIIVMYAGQVV 233
Cdd:COG3845 144 VGEQQRVEILKALYRGARILILDEPTAVL--TPQ-EADELFEILRRlaAEGKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
....*..
gi 521291413 234 ETGEAKD 240
Cdd:COG3845 221 GTVDTAE 227
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-246 |
1.54e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.83 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 1 MALLNVDKLSVHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDfPGrvmAEKLEFNGQDLKRISE 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGDT----TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLT-PT---AGTVLVAGDDVEALSA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 81 KErrslVGSEVAMIFQDpmTSLNPCYTVGfQIMEAIKV-HQG--GNKKTRRQRAID-LLNQVGIPDPASRlDVypHQLSG 156
Cdd:PRK09536 73 RA----ASRRVASVPQD--TSLSFEFDVR-QVVEMGRTpHRSrfDTWTETDRAAVErAMERTGVAQFADR-PV--TSLSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 157 GMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILItHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:PRK09536 143 GERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAG 221
|
250
....*....|
gi 521291413 237 EAKDIFRAPR 246
Cdd:PRK09536 222 PPADVLTADT 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-241 |
1.60e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 97.79 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKLSVHfGDVGSEfrAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIdfpgRVMAEKLEFNGQDLKRISEKE 82
Cdd:COG3845 257 VLEVENLSVR-DDRGVP--ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLR----PPASGSIRLDGEDITGLSPRE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 83 RRSLvGseVAMIFQDPM-TSLNPCYTVGFQIM----EAIKVHQGG--NKKTRRQRAIDLLNQVGI--PDPASRLDvyphQ 153
Cdd:COG3845 330 RRRL-G--VAYIPEDRLgRGLVPDMSVAENLIlgryRRPPFSRGGflDRKAIRAFAEELIEEFDVrtPGPDTPAR----S 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 154 LSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALILITHDLALVAEAAHKIIVMYAGQVV 233
Cdd:COG3845 403 LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
....*...
gi 521291413 234 ETGEAKDI 241
Cdd:COG3845 482 GEVPAAEA 489
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-266 |
1.61e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 94.78 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 23 VDRVSYSVSQGEVVGIVGESGSGKS------------VSSLAIMGLIDFPGRVMaekleFNGQDlkrISEKERRslvgse 90
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTtflrtlnrmndkVSGYRYSGDVLLGGRSI-----FNYRD---VLEFRRR------ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 91 VAMIFQDPmtslNPC-YTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPAS-RLDVYPHQLSGGMSQRVMIAMAI 168
Cdd:PRK14271 103 VGMLFQRP----NPFpMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKdRLSDSPFRLSGGQQQLLCLARTL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 169 ACQPKLLIADEPTTALDVTIQAQIIELLLELQQKenMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDIFRAPRHP 248
Cdd:PRK14271 179 AVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHA 256
|
250
....*....|....*...
gi 521291413 249 YTQALLRALPEFAQDKAR 266
Cdd:PRK14271 257 ETARYVAGLSGDVKDAKR 274
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
22-279 |
3.50e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 95.67 E-value: 3.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 22 AVDRVSYSVSQGEVVGIVGESGSGKSvSSLAIMGLIDFP--GRVMaekleFNGQDLKRISEKERrslvgsEVAMIFQDpm 99
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKS-TLLRMLAGFEQPtaGQIM-----LDGVDLSHVPPYQR------PINMMFQS-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 100 TSLNPCYTVGFQIMEAIKvHQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACQPKLLIADE 179
Cdd:PRK11607 100 YALFPHMTVEQNIAFGLK-QDKLPKAEIASRVNEMLGLVHMQEFAKR---KPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 180 PTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDIFRAPRHPYTQALLRALPE 259
Cdd:PRK11607 176 PMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNV 255
|
250 260
....*....|....*....|....*..
gi 521291413 260 FA------QDKARLASLPGVV-PGKYD 279
Cdd:PRK11607 256 FEgvlkerQEDGLVIDSPGLVhPLKVD 282
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-227 |
9.01e-22 |
|
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: 95.43 E-value: 9.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 4 LNVDKLSVHFGDVGSefrAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDfPGRvmaEKLEFNGQDLKRISEKER 83
Cdd:TIGR02857 322 LEFSGVSVAYPGRRP---ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVD-PTE---GSIAVNGVPLADADADSW 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 84 RSLVG--SEVAMIFQDpmtslnpcytvgfQIMEAIKVHQGGNKKTRRQRAIDL--LNQV--GIPDP-ASRLDVYPHQLSG 156
Cdd:TIGR02857 395 RDQIAwvPQHPFLFAG-------------TIAENIRLARPDASDAEIREALERagLDEFvaALPQGlDTPIGEGGAGLSG 461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521291413 157 GMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQkeNMALILITHDLALvAEAAHKIIVM 227
Cdd:TIGR02857 462 GQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLAL-AALADRIVVL 529
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-236 |
1.08e-21 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 91.19 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 4 LNVDKLSVHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLI--DfpgrvmAEKLEFNGQDLKrISEK 81
Cdd:cd03269 1 LEVENVTKRFGRV----TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIIlpD------SGEVLFDGKPLD-IAAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 82 ERRSLVGSEvamifqdpmTSLNPCYTVGFQIMEAIKVHqGGNKKTRRQRAIDLLNQVGIPDPAS-RLDvyphQLSGGMSQ 160
Cdd:cd03269 70 NRIGYLPEE---------RGLYPKMKVIDQLVYLAQLK-GLKKEEARRRIDEWLERLELSEYANkRVE----ELSKGNQQ 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521291413 161 RVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALILITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:cd03269 136 KVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-239 |
1.18e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 92.07 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 4 LNVDKLSVHFG-DVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSvsSL--AIMGliDFP---GRVMaekleFNGQDLKR 77
Cdd:COG1101 2 LELKNLSKTFNpGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKS--TLlnAIAG--SLPpdsGSIL-----IDGKDVTK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 78 ISEKERRSLVGSevamIFQDPM--TSLNpcytvgFQIME--AIKVHQG-------GNKKTRRQRAIDLLNQV--GIPDpa 144
Cdd:COG1101 73 LPEYKRAKYIGR----VFQDPMmgTAPS------MTIEEnlALAYRRGkrrglrrGLTKKRRELFRELLATLglGLEN-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 145 sRLDVYPHQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDL--ALvaEAAH 222
Cdd:COG1101 141 -RLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMeqAL--DYGN 217
|
250
....*....|....*....
gi 521291413 223 KIIVMYAGQVVE--TGEAK 239
Cdd:COG1101 218 RLIMMHEGRIILdvSGEEK 236
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
13-241 |
1.81e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 94.61 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 13 FGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLI---DFPGRVMaekleFNGQDLK--RISEKERRSlv 87
Cdd:PRK13549 15 FGGV----KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYphgTYEGEII-----FEGEELQasNIRDTERAG-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 88 gseVAMIFQDPMtsLNPCYTVGFQIMEAIKVHQGG--NKKTRRQRAIDLLNQVGIP-DPASRLdvypHQLSGGMSQRVMI 164
Cdd:PRK13549 84 ---IAIIHQELA--LVKELSVLENIFLGNEITPGGimDYDAMYLRAQKLLAQLKLDiNPATPV----GNLGLGQQQLVEI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521291413 165 AMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDI 241
Cdd:PRK13549 155 AKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGM 230
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
21-233 |
2.52e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 90.32 E-value: 2.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 21 RAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLidfpGRVMAEKLEFNGQDLKRISEKE----RRslvgsEVAMIFQ 96
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGI----ERPSAGKIWFSGHDITRLKNREvpflRR-----QIGMIFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 97 DPMTSLNPCYTVGFQIMEAIKvhqGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACQPKLLI 176
Cdd:PRK10908 87 DHHLLMDRTVYDNVAIPLIIA---GASGDDIRRRVSAALDKVGLLDKAKN---FPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 521291413 177 ADEPTTALDVTIQAQIIELLLELqQKENMALILITHDLALVAEAAHKIIVMYAGQVV 233
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
11-236 |
2.78e-21 |
|
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: 90.75 E-value: 2.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 11 VHFGdVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDfpgrVMAEKLEFNGQDLKRISEKERRSLVGse 90
Cdd:cd03253 6 VTFA-YDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYD----VSSGSILIDGQDIREVTLDSLRRAIG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 91 vaMIFQDpmtslnpcyTVGFQ--IMEAIKVhqgGNKKTRRQRAIDLLNQVGIPDPASRL-DVYPHQ-------LSGGMSQ 160
Cdd:cd03253 79 --VVPQD---------TVLFNdtIGYNIRY---GRPDATDEEVIEAAKAAQIHDKIMRFpDGYDTIvgerglkLSGGEKQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521291413 161 RVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALILITHDLALVAEaAHKIIVMYAGQVVETG 236
Cdd:cd03253 145 RVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDV--SKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERG 217
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-246 |
3.63e-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: 90.04 E-value: 3.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 1 MALLNVDKLSVHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSvsSL--AIMGLIdfpgRVMAEKLEFNGQDLKRI 78
Cdd:COG0410 1 MPMLEVENLHAGYGGI----HVLHGVSLEVEEGEIVALLGRNGAGKT--TLlkAISGLL----PPRSGSIRFDGEDITGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 79 SEKERRSL-VG--SEVAMIFQDpMTslnpcytvgfqIME-----AIKVHQGGNKKTRRQRAIDLLnqvgiPDPASRLDVY 150
Cdd:COG0410 71 PPHRIARLgIGyvPEGRRIFPS-LT-----------VEEnlllgAYARRDRAEVRADLERVYELF-----PRLKERRRQR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 151 PHQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALILITHDLALVAEAAHKIIVMYAG 230
Cdd:COG0410 134 AGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERG 212
|
250
....*....|....*.
gi 521291413 231 QVVETGEAKDIFRAPR 246
Cdd:COG0410 213 RIVLEGTAAELLADPE 228
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
22-236 |
4.79e-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: 89.59 E-value: 4.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 22 AVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLID-FPGRVMaekleFNGQDLKRISEKERRSLVGsevaMIFQDPMT 100
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDpQKGQIL-----IDGIDIRDISRKSLRSMIG----VVLQDTFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 101 slnpcytvgFQ--IMEAIKVhqgGNKKTRRQRAIDLLNQVGIPDPASRL-DVYPHQ-------LSGGMSQRVMIAMAIAC 170
Cdd:cd03254 89 ---------FSgtIMENIRL---GRPNATDEEVIEAAKEAGAHDFIMKLpNGYDTVlgenggnLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521291413 171 QPKLLIADEPTTALDVTIQAQIIELLLELQqkENMALILITHDLALVAEaAHKIIVMYAGQVVETG 236
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLM--KGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEG 219
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
11-236 |
9.29e-21 |
|
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: 89.14 E-value: 9.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 11 VHFGDVgsEFRAVDR--------VSYSVSQGEVVGIVGESGSGKSvsslAIMGLID-----FPGRVMaekleFNGQDLKR 77
Cdd:cd03249 1 IEFKNV--SFRYPSRpdvpilkgLSLTIPPGKTVALVGSSGCGKS----TVVSLLErfydpTSGEIL-----LDGVDIRD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 78 ISEKERRSLVGsevaMIFQDPMtsLNPCytvgfQIMEAIKVHQGGNKKTRRQRAIDLLNQ----VGIPDpasRLD--VYP 151
Cdd:cd03249 70 LNLRWLRSQIG----LVSQEPV--LFDG-----TIAENIRYGKPDATDEEVEEAAKKANIhdfiMSLPD---GYDtlVGE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 152 H--QLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALILITHDLALVaEAAHKIIVMYA 229
Cdd:cd03249 136 RgsQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRA--MKGRTTIVIAHRLSTI-RNADLIAVLQN 212
|
....*..
gi 521291413 230 GQVVETG 236
Cdd:cd03249 213 GQVVEQG 219
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-236 |
1.05e-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: 88.32 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 25 RVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLiDFP--GRVMaekleFNGQDLKRISEKERrslvgsEVAMIFQDpmTSL 102
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGF-ETPqsGRVL-----INGVDVTAAPPADR------PVSMLFQE--NNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 103 NPCYTVGFQImeAIKVHQGGNKKTRRQRAID-LLNQVGIPDPASRLdvyPHQLSGGMSQRVMIAMAIACQPKLLIADEPT 181
Cdd:cd03298 82 FAHLTVEQNV--GLGLSPGLKLTAEDRQAIEvALARVGLAGLEKRL---PGELSGGERQRVALARVLVRDKPVLLLDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 521291413 182 TALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:cd03298 157 AALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-243 |
2.27e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 89.03 E-value: 2.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 19 EFRAVDRVSYSVSQGEVVGIVGESGSGKSvsslAIMGLID---FP--GRVMAEKLEFNGQ----DLKRISEKerrslvgs 89
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKS----TIMQLLNglhVPtqGSVRVDDTLITSTsknkDIKQIRKK-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 90 eVAMIFQDPMTslnpcytvgfQIMEAIKVHQ--------GGNKKTRRQRAIDLLNQVGIPDpaSRLDVYPHQLSGGMSQR 161
Cdd:PRK13649 87 -VGLVFQFPES----------QLFEETVLKDvafgpqnfGVSQEEAEALAREKLALVGISE--SLFEKNPFELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 162 VMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDI 241
Cdd:PRK13649 154 VAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
..
