|
Name |
Accession |
Description |
Interval |
E-value |
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-322 |
4.41e-159 |
|
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: 446.81 E-value: 4.41e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFPTQNGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQARITcDELVLDGKNLLQLTATE 82
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGITS-GEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 RRRLNGGTVAMIFQEPMTSLNPCFTVGYQIDEAVKTHVGGGRKERKEQVLSLLESVGIPDPARRYDAYPHQMSGGMSQRA 162
Cdd:COG0444 80 LRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 163 MIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYELF 242
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 243 NHPHHPYTAALLSALPERALPTGLLPTIPGLVPGQHNRPQGCLFAPRCAYQQARCQTEVPALAQQQQG-WIRCFYPLETE 321
Cdd:COG0444 240 ENPRHPYTRALLSSIPRLDPDGRRLIPIPGEPPSLLNPPSGCRFHPRCPYAMDRCREEEPPLREVGPGhRVACHLYEEEA 319
|
.
gi 522049469 322 T 322
Cdd:COG0444 320 P 320
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-319 |
6.53e-138 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 393.72 E-value: 6.53e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MSLLSVRNLSVAFPTQNGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQARITCDELVLDGKNLLQLTA 80
Cdd:PRK11022 1 MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 81 TERRRLNGGTVAMIFQEPMTSLNPCFTVGYQIDEAVKTHVGGGRKERKEQVLSLLESVGIPDPARRYDAYPHQMSGGMSQ 160
Cdd:PRK11022 81 KERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 161 RAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYE 240
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522049469 241 LFNHPHHPYTAALLSALPERALPTGLLPTIPGLVPGQHNRPQGCLFAPRCAYQQARCQTEVPALAQQQQGWIRCFYPLE 319
Cdd:PRK11022 241 IFRAPRHPYTQALLRALPEFAQDKARLASLPGVVPGKYDRPNGCLLNPRCPYATDRCRAEEPALNMLAGRQSKCHYPLD 319
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-263 |
3.21e-126 |
|
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: 371.32 E-value: 3.21e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MSLLSVRNLSVAFPTQNGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQARITCDELVLDGKNLLQLTA 80
Cdd:COG4172 4 MPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 81 TERRRLNGGTVAMIFQEPMTSLNPCFTVGYQIDEAVKTHVGGGRKERKEQVLSLLESVGIPDPARRYDAYPHQMSGGMSQ 160
Cdd:COG4172 84 RELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 161 RAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYE 240
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAE 243
|
250 260
....*....|....*....|...
gi 522049469 241 LFNHPHHPYTAALLSALPERALP 263
Cdd:COG4172 244 LFAAPQHPYTRKLLAAEPRGDPR 266
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-322 |
1.89e-108 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 318.77 E-value: 1.89e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MSLLSVRNLSVAFPTQNGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQARITCDELVLDGKNLLQLTA 80
Cdd:COG4170 1 MPLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADRFRWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 81 TERRRLNGGTVAMIFQEPMTSLNPCFTVGYQIDEAVKTHVGGGR-----KERKEQVLSLLESVGIPDPARRYDAYPHQMS 155
Cdd:COG4170 81 RERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIPSWTFKGKwwqrfKWRKKRAIELLHRVGIKDHKDIMNSYPHELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 156 GGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEK 235
Cdd:COG4170 161 EGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVES 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 236 NSAYELFNHPHHPYTAALLSALPE--RALPT-GLLPTIPGLVPGQHNRPQGCLFAPRCAYQQARCqTEVPALAQQQQGWI 312
Cdd:COG4170 241 GPTEQILKSPHHPYTKALLRSMPDfrQPLPHkSRLNTLPGSIPPLQHLPIGCRLGPRCPYAQKKC-VETPRLRKIKGHEF 319
|
330
....*....|
gi 522049469 313 RCFYPLETET 322
Cdd:COG4170 320 ACHFPLNMEE 329
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-320 |
4.25e-106 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 312.81 E-value: 4.25e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MSLLSVRNLSVAFPTQNGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQARITcDELVLDGKNLLQLTA 80
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIG-GSATFNGREILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 81 TERRRLNGGTVAMIFQEPMTSLNPCFTVGYQIDEAVKTHVGGGRKERKEQVLSLLESVGIPDPARRYDAYPHQMSGGMSQ 160
Cdd:PRK09473 89 KELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGGMRQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 161 RAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYE 240
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 241 LFNHPHHPYTAALLSALPERALPTGLLPTIPGLVPGQHNRPQGCLFAPRCAYQQARCQTEvPALAQQQQGWIR-CFYPLE 319
Cdd:PRK09473 249 VFYQPSHPYSIGLLNAVPRLDAEGESLLTIPGNPPNLLRLPKGCPFQPRCPHAMEICSSA-PPLEEFGPGRLRaCFKPVE 327
|
.