gi 521291413 242 FR 243
Cdd:PRK13649 233 FQ 234
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-237 |
4.64e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 87.33 E-value: 4.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 25 RVSYSVSQGEVVGIVGESGSGKSvsslAIMGLIdfPGRVMAEK--LEFNGQDLKRISEKERrslvgsEVAMIFQDpmTSL 102
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKS----TLLNLI--AGFLTPASgsLTLNGQDHTTTPPSRR------PVSMLFQE--NNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 103 NPCYTVGFQImeAIKVHQGgNKKTRRQRAI--DLLNQVGIPDPASRLdvyPHQLSGGMSQRVMIAMAIACQPKLLIADEP 180
Cdd:PRK10771 83 FSHLTVAQNI--GLGLNPG-LKLNAAQREKlhAIARQMGIEDLLARL---PGQLSGGQRQRVALARCLVREQPILLLDEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 521291413 181 TTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGE 237
Cdd:PRK10771 157 FSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGP 213
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
21-236 |
4.96e-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: 86.31 E-value: 4.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 21 RAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDfpgrVMAEKLEFNGQDLKRIS-EKERRSLvgsevAMIFQDPM 99
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLE----AEEGKIEIDGIDISTIPlEDLRSSL-----TIIPQDPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 100 -------TSLNPC--YTvGFQIMEAIKVHQGGNkktrrqraidllnqvgipdpasrldvyphQLSGGMSQRVMIAMAIAC 170
Cdd:cd03369 93 lfsgtirSNLDPFdeYS-DEEIYGALRVSEGGL-----------------------------NLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521291413 171 QPKLLIADEPTTALDVTIQAQIIELLLELQQkeNMALILITHDLALVAEAAhKIIVMYAGQVVETG 236
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIIDYD-KILVMDAGEVKEYD 205
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-246 |
5.26e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 87.20 E-value: 5.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 26 VSYSVSQGEVVGIVGESGSGKSvSSLAIM-GLIDFPGRVMaekleFNGQDLKRISEKE---RRslvgsevAMIFQDPMTS 101
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKS-TLLARMaGLLPGQGEIL-----LNGRPLSDWSAAElarHR-------AYLSQQQSPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 102 LN-PCYtvgfqimEAIKVHQGGNkkTRRQRAIDLLNQVgipdpASRL---DVYP---HQLSGGMSQRVMIAmAIACQ--- 171
Cdd:COG4138 82 FAmPVF-------QYLALHQPAG--ASSEAVEQLLAQL-----AEALgleDKLSrplTQLSGGEWQRVRLA-AVLLQvwp 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 172 -----PKLLIADEPTTALDVTIQAQIIELLLELQQKENmALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDIFRAPR 246
Cdd:COG4138 147 tinpeGQLLLLDEPMNSLDVAQQAALDRLLRELCQQGI-TVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPEN 225
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-240 |
9.46e-20 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 89.46 E-value: 9.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 21 RAVDRVSYSVSQGEVVGIVGESGSGKSvsslAIM-------------GLIDFPGRVMaeklEFngqdlKRISEKERRSLV 87
Cdd:NF040905 15 KALDDVNLSVREGEIHALCGENGAGKS----TLMkvlsgvyphgsyeGEILFDGEVC----RF-----KDIRDSEALGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 88 --GSEVAMIfqdPMTSlnpcytvgfqIMEAIKVhqgGNKKTRR---------QRAIDLLNQVGIP-DPASRLDvyphQLS 155
Cdd:NF040905 82 iiHQELALI---PYLS----------IAENIFL---GNERAKRgvidwnetnRRARELLAKVGLDeSPDTLVT----DIG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 156 GGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALILITHDLALVAEAAHKIIVMYAGQVVET 235
Cdd:NF040905 142 VGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIET 220
|
....*
gi 521291413 236 GEAKD 240
Cdd:NF040905 221 LDCRA 225
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-236 |
1.10e-19 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 85.88 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKLSVHFGDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIdfpgRVMAEKLEFNGQDLKRISEKE 82
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLL----EPDAGFATVDGFDVVKEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 83 RRSLVGSEVAMIFQDPMTSL-NPCYTVGFQIMeaikvhQGGNKKTRRQRAIDLLnqvgipDPASRLDVYPHQLSGGMSQR 161
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTAReNLEYFAGLYGL------KGDELTARLEELADRL------GMEELLDRRVGGFSTGMRQK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521291413 162 VMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALILITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:cd03266 145 VAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRA-LGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
22-245 |
2.53e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 86.01 E-value: 2.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 22 AVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLID-FPGRVMAEklefnGQDLKRISEKERRSLVGsevaMIFQDPMT 100
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKpTSGSVLIR-----GEPITKENIREVRKFVG----LVFQNPDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 101 SL-NPcyTVGfQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLdvyPHQLSGGMSQRVMIAMAIACQPKLLIADE 179
Cdd:PRK13652 90 QIfSP--TVE-QDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRV---PHHLSGGEKKRVAIAGVIAMEPQVLVLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521291413 180 PTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDIFRAP 245
Cdd:PRK13652 164 PTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
22-244 |
3.07e-19 |
|
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: 85.23 E-value: 3.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 22 AVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGL-IDFPGRVMAEklefnGQDLKRISEKERRSLVGsevaMIFQDPmT 100
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRVLVD-----GHDLALADPAWLRRQVG----VVLQEN-V 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 101 SLNPcytvgfQIMEAIKVhqgGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQ--------LSGGMSQRVMIAMAIACQP 172
Cdd:cd03252 87 LFNR------SIRDNIAL---ADPGMSMERVIEAAKLAGAHDFISELPEGYDTivgeqgagLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521291413 173 KLLIADEPTTALDVTIQAQIIELLLELQqkENMALILITHDLALVaEAAHKIIVMYAGQVVETGEAKDIFRA 244
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDIC--AGRTVIIIAHRLSTV-KNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
21-245 |
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 521291413 21 RAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIdfpgRVMAEKLEFNGQDLKRISEKERRSL-VG--SEVAMIFQD 97
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLV----KPDSGKILLDGQDITKLPMHKRARLgIGylPQEASIFRK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 98 pmtslnpcYTVGFQIMEAIKVHqGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACQPKLLIA 177
Cdd:cd03218 90 --------LTVEENILAVLEIR-GLSKKEREEKLEELLEEFHI---THLRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521291413 178 DEPTTALDVTIQAQIIELLLELQQKeNMAlILIT-HDLALVAEAAHKIIVMYAGQVVETGEAKDIFRAP 245
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKILKDR-GIG-VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
10-236 |
4.55e-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: 84.59 E-value: 4.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 10 SVHFGDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSvsslAIMGLIDFPGRVMAEKLEFNGQDLKRISEKERRSLVG- 88
Cdd:cd03251 5 NVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKS----TLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 89 -SEVAMIFQDpmtslnpcytvgfQIMEAIKVhqgGNKKTRRQRAIDLLNQVGIPDPASRLDVYPH--------QLSGGMS 159
Cdd:cd03251 81 vSQDVFLFND-------------TVAENIAY---GRPGATREEVEEAARAANAHEFIMELPEGYDtvigergvKLSGGQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521291413 160 QRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQqkENMALILITHDLALVaEAAHKIIVMYAGQVVETG 236
Cdd:cd03251 145 QRIAIARALLKDPPILILDEATSALDTESERLVQAALERLM--KNRTTFVIAHRLSTI-ENADRIVVLEDGKIVERG 218
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-255 |
8.68e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 84.30 E-value: 8.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 4 LNVDKLSVHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSvSSLAIMGLIDFPgrvMAEKLEFNGQDLKRISEKEr 83
Cdd:PRK11231 3 LRTENLTVGYGTK----RILNDLSLSLPTGKITALIGPNGCGKS-TLLKCFARLLTP---QSGTVFLGDKPISMLSSRQ- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 84 rslVGSEVAMIFQDPMTSlnpcytvgfqimEAIKVHQ----------------GGNKKTRRQRAidlLNQVGIPDPASRL 147
Cdd:PRK11231 74 ---LARRLALLPQHHLTP------------EGITVRElvaygrspwlslwgrlSAEDNARVNQA---MEQTRINHLADRR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 148 dvyPHQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALILITHDLALVAEAAHKIIVM 227
Cdd:PRK11231 136 ---LTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNT-QGKTVVTVLHDLNQASRYCDHLVVL 211
|
250 260
....*....|....*....|....*...
gi 521291413 228 YAGQVVETGEAKDIFraprhpyTQALLR 255
Cdd:PRK11231 212 ANGHVMAQGTPEEVM-------TPGLLR 232
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
33-272 |
9.60e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 87.02 E-value: 9.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 33 GEVVGIVGESGSGKSVSSLAIMGLIDfPGRVMAEKLEFNGQDLKRiSEKERRSlvgsevAMIFQDPMtsLNPCYTV--GF 110
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSP-KGVKGSGSVLLNGMPIDA-KEMRAIS------AYVQQDDL--FIPTLTVreHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 111 QIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQ---LSGGMSQRVMIAMAIACQPKLLIADEPTTALDVT 187
Cdd:TIGR00955 121 MFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSF 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 188 IQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETG---EAKDIFRAPRHP----YTQAllralpEF 260
Cdd:TIGR00955 201 MAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGspdQAVPFFSDLGHPcpenYNPA------DF 274
|
250
....*....|..
gi 521291413 261 AQDKarLASLPG 272
Cdd:TIGR00955 275 YVQV--LAVIPG 284
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-244 |
1.18e-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: 83.60 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 1 MALLNVDKLSVHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSvsSLaiMGLI---DFPGRvmAEKLEFNGQDLKR 77
Cdd:COG1119 1 DPLLELRNVTVRRGGK----TILDDISWTVKPGEHWAILGPNGAGKS--TL--LSLItgdLPPTY--GNDVRLFGERRGG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 78 ISEKERRSLVG---SEVAMIFQDPMTSLNpcyTV--GF----QIMEAIKVHQggnkktrRQRAIDLLNQVGIpdpASRLD 148
Cdd:COG1119 71 EDVWELRKRIGlvsPALQLRFPRDETVLD---VVlsGFfdsiGLYREPTDEQ-------RERARELLELLGL---AHLAD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 149 VYPHQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMY 228
Cdd:COG1119 138 RPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLK 217
|
250
....*....|....*.
gi 521291413 229 AGQVVETGEAKDIFRA 244
Cdd:COG1119 218 DGRVVAAGPKEEVLTS 233
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-241 |
1.30e-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: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 1 MALLNVDKLSVHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIdFP--GRVMaekleFNGQDLKRI 78
Cdd:COG1137 1 MMTLEAENLVKSYGKR----TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLV-KPdsGRIF-----LDGEDITHL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 79 SeKERRSLVG-----SEvAMIFQDpmtsLnpcyTVGFQIMeAIKVHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQ 153
Cdd:COG1137 71 P-MHKRARLGigylpQE-ASIFRK----L----TVEDNIL-AVLELRKLSKKEREERLEELLEEFGI---THLRKSKAYS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 154 LSGGMSQRVMIAMAIACQPKLLIADEPTTALD-VTIqAQIIELLLELQQKeNMAlILIT-HD----LALVAEAAhkiiVM 227
Cdd:COG1137 137 LSGGERRRVEIARALATNPKFILLDEPFAGVDpIAV-ADIQKIIRHLKER-GIG-VLITdHNvretLGICDRAY----II 209
|
250
....*....|....
gi 521291413 228 YAGQVVETGEAKDI 241
Cdd:COG1137 210 SEGKVLAEGTPEEI 223
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
17-236 |
1.42e-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: 82.64 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 17 GSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDfP--GRVMaekleFNGQDLKRISEKERR---SLVGSEV 91
Cdd:cd03245 14 NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYK-PtsGSVL-----LDGTDIRQLDPADLRrniGYVPQDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 92 AMIF---QDPMTSLNPcYTVGFQIMEAIKVhQGGNKKTRRQ-RAIDLlnQVGipdpaSRLDvyphQLSGGMSQRVMIAMA 167
Cdd:cd03245 88 TLFYgtlRDNITLGAP-LADDERILRAAEL-AGVTDFVNKHpNGLDL--QIG-----ERGR----GLSGGQRQAVALARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521291413 168 IACQPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALILITHDLALVaEAAHKIIVMYAGQVVETG 236
Cdd:cd03245 155 LLNDPPILLLDEPTSAMDMNSEERLKERLRQL--LGDKTLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
22-245 |
3.73e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 84.23 E-value: 3.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 22 AVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDF-PGRVMaekleFNGQDLKRISEKERrslvgsEVAMIFQDpmT 100
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPdSGRIM-----LDGQDITHVPAENR------HVNTVFQS--Y 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 101 SLNPCYTVGFQIMEAIKVHQGGNKKTRRqRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACQPKLLIADEP 180
Cdd:PRK09452 96 ALFPHMTVFENVAFGLRMQKTPAAEITP-RVMEALRMVQLEEFAQR---KPHQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521291413 181 TTALDVTIQAQIIELLLELQQKENMALILITHDLalvAEA---AHKIIVMYAGQVVETGEAKDIFRAP 245
Cdd:PRK09452 172 LSALDYKLRKQMQNELKALQRKLGITFVFVTHDQ---EEAltmSDRIVVMRDGRIEQDGTPREIYEEP 236
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-239 |
5.23e-18 |
|
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: 84.49 E-value: 5.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKLSVHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLidFPGRVMAEKLEFNGQDLK--RISE 80
Cdd:TIGR02633 1 LLEMKGIVKTFGGV----KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV--YPHGTWDGEIYWSGSPLKasNIRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 81 KERRSLVgsevaMIFQDPMtsLNPCYTVGFQIMEAIKV-HQGG--NKKTRRQRAIDLLNQVGIPDPASRLDVypHQLSGG 157
Cdd:TIGR02633 75 TERAGIV-----IIHQELT--LVPELSVAENIFLGNEItLPGGrmAYNAMYLRAKNLLRELQLDADNVTRPV--GDYGGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 158 MSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALILITHDLALVAEAAHKIIVMYAGQVVETGE 237
Cdd:TIGR02633 146 QQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVATKD 224
|
..
gi 521291413 238 AK 239
Cdd:TIGR02633 225 MS 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-251 |
5.97e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 82.01 E-value: 5.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 21 RAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDFPGRVMAE-KLEFNGQDL--KRISEKERRSlvgsEVAMIFQD 97
Cdd:PRK14258 21 KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEgRVEFFNQNIyeRRVNLNRLRR----QVSMVHPK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 98 PmtSLNPcYTVGFQIMEAIKVhQGGNKKTRRQ-------RAIDLLNQVGIPDPASRLDvyphqLSGGMSQRVMIAMAIAC 170
Cdd:PRK14258 97 P--NLFP-MSVYDNVAYGVKI-VGWRPKLEIDdivesalKDADLWDEIKHKIHKSALD-----LSGGQQQRLCIARALAV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 171 QPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYA-----GQVVETGEAKDIFRAP 245
Cdd:PRK14258 168 KPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSP 247
|
....*.
gi 521291413 246 RHPYTQ 251
Cdd:PRK14258 248 HDSRTR 253
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-241 |
7.06e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.91 E-value: 7.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKLSVHfgdvgsefRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIdfpgRVMAEKLEFNGQDLKRISEKE 82
Cdd:COG1129 256 VLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGAD----PADSGEIRLDGKPVRIRSPRD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 83 RrslVGSEVAMIFQDPMTS-LNPCYTVGFQIMEAI--KVHQGG--NKKTRRQRAIDLLNQVGI--PDPASRLDvyphQLS 155
Cdd:COG1129 324 A---IRAGIAYVPEDRKGEgLVLDLSIRENITLASldRLSRGGllDRRRERALAEEYIKRLRIktPSPEQPVG----NLS 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 156 GGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALILITHDLALVAEAAHKIIVMYAGQVVET 235
Cdd:COG1129 397 GGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIREL-AAEGKAVIVISSELPELLGLSDRILVMREGRIVGE 475
|
....*.
gi 521291413 236 GEAKDI 241
Cdd:COG1129 476 LDREEA 481
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
22-262 |
8.37e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.96 E-value: 8.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 22 AVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIdfpgRVMAEKLEFNGQDLKRISE-KERRSLVGsevaMIFQDPMT 100
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLL----RPQKGKVLVSGIDTGDFSKlQGIRKLVG----IVFQNPET 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 101 SLnpcytVGFQIMEAIKVhqgGNKK------TRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACQPKL 174
Cdd:PRK13644 89 QF-----VGRTVEEDLAF---GPENlclppiEIRKRVDRALAEIGLEKYRHR---SPKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 175 LIADEPTTALDVTIQAQIIELLLELQQKeNMALILITHDLALVaEAAHKIIVMYAGQVVETGEAKDIFRAPRHPYTQALL 254
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGLTP 235
|
....*...
gi 521291413 255 RALPEFAQ 262
Cdd:PRK13644 236 PSLIELAE 243
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-252 |
1.14e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 81.37 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKLSVHFGDvgseFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDF-PGRVMAEKLEFNGQDL--KRIS 79
Cdd:PRK14243 10 VLRTENLNVYYGS----FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLiPGFRVEGKVTFHGKNLyaPDVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 80 EKERRSLVGsevaMIFQDPmtslNPC-YTVGFQIMEAIKV--HQGGN----KKTRRQRAI-----DLLNQVGIpdpasrl 147
Cdd:PRK14243 86 PVEVRRRIG----MVFQKP----NPFpKSIYDNIAYGARIngYKGDMdelvERSLRQAALwdevkDKLKQSGL------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 148 dvyphQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALILITHDLALVAEAAHKIIVM 227
Cdd:PRK14243 151 -----SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL--KEQYTIIIVTHNMQQAARVSDMTAFF 223
|
250 260 270
....*....|....*....|....*....|....
gi 521291413 228 YA---------GQVVETGEAKDIFRAPRHPYTQA 252
Cdd:PRK14243 224 NVeltegggryGYLVEFDRTEKIFNSPQQQATRD 257
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
27-239 |
1.84e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 83.23 E-value: 1.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 27 SYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDFPGrvmaeklefnGQ---DLKRISEKERRSLvGSEVAMIFQDPM---- 99
Cdd:TIGR00958 501 TFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTG----------GQvllDGVPLVQYDHHYL-HRQVALVGQEPVlfsg 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 100 -TSLNPCYTVGF----QIMEAIKVHQGGNKKTRRQRAIDLlnqvgipdpasrlDVYPH--QLSGGMSQRVMIAMAIACQP 172
Cdd:TIGR00958 570 sVRENIAYGLTDtpdeEIMAAAKAANAHDFIMEFPNGYDT-------------EVGEKgsQLSGGQKQRIAIARALVRKP 636
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521291413 173 KLLIADEPTTALDVTIQAqiieLLLELQQKENMALILITHDLALVaEAAHKIIVMYAGQVVETGEAK 239
Cdd:TIGR00958 637 RVLILDEATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTV-ERADQILVLKKGSVVEMGTHK 698
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-246 |
1.88e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 82.00 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 1 MA---LLNVDKlsvHFGDVgsefrAVDR-VSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDfpgrVMAEKLEFNGQDLK 76
Cdd:PRK11000 1 MAsvtLRNVTK---AYGDV-----VISKdINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLED----ITSGDLFIGEKRMN 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 77 RISEKERrslvgsEVAMIFQDpmTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRaidlLNQVG-IPDPASRLDVYPHQLS 155
Cdd:PRK11000 69 DVPPAER------GVGMVFQS--YALYPHLSVAENMSFGLKL-AGAKKEEINQR----VNQVAeVLQLAHLLDRKPKALS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 156 GGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQI-IElLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVE 234
Cdd:PRK11000 136 GGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMrIE-ISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQ 214
|
250
....*....|..