gi 522049469 320 T 320
Cdd:PRK09473 328 E 328
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-236 |
1.75e-98 |
|
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: 289.79 E-value: 1.75e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFPTQNGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPqariTCDELVLDGKNLLQLTAtE 82
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKP----TSGSIIFDGKDLLKLSR-R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 RRRLNGGTVAMIFQEPMTSLNPCFTVGYQIDEAVKTHVGGGRKERKEQVLsLLESVGIPDPARRYDAYPHQMSGGMSQRA 162
Cdd:cd03257 76 LRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAV-LLLLVGVGLPEEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522049469 163 MIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKN 236
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-319 |
1.08e-89 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 271.22 E-value: 1.08e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFPTQNGWF-------QAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPqariTCDELVLDGKNL 75
Cdd:COG4608 7 LLEVRDLKKHFPVRGGLFgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEP----TSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 76 LQLTATERRRLNGgTVAMIFQEPMTSLNPCFTVGYQIDEAVKTHVGGGRKERKEQVLSLLESVGI-PDPARRYdayPHQM 154
Cdd:COG4608 83 TGLSGRELRPLRR-RMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLrPEHADRY---PHEF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 155 SGGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAqilelllklqqqfqMGL--ILITHDMGVVAETAQQVVVQYAGQQ 232
Cdd:COG4608 159 SGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAqvlnll--edlqdeLGLtyLFISHDLSVVRHISDRVAVMYLGKI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 233 VEKNSAYELFNHPHHPYTAALLSALP--------ERALPTGLLPT-IpglvpgqhNRPQGCLFAPRCAYQQARCQTEVPA 303
Cdd:COG4608 237 VEIAPRDELYARPLHPYTQALLSAVPvpdperrrERIVLEGDVPSpL--------NPPSGCRFHTRCPYAQDRCATEEPP 308
|
330
....*....|....*..
gi 522049469 304 LAQQQQG-WIRCFYPLE 319
Cdd:COG4608 309 LREVGPGhQVACHLAEE 325
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-271 |
6.50e-89 |
|
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: 275.24 E-value: 6.50e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MS-LLSVRNLSVAFPtqNGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQARITcDELVLDGKNLLQLT 79
Cdd:COG1123 1 MTpLLEVRDLSVRYP--GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRIS-GEVLLDGRDLLELS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 80 ATERrrlnGGTVAMIFQEPMTSLNPcFTVGYQIDEAVKTHvGGGRKERKEQVLSLLESVGIpdpARRYDAYPHQMSGGMS 159
Cdd:COG1123 78 EALR----GRRIGMVFQDPMTQLNP-VTVGDQIAEALENL-GLSRAEARARVLELLEAVGL---ERRLDRYPHQLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 160 QRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAY 239
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE 228
|
250 260 270
....*....|....*....|....*....|..
gi 522049469 240 ELFNHPhhpytaALLSALPERALPTGLLPTIP 271
Cdd:COG1123 229 EILAAP------QALAAVPRLGAARGRAAPAA 254
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-259 |
2.79e-85 |
|
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: 265.61 E-value: 2.79e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFPTQ-NGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQA-RITcdelvLDGKNLLQLTA 80
Cdd:COG1123 260 LLEVRNLSKRYPVRgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSgSIL-----FDGKDLTKLSR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 81 TERRRLnGGTVAMIFQEPMTSLNPCFTVGYQIDEAVKTHVGGGRKERKEQVLSLLESVGIPdpARRYDAYPHQMSGGMSQ 160
Cdd:COG1123 335 RSLREL-RRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLP--PDLADRYPHELSGGQRQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 161 RAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYE 240
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEE 491
|
250
....*....|....*....
gi 522049469 241 LFNHPHHPYTAALLSALPE 259
Cdd:COG1123 492 VFANPQHPYTRALLAAVPS 510
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-322 |
1.05e-83 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 255.88 E-value: 1.05e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MSLLSVRNLSVAFPTQNGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQARITCDELVLDGKNLLQLTA 80
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 81 TERRRLNGGTVAMIFQEPMTSLNPCFTVGYQIDEAVKTHVGGGR-----KERKEQVLSLLESVGIPDPARRYDAYPHQMS 155
Cdd:PRK15093 81 RERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPGWTYKGRwwqrfGWRKRRAIELLHRVGIKDHKDAMRSFPYELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 156 GGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEK 235
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVET 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 236 NSAYELFNHPHHPYTAALLSALPE--RALP-TGLLPTIPGLVPGQHNRPQGCLFAPRCAYQQARCqTEVPALAQQQQGWI 312
Cdd:PRK15093 241 APSKELVTTPHHPYTQALIRAIPDfgSAMPhKSRLNTLPGAIPLLEHLPIGCRLGPRCPYAQREC-IETPRLTGAKNHLY 319
|
330
....*....|
gi 522049469 313 RCFYPLETET 322
Cdd:PRK15093 320 ACHFPLNMEE 329
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-259 |
5.46e-82 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 260.17 E-value: 5.46e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFPTQNGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQ-ARITCDELVLDGKN-----LL 76
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAgGLVQCDKMLLRRRSrqvieLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 77 QLTATERRRLNGGTVAMIFQEPMTSLNPCFTVGYQIDEAVKTHVGGGRKERKEQVLSLLESVGIPDPARRYDAYPHQMSG 156
Cdd:PRK10261 92 EQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 157 GMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKN 236
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
|
250 260
....*....|....*....|...
gi 522049469 237 SAYELFNHPHHPYTAALLSALPE 259
Cdd:PRK10261 252 SVEQIFHAPQHPYTRALLAAVPQ 274
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-263 |
1.06e-81 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 256.94 E-value: 1.06e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MSLLSVRNLSVAFPTQNGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLP-PQARITCDELVLDGKNLLQLT 79
Cdd:PRK15134 3 QPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPsPPVVYPSGDIRFHGESLLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 80 ATERRRLNGGTVAMIFQEPMTSLNPCFTVGYQIDEAVKTHVGGGRKERKEQVLSLLESVGIPDPARRYDAYPHQMSGGMS 159
Cdd:PRK15134 83 EQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGGER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 160 QRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAY 239
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAA 242
|
250 260
....*....|....*....|....*
gi 522049469 240 ELFNHPHHPYTAALLSALPE-RALP 263
Cdd:PRK15134 243 TLFSAPTHPYTQKLLNSEPSgDPVP 267
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
22-256 |
1.18e-72 |
|
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: 224.17 E-value: 1.18e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 22 AVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQARITCDELVLDGKNLLQLtaterrRLNGGTVAMIFQEPMTS 101
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTQTSGEILLDGRPLLPL------SIRGRHIATIMQNPRTA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 102 LNPCFTVGYQIDEAVKTHvGGGRKERKEQVLSLLESVGIPDPARRYDAYPHQMSGGMSQRAMIAMALAGQPKLLIADEPT 181
Cdd:TIGR02770 75 FNPLFTMGNHAIETLRSL-GKLSKQARALILEALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPT 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522049469 182 TALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYELFNHPHHPYTAALLSA 256
Cdd:TIGR02770 154 TDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLSA 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-263 |
2.74e-72 |
|
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: 223.91 E-value: 2.74e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFPTQNGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPqariTCDELVLDGKNLLQLTATE 82
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERP----WSGEVTFDGRPVTRRRRKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 RRRlnggTVAMIFQEPMTSLNPCFTVGYQIDEAVKTHvggGRKERKEQVLSLLESVGIPDPARryDAYPHQMSGGMSQRA 162
Cdd:COG1124 77 FRR----RVQMVFQDPYASLHPRHTVDRILAEPLRIH---GLPDREERIAELLEQVGLPPSFL--DRYPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 163 MIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYELF 242
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
250 260
....*....|....*....|.