gi 521291413 235 TGEAKDIFRAPR 246
Cdd:PRK11000 215 VGKPLELYHYPA 226
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
11-236 |
2.18e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 82.70 E-value: 2.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 11 VHFGDVGSEF----RAVDRVSYSVSQGEVVGIVGESGSGKSVsslaimgLIDFPGRVM---AEKLEFNGQDLKRISekeR 83
Cdd:PRK13657 335 VEFDDVSFSYdnsrQGVEDVSFEAKPGQTVAIVGPTGAGKST-------LINLLQRVFdpqSGRILIDGTDIRTVT---R 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 84 RSLVGSeVAMIFQDPM---TSLNPCYTVG------FQIMEAIKvhqggnkktrRQRAIDLLnqvgipdpASRLDVYP--- 151
Cdd:PRK13657 405 ASLRRN-IAVVFQDAGlfnRSIEDNIRVGrpdatdEEMRAAAE----------RAQAHDFI--------ERKPDGYDtvv 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 152 ----HQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQkeNMALILITHDLALVAEAAhKIIVM 227
Cdd:PRK13657 466 gergRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRNAD-RILVF 542
|
....*....
gi 521291413 228 YAGQVVETG 236
Cdd:PRK13657 543 DNGRVVESG 551
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-246 |
2.88e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 80.90 E-value: 2.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 19 EFRAVDRVSYSVSQGEVVGIVGESGSGKSvSSLAIM-GLIdFP--GRVmaeklEFNGqdlkRISEKERRSLVgSEVAMIF 95
Cdd:COG4586 34 EVEAVDDISFTIEPGEIVGFIGPNGAGKS-TTIKMLtGIL-VPtsGEV-----RVLG----YVPFKRRKEFA-RRIGVVF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 96 -Q------D--PMTSlnpcytvgFQIMEAI-----KVHqggnkKTRRQRAIDLLNQVGIpdpasrLDVYPHQLSGGmsQR 161
Cdd:COG4586 102 gQrsqlwwDlpAIDS--------FRLLKAIyripdAEY-----KKRLDELVELLDLGEL------LDTPVRQLSLG--QR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 162 vM---IAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETG-- 236
Cdd:COG4586 161 -MrceLAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGsl 239
|
250
....*....|.
gi 521291413 237 -EAKDIFRAPR 246
Cdd:COG4586 240 eELKERFGPYK 250
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
26-236 |
6.49e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 78.57 E-value: 6.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 26 VSYSVSQGEVVGIVGESGSGKSVSSLAIMGlidFPG-RVMAEKLEFNGQDLKRISEKERrSLVGseVAMIFQDPMTSlnP 104
Cdd:COG0396 19 VNLTIKPGEVHAIMGPNGSGKSTLAKVLMG---HPKyEVTSGSILLDGEDILELSPDER-ARAG--IFLAFQYPVEI--P 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 105 CYTVGFQIMEAIKVHQGGNKKTR--RQRAIDLLNQVGI-PDPASR-LDVyphQLSGGMSQRVMIAMAIACQPKLLIADEP 180
Cdd:COG0396 91 GVSVSNFLRTALNARRGEELSARefLKLLKEKMKELGLdEDFLDRyVNE---GFSGGEKKRNEILQMLLLEPKLAILDET 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 181 TTALDV---TIQAQIIELLlelqQKENMALILITHDLALVAE-AAHKIIVMYAGQVVETG 236
Cdd:COG0396 168 DSGLDIdalRIVAEGVNKL----RSPDRGILIITHYQRILDYiKPDFVHVLVDGRIVKSG 223
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-246 |
7.70e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 78.44 E-value: 7.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 26 VSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDFPGRVMaekleFNGQDLKRISEKE---RRSLVGSEVAMIFQDPMtsl 102
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQ-----FAGQPLEAWSAAElarHRAYLSQQQTPPFAMPV--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 103 npcytvgFQiMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAI-----ACQP--KLL 175
Cdd:PRK03695 87 -------FQ-YLTLHQPDKTRTEAVASALNEVAEALGLDDKLGR---SVNQLSGGEWQRVRLAAVVlqvwpDINPagQLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521291413 176 IADEPTTALDVTIQAQIIELLLELQQKeNMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDIFRAPR 246
Cdd:PRK03695 156 LLDEPMNSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
23-232 |
2.33e-16 |
|
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: 75.33 E-value: 2.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 23 VDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIdfpgRVMAEKLEFNGQDLKRISEKERRSLVGSevamIFQDPMTsl 102
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLL----RPTSGRVRLDGADISQWDPNELGDHVGY----LPQDDEL-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 103 npcytvgFQ--IMEAIkvhqggnkktrrqraidllnqvgipdpasrldvyphqLSGGMSQRVMIAMAIACQPKLLIADEP 180
Cdd:cd03246 88 -------FSgsIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEP 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 521291413 181 TTALDVTIQAQIIELLLELqQKENMALILITHDLALVAeAAHKIIVMYAGQV 232
Cdd:cd03246 124 NSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-236 |
2.72e-16 |
|
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: 76.60 E-value: 2.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 19 EFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIdFP--GRVmaeklEFNGQD--LKRISEKERRSLV-GSEVAM 93
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLL-QPtsGEV-----RVAGLVpwKRRKKFLRRIGVVfGQKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 94 IFQDPMTSlnpcytvGFQIMEAIKVHQGGNKKTRRQRAIDLLnqvgipDPASRLDVYPHQLSGGMSQRVMIAMAIACQPK 173
Cdd:cd03267 107 WWDLPVID-------SFYLLAAIYDLPPARFKKRLDELSELL------DLEELLDTPVRQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521291413 174 LLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
19-236 |
2.81e-16 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 76.03 E-value: 2.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 19 EFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGlidFPG-RVMAEKLEFNGQDLKRISEKERrSLVGseVAMIFQD 97
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG---HPKyEVTEGEILFKGEDITDLPPEER-ARLG--IFLAFQY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 98 PMTslnpcytvgfqiMEAIKVhqggnkktrrqraIDLLNQVGIpdpasrldvyphQLSGGMSQRVMIAMAIACQPKLLIA 177
Cdd:cd03217 86 PPE------------IPGVKN-------------ADFLRYVNE------------GFSGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521291413 178 DEPTTALDVT---IQAQIIELLLElqqkENMALILITH--DLA--LVAEAAHkiiVMYAGQVVETG 236
Cdd:cd03217 129 DEPDSGLDIDalrLVAEVINKLRE----EGKSVLIITHyqRLLdyIKPDRVH---VLYDGRIVKSG 187
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
13-212 |
3.01e-16 |
|
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: 76.54 E-value: 3.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 13 FGDVGSEFRAVDR-------VSYSVSQGEVVGIVGESGSGKSVSSLAIMGLID----FPGRVMaekleFNGQDLKRisek 81
Cdd:cd03234 6 WWDVGLKAKNWNKyarilndVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggtTSGQIL-----FNGQPRKP---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 82 errSLVGSEVAMIFQDpmTSLNPCYTVG----FQIMEAIKVHQggNKKTRRQRAID-LLNQVGIPDPAsrlDVYPHQLSG 156
Cdd:cd03234 77 ---DQFQKCVAYVRQD--DILLPGLTVRetltYTAILRLPRKS--SDAIRKKRVEDvLLRDLALTRIG---GNLVKGISG 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 521291413 157 GMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALILITH 212
Cdd:cd03234 147 GERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQL-ARRNRIVILTIH 201
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
20-245 |
4.96e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 76.75 E-value: 4.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 20 FRAVDRV-----SYSVSQGEVVGIVGESGSGKSvSSLAIMGLIDFP--GRVMaekleFNGQDLKRISEKerrsLVGSEVA 92
Cdd:PRK10575 19 FRVPGRTllhplSLTFPAGKVTGLIGHNGSGKS-TLLKMLGRHQPPseGEIL-----LDAQPLESWSSK----AFARKVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 93 MIFQD-PMTSlnpcytvGFQIMEAIKVHQ----------GGNKKTRRQRAIDLlnqVGIPDPASRLdvyPHQLSGGMSQR 161
Cdd:PRK10575 89 YLPQQlPAAE-------GMTVRELVAIGRypwhgalgrfGAADREKVEEAISL---VGLKPLAHRL---VDSLSGGERQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 162 VMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDI 241
Cdd:PRK10575 156 AWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
....
gi 521291413 242 FRAP 245
Cdd:PRK10575 236 MRGE 239
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-244 |
5.79e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 76.56 E-value: 5.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 2 ALLNVDKLSVHFGdvgsEFRAVDRVSYSVSQGEVVGIVGESGSGKSVsslaimgLIDFPGRVMAE---KLEFNGQDLKRI 78
Cdd:PRK10253 6 ARLRGEQLTLGYG----KYTVAENLTVEIPDGHFTAIIGPNGCGKST-------LLRTLSRLMTPahgHVWLDGEHIQHY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 79 SEKErrslVGSEVAMIFQDPMTSLNpcYTVGFQIMEAIKVHQGGNKKTRRQRAIDL---LNQVGIPDPASR-LDVyphqL 154
Cdd:PRK10253 75 ASKE----VARRIGLLAQNATTPGD--ITVQELVARGRYPHQPLFTRWRKEDEEAVtkaMQATGITHLADQsVDT----L 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 155 SGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVE 234
Cdd:PRK10253 145 SGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVA 224
|
250
....*....|
gi 521291413 235 TGEAKDIFRA 244
Cdd:PRK10253 225 QGAPKEIVTA 234
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-239 |
8.06e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 75.82 E-value: 8.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKLSVHFgdvgSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLI--DFPGRVMAEKLEFNGQDLKRISE 80
Cdd:PRK09984 4 IIRVEKLAKTF----NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGSHIELLGRTVQREGRLAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 81 KERRSLvgSEVAMIFQDpMTSLNPcytvgFQIMEAIKVHQGGN-----------KKTRRQRAIDLLNQVGIPDpasrldv 149
Cdd:PRK09984 80 DIRKSR--ANTGYIFQQ-FNLVNR-----LSVLENVLIGALGStpfwrtcfswfTREQKQRALQALTRVGMVH------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 150 YPHQ----LSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKII 225
Cdd:PRK09984 145 FAHQrvstLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIV 224
|
250
....*....|....
gi 521291413 226 VMYAGQVVETGEAK 239
Cdd:PRK09984 225 ALRQGHVFYDGSSQ 238
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-232 |
1.59e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 75.10 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 4 LNVDKLSVHFGDvgsefRAV-DRVSYSVSQGEVVGIVGESGSGKSvSSLAIMGLIDFP--GRVMAeklefNGQDLKRISE 80
Cdd:PRK11247 13 LLLNAVSKRYGE-----RTVlNQLDLHIPAGQFVAVVGRSGCGKS-TLLRLLAGLETPsaGELLA-----GTAPLAEARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 81 KERrslvgsevaMIFQDpmTSLNPCYTVgfqiMEAIKVHQGGNkktRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQ 160
Cdd:PRK11247 82 DTR---------LMFQD--ARLLPWKKV----IDNVGLGLKGQ---WRDAALQALAAVGL---ADRANEWPAALSGGQKQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521291413 161 RVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDlalVAEA---AHKIIVMYAGQV 232
Cdd:PRK11247 141 RVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHD---VSEAvamADRVLLIEEGKI 212
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
22-244 |
1.77e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 75.30 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 22 AVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIdfpgRVMAEKLEFNGQDLkrisekeRRSLVGSEVAMIFQDPMTS 101
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFV----RLASGKISILGQPT-------RQALQKNLVAYVPQSEEVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 102 LNPCYTVGFQIMEAIKVHQG---GNKKTRRQRAIDLLNQVGIPDpasrldvYPH----QLSGGMSQRVMIAMAIACQPKL 174
Cdd:PRK15056 91 WSFPVLVEDVVMMGRYGHMGwlrRAKKRDRQIVTAALARVDMVE-------FRHrqigELSGGQKKRVFLARAIAQQGQV 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 175 LIADEPTTALDVTIQAQIIELLLELQQkENMALILITHDLALVAEAAhKIIVMYAGQVVETGEAKDIFRA 244
Cdd:PRK15056 164 ILLDEPFTGVDVKTEARIISLLRELRD-EGKTMLVSTHNLGSVTEFC-DYTVMVKGTVLASGPTETTFTA 231
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-232 |
3.99e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.86 E-value: 3.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKLSvhfgdvGSEFRavdRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLidfpGRVMAEKLEFNGQDLKRISEKE 82
Cdd:PRK15439 268 VLTVEDLT------GEGFR---NISLEVRAGEILGLAGVVGAGRTELAETLYGL----RPARGGRIMLNGKEINALSTAQ 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 83 R--RSLV----GSEVAMIFQDPMTSLNPCytvgfqimeAIKVHQGGN-KKTRRQRAI--DLLNQVGI----PDPASRldv 149
Cdd:PRK15439 335 RlaRGLVylpeDRQSSGLYLDAPLAWNVC---------ALTHNRRGFwIKPARENAVleRYRRALNIkfnhAEQAAR--- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 150 yphQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALILITHDLALVAEAAHKIIVMYA 229
Cdd:PRK15439 403 ---TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSI-AAQNVAVLFISSDLEEIEQMADRVLVMHQ 478
|
...
gi 521291413 230 GQV 232
Cdd:PRK15439 479 GEI 481
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
31-242 |
5.13e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.89 E-value: 5.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 31 SQGEVVGIVGESGSGKSVSSLAIMGLIdfpgRVMAEKLEFNGQDLkrisEKERRSLVG--SEVAMIFQDPMTSLnpCYT- 107
Cdd:PRK13638 25 SLSPVTGLVGANGCGKSTLFMNLSGLL----RPQKGAVLWQGKPL----DYSKRGLLAlrQQVATVFQDPEQQI--FYTd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 108 VGFQIMEAIKvHQGGNKKTRRQRAIDLLNQVGipdpASRLDVYPHQ-LSGGMSQRVMIAMAIACQPKLLIADEPTTALDV 186
Cdd:PRK13638 95 IDSDIAFSLR-NLGVPEAEITRRVDEALTLVD----AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 521291413 187 TIQAQIIELLLELQQKENMaLILITHDLALVAEAAHKIIVMYAGQVVETGEAKDIF 242
Cdd:PRK13638 170 AGRTQMIAIIRRIVAQGNH-VIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
23-232 |
5.68e-15 |
|
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: 75.25 E-value: 5.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 23 VDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLidFPGRVMAEKLeFNGqdlKRISEKERRSLVGSEVAMIFQD-PMTS 101
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGA--YPGKFEGNVF-ING---KPVDIRNPAQAIRAGIAMVPEDrKRHG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 102 LNPCYTVGFQIMEAIKvhqggNKKTRRQRAIDLLNQVGIPDPASRLDV---YPH----QLSGGMSQRVMIAMAIACQPKL 174
Cdd:TIGR02633 350 IVPILGVGKNITLSVL-----KSFCFKMRIDAAAELQIIGSAIQRLKVktaSPFlpigRLSGGNQQKAVLAKMLLTNPRV 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 521291413 175 LIADEPTTALDVTIQAQIIELLLELQQkENMALILITHDLALVAEAAHKIIVMYAGQV 232
Cdd:TIGR02633 425 LILDEPTRGVDVGAKYEIYKLINQLAQ-EGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
133-227 |
1.26e-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: 69.78 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 133 DLLNQVGIPDPASRLDV-YPHQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQkenmALILIT 211
Cdd:cd03221 49 ELEPDEGIVTWGSTVKIgYFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPG----TVILVS 124
|
90
....*....|....*.