gi 522049469 243 NHPHHPYTAALLSALPERALP 263
Cdd:COG1124 228 AGPKHPYTRELLAASLAFERA 248
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
3-316 |
1.09e-71 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 224.84 E-value: 1.09e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFPTQNGWF------QAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPqariTCDELVLDGKNLL 76
Cdd:PRK11308 5 LLQAIDLKKHYPVKRGLFkperlvKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETP----TGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 77 QLTATERRRLNGgTVAMIFQEPMTSLNPCFTVGYQIDEAVKTHVGGGRKERKEQVLSLLESVGIPdpARRYDAYPHQMSG 156
Cdd:PRK11308 81 KADPEAQKLLRQ-KIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLR--PEHYDRYPHMFSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 157 GMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKN 236
Cdd:PRK11308 158 GQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 237 SAYELFNHPHHPYTAALLSALPeRALPTGLLPTIP--GLVPGQHNRPQGCLFAPRCAYQQARCQTEVPALAQQQQGWIRC 314
Cdd:PRK11308 238 TKEQIFNNPRHPYTQALLSATP-RLNPDDRRERIKltGELPSPLNPPPGCAFNARCPRAFGRCRQEQPQLRDYDGRLVAC 316
|
..
gi 522049469 315 FY 316
Cdd:PRK11308 317 FA 318
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-259 |
1.41e-71 |
|
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: 230.73 E-value: 1.41e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFPTQNGWFQ-------AVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQARItcdelVLDGKNL 75
Cdd:COG4172 275 LLEARDLKVWFPIKRGLFRrtvghvkAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEI-----RFDGQDL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 76 LQLTATERRRLNGGtVAMIFQEPMTSLNPCFTVGYQIDEAVKTH-VGGGRKERKEQVLSLLESVGIpDPARRyDAYPHQM 154
Cdd:COG4172 350 DGLSRRALRPLRRR-MQVVFQDPFGSLSPRMTVGQIIAEGLRVHgPGLSAAERRARVAEALEEVGL-DPAAR-HRYPHEF 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 155 SGGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVE 234
Cdd:COG4172 427 SGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVE 506
|
250 260
....*....|....*....|....*
gi 522049469 235 KNSAYELFNHPHHPYTAALLSALPE 259
Cdd:COG4172 507 QGPTEQVFDAPQHPYTRALLAAAPL 531
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-304 |
6.75e-67 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 213.03 E-value: 6.75e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFPTQNG--WF-------QAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPpqarITCDELVLDGK 73
Cdd:PRK15079 8 LLEVADLKVHFDIKDGkqWFwqppktlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVK----ATDGEVAWLGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 74 NLLQLTATERRRLNGgTVAMIFQEPMTSLNPCFTVGYQIDEAVKT-HVGGGRKERKEQVLSLLESVGI-PDPARRYdayP 151
Cdd:PRK15079 84 DLLGMKDDEWRAVRS-DIQMIFQDPLASLNPRMTIGEIIAEPLRTyHPKLSRQEVKDRVKAMMLKVGLlPNLINRY---P 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 152 HQMSGGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQ 231
Cdd:PRK15079 160 HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522049469 232 QVEKNSAYELFNHPHHPYTAALLSALP------ERALPTGLLptiPGLVPGQHNRPQGCLFAPRCAYQQARCQTEVPAL 304
Cdd:PRK15079 240 AVELGTYDEVYHNPLHPYTKALMSAVPipdpdlERNKTIQLL---EGELPSPINPPSGCVFRTRCPIAGPECAKTRPVL 315
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
23-256 |
5.24e-58 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 187.60 E-value: 5.24e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 23 VEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQARITCDELVLDGKNLLQLTaterrrLNGGTVAMIFQEPMTSL 102
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTAGRVLLDGKPVAPCA------LRGRKIATIMQNPRSAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 103 NPCFTVGyqiDEAVKTHVGGGRKERKEQVLSLLESVGIPDPARRYDAYPHQMSGGMSQRAMIAMALAGQPKLLIADEPTT 182
Cdd:PRK10418 93 NPLHTMH---THARETCLALGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522049469 183 ALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYELFNHPHHPYTAALLSA 256
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-278 |
1.34e-51 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 173.34 E-value: 1.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPTQNGWFQAVEGINLTVNPNEILAIVGESGSGKSVaMLALMNLL--PPQARITcdelvLDGKNLLQLTAT 81
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKST-LIRCINLLerPTSGSVL-----VDGVDLTALSER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 82 E----RRRlnggtVAMIFQEP--MTSlnpcftvgyqideavKT----------HVGGGRKERKEQVLSLLESVGIPDPAr 145
Cdd:COG1135 76 ElraaRRK-----IGMIFQHFnlLSS---------------RTvaenvalpleIAGVPKAEIRKRVAELLELVGLSDKA- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 146 ryDAYPHQMSGGMSQRAMIAMALAGQPKLLIADEPTTALD-------------------VTVqaqilelllklqqqfqmg 206
Cdd:COG1135 135 --DAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDpettrsildllkdinrelgLTI------------------ 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522049469 207 lILITHDMGVVAETAQQVVVQYAGQQVEKNSAYELFNHPHHPYTAALLSALPERALPTGLLPTIPGLVPGQH 278
Cdd:COG1135 195 -VLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRFLPTVLNDELPEELLARLREAAGGGR 265
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-255 |
7.32e-50 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 173.74 E-value: 7.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFPTQNGWF-------QAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQARITCDELVLDGKNL 75
Cdd:PRK15134 275 LLDVEQLQVAFPIRKGILkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFDGQPLHNLNR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 76 LQLTATERRrlnggtVAMIFQEPMTSLNPCFTVGYQIDEAVKTHVGG-GRKERKEQVLSLLESVGIpDPARRYdAYPHQM 154
Cdd:PRK15134 355 RQLLPVRHR------IQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTlSAAQREQQVIAVMEEVGL-DPETRH-RYPAEF 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 155 SGGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVE 234
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVE 506
|
250 260
....*....|....*....|.
gi 522049469 235 KNSAYELFNHPHHPYTAALLS 255
Cdd:PRK15134 507 QGDCERVFAAPQQEYTRQLLA 527
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-256 |
9.08e-49 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 163.85 E-value: 9.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MSLLSVRNLSVAFPTQNGWF-----QAVEGINLTVNPNEILAIVGESGSGKS--VAMLALMNllPPqariTCDELVLDGK 73
Cdd:COG4167 2 SALLEVRNLSKTFKYRTGLFrrqqfEAVKPVSFTLEAGQTLAIIGENGSGKStlAKMLAGII--EP----TSGEILINGH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 74 NLLQLTATERRRLnggtVAMIFQEPMTSLNPCFTVGYQIDEAVKTHVGGGRKERKEQVLSLLESVGI-PDPArryDAYPH 152
Cdd:COG4167 76 KLEYGDYKYRCKH----IRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLlPEHA---NFYPH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 153 QMSGGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQ 232
Cdd:COG4167 149 MLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEV 228
|
250 260
....*....|....*....|....
gi 522049469 233 VEKNSAYELFNHPHHPYTAALLSA 256
Cdd:COG4167 229 VEYGKTAEVFANPQHEVTKRLIES 252
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-258 |
1.26e-45 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 163.49 E-value: 1.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFPTQNGWF-------QAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQAritcDELVLDGKNL 75
Cdd:PRK10261 313 ILQVRNLVTRFPLRSGLLnrvtrevHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQG----GEIIFNGQRI 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 76 LQLTATERRRLNGgTVAMIFQEPMTSLNPCFTVGYQIDEAVKTHVGGGRKERKEQVLSLLESVGI-PDPARRYdayPHQM 154
Cdd:PRK10261 389 DTLSPGKLQALRR-DIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLlPEHAWRY---PHEF 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 155 SGGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVE 234
Cdd:PRK10261 465 SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVE 544
|
250 260
....*....|....*....|....