gi 521291413 212 HDLALVAEAAHKIIVM 227
Cdd:cd03221 125 HDRYFLDQVATKIIEL 140
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
11-236 |
1.39e-14 |
|
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: 70.80 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 11 VHFGDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDfpgrVMAEKLEFNGQDLKrISEKERRSLVGse 90
Cdd:cd03247 6 VSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLK----PQQGEITLDGVPVS-DLEKALSSLIS-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 91 vaMIFQDPMTslnpcytvgFqimeaikvhqggnkktrrqrAIDLLNQVGIpdpasrldvyphQLSGGMSQRVMIAMAIAC 170
Cdd:cd03247 79 --VLNQRPYL---------F--------------------DTTLRNNLGR------------RFSGGERQRLALARILLQ 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521291413 171 QPKLLIADEPTTALDVTIQAQIIELLLElqQKENMALILITHDLALVaEAAHKIIVMYAGQVVETG 236
Cdd:cd03247 116 DAPIVLLDEPTVGLDPITERQLLSLIFE--VLKDKTLIWITHHLTGI-EHMDKILFLENGKIIMQG 178
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
26-232 |
1.47e-14 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 71.73 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 26 VSYSVSQGEVVGIVGESGSGKSvSSLAIMGLIDFP--GRVMAeklefngqDLKRISEKERRSLvGSEVAMIFQDPMT--- 100
Cdd:cd03248 33 VSFTLHPGEVTALVGPSGSGKS-TVVALLENFYQPqgGQVLL--------DGKPISQYEHKYL-HSKVSLVGQEPVLfar 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 101 SLNPCYTVGFQ------IMEA-IKVHQGGNkktrrqraIDLLNQvgipDPASRLDVYPHQLSGGMSQRVMIAMAIACQPK 173
Cdd:cd03248 103 SLQDNIAYGLQscsfecVKEAaQKAHAHSF--------ISELAS----GYDTEVGEKGSQLSGGQKQRVAIARALIRNPQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 521291413 174 LLIADEPTTALDVTIQAQIIELLleLQQKENMALILITHDLALVaEAAHKIIVMYAGQV 232
Cdd:cd03248 171 VLILDEATSALDAESEQQVQQAL--YDWPERRTVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-236 |
1.78e-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: 71.41 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 19 EFRAVDRVSYSVSQGEVVGIVGESGSGKSvSSLAIMGLIDFP--GRVmaeklefngqdlkrisekERRslvGSEVAMIfq 96
Cdd:cd03220 34 EFWALKDVSFEVPRGERIGLIGRNGAGKS-TLLRLLAGIYPPdsGTV------------------TVR---GRVSSLL-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 97 DPMTSLNPCYTVgfqiMEAIKVH---QGGNKKTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMSQRVMIAMAIACQPK 173
Cdd:cd03220 90 GLGGGFNPELTG----RENIYLNgrlLGLSRKEIDEKIDEIIEFSELGD---FIDLPVKTYSSGMKARLAFAIATALEPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521291413 174 LLIADEPTTALDVTIQAQIIELLLELQQKeNMALILITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:cd03220 163 ILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
10-236 |
3.46e-14 |
|
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: 70.60 E-value: 3.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 10 SVHFGDVGSEFR-----AVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDfpgrVMAEKLEFNGQDLKRISEKERR 84
Cdd:cd03244 2 DIEFKNVSLRYRpnlppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVE----LSSGSILIDGVDISKIGLHDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 85 SLVgsevAMIFQDPMT-------SLNPC--YTVGfQIMEAIKvhQGGNKKTrrqraidLLNQVGIPDpaSRLDVYPHQLS 155
Cdd:cd03244 78 SRI----SIIPQDPVLfsgtirsNLDPFgeYSDE-ELWQALE--RVGLKEF-------VESLPGGLD--TVVEEGGENLS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 156 GGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLlelqqKENMA---LILITHDLALVAEAaHKIIVMYAGQV 232
Cdd:cd03244 142 VGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTI-----REAFKdctVLTIAHRLDTIIDS-DRILVLDKGRV 215
|
....
gi 521291413 233 VETG 236
Cdd:cd03244 216 VEFD 219
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
19-244 |
3.79e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 70.88 E-value: 3.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 19 EFRAVDRVSYSVSQGEVVGIVGESGSGKSvSSLAIMGLIDFP--GRVmaeklEFNGqdlkRISekerrSLVgsEVAMIFQ 96
Cdd:COG1134 38 EFWALKDVSFEVERGESVGIIGRNGAGKS-TLLKLIAGILEPtsGRV-----EVNG----RVS-----ALL--ELGAGFH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 97 DPMTSLNPCYTVGfQIMeaikvhqGGNKKTRRQR------------AIDLlnqvgipdpasrldvyP-HQLSGGMSQRVM 163
Cdd:COG1134 101 PELTGRENIYLNG-RLL-------GLSRKEIDEKfdeivefaelgdFIDQ----------------PvKTYSSGMRARLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 164 IAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDIFR 243
Cdd:COG1134 157 FAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIA 235
|
.
gi 521291413 244 A 244
Cdd:COG1134 236 A 236
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
21-243 |
4.25e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 71.30 E-value: 4.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 21 RAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLID-FPGRVMAEKLEfngqdLKRISEKERRSLVGSEVAMIFQDPM 99
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQpTEGKVTVGDIV-----VSSTSKQKEIKPVRKKVGVVFQFPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 100 TSLnpcytvgFQ--IMEAIKV---HQGGNKKTRRQRAIDLLNQVGIPDpaSRLDVYPHQLSGGMSQRVMIAMAIACQPKL 174
Cdd:PRK13643 95 SQL-------FEetVLKDVAFgpqNFGIPKEKAEKIAAEKLEMVGLAD--EFWEKSPFELSGGQMRRVAIAGILAMEPEV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521291413 175 LIADEPTTALDVTIQAQIIELLLELQQKeNMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDIFR 243
Cdd:PRK13643 166 LVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-236 |
8.09e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 71.80 E-value: 8.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 26 VSYSVSQGEVVGIVGESGSGKSvsSL--AIMGLIDFPGrvmaeKLEFNGQDLKRISEKERRSlvgsEVAMIFQDPMTsln 103
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKT--SLlnALLGFLPYQG-----SLKINGIELRELDPESWRK----HLSWVGQNPQL--- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 104 PCYTvgfqIMEAIKVhqgGNKKTRRQRAIDLLNQVGIPDPASRLDV---YPHQ-----LSGGMSQRVMIAMAIACQPKLL 175
Cdd:PRK11174 435 PHGT----LRDNVLL---GNPDASDEQLQQALENAWVSEFLPLLPQgldTPIGdqaagLSVGQAQRLALARALLQPCQLL 507
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521291413 176 IADEPTTALDVTIQAQIIELLLELQQKEnmALILITHDLALVAEaAHKIIVMYAGQVVETG 236
Cdd:PRK11174 508 LLDEPTASLDAHSEQLVMQALNAASRRQ--TTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQG 565
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
22-225 |
8.46e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 68.80 E-value: 8.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 22 AVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIdfpgRVMAEKLefngqdlkRISEKERRSLVGSEVAMIFQDPMTS 101
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVL----RPTSGTV--------RRAGGARVAYVPQRSEVPDSLPLTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 102 LNpCYTVG-FQimeaikvHQGGNKK-TRRQRAI--DLLNQVGIPDPASR-LDvyphQLSGGMSQRVMIAMAIACQPKLLI 176
Cdd:NF040873 75 RD-LVAMGrWA-------RRGLWRRlTRDDRAAvdDALERVGLADLAGRqLG----ELSGGQRQRALLAQGLAQEADLLL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 521291413 177 ADEPTTALDVTIQAQIIELLLELqQKENMALILITHDLALVAEAAHKII 225
Cdd:NF040873 143 LDEPTTGLDAESRERIIALLAEE-HARGATVVVVTHDLELVRRADPCVL 190
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
11-214 |
1.12e-13 |
|
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: 71.62 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 11 VHFGDVGSEfRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDFP-GRVMaekleFNGQDLKRISEKERRSLVG- 88
Cdd:TIGR02868 340 LSAGYPGAP-PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLqGEVT-----LDGVPVSSLDQDEVRRRVSv 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 89 -SEVAMIFQdpmTSlnpcytvgfqIMEAIKVhqgGNKKTRRQRAIDLLNQVGIPDPASRL------DVYPH--QLSGGMS 159
Cdd:TIGR02868 414 cAQDAHLFD---TT----------VRENLRL---ARPDATDEELWAALERVGLADWLRALpdgldtVLGEGgaRLSGGER 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 521291413 160 QRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLleLQQKENMALILITHDL 214
Cdd:TIGR02868 478 QRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
11-267 |
1.19e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 71.39 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 11 VHFGDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSvsslAIMGLIDFPGRVMAEKLEFNGQDLKRISEKERRSLvgse 90
Cdd:PRK11160 344 VSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKS----TLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQA---- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 91 vamifqdpMTSLNpcytvgfQimeaiKVH----------QGGNKKTRRQRAIDLLNQVGIP---DPASRLDVY----PHQ 153
Cdd:PRK11160 416 --------ISVVS-------Q-----RVHlfsatlrdnlLLAAPNASDEALIEVLQQVGLEkllEDDKGLNAWlgegGRQ 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 154 LSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQkeNMALILITHDLALVaEAAHKIIVMYAGQVV 233
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGL-EQFDRICVMDNGQII 552
|
250 260 270
....*....|....*....|....*....|....
gi 521291413 234 ETGEakdifraprHpytQALLRALPEFAQDKARL 267
Cdd:PRK11160 553 EQGT---------H---QELLAQQGRYYQLKQRL 574
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
19-212 |
2.59e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.06 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 19 EFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDFPgrvmAEKLEFNGQDLKrisekerrslVGSEVAMIfqdp 98
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGT----PVAGCVDVPDNQ----------FGREASLI---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 99 mtslnpcytvgfqimEAIkvHQGGNKKTrrqrAIDLLNQVGIPDPASRLDVYPHqLSGGMSQRVMIAMAIACQPKLLIAD 178
Cdd:COG2401 104 ---------------DAI--GRKGDFKD----AVELLNAVGLSDAVLWLRRFKE-LSTGQKFRFRLALLLAERPKLLVID 161
|
170 180 190
....*....|....*....|....*....|....*
gi 521291413 179 EPTTALDVTiQAQIIEL-LLELQQKENMALILITH 212
Cdd:COG2401 162 EFCSHLDRQ-TAKRVARnLQKLARRAGITLVVATH 195
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
4-236 |
2.62e-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: 70.62 E-value: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 4 LNVDKLSVHFGDVGSEFRAvDR-----VSYSVSQGEVVGIVGESGSGKS-----------VSSLAImgLIDfpgrvmaek 67
Cdd:COG5265 351 LVVGGGEVRFENVSFGYDP-ERpilkgVSFEVPAGKTVAIVGPSGAGKStlarllfrfydVTSGRI--LID--------- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 68 lefnGQDLKRISEKERRSLVGsevaMIFQDpmTSL-NPcyTVGFQI--------MEAIkvhqggnkktrrQRAIDLLNqv 138
Cdd:COG5265 419 ----GQDIRDVTQASLRAAIG----IVPQD--TVLfND--TIAYNIaygrpdasEEEV------------EAAARAAQ-- 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 139 gIPDPASRL-DVYPHQ-------LSGGMSQRVMIAMAIACQPKLLIADEPTTALDV----TIQAQIIELllelqqKENMA 206
Cdd:COG5265 473 -IHDFIESLpDGYDTRvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSrterAIQAALREV------ARGRT 545
|
250 260 270
....*....|....*....|....*....|
gi 521291413 207 LILITHDLALVAEaAHKIIVMYAGQVVETG 236
Cdd:COG5265 546 TLVIAHRLSTIVD-ADEILVLEAGRIVERG 574
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
4-244 |
2.67e-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: 70.16 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 4 LNVDKLSVHFGdvGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSvsSLA--IMGLIdfpgRVMAEKLEFNGQDLKRISEK 81
Cdd:COG4618 331 LSVENLTVVPP--GSKRPILRGVSFSLEPGEVLGVIGPSGSGKS--TLArlLVGVW----PPTAGSVRLDGADLSQWDRE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 82 ERRSLVGsevamiF--QDP-------------MTSLNPCytvgfQIMEAIK---VHQggnkktrrqrAIDLLNQvGIpdp 143
Cdd:COG4618 403 ELGRHIG------YlpQDVelfdgtiaeniarFGDADPE-----KVVAAAKlagVHE----------MILRLPD-GY--- 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 144 ASRLDVYPHQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALILITHDLALVAeAAHK 223
Cdd:COG4618 458 DTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKA-RGATVVVITHRPSLLA-AVDK 535
|
250 260
....*....|....*....|.
gi 521291413 224 IIVMYAGQVVETGEAKDIFRA 244
Cdd:COG4618 536 LLVLRDGRVQAFGPRDEVLAR 556
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-217 |
3.19e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.22 E-value: 3.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKLSVHFGdvgsEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIdfpgrvmaeklefngQDLKRISEKE 82
Cdd:PRK09544 4 LVSLENVSVSFG----QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLV---------------APDEGVIKRN 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 83 RRSLVGSEVAMIFQDPmtslnpcyTVGFQIMEAIKVHQGgnkkTRRQRAIDLLNQVgipdPASRLDVYPHQ-LSGGMSQR 161
Cdd:PRK09544 65 GKLRIGYVPQKLYLDT--------TLPLTVNRFLRLRPG----TKKEDILPALKRV----QAGHLIDAPMQkLSGGETQR 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 521291413 162 VMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALV 217
Cdd:PRK09544 129 VLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLV 184
|
|
| 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 521291413 1 MALLNVDKLSVHFgdvgSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDF-PGRVMAEKLEFNgqdLKRIS 79
Cdd:PRK10895 1 MATLTAKNLAKAY----KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRdAGNIIIDDEDIS---LLPLH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 80 EKERRSL-VGSEVAMIFQDpmtslnpcYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGM 158
Cdd:PRK10895 74 ARARRGIgYLPQEASIFRR--------LSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHI---EHLRDSMGQSLSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 159 SQRVMIAMAIACQPKLLIADEPTTALDvTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEA 238
Cdd:PRK10895 143 RRRVEIARALAANPKFILLDEPFAGVD-PISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTP 221
|
....
gi 521291413 239 KDIF 242
Cdd:PRK10895 222 TEIL 225
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-245 |
5.27e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 67.80 E-value: 5.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 6 VDKLSVHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSvSSLAIMG-LIDF-PGRVmaeklEFNGQDLKRISEKE- 82
Cdd:COG4604 4 IKNVSKRYGGK----VVLDDVSLTIPKGGITALIGPNGAGKS-TLLSMISrLLPPdSGEV-----LVDGLDVATTPSREl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 83 -RRslvgseVAMIFQDPMTSLNpcytvgfqimeaIKV----------HQGG--NKKTRR--QRAIDLLNQVGIPDpaSRL 147
Cdd:COG4604 74 aKR------LAILRQENHINSR------------LTVrelvafgrfpYSKGrlTAEDREiiDEAIAYLDLEDLAD--RYL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 148 DvyphQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVM 227
Cdd:COG4604 134 D----ELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAM 209
|
250
....*....|....*...
gi 521291413 228 YAGQVVETGEAKDIFRAP 245
Cdd:COG4604 210 KDGRVVAQGTPEEIITPE 227
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-249 |
5.75e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.21 E-value: 5.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 1 MALLNVDKLSVHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSvsslAIMGLIDFPGRVMAEKLEFNGQDlkrISE 80
Cdd:PRK11614 3 KVMLSFDKVSAHYGKI----QALHEVSLHINQGEIVTLIGANGAGKT----TLLGTLCGDPRATSGRIVFDGKD---ITD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 81 KERRSLVGSEVAMIFQdpmtslnpcytvGFQIMEAIKVHQ----GG--NKKTRRQRAIDLLNQVgIPDPASRLDVYPHQL 154
Cdd:PRK11614 72 WQTAKIMREAVAIVPE------------GRRVFSRMTVEEnlamGGffAERDQFQERIKWVYEL-FPRLHERRIQRAGTM 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 155 SGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALILITHDLALVAEAAHKIIVMYAGQVV- 233
Cdd:PRK11614 139 SGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLRE-QGMTIFLVEQNANQALKLADRGYVLENGHVVl 217
|
250
....*....|....*..
gi 521291413 234 -ETGEAKDIFRAPRHPY 249
Cdd:PRK11614 218 eDTGDALLANEAVRSAY 234
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
20-245 |
6.15e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 68.72 E-value: 6.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 20 FRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLidfpGRVMAEKLEFNGQDLKRISEKERrslvgsEVAMIFQDpm 99
Cdd:PRK11650 17 TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGL----ERITSGEIWIGGRVVNELEPADR------DIAMVFQN-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 100 TSLNPCYTVgFQIME-AIKVhQGGNKKTRRQRaidLLNQVGIPDPASRLDVYPHQLSGGMSQRVMIAMAIACQPKLLIAD 178
Cdd:PRK11650 85 YALYPHMSV-RENMAyGLKI-RGMPKAEIEER---VAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521291413 179 EPTTALDVTIQAQI-IElLLELQQKENMALILITHDLalvAEA---AHKIIVMYAGQVVETGEAKDIFRAP 245
Cdd:PRK11650 160 EPLSNLDAKLRVQMrLE-IQRLHRRLKTTSLYVTHDQ---VEAmtlADRVVVMNGGVAEQIGTPVEVYEKP 226
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
23-224 |
6.43e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 69.07 E-value: 6.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 23 VDRVSYSVSQGEVVGIVGESGSGKSvsSL--AIMGL-------IDFPGrvmaeklefngqdlkrisekerrslvGSEVAM 93
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKS--TLlrAIAGLwpygsgrIARPA--------------------------GARVLF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 94 IFQDP---MTSLnpcytvgfqiMEAIkVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDV---YPHQLSGGMSQRVMIAMA 167
Cdd:COG4178 431 LPQRPylpLGTL----------REAL-LYPATAEAFSDAELREALEAVGLGHLAERLDEeadWDQVLSLGEQQRLAFARL 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 521291413 168 IACQPKLLIADEPTTALDVTIQAQIIELLLElqQKENMALILITHDLALVAEAAHKI 224
Cdd:COG4178 500 LLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGHRSTLAAFHDRVL 554
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
24-241 |
7.57e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 67.48 E-value: 7.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 24 DRVSYSVSQGEVVGIVGESGSGKSvSSLAIMGlidfpGRVMAEKLE--FNGQDLKRISeKERRSLVGSEVAMIFQDP--M 99
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKT-TLLRLIG-----GQIAPDHGEilFDGENIPAMS-RSRLYTVRKRMSMLFQSGalF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 100 TSLNPCYTVGFQIMEaikvHQGGNKKTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQRVMIAMAIACQPKLLIADE 179
Cdd:PRK11831 97 TDMNVFDNVAYPLRE----HTQLPAPLLHSTVMMKLEAVGLRGAA---KLMPSELSGGMARRAALARAIALEPDLIMFDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521291413 180 PTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDI 241
Cdd:PRK11831 170 PFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
3-246 |
7.94e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 67.32 E-value: 7.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKLSVHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIdfpgRVMAEKLEFNGQDLKRISEKE 82
Cdd:PRK11300 5 LLSVSGLMMRFGGL----LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFY----KPTGGTILLRGQHIEGLPGHQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 83 --RRSLVGSevamiFQD-----PMTslnpcytvgfqIMEAIKVHQ---------GGNKKT---RR------QRAIDLLNQ 137
Cdd:PRK11300 77 iaRMGVVRT-----FQHvrlfrEMT-----------VIENLLVAQhqqlktglfSGLLKTpafRRaesealDRAATWLER 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 138 VGIPDPASRldvYPHQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALV 217
Cdd:PRK11300 141 VGLLEHANR---QAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLV 217
|
250 260
....*....|....*....|....*....
gi 521291413 218 AEAAHKIIVMYAGQVVETGEAKDIFRAPR 246
Cdd:PRK11300 218 MGISDRIYVVNQGTPLANGTPEEIRNNPD 246
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
31-236 |
8.79e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 67.98 E-value: 8.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 31 SQGeVVGIVGESGSGKSvsSL--AIMGLIDfP--GRVMaekleFNGQDL----KRIS---EKERrslvgseVAMIFQDpm 99
Cdd:PRK11144 23 AQG-ITAIFGRSGAGKT--SLinAISGLTR-PqkGRIV-----LNGRVLfdaeKGIClppEKRR-------IGYVFQD-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 100 TSLNPCYTVgfqimeaikvhQG----GNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACQPKLL 175
Cdd:PRK11144 85 ARLFPHYKV-----------RGnlryGMAKSMVAQFDKIVALLGI---EPLLDRYPGSLSGGEKQRVAIGRALLTAPELL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521291413 176 IADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:PRK11144 151 LMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFG 211
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
9-233 |
1.27e-12 |
|
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: 65.65 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 9 LSVHFGDVGSEFRAVDRVSYSVSQGEVVGIVGESGSGKSvsSL--AIMGLIDFPGrvMAEKLEFNGQDLKRISEKERrsl 86
Cdd:cd03213 11 VTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKS--TLlnALAGRRTGLG--VSGEVLINGRPLDKRSFRKI--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 87 vgseVAMIFQDPMtsLNPCYTVgfqiMEAIKVhqggnkktrrqraidllnqvgipdpASRLdvypHQLSGGMSQRVMIAM 166
Cdd:cd03213 84 ----IGYVPQDDI--LHPTLTV----RETLMF-------------------------AAKL----RGLSGGERKRVSIAL 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521291413 167 AIACQPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALILITHDL-ALVAEAAHKIIVMYAGQVV 233
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAD-TGRTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
23-213 |
1.65e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.89 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 23 VDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDfPGRvmaEKLEFNGQDLKRISEKERRSlvgsEVAMIFQDPMTSL 102
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLIS-PTS---GTLLFEGEDISTLKPEIYRQ----QVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 103 NPCYTvgfqimEAIKVHQGGNKKTRRQRAIDLLNQVGIPDpaSRLDVYPHQLSGGMSQRVMIAMAIACQPKLLIADEPTT 182
Cdd:PRK10247 95 DTVYD------NLIFPWQIRNQQPDPAIFLDDLERFALPD--TILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
170 180 190
....*....|....*....|....*....|.
gi 521291413 183 ALDVTIQAQIIELLLELQQKENMALILITHD 213
Cdd:PRK10247 167 ALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-232 |
1.84e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.78 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 6 VDKLSVHFGDvgsefRAV-DRVSYSVSQGEVVGIVGESGSGKSvsSL--AIMGLIDfP--GRVMAEK------------- 67
Cdd:COG0488 1 LENLSKSFGG-----RPLlDDVSLSINPGDRIGLVGRNGAGKS--TLlkILAGELE-PdsGEVSIPKglrigylpqeppl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 68 ------LEFNGQDLKRISEKERR-SLVGSEVAMIFQDPMTslnpcYTVGFQIMEAIKVHqggnkkTRRQRAIDLLNQVGI 140
Cdd:COG0488 73 dddltvLDTVLDGDAELRALEAElEELEAKLAEPDEDLER-----LAELQEEFEALGGW------EAEARAEEILSGLGF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 141 PDPASRLDVypHQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDvtIQAqiIELLLELQQKENMALILITHDLALVAEA 220
Cdd:COG0488 142 PEEDLDRPV--SELSGGWRRRVALARALLSEPDLLLLDEPTNHLD--LES--IEWLEEFLKNYPGTVLVVSHDRYFLDRV 215
|
250
....*....|..
gi 521291413 221 AHKIIVMYAGQV 232
Cdd:COG0488 216 ATRILELDRGKL 227
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
11-241 |
2.06e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 67.74 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 11 VHFGDV-----GSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVsslaIMGLIDFPGRVMAEKLEFNGQDLKRI---SEKE 82
Cdd:PRK11176 342 IEFRNVtftypGKEVPALRNINFKIPAGKTVALVGRSGSGKST----IANLLTRFYDIDEGEILLDGHDLRDYtlaSLRN 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 83 RRSLVGSEVAMiFQDpmtslnpcyTVGFQIMEAIKvhqggNKKTRRQ--------RAIDLLNQVgipdpASRLDVYPHQ- 153
Cdd:PRK11176 418 QVALVSQNVHL-FND---------TIANNIAYART-----EQYSREQieeaarmaYAMDFINKM-----DNGLDTVIGEn 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 154 ---LSGGMSQRVMIAMAIACQPKLLIADEPTTALDV----TIQAQIIELllelqQKENMALIlITHDLALVaEAAHKIIV 226
Cdd:PRK11176 478 gvlLSGGQRQRIAIARALLRDSPILILDEATSALDTeserAIQAALDEL-----QKNRTSLV-IAHRLSTI-EKADEILV 550
|
250
....*....|....*
gi 521291413 227 MYAGQVVETGEAKDI 241
Cdd:PRK11176 551 VEDGEIVERGTHAEL 565
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-232 |
2.79e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.26 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 21 RAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLidFPGRVMAEKLeFNGqdlKRISEKERRSLVGSEVAMIFQD-PM 99
Cdd:PRK13549 276 KRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGA--YPGRWEGEIF-IDG---KPVKIRNPQQAIAQGIAMVPEDrKR 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 100 TSLNPCYTVGFQIMEAIKvhqggNKKTRRQRAIDLLNQVGIPDPASRLDV---YPHQ----LSGGMSQRVMIAMAIACQP 172
Cdd:PRK13549 350 DGIVPVMGVGKNITLAAL-----DRFTGGSRIDDAAELKTILESIQRLKVktaSPELaiarLSGGNQQKAVLAKCLLLNP 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 173 KLLIADEPTTALDVTIQAQIIELLLELQQkENMALILITHDLALVAEAAHKIIVMYAGQV 232
Cdd:PRK13549 425 KILILDEPTRGIDVGAKYEIYKLINQLVQ-QGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
9-247 |
7.43e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.85 E-value: 7.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 9 LSVHFGDVGSEFRAV-DRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGliDFPGRVMAE------KLEFNGQDLKRISEK 81
Cdd:PRK13547 2 LTADHLHVARRHRAIlRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTGGGAPRgarvtgDVTLNGEPLAAIDAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 82 E---RRSLV--GSEVAMIFQDPMTSLNPCYTvgfqimeaiKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYphQLSG 156
Cdd:PRK13547 80 RlarLRAVLpqAAQPAFAFSAREIVLLGRYP---------HARRAGALTHRDGEIAWQALALAGATALVGRDVT--TLSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 157 GMSQRVMIAMAIA---------CQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVM 227
Cdd:PRK13547 149 GELARVQFARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAML 228
|
250 260
....*....|....*....|
gi 521291413 228 YAGQVVETGEAKDIFRaPRH 247
Cdd:PRK13547 229 ADGAIVAHGAPADVLT-PAH 247
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-241 |
1.03e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.42 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 27 SYSVSQGEVVGIVGESGSGKSVSSLAIMG-LIDFPGRvmaekLEFNGQDLKRISEKERRSLVGSEvamiFQD---PMTSL 102
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGeLPLLSGE-----RQSQFSHITRLSFEQLQKLVSDE----WQRnntDMLSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 103 NPCYTvGFQIMEAIkvhQGGNKKTrrQRAIDLLNQVGIPDPASRLDVYphqLSGGMSQRVMIAMAIACQPKLLIADEPTT 182
Cdd:PRK10938 94 GEDDT-GRTTAEII---QDEVKDP--ARCEQLAQQFGITALLDRRFKY---LSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 521291413 183 ALDVTIQAQIIELLLELQQKeNMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDI 241
Cdd:PRK10938 165 GLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-241 |
1.08e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.58 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKLSVHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSvSSLAIMGLIDFP--GRVMAEKLEFNGQDLKrISE 80
Cdd:PRK09700 5 YISMAGIGKSFGPV----HALKSVNLTVYPGEIHALLGENGAGKS-TLMKVLSGIHEPtkGTITINNINYNKLDHK-LAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 81 KERRSLVGSEVAMIfqDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTrRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQ 160
Cdd:PRK09700 79 QLGIGIIYQELSVI--DELTVLENLYIGRHLTKKVCGVNIIDWREM-RVRAAMMLLRVGL---KVDLDEKVANLSISHKQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 161 RVMIAMAIACQPKLLIADEPTTALdvtIQAQIIELLLELQQ--KENMALILITHDLALVAEAAHKIIVMYAGQVVETGEA 238
Cdd:PRK09700 153 MLEIAKTLMLDAKVIIMDEPTSSL---TNKEVDYLFLIMNQlrKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMV 229
|
...