gi 522049469 235 KNSAYELFNHPHHPYTAALLSALP 258
Cdd:PRK10261 545 IGPRRAVFENPQHPYTRKLMAAVP 568
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-225 |
1.93e-44 |
|
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: 151.10 E-value: 1.93e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPTQNGWFQAVEGINLTVNPNEILAIVGESGSGKSvamlALMNLLPPQARITCDELVLDGKNLLQLTATER 83
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS----TLLNILGGLDRPTSGEVRVDGTDISKLSEKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 84 RRLNGGTVAMIFQEPmtSLNPCFTVgyqiDEAVK---THVGGGRKERKEQVLSLLESVGIPDparRYDAYPHQMSGGMSQ 160
Cdd:cd03255 77 AAFRRRHIGFVFQSF--NLLPDLTA----LENVElplLLAGVPKKERRERAEELLERVGLGD---RLNHYPSELSGGQQQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522049469 161 RAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMgVVAETAQQVV 225
Cdd:cd03255 148 RVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRII 211
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-245 |
1.73e-43 |
|
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: 149.27 E-value: 1.73e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFPTQNGWFQAVEGINLTVNPNEILAIVGESGSGKSvAMLALMNLLppqARITCDELVLDGKNLLQLTATE 82
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKS-TLIRCINGL---ERPTSGSVLVDGTDLTLLSGKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 RR--RLNggtVAMIFQE--PMTSLnpcfTVGYQIDEAVKTHvGGGRKERKEQVLSLLESVGIPDPArryDAYPHQMSGGM 158
Cdd:cd03258 77 LRkaRRR---IGMIFQHfnLLSSR----TVFENVALPLEIA-GVPKAEIEERVLELLELVGLEDKA---DAYPAQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 159 SQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSA 238
Cdd:cd03258 146 KQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTV 225
|
....*..
gi 522049469 239 YELFNHP 245
Cdd:cd03258 226 EEVFANP 232
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-257 |
2.53e-42 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 146.29 E-value: 2.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSvAMLALMNLL-PPQA-RITCD--ELVLDGKNLLQL 78
Cdd:COG1126 1 MIEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKS-TLLRCINLLeEPDSgTITVDgeDLTDSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 79 tateRRRlnggtVAMIFQepmtSLN--PCFTVGYQIDEAVKTHVGGGRKERKEQVLSLLESVGIPDparRYDAYPHQMSG 156
Cdd:COG1126 76 ----RRK-----VGMVFQ----QFNlfPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLAD---KADAYPAQLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 157 GMSQRAMIAMALAGQPKLLIADEPTTALD---------VTVQAqilelllklqQQFQMGLILITHDMGVVAETAQQVVVQ 227
Cdd:COG1126 140 GQQQRVAIARALAMEPKVMLFDEPTSALDpelvgevldVMRDL----------AKEGMTMVVVTHEMGFAREVADRVVFM 209
|
250 260 270
....*....|....*....|....*....|
gi 522049469 228 YAGQQVEKNSAYELFNHPHHPYTAALLSAL 257
Cdd:COG1126 210 DGGRIVEEGPPEEFFENPQHERTRAFLSKV 239
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-267 |
1.96e-41 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 146.87 E-value: 1.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 7 RNLSVAFPTQNGWFQAVEGINLTVNPNEILAIVGESGSGKSvAMLALMNLLppqARITCDELVLDGKNLLQLTATE---- 82
Cdd:PRK11153 5 KNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKS-TLIRCINLL---ERPTSGRVLVDGQDLTALSEKElrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 RRRlnggtVAMIFQEpmtslnpcF------TVGYQIDEAVKThVGGGRKERKEQVLSLLESVGIPDPArryDAYPHQMSG 156
Cdd:PRK11153 81 RRQ-----IGMIFQH--------FnllssrTVFDNVALPLEL-AGTPKAEIKARVTELLELVGLSDKA---DRYPAQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 157 GMSQRAMIAMALAGQPKLLIADEPTTALD-VTVQAQILELLLKLQQqfqMGL--ILITHDMGVVAETAQQVVVQYAGQQV 233
Cdd:PRK11153 144 GQKQRVAIARALASNPKVLLCDEATSALDpATTRSILELLKDINRE---LGLtiVLITHEMDVVKRICDRVAVIDAGRLV 220
|
250 260 270
....*....|....*....|....*....|....