gi 521291413 239 KDI 241
Cdd:PRK09700 230 SDV 232
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
24-224 |
1.34e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.90 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 24 DRVSYSVSQGEVVGIVGESGSGKSvSSLAIM-GLidfpGRVMAEKLEFNGQDLKRISEKERRSLvgsevamifqdpmtsl 102
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKT-SLLRILaGL----ARPDAGEVLWQGEPIRRQRDEYHQDL---------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 103 npCYtVGfqimeaikvHQGGNK-----------------KTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIA 165
Cdd:PRK13538 77 --LY-LG---------HQPGIKteltalenlrfyqrlhgPGDDEALWEALAQVGL---AGFEDVPVRQLSAGQQRRVALA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 166 MAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMAlILITH-DLALVAEAAHKI 224
Cdd:PRK13538 142 RLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMV-ILTTHqDLPVASDKVRKL 200
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-235 |
1.44e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.93 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 1 MALLNVDKLSVHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSvSSLAIMGLIDFPGrvmAEKLEFNGQDLKRISE 80
Cdd:PRK11288 2 SPYLSFDGIGKTFPGV----KALDDISFDCRAGQVHALMGENGAGKS-TLLKILSGNYQPD---AGSILIDGQEMRFAST 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 81 KERrslVGSEVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGG--NKKTRRQRAIDLLNQVGIP-DPASRLdvypHQLSGG 157
Cdd:PRK11288 74 TAA---LAAGVAIIYQE--LHLVPEMTVAENLYLGQLPHKGGivNRRLLNYEAREQLEHLGVDiDPDTPL----KYLSIG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521291413 158 MSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALILITHDLALVAEAAHKIIVMYAGQVVET 235
Cdd:PRK11288 145 QRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDGRYVAT 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
17-240 |
1.84e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.81 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 17 GSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGlIDfpgRVMAEKLEFNGQDLKRISEKERrslVGSEVAMIFQ 96
Cdd:PRK09700 273 SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFG-VD---KRAGGEIRLNGKDISPRSPLDA---VKKGMAYITE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 97 DPM-TSLNPCYTVGFQIMEAIKVHQGG--------NKKTRRQRAIDLLNQVGIPdpASRLDVYPHQLSGGMSQRVMIAMA 167
Cdd:PRK09700 346 SRRdNGFFPNFSIAQNMAISRSLKDGGykgamglfHEVDEQRTAENQRELLALK--CHSVNQNITELSGGNQQKVLISKW 423
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521291413 168 IACQPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKD 240
Cdd:PRK09700 424 LCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-237 |
4.13e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.48 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 23 VDRVSYSVSQGEVVGIVGESGSGKSvsslAIMGLIDFPGRVMAEKLEFNGQDLKR-------------ISEKERRSlvGS 89
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRT----ELMKVLYGALPRTSGYVTLDGHEVVTrspqdglangivyISEDRKRD--GL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 90 EVAMIFQDPM--TSLNPCYTVGFQImeaikvhqggNKKTRRQRAIDLLNQVGIPDPAsrLDVYPHQLSGGMSQRVMIAMA 167
Cdd:PRK10762 342 VLGMSVKENMslTALRYFSRAGGSL----------KHADEQQAVSDFIRLFNIKTPS--MEQAIGLLSGGNQQKVAIARG 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 168 IACQPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALILITHDLALVAEAAHKIIVMYAGQVveTGE 237
Cdd:PRK10762 410 LMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKA-EGLSIILVSSEMPEVLGMSDRILVMHEGRI--SGE 476
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-234 |
7.74e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 62.77 E-value: 7.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 3 LLNVDKLSVHFGDvgsefRAV-DRVSYSVSQGEVVGIVGESGSGKSVsslaimgLIdfpgRVMAEKLEFNGQDLKRisek 81
Cdd:COG0488 315 VLELEGLSKSYGD-----KTLlDDLSLRIDRGDRIGLIGPNGAGKST-------LL----KLLAGELEPDSGTVKL---- 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 82 errslvGSEVAMIF--QDpMTSLNPCYTVgfqiMEAIkvhQGGNKKTRRQRAIDLLNQVGIPdpASRLDVYPHQLSGGMS 159
Cdd:COG0488 375 ------GETVKIGYfdQH-QEELDPDKTV----LDEL---RDGAPGGTEQEVRGYLGRFLFS--GDDAFKPVGVLSGGEK 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521291413 160 QRVMIAMAIACQPKLLIADEPTTALDV-TIQAqIIELLLELQQkenmALILITHDLALVAEAAHKIIVMYAGQVVE 234
Cdd:COG0488 439 ARLALAKLLLSPPNVLLLDEPTNHLDIeTLEA-LEEALDDFPG----TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
23-224 |
1.04e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 61.77 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 23 VDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDfPGrvmAEKLEFNGqdlkrISEKERRSLVGSEVAMIFQdpMTSL 102
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTS-PD---AGKITVLG-----VPVPARARLARARIGVVPQ--FDNL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 103 NPCYTVgfqiMEAIKVH-QGGNKKTRRQRAI--DLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACQPKLLIADE 179
Cdd:PRK13536 126 DLEFTV----RENLLVFgRYFGMSTREIEAVipSLLEFARL---ESKADARVSDLSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 521291413 180 PTTALDVTIQAQIIELLLELQQKeNMALILITH---------DLALVAEAAHKI 224
Cdd:PRK13536 199 PTTGLDPHARHLIWERLRSLLAR-GKTILLTTHfmeeaerlcDRLCVLEAGRKI 251
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-230 |
3.84e-10 |
|
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: 58.88 E-value: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 17 GSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIdfpgRVMAEKLEFNGQDLKRISEKERRSLVGSEVAMIFQ 96
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEM----QTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 97 DPmtslnpcYTVGFQIMEAIKVHQGGNKKtRRQRAIDLLNQVgiPDpasrLDVYPH-----------QLSGGMSQRVMIA 165
Cdd:cd03290 87 KP-------WLLNATVEENITFGSPFNKQ-RYKAVTDACSLQ--PD----IDLLPFgdqteigergiNLSGGQRQRICVA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521291413 166 MAIACQPKLLIADEPTTALDVTIQAQII-ELLLELQQKENMALILITHDLALVAEaAHKIIVMYAG 230
Cdd:cd03290 153 RALYQNTNIVFLDDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
112-226 |
7.95e-10 |
|
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: 56.98 E-value: 7.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 112 IMEAIKVHQGGNKKTRRQRaidLLNQVGIPDPASRLDVYP--HQLSGGMSQRVMIAMAIA---CQPK-LLIADEPTTALD 185
Cdd:cd03227 37 ILDAIGLALGGAQSATRRR---SGVKAGCIVAAVSAELIFtrLQLSGGEKELSALALILAlasLKPRpLYILDEIDRGLD 113
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 521291413 186 VTIQAQIIELLLELQQKENMaLILITHDLALVAEAAHKIIV 226
Cdd:cd03227 114 PRDGQALAEAILEHLVKGAQ-VIVITHLPELAELADKLIHI 153
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
26-237 |
9.09e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.36 E-value: 9.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 26 VSYSVSQGEVVGIVGESGSGKSVSSLAIMGL-------IDFPGRVMAEKLEF----NGQDLkrISEKERRSLVGSEVAMI 94
Cdd:PRK10982 267 VSFDLHKGEILGIAGLVGAKRTDIVETLFGIreksagtITLHGKKINNHNANeainHGFAL--VTEERRSTGIYAYLDIG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 95 FQDPMTSLNPcYTVGFQIMEAIKVhqggnkKTRRQRAIDLLNqvgIPDPASRLDVypHQLSGGMSQRVMIAMAIACQPKL 174
Cdd:PRK10982 345 FNSLISNIRN-YKNKVGLLDNSRM------KSDTQWVIDSMR---VKTPGHRTQI--GSLSGGNQQKVIIGRWLLTQPEI 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521291413 175 LIADEPTTALDVTIQAQIIELLLELQQKENmALILITHDLALVAEAAHKIIVMYAGQV---VETGE 237
Cdd:PRK10982 413 LMLDEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEMPELLGITDRILVMSNGLVagiVDTKT 477
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-241 |
1.26e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 58.59 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 4 LNVDKLSVHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDFPGRVMAEKLEF--NGQDLKRISEK 81
Cdd:NF000106 14 VEVRGLVKHFGEV----KAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*TWcaNRRALRRTIG* 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 82 ERRSLVGSevamifQDPMTSLNPCYTVGFQImeaikvhqGGNKKTRRQRAIDLLNQVGIPDPASRLDVyphQLSGGMSQR 161
Cdd:NF000106 90 HRPVR*GR------RESFSGRENLYMIGR*L--------DLSRKDARARADELLERFSLTEAAGRAAA---KYSGGMRRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 162 VMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDI 241
Cdd:NF000106 153 LDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSM-VRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
30-240 |
1.79e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 58.74 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 30 VSQGEVVGIVGESGSGKSVSSLAIMGLI---DFPGRVMAEKLEFNGQDLKRIsekerrslvgsevAMIFQDPMtsLNPCY 106
Cdd:PLN03211 91 ASPGEILAVLGPSGSGKSTLLNALAGRIqgnNFTGTILANNRKPTKQILKRT-------------GFVTQDDI--LYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 107 TVGFQIM--EAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRL--DVYPHQLSGGMSQRVMIAMAIACQPKLLIADEPTT 182
Cdd:PLN03211 156 TVRETLVfcSLLRLPKSLTKQEKILVAESVISELGLTKCENTIigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 521291413 183 ALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKD 240
Cdd:PLN03211 236 GLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-241 |
1.84e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 57.89 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 2 ALLNVDKLSVHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIdFPgrvMAEKLEFNGQDLKRISEK 81
Cdd:PRK13537 6 APIDFRNVEKRYGDK----LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLT-HP---DAGSISLCGEPVPSRARH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 82 ERRslvgsEVAMIFQdpMTSLNPCYTVgfqiMEAIKV---HQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGM 158
Cdd:PRK13537 78 ARQ-----RVGVVPQ--FDNLDPDFTV----RENLLVfgrYFGLSAAAARALVPPLLEFAKL---ENKADAKVGELSGGM 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 159 SQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALILITHDLALVAEAAHKIIVMYAGQVVETGEA 238
Cdd:PRK13537 144 KRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAP 222
|
...
gi 521291413 239 KDI 241
Cdd:PRK13537 223 HAL 225
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-233 |
2.50e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.42 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 1 MALLNVDKLSVHFGDVGsefrAVDRVSYSVSQGEVVGIVGESGSGKSvSSLAIMG---LIDfPGRVMAEklefngQDLK- 76
Cdd:PRK11147 1 MSLISIHGAWLSFSDAP----LLDNAELHIEDNERVCLVGRNGAGKS-TLMKILNgevLLD-DGRIIYE------QDLIv 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 77 -RISEKERRSLVGS----------EVA-----------MIFQDPMTS-LNPCYtvgfQIMEAIKVHQGGNKKTRRQraiD 133
Cdd:PRK11147 69 aRLQQDPPRNVEGTvydfvaegieEQAeylkryhdishLVETDPSEKnLNELA----KLQEQLDHHNLWQLENRIN---E 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 134 LLNQVGIpDPASRLDvyphQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTiqaqIIELLLELQQKENMALILITHD 213
Cdd:PRK11147 142 VLAQLGL-DPDAALS----SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIE----TIEWLEGFLKTFQGSIIFISHD 212
|
250 260
....*....|....*....|
gi 521291413 214 LALVAEAAHKIIVMYAGQVV 233
Cdd:PRK11147 213 RSFIRNMATRIVDLDRGKLV 232
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
26-236 |
2.96e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 58.19 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 26 VSYSVSQGEVVGIVGESGSGKSVSSLAIMGLidFPgrVMAEKLEFNGQDLKRISEKERRslvgSEVAMIFQDPMT---SL 102
Cdd:PRK10790 360 INLSVPSRGFVALVGHTGSGKSTLASLLMGY--YP--LTEGEIRLDGRPLSSLSHSVLR----QGVAMVQQDPVVladTF 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 103 NPCYTVGFQIMEAiKVHQGgnkktrrQRAIDLLNQV-GIPDPA-SRLDVYPHQLSGGMSQRVMIAMAIACQPKLLIADEP 180
Cdd:PRK10790 432 LANVTLGRDISEE-QVWQA-------LETVQLAELArSLPDGLyTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEA 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 521291413 181 TTALDVTIQAQIIELLLELqqKENMALILITHDLALVAEAAHkIIVMYAGQVVETG 236
Cdd:PRK10790 504 TANIDSGTEQAIQQALAAV--REHTTLVVIAHRLSTIVEADT-ILVLHRGQAVEQG 556
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-241 |
3.95e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.83 E-value: 3.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 6 VDKLSVHFGDVgsefRAVDRVSYSVSQGEVVGIVGESGSGKSvsSLaiMGLIDFPGRVMAEKLEFNGQDlkrISEKERRS 85
Cdd:NF033858 4 LEGVSHRYGKT----VALDDVSLDIPAGCMVGLIGPDGVGKS--SL--LSLIAGARKIQQGRVEVLGGD---MADARHRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 86 LVGSEVAMIFQDPMTSLNPCYTVgfqiMEAIKVHQ---GGNKKTRRQRAIDLLNQVGI---PD-PASrldvyphQLSGGM 158
Cdd:NF033858 73 AVCPRIAYMPQGLGKNLYPTLSV----FENLDFFGrlfGQDAAERRRRIDELLRATGLapfADrPAG-------KLSGGM 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 159 SQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLEL-QQKENMALILIThdlALVAEAAH--KIIVMYAGQVVET 235
Cdd:NF033858 142 KQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIrAERPGMSVLVAT---AYMEEAERfdWLVAMDAGRVLAT 218
|
....*.
gi 521291413 236 GEAKDI 241
Cdd:NF033858 219 GTPAEL 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-265 |
8.70e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.46 E-value: 8.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 26 VSYSVSQGEVVGIVGESGSGKSvsslAIMGLIDFPGRVMAEKLEFNGqdlKRISEKERRSLVGSEVAMIFQD-PMTSLNP 104
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRS----ELMKLLYGATRRTAGQVYLDG---KPIDIRSPRDAIRAGIMLCPEDrKAEGIIP 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 105 CYTVGFQIMEAIKVHQ--GG---NKKTRRQRA---IDLLNqvgIPDPASRLDVypHQLSGGMSQRVMIAMAIACQPKLLI 176
Cdd:PRK11288 345 VHSVADNINISARRHHlrAGcliNNRWEAENAdrfIRSLN---IKTPSREQLI--MNLSGGNQQKAILGRWLSEDMKVIL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 177 ADEPTTALDVTIQAQIIELLLELQQKeNMALILITHDLALVAEAAHKIIVMYAGQVveTGEakdifrAPRHPYT--QALL 254
Cdd:PRK11288 420 LDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI--AGE------LAREQATerQALS 490
|
250
....*....|.
gi 521291413 255 RALPEFAQDKA 265
Cdd:PRK11288 491 LALPRTSAAVA 501
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
21-224 |
1.00e-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: 54.42 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 21 RAV-DRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIdfpgRVMAEKLEFNGQDLKRISEKERRSL--VGSEVAMifqd 97
Cdd:cd03231 13 RALfSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLS----PPLAGRVLLNGGPLDFQRDSIARGLlyLGHAPGI---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 98 pMTSLNPCYTVGF--------QIMEAikvhqggnkktrrqraidlLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIA 169
Cdd:cd03231 85 -KTTLSVLENLRFwhadhsdeQVEEA-------------------LARVGL---NGFEDRPVAQLSAGQQRRVALARLLL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 521291413 170 CQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKI 224
Cdd:cd03231 142 SGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
30-237 |
1.07e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.18 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 30 VSQGEVVGIVGESGSGKSVSSLAIMGLIDFpgRVMAEKLEFNGQDLKRISEKERrslVGSEVAMIFQDPMTSlnPCYTVG 109
Cdd:PRK09580 24 VRPGEVHAIMGPNGSGKSTLSATLAGREDY--EVTGGTVEFKGKDLLELSPEDR---AGEGIFMAFQYPVEI--PGVSNQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 110 FQIMEAIKvhqgGNKKTRRQRAIDLLN-QVGIPDPASRLDVYPHQL--------SGGMSQRVMIAMAIACQPKLLIADEP 180
Cdd:PRK09580 97 FFLQTALN----AVRSYRGQEPLDRFDfQDLMEEKIALLKMPEDLLtrsvnvgfSGGEKKRNDILQMAVLEPELCILDES 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521291413 181 TTALDV---TIQAQIIELLlelqQKENMALILITHDLALVAEAAHKII-VMYAGQVVETGE 237
Cdd:PRK09580 173 DSGLDIdalKIVADGVNSL----RDGKRSFIIVTHYQRILDYIKPDYVhVLYQGRIVKSGD 229
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
26-227 |
1.34e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.19 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 26 VSYSVSQGEVVGIVGESGSGKSVSSLAIMGLID-FPGRVMAEklefNGQDLKRISEKERRSLVGsevaMIFQDPMT---- 100
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDpTEGDIIIN----DSHNLKDINLKWWRSKIG----VVSQDPLLfsns 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 101 ----------SLNPCYTVGFQIMEAIKVHQGGNKKTRRQRA---------------------------------IDLLNQ 137
Cdd:PTZ00265 476 iknnikyslySLKDLEALSNYYNEDGNDSQENKNKRNSCRAkcagdlndmsnttdsneliemrknyqtikdsevVDVSKK 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 138 VGIPDPASRL-DVY-------PHQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALIL 209
Cdd:PTZ00265 556 VLIHDFVSALpDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITII 635
|
250
....*....|....*...
gi 521291413 210 ITHDLALVaEAAHKIIVM 227
Cdd:PTZ00265 636 IAHRLSTI-RYANTIFVL 652
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
38-226 |
3.12e-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: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 38 IVGESGSGKSVSSLAI-MGLidFPgrVMAEKLEFNGQDLKRISEKERRSlvgsEVAMIFQDPMTSLnpcYTV--GFQIME 114
Cdd:cd03240 27 IVGQNGAGKTTIIEALkYAL--TG--ELPPNSKGGAHDPKLIREGEVRA----QVKLAFENANGKK---YTItrSLAILE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 115 -AIKVHQGGNKKTrrqraidllnqvgIPDPASRLdvyphqlSGGmsQRVMIAMAIAC--------QPKLLIADEPTTALD 185
Cdd:cd03240 96 nVIFCHQGESNWP-------------LLDMRGRC-------SGG--EKVLASLIIRLalaetfgsNCGILALDEPTTNLD 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 521291413 186 V-TIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIV 226
Cdd:cd03240 154 EeNIEESLAEIIEERKSQKNFQLIVITHDEELVDAADHIYRV 195
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
149-212 |
3.38e-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: 52.16 E-value: 3.38e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521291413 149 VYP--HQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLlelqQKENMALILITH 212
Cdd:cd03223 85 IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL----KELGITVISVGH 146
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
150-226 |
3.42e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.04 E-value: 3.42e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521291413 150 YPHQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVaEAAHKIIV 226
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI-KRSDKIVV 1430
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
5-241 |
4.73e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.78 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 5 NVDKLSVHFGDVGSEFR-----AVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDfpgrVMAEKLEFNGQDLKRIS 79
Cdd:PTZ00243 1303 PVQAGSLVFEGVQMRYReglplVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVE----VCGGEIRVNGREIGAYG 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 80 EKERRslvgSEVAMIFQDPM-------TSLNPcytvgfqIMEAikvhqggnKKTRRQRAIDLlnqVGIPDPA-------- 144
Cdd:PTZ00243 1379 LRELR----RQFSMIPQDPVlfdgtvrQNVDP-------FLEA--------SSAEVWAALEL---VGLRERVasesegid 1436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 145 SRLdvyphqLSGG----MSQRVMIAMAIACQPK---LLIADEPTT----ALDVTIQAQIIELLlelqqkENMALILITHD 213
Cdd:PTZ00243 1437 SRV------LEGGsnysVGQRQLMCMARALLKKgsgFILMDEATAnidpALDRQIQATVMSAF------SAYTVITIAHR 1504
|
250 260
....*....|....*....|....*...
gi 521291413 214 LALVAEaAHKIIVMYAGQVVETGEAKDI 241
Cdd:PTZ00243 1505 LHTVAQ-YDKIIVMDHGAVAEMGSPREL 1531
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
19-217 |
4.95e-08 |
|
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: 52.36 E-value: 4.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 19 EFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIdfpgRVMAEKLEFNGQDLKrisekERRSLVGSEVAMIFQDP 98
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLL----RPDSGEVRWNGTPLA-----EQRDEPHENILYLGHLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 99 mtSLNPCYTV--GFQIMEAIkvHQGgnkktrRQRAI-DLLNQVGIPDPAsrlDVYPHQLSGGMSQRVMIAMAIACQPKLL 175
Cdd:TIGR01189 83 --GLKPELSAleNLHFWAAI--HGG------AQRTIeDALAAVGLTGFE---DLPAAQLSAGQQRRLALARLWLSRRPLW 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 521291413 176 IADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALV 217
Cdd:TIGR01189 150 ILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
10-262 |
5.21e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.60 E-value: 5.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 10 SVHFGDVGSEFR-----AVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDFP-GRVMAEKLE---FNGQDLKRIse 80
Cdd:PLN03232 1234 SIKFEDVHLRYRpglppVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEkGRIMIDDCDvakFGLTDLRRV-- 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 81 kerrslvgseVAMIFQDPMTSLNpcyTVGFQImEAIKVHQGGNKKTRRQRAidllnqvGIPDPASR----LDVYPHQ--- 153
Cdd:PLN03232 1312 ----------LSIIPQSPVLFSG---TVRFNI-DPFSEHNDADLWEALERA-------HIKDVIDRnpfgLDAEVSEgge 1370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 154 -LSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLElqQKENMALILITHDLALVAEaAHKIIVMYAGQV 232
Cdd:PLN03232 1371 nFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIRE--EFKSCTMLVIAHRLNTIID-CDKILVLSSGQV 1447
|
250 260 270
....*....|....*....|....*....|
gi 521291413 233 VETGEAKDIFRAPRHPYTQALLRALPEFAQ 262
Cdd:PLN03232 1448 LEYDSPQELLSRDTSAFFRMVHSTGPANAQ 1477
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-221 |
6.40e-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: 51.22 E-value: 6.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 32 QGEVVGIVGESGSGKSVSSLAIMGLIDFPGRVMaekLEFNGQDLkrisekerrslvgsevamifqdpmtslnpcytvgfq 111
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV---IYIDGEDI------------------------------------ 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 112 imeaikvhqggnkktrRQRAIDLLNQVGIpdpasrlDVYPHQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQ 191
Cdd:smart00382 42 ----------------LEEVLDQLLLIIV-------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEAL 98
|
170 180 190
....*....|....*....|....*....|....*
gi 521291413 192 IIEL-----LLELQQKENMALILITHDLALVAEAA 221
Cdd:smart00382 99 LLLLeelrlLLLLKSEKNLTVILTTNDEKDLGPAL 133
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-241 |
6.43e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 53.74 E-value: 6.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 22 AVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGL-------IDFPGR--VMAEKLEFNGQdLKRISEKERRSLVGSeva 92
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVtmpnkgtVDIKGSaaLIAISSGLNGQ-LTGIENIELKGLMMG--- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 93 mIFQDPMTSLNPcytvgfQIMEAIKVHQggnkktrrqraidLLNQvgipdPASrldvyphQLSGGMSQRVMIAMAIACQP 172
Cdd:PRK13545 115 -LTKEKIKEIIP------EIIEFADIGK-------------FIYQ-----PVK-------TYSSGMKSRLGFAISVHINP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521291413 173 KLLIADEPTTALDVTIQAQIIELLLELQQKeNMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDI 241
Cdd:PRK13545 163 DILVIDEALSVGDQTFTKKCLDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-228 |
8.62e-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: 52.37 E-value: 8.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 33 GEVVGIVGESGSGKSvSSLAIM--------GLIDFPGRVMAEKLEFNGQDLKRISEKerrsLVGSEVAMIFQDPMTSLNP 104
Cdd:cd03236 26 GQVLGLVGPNGIGKS-TALKILagklkpnlGKFDDPPDWDEILDEFRGSELQNYFTK----LLEGDVKVIVKPQYVDLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 105 CYTVGfqimeaiKVHQGGNKKTRRQRAIDLLNQVGIpDPAsrLDVYPHQLSGGMSQRVMIAMAIACQPKLLIADEPTTAL 184
Cdd:cd03236 101 KAVKG-------KVGELLKKKDERGKLDELVDQLEL-RHV--LDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 521291413 185 DVTIQAQIIELLLELQQKENmALILITHDLALVAEAAHKIIVMY 228
Cdd:cd03236 171 DIKQRLNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
9-236 |
1.07e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.20 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 9 LSVHFGDvgseFRAVDRVSYSVSQGEVVGIVGESGSGKSVSslaiM----GLIDfpgrvmaeklefngqdlkrISEKERR 84
Cdd:NF033858 272 LTMRFGD----FTAVDHVSFRIRRGEIFGFLGSNGCGKSTT----MkmltGLLP-------------------ASEGEAW 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 85 sLVGSEVamifqDPmTSLNPCYTVG-----FQIMEAIKVHQggN-----------KKTRRQRAIDLLNQVGIpdpASRLD 148
Cdd:NF033858 325 -LFGQPV-----DA-GDIATRRRVGymsqaFSLYGELTVRQ--NlelharlfhlpAAEIAARVAEMLERFDL---ADVAD 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 149 VYPHQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHdlaLVAEAAH--KIIV 226
Cdd:NF033858 393 ALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTH---FMNEAERcdRISL 469
|
250
....*....|
gi 521291413 227 MYAGQVVETG 236
Cdd:NF033858 470 MHAGRVLASD 479
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
26-231 |
2.12e-07 |
|
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: 50.55 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 26 VSYSVSQGEVVGIVGESGSGKSvsSL--AIMGlidfpgrvmaeklefngqDLKRISEKerrSLVGSEVAMIFQDP----M 99
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKS--SLlsALLG------------------ELEKLSGS---VSVPGSIAYVSQEPwiqnG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 100 TslnpcytvgfqIMEAIkvhQGGNK--KTRRQRAIDL--LNqvgiPDpasrLDVYPHQ-----------LSGGMSQRVMI 164
Cdd:cd03250 81 T-----------IRENI---LFGKPfdEERYEKVIKAcaLE----PD----LEILPDGdlteigekginLSGGQKQRISL 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521291413 165 AMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHkIIVMYAGQ 231
Cdd:cd03250 139 ARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPHADQ-IVVLDNGR 204
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
26-238 |
2.23e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.18 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 26 VSYSVSQGEVVGIVGESGSGKSVSSLAIMGlidFPG-RVMAEKLEFNGQDLKRIsEKERRSLVGseVAMIFQDPMTslnp 104
Cdd:CHL00131 26 LNLSINKGEIHAIMGPNGSGKSTLSKVIAG---HPAyKILEGDILFKGESILDL-EPEERAHLG--IFLAFQYPIE---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 105 cyTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRL-DVYPHQL--------SGGMSQRVMIAMAIACQPKLL 175
Cdd:CHL00131 96 --IPGVSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLKLvGMDPSFLsrnvnegfSGGEKKRNEILQMALLDSELA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521291413 176 IADEPTTALDVTIQAQIIELLLELQQKENmALILITHDLAL----VAEAAHkiiVMYAGQVVETGEA 238
Cdd:CHL00131 174 ILDETDSGLDIDALKIIAEGINKLMTSEN-SIILITHYQRLldyiKPDYVH---VMQNGKIIKTGDA 236
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-238 |
7.82e-07 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 49.33 E-value: 7.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 29 SVSQGEVVGIVGESGSGKSVSSlaimglidfpgRVMAEKLEFNGQDlkrisekerrslVGSEVAMIFQDPMTsLNPCY-- 106
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFI-----------KMLAGVLKPDEGD------------IEIELDTVSYKPQY-IKADYeg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 107 TVGFQIMEAIKvhqggNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDV 186
Cdd:cd03237 77 TVRDLLSSITK-----DFYTHPYFKTEIAKPLQI---EQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 521291413 187 ---TIQAQIIELLLELQQKENMaliLITHDLALVAEAAHKIIVmYAGQVVETGEA 238
Cdd:cd03237 149 eqrLMASKVIRRFAENNEKTAF---VVEHDIIMIDYLADRLIV-FEGEPSVNGVA 199
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
15-241 |
8.80e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 50.43 E-value: 8.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 15 DVGSEFRAVD---RVSYSVSQGEVVGIVGESGSGKSvSSLAIMGLIDFPGrvmAEKLEFNGQDLKRISEKERRSLvgsEV 91
Cdd:PRK15439 16 SISKQYSGVEvlkGIDFTLHAGEVHALLGGNGAGKS-TLMKIIAGIVPPD---SGTLEIGGNPCARLTPAKAHQL---GI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 92 AMIFQDPMtsLNPCYTVGFQIMEAIKVHQGGNKKTRrqraiDLLNQVGI---PD-PASRLDVYPHQLsggmsqrVMIAMA 167
Cdd:PRK15439 89 YLVPQEPL--LFPNLSVKENILFGLPKRQASMQKMK-----QLLAALGCqldLDsSAGSLEVADRQI-------VEILRG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521291413 168 IACQPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDI 241
Cdd:PRK15439 155 LMRDSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
26-256 |
9.20e-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: 49.52 E-value: 9.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 26 VSYSVSQGEVVGIVGESGSGKSVSSLAIMGLID-FPGRVMaekleFNGQDLKRISEKERRslvgSEVAMIFQDPMT---- 100
Cdd:cd03288 40 VKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDiFDGKIV-----IDGIDISKLPLHTLR----SRLSIILQDPILfsgs 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 101 ---SLNP-CYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGipdpasrldvyPHQLSGGMSQRVMIAMAIACQPKLLI 176
Cdd:cd03288 111 irfNLDPeCKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEG-----------GENFSVGQRQLFCLARAFVRKSSILI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 177 ADEPTTALDVTIQaQIIELLLeLQQKENMALILITHDLALVAEaAHKIIVMYAGQVVETGEAKDIFRAPRHPYTqALLRA 256
Cdd:cd03288 180 MDEATASIDMATE-NILQKVV-MTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVFA-SLVRT 255
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
154-236 |
1.12e-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: 48.09 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 154 LSGGMSQRVMIA--MAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENmALILITHDLAlVAEAAHKIIVM---- 227
Cdd:cd03238 88 LSGGELQRVKLAseLFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGN-TVILIEHNLD-VLSSADWIIDFgpgs 165
|
90
....*....|.
gi 521291413 228 --YAGQVVETG 236
Cdd:cd03238 166 gkSGGKVVFSG 176
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-237 |
1.51e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 49.71 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 17 GSEFRAVDRVSYSVSQGEVVGIVGESGSGKSvsslAIMGLIDFPGRVMAEKLEFNGQDLKRISEKERRS--LVGSEVAMI 94
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKS----TLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSrlAVVSQTPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 95 FQDPMTS---LNPCYTVGFQIMEAIK---VHQggnkktrrqraiDLLN-------QVGipdpasRLDVyphQLSGGMSQR 161
Cdd:PRK10789 401 FSDTVANniaLGRPDATQQEIEHVARlasVHD------------DILRlpqgydtEVG------ERGV---MLSGGQKQR 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521291413 162 VMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLleLQQKENMALILITHDLALVAEAAhKIIVMYAGQVVETGE 237
Cdd:PRK10789 460 ISIARALLLNAEILILDDALSAVDGRTEHQILHNL--RQWGEGRTVIISAHRLSALTEAS-EILVMQHGHIAQRGN 532
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-231 |
2.72e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.85 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 21 RAVDRVSYSVSQGEVVGIVGESGSGKSVsslaIM-----------GLIDFPGrvmaEKLEFNGqdlKRISEKERRSLVGS 89
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKST----MMkvltgiytrdaGSILYLG----KEVTFNG---PKSSQEAGIGIIHQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 90 EVAMIFQdpmtslnpcytvgFQIMEAIKVhqgGNKKTRRQRAID----------LLNQVGIPDPASRLdvyPHQLSGGMS 159
Cdd:PRK10762 87 ELNLIPQ-------------LTIAENIFL---GREFVNRFGRIDwkkmyaeadkLLARLNLRFSSDKL---VGELSIGEQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521291413 160 QRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQkENMALILITHDLALVAEAAHKIIVMYAGQ 231
Cdd:PRK10762 148 QMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKS-QGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
26-213 |
4.10e-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: 48.39 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 26 VSYSVSQGEVVGIVGESGSGKSvSSLAIMGLIDfpgrvmaekLEFNGqdlkrisekERRSLVGSEVAMIFQDPmtSLNPC 105
Cdd:TIGR03719 24 ISLSFFPGAKIGVLGLNGAGKS-TLLRIMAGVD---------KDFNG---------EARPQPGIKVGYLPQEP--QLDPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 106 YTVGFQIMEAIKVHQG----------------------GNKKTRRQRAID------LLNQVGIPDPASRL---DVYPHQL 154
Cdd:TIGR03719 83 KTVRENVEEGVAEIKDaldrfneisakyaepdadfdklAAEQAELQEIIDaadawdLDSQLEIAMDALRCppwDADVTKL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 521291413 155 SGGMSQRVMIAMAIACQPKLLIADEPTTALDvtiqAQIIELLLELQQKENMALILITHD 213
Cdd:TIGR03719 163 SGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHD 217
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-228 |
5.59e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.86 E-value: 5.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 32 QGEVVGIVGESGSGKSvSSLAIM-GLI-----DFPGRVMAEKL--EFNG---QD-LKRISEKERRslvgsevamifqdpm 99
Cdd:COG1245 98 KGKVTGILGPNGIGKS-TALKILsGELkpnlgDYDEEPSWDEVlkRFRGtelQDyFKKLANGEIK--------------- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 100 TSLNPcytvgfQIMEAI-KVHQGgnkktrrqRAIDLLNQV---GIPDP-ASRLDVYP------HQLSGGMSQRVMIAMAI 168
Cdd:COG1245 162 VAHKP------QYVDLIpKVFKG--------TVRELLEKVderGKLDElAEKLGLENildrdiSELSGGELQRVAIAAAL 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521291413 169 ACQPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALILITHDLAL---VAEAAHkiiVMY 228
Cdd:COG1245 228 LRDADFYFFDEPSSYLDIYQRLNVARLIREL-AEEGKYVLVVEHDLAIldyLADYVH---ILY 286
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-228 |
5.74e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.88 E-value: 5.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 30 VSQGEVVGIVGESGSGKSvSSLAIM-GLI-----DFPGRVMAEKL--EFNG---QD-LKRISEKERRslvgsevamifqd 97
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKT-TAVKILsGELipnlgDYEEEPSWDEVlkRFRGtelQNyFKKLYNGEIK------------- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 98 pmTSLNPcytvgfQIMEAI-KVHQGgnkKTRrqraiDLLNQV---GIPDP-ASRLDVYP------HQLSGGMSQRVMIAM 166
Cdd:PRK13409 162 --VVHKP------QYVDLIpKVFKG---KVR-----ELLKKVderGKLDEvVERLGLENildrdiSELSGGELQRVAIAA 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521291413 167 AIACQPKLLIADEPTTALDVTIQAQIIELLLELQqkENMALILITHDLALVAEAAHKIIVMY 228
Cdd:PRK13409 226 ALLRDADFYFFDEPTSYLDIRQRLNVARLIRELA--EGKYVLVVEHDLAVLDYLADNVHIAY 285
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-232 |
8.17e-06 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 46.77 E-value: 8.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 4 LNVDKLSVHFGDVGSEfrAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDFPGRVMAEKLEFNGQDLkrisEKER 83
Cdd:cd03289 3 MTVKDLTAKYTEGGNA--VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPL----QKWR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 84 RSL-VGSEVAMIFQDPM-TSLNPcytvgfqimeaikvhqggNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQ-------- 153
Cdd:cd03289 77 KAFgVIPQKVFIFSGTFrKNLDP------------------YGKWSDEEIWKVAEEVGL---KSVIEQFPGQldfvlvdg 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 154 ---LSGGMSQRVMIAMAIACQPKLLIADEPTTALDvTIQAQIIELLLElQQKENMALILITHDLALVAEaAHKIIVMYAG 230
Cdd:cd03289 136 gcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD-PITYQVIRKTLK-QAFADCTVILSEHRIEAMLE-CQRFLVIEEN 212
|
..