gi 522049469 234 EKNSAYELFNHPHHPYTAALLSALPERALPTGLL 267
Cdd:PRK11153 221 EQGTVSEVFSHPKHPLTREFIQSTLHLDLPEDYL 254
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-185 |
1.27e-40 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 141.72 E-value: 1.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 2 SLLSVRNLSVAFPTQNGWFQAVEGINLTVNPNEILAIVGESGSGKSVamlaLMNLL----PPqariTCDELVLDGKNLLQ 77
Cdd:COG1136 3 PLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKST----LLNILggldRP----TSGEVLIDGQDISS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 78 LTATERRRLNGGTVAMIFQEPmtSLNPCFTVGYQIdEAVKTHVGGGRKERKEQVLSLLESVGIPDparRYDAYPHQMSGG 157
Cdd:COG1136 75 LSERELARLRRRHIGFVFQFF--NLLPELTALENV-ALPLLLAGVSRKERRERARELLERVGLGD---RLDHRPSQLSGG 148
|
170 180
....*....|....*....|....*...
gi 522049469 158 MSQRAMIAMALAGQPKLLIADEPTTALD 185
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLD 176
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-226 |
1.38e-39 |
|
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: 138.76 E-value: 1.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPTQNGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQAritcDELVLDGKnllQLTATER 83
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTS----GEVLVDGE---PVTGPGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 84 RRlnggtvAMIFQEPmtSLNPCFTV------GYQIdeavkthVGGGRKERKEQVLSLLESVGIPDPArryDAYPHQMSGG 157
Cdd:cd03293 74 DR------GYVFQQD--ALLPWLTVldnvalGLEL-------QGVPKAEARERAEELLELVGLSGFE---NAYPHQLSGG 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522049469 158 MSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVV 226
Cdd:cd03293 136 MRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVV 204
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-186 |
4.08e-39 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 138.68 E-value: 4.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MSLLSVRNLSVAFPTQNGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQA-RITcdelvLDGKnllQLT 79
Cdd:COG1116 5 APALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSgEVL-----VDGK---PVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 80 ATERRRlnggtvAMIFQEPmtSLNPCFTVGYQIDEAVKtHVGGGRKERKEQVLSLLESVGIPDPArryDAYPHQMSGGMS 159
Cdd:COG1116 77 GPGPDR------GVVFQEP--ALLPWLTVLDNVALGLE-LRGVPKAERRERARELLELVGLAGFE---DAYPHQLSGGMR 144
|
170 180
....*....|....*....|....*..
gi 522049469 160 QRAMIAMALAGQPKLLIADEPTTALDV 186
Cdd:COG1116 145 QRVAIARALANDPEVLLMDEPFGALDA 171
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
3-257 |
7.75e-39 |
|
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: 137.65 E-value: 7.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFPTQNGWFQavegINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQA-RITCDELVLDGKNLLQLTAT 81
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRD----VSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHgTATYIMRSGAELELYQLSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 82 ERRRLNGGTVAMIFQEPMTSLNPCFTVGYQIDEAV----KTHVGGGRKERKEqvlsLLESVGIPdpARRYDAYPHQMSGG 157
Cdd:TIGR02323 79 ERRRLMRTEWGFVHQNPRDGLRMRVSAGANIGERLmaigARHYGNIRATAQD----WLEEVEID--PTRIDDLPRAFSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 158 MSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNS 237
Cdd:TIGR02323 153 MQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGL 232
|
250 260
....*....|....*....|
gi 522049469 238 AYELFNHPHHPYTAALLSAL 257
Cdd:TIGR02323 233 TDQVLDDPQHPYTQLLVSSI 252
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-260 |
1.30e-37 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 134.81 E-value: 1.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MSLLSVRNLSVAFPTQN-----GWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNL-LPPQARITCDelvldGKN 74
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGGlsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLeSPSQGNVSWR-----GEP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 75 LLQLtATERRRLNGGTVAMIFQEPMTSLNPCFTVGYQIDEAVKTHVGGGRKERKEQVLSLLESVGIPDpaRRYDAYPHQM 154
Cdd:PRK10419 76 LAKL-NRAQRKAFRRDIQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDD--SVLDKRPPQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 155 SGGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVE 234
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
250 260
....*....|....*....|....*..