gi 521291413 231 QV 232
Cdd:cd03289 213 KV 214
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
26-236 |
9.43e-06 |
|
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: 47.25 E-value: 9.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 26 VSYSVSQGEVVGIVGESGSGKSVSSLAIMGLID-FPGRV-MAEKLEFNGQD--LKRISEKERrslvgsevaMIFQDPmts 101
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDkVEGHVhMKGSVAYVPQQawIQNDSLREN---------ILFGKA--- 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 102 LNPCYTVgfQIMEA------IKVHQGGNKKTRRQRAIDLlnqvgipdpasrldvyphqlSGGMSQRVMIAMAIACQPKLL 175
Cdd:TIGR00957 725 LNEKYYQ--QVLEAcallpdLEILPSGDRTEIGEKGVNL--------------------SGGQKQRVSLARAVYSNADIY 782
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521291413 176 IADEPTTALDVTIQAQIIELLL-ELQQKENMALILITHDLALVAEaAHKIIVMYAGQVVETG 236
Cdd:TIGR00957 783 LFDDPLSAVDAHVGKHIFEHVIgPEGVLKNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMG 843
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
18-233 |
9.68e-06 |
|
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: 45.72 E-value: 9.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 18 SEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDFPGRVMAeKLEFNGQDLKRISEKERRslvgsEVAMIFQD 97
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEG-DIHYNGIPYKEFAEKYPG-----EIIYVSEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 98 pmTSLNPCYTVGfQIME-AIKVHqgGNKKTRrqraidllnqvGIpdpasrldvyphqlSGGMSQRVMIAMAIACQPKLLI 176
Cdd:cd03233 92 --DVHFPTLTVR-ETLDfALRCK--GNEFVR-----------GI--------------SGGERKRVSIAEALVSRASVLC 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 177 ADEPTTALDVTIQAQIIELLLELQQKENMALILIThdLALVAEAAH---KIIVMYAGQVV 233
Cdd:cd03233 142 WDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSL--YQASDEIYDlfdKVLVLYEGRQI 199
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-236 |
1.22e-05 |
|
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: 47.32 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 22 AVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLID-FPGRVMAeklefNGQDLKRISEKERRSLvgsevamifqdpmt 100
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPpTSGTVLV-----GGKDIETNLDAVRQSL-------------- 1005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 101 SLNPCYTVGFQ---IMEAIKVHqgGNKKTRRQRAIDLLNQVGIPDPA--SRLDVYPHQLSGGMSQRVMIAMAIACQPKLL 175
Cdd:TIGR01257 1006 GMCPQHNILFHhltVAEHILFY--AQLKGRSWEEAQLEMEAMLEDTGlhHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVV 1083
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521291413 176 IADEPTTALDVTIQAQIIELLleLQQKENMALILITHDLALVAEAAHKIIVMYAGQVVETG 236
Cdd:TIGR01257 1084 VLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-241 |
1.54e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.58 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 17 GSEFRAVDRVSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDfpgrVMAEKLEFNGqdlkrisekerrslvgsEVAMIFQ 96
Cdd:PRK13546 34 NKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLS----PTVGKVDRNG-----------------EVSVIAI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 97 DpmTSLNPCYTvGFQIMEAIKVHQGGNKKTRRQRAIDLLNqvgipdpASRLDVYPHQ----LSGGMSQRVMIAMAIACQP 172
Cdd:PRK13546 93 S--AGLSGQLT-GIENIEFKMLCMGFKRKEIKAMTPKIIE-------FSELGEFIYQpvkkYSSGMRAKLGFSINITVNP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521291413 173 KLLIADEPTTALDVTIQAQIIELLLELQQkENMALILITHDLALVAEAAHKIIVMYAGQVVETGEAKDI 241
Cdd:PRK13546 163 DILVIDEALSVGDQTFAQKCLDKIYEFKE-QNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
155-239 |
1.80e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.64 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 155 SGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQkenmalilITHDLALVA---------EAAHKII 225
Cdd:TIGR00956 211 SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSAN--------ILDTTPLVAiyqcsqdayELFDKVI 282
|
90
....*....|....
gi 521291413 226 VMYAGQVVETGEAK 239
Cdd:TIGR00956 283 VLYEGYQIYFGPAD 296
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
26-245 |
2.91e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.93 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 26 VSYSVSQGEVVGIVGESGSGKSVSSLAIMGLIDFP-GRVMAEK--------------------LEFNGQDLKRISEKERR 84
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISeGRVWAERsiayvpqqawimnatvrgniLFFDEEDAARLADAVRV 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 85 SLVGSEVAMIfqdpmtslnpcytvgfqimeaikvhqGGNKKTRrqraidlLNQVGIpdpasrldvyphQLSGGMSQRVMI 164
Cdd:PTZ00243 759 SQLEADLAQL--------------------------GGGLETE-------IGEKGV------------NLSGGQKARVSL 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 165 AMAIACQPKLLIADEPTTALDVTIQAQIIE--LLLELQQKENmalILITHDLALVAEAAHkIIVMYAGQVVETGEAKDIF 242
Cdd:PTZ00243 794 ARAVYANRDVYLLDDPLSALDAHVGERVVEecFLGALAGKTR---VLATHQVHVVPRADY-VVALGDGRVEFSGSSADFM 869
|
...
gi 521291413 243 RAP 245
Cdd:PTZ00243 870 RTS 872
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
154-236 |
6.29e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.73 E-value: 6.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 154 LSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLL--ELQQKENmalILITHDLALVAEaAHKIIVMYAGQ 231
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIkdELRGKTR---VLVTNQLHFLSQ-VDRIILVHEGM 816
|
....*
gi 521291413 232 VVETG 236
Cdd:PLN03130 817 IKEEG 821
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-226 |
7.26e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 44.39 E-value: 7.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 29 SVSQGEVVGIVGESGSGKS--VSSLAimGLIDfP--GRV-MAEKLEFNGQDLKRISEKERRSLVGSEVAMIFQDpmtslN 103
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTtfAKILA--GVLK-PdeGEVdEDLKISYKPQYISPDYDGTVEEFLRSANTDDFGS-----S 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 104 PCYTvgfQIMEAIKVHQggnkktrrqraidLLNQvgipdpasRLDvyphQLSGGMSQRVMIAMAIACQPKLLIADEPTTA 183
Cdd:COG1245 434 YYKT---EIIKPLGLEK-------------LLDK--------NVK----DLSGGELQRVAIAACLSRDADLYLLDEPSAH 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 521291413 184 LDV---TIQAQIIELLLELQQKenmALILITHDLALVAEAAHKIIV 226
Cdd:COG1245 486 LDVeqrLAVAKAIRRFAENRGK---TAMVVDHDIYLIDYISDRLMV 528
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
126-225 |
8.84e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.01 E-value: 8.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 126 TRRQRAIDLLNQVGIPDPasRLDVYPHQLSGGMSQRVMIAMAIACQPKLLIADEPTTALDvtIQAQIielLLELQQKE-N 204
Cdd:PRK10636 124 TIRSRAASLLHGLGFSNE--QLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD--LDAVI---WLEKWLKSyQ 196
|
90 100
....*....|....*....|.
gi 521291413 205 MALILITHDLALVAEAAHKII 225
Cdd:PRK10636 197 GTLILISHDRDFLDPIVDKII 217
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
130-213 |
9.98e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.73 E-value: 9.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 130 RAIDLLNQVGIPDpasrldvypHQLSGGMSQ-------RVMIAMAIACQPKLLIADEPTTALDV-TIQaqiieLLLELQQ 201
Cdd:PRK15064 134 RAGELLLGVGIPE---------EQHYGLMSEvapgwklRVLLAQALFSNPDILLLDEPTNNLDInTIR-----WLEDVLN 199
|
90
....*....|..
gi 521291413 202 KENMALILITHD 213
Cdd:PRK15064 200 ERNSTMIIISHD 211
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
153-232 |
1.21e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.62 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 153 QLSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQkenmALILITHDLALVAEAAHKIIVMYAGQV 232
Cdd:PRK10636 430 RFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEG----ALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
154-244 |
1.65e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.43 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 154 LSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLL--ELQQKENmalILITHDLALVAEaAHKIIVMYAGQ 231
Cdd:PLN03232 741 ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMkdELKGKTR---VLVTNQLHFLPL-MDRIILVSEGM 816
|
90
....*....|...
gi 521291413 232 VVETGEAKDIFRA 244
Cdd:PLN03232 817 IKEEGTFAELSKS 829
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
26-237 |
2.51e-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: 41.86 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 26 VSYSVSQGEVVGIVGESGSGKSvsSLAIMGLIDFPGRVMAEKLE-FNGQDLKRISEKERRSLVGSEVAMIFQDPMTSLNP 104
Cdd:cd03270 14 VDVDIPRNKLVVITGVSGSGKS--SLAFDTIYAEGQRRYVESLSaYARQFLGQMDKPDVDSIEGLSPAIAIDQKTTSRNP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 105 CYTVGfQIMEAikvhqggNKKTR--------RQRaIDLLNQVGIPdpASRLDVYPHQLSGGMSQRVMIAMAIACQPK--L 174
Cdd:cd03270 92 RSTVG-TVTEI-------YDYLRllfarvgiRER-LGFLVDVGLG--YLTLSRSAPTLSGGEAQRIRLATQIGSGLTgvL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521291413 175 LIADEPTTALDVTIQAQIIELLLELQQKENmALILITHDLALVAEAAHkIIVMYAGQVVETGE 237
Cdd:cd03270 161 YVLDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVVEHDEDTIRAADH-VIDIGPGAGVHGGE 221
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
154-226 |
2.63e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.49 E-value: 2.63e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 521291413 154 LSGGMSQRVMIAMAIACQPKLLIADEPTTALDV---TIQAQIIELLLELQQKenmALILITHDLALVAEAAHKIIV 226
Cdd:PRK13409 454 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrLAVAKAIRRIAEEREA---TALVVDHDIYMIDYISDRLMV 526
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
154-236 |
2.65e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 41.83 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 154 LSGGMSQRVMIAMAIACQ---PKLLIADEPTTAL---DVtiqAQIIELLLELQQKENMALIlITHDLALVAEAAHkIIVM 227
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLhfhDV---KKLLEVLQRLVDKGNTVVV-IEHNLDVIKCADW-IIDL 244
|
90
....*....|....*
gi 521291413 228 ------YAGQVVETG 236
Cdd:cd03271 245 gpeggdGGGQVVASG 259
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
154-228 |
3.22e-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: 41.02 E-value: 3.22e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 521291413 154 LSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLALVAEAAHKIIVMY 228
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
146-224 |
9.77e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 9.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 146 RLDVYP-----HQLSGGMSQRVMIA---MAIACQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALIlITHDLALV 217
Cdd:PRK00635 797 GLDYLPlgrplSSLSGGEIQRLKLAyelLAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVI-IEHNMHVV 875
|
....*..
gi 521291413 218 AEAAHKI 224
Cdd:PRK00635 876 KVADYVL 882
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
26-216 |
1.18e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 39.47 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 26 VSYSVSQGEVVGIVGESGSGKSvsSL--AIMGLIdfpgRVMAEKLEFNGQDLKRISEKERRSLVGSEVAMifqdpmtslN 103
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKT--TLlrLIAGLL----PPAAGTIKLDGGDIDDPDVAEACHYLGHRNAM---------K 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 104 PCYTVgfqiMEAIKVHQG--GNKKTRRQRAIDLLNQVGIPD-PAsrldvypHQLSGGMSQRVMIAmaiacqpKLLIA--- 177
Cdd:PRK13539 86 PALTV----AENLEFWAAflGGEELDIAAALEAVGLAPLAHlPF-------GYLSAGQKRRVALA-------RLLVSnrp 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 521291413 178 ----DEPTTALDVTIQAQIIELLLElQQKENMALILITH-DLAL 216
Cdd:PRK13539 148 iwilDEPTAALDAAAVALFAELIRA-HLAQGGIVIAATHiPLGL 190
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
154-237 |
1.34e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.16 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 154 LSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALILITHDLALVAEAAHKIIVMYAGQVv 233
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINEL-AAEGKGVIVISSELPELLGMCDRIYVMNEGRI- 482
|
....
gi 521291413 234 eTGE 237
Cdd:NF040905 483 -TGE 485
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
152-216 |
1.56e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 39.64 E-value: 1.56e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521291413 152 HQLSGGMsQRVM-IAMAIA---CQPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALILITHDLAL 216
Cdd:COG1106 201 SEESDGT-KRLLaLAGALLdalAKGGVLLIDEIEASLHPSLLRKLLKLFLDLANKNNAQLIFTTHSTEL 268
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
154-217 |
1.87e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 39.93 E-value: 1.87e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521291413 154 LSGGMSQRVMIAMAIACQPKLLIADEPTTALDVtiqaQIIELLLELQQKENMALILITHDLALV 217
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHDRQFV 500
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
154-236 |
2.16e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.00 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 154 LSGGMSQRVMIAMAI---ACQPKLLIADEPTTAL---DVtiqAQIIELLLELQQKENmALILITHDLALVAEAAHKIIV- 226
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLhfdDI---KKLLEVLQRLVDKGN-TVVVIEHNLDVIKTADYIIDLg 905
|
90
....*....|....
gi 521291413 227 ----MYAGQVVETG 236
Cdd:TIGR00630 906 peggDGGGTVVASG 919
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
154-233 |
3.97e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 38.72 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 154 LSGGMSQRVMIAMAIACQPKLLIADEPTTALDVtiqaQIIELLlelqqkeNMAL-------ILITHDLALVAEAAHKIIV 226
Cdd:PRK15064 439 LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDM----ESIESL-------NMALekyegtlIFVSHDREFVSSLATRIIE 507
|
....*..
gi 521291413 227 MYAGQVV 233
Cdd:PRK15064 508 ITPDGVV 514
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
154-212 |
4.80e-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: 38.58 E-value: 4.80e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 521291413 154 LSGGMSQRVMIAMAIACQPKLLIADEPTTALDVTIQAQIIELLlelqQKENMALILITH 212
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLC----REFGITLFSVSH 637
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
154-274 |
6.48e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.46 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291413 154 LSGGMSQRVMIAMAIACQPK--LLIADEPTTALDVTIQAQIIELLLELQQKENmALILITHDLALVAEAAHkIIVM---- 227
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRLRDLGN-TLIVVEHDEDTIRAADY-VIDIgpga 566
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 521291413 228 --YAGQVVETGEAKDIFRAPrHPYTQALLRALPEFAQDKARLASLPGVV 274
Cdd:TIGR00630 567 geHGGEVVASGTPEEILANP-DSLTGQYLSGRKKIEVPAERRPGNGKFL 614
|
|
| |