gi 522049469 235 KNSAYELFnHPHHPYTAALLSA-LPER 260
Cdd:PRK10419 233 TQPVGDKL-TFSSPAGRVLQNAvLPAF 258
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-246 |
2.12e-37 |
|
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: 133.57 E-value: 2.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQA-RITcdelvLDGKNLLQLTAT 81
Cdd:COG1127 5 MIEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSgEIL-----VDGQDITGLSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 82 ERRRLNGGtVAMIFQEP-----MTSL-NpcftVGYQIDEavktHVGGGRKERKEQVLSLLESVGIPDPArryDAYPHQMS 155
Cdd:COG1127 76 ELYELRRR-IGMLFQGGalfdsLTVFeN----VAFPLRE----HTDLSEAEIRELVLEKLELVGLPGAA---DKMPSELS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 156 GGMSQRAMIAMALAGQPKLLIADEPTTALD-----------VTVQAqilelllklqqqfQMGL--ILITHDMGVVAETAQ 222
Cdd:COG1127 144 GGMRKRVALARALALDPEILLYDEPTAGLDpitsavideliRELRD-------------ELGLtsVVVTHDLDSAFAIAD 210
|
250 260
....*....|....*....|....
gi 522049469 223 QVVVQYAGQQVEKNSAYELFNHPH 246
Cdd:COG1127 211 RVAVLADGKIIAEGTPEELLASDD 234
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-246 |
4.35e-37 |
|
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: 132.63 E-value: 4.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQAritcDELVLDGKNLLQLTATER 83
Cdd:cd03261 1 IELRGLTKSF----GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDS----GEVLIDGEDISGLSEAEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 84 RRLnGGTVAMIFQEP--MTSLNPCFTVGYQIDEavktHVGGGRKERKEQVLSLLESVGIPDPArryDAYPHQMSGGMSQR 161
Cdd:cd03261 73 YRL-RRRMGMLFQSGalFDSLTVFENVAFPLRE----HTRLSEEEIREIVLEKLEAVGLRGAE---DLYPAELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 162 AMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYEL 241
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
....*
gi 522049469 242 FNHPH 246
Cdd:cd03261 225 RASDD 229
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-256 |
5.62e-37 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 133.13 E-value: 5.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQA-RITCDELVLDGKNLLQLTAT 81
Cdd:PRK11701 6 LLSVRGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAgEVHYRMRDGQLRDLYALSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 82 ERRRLNGGTVAMIFQEPMTSLNPCFTVGYQIDE---AV-KTHVGGGRkerkEQVLSLLESVGIPdpARRYDAYPHQMSGG 157
Cdd:PRK11701 82 ERRRLLRTEWGFVHQHPRDGLRMQVSAGGNIGErlmAVgARHYGDIR----ATAGDWLERVEID--AARIDDLPTTFSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 158 MSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNS 237
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGL 235
|
250
....*....|....*....
gi 522049469 238 AYELFNHPHHPYTAALLSA 256
Cdd:PRK11701 236 TDQVLDDPQHPYTQLLVSS 254
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2-261 |
1.10e-36 |
|
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: 132.62 E-value: 1.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 2 SLLSVRNLSVAFPT-----QNGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQAritcDELVLDGKNLL 76
Cdd:TIGR02769 1 SLLEVRDVTHTYRTgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQ----GTVSFRGQDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 77 QLTATERRRLNGgTVAMIFQEPMTSLNPCFTVGYQIDEAVKTHVGGGRKERKEQVLSLLESVGIPDpaRRYDAYPHQMSG 156
Cdd:TIGR02769 77 QLDRKQRRAFRR-DVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRS--EDADKLPRQLSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 157 GMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKN 236
Cdd:TIGR02769 154 GQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEEC 233
|
250 260
....*....|....*....|....*...
gi 522049469 237 SAYELFNHPH---HPYTAALLSALPERA 261
Cdd:TIGR02769 234 DVAQLLSFKHpagRNLQSAVLPEHPVRR 261
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-245 |
1.29e-36 |
|
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: 131.30 E-value: 1.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPTQNgwfQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQA-RITcdelvLDGKNLLQLTATE 82
Cdd:COG1122 1 IELENLSFSYPGGT---PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSgEVL-----VDGKDITKKNLRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 RRRlnggTVAMIFQEPMTslnpcftvgyQIdeaVKTHV-----------GGGRKERKEQVLSLLESVGIPDPARRYdayP 151
Cdd:COG1122 73 LRR----KVGLVFQNPDD----------QL---FAPTVeedvafgpenlGLPREEIRERVEEALELVGLEHLADRP---P 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 152 HQMSGGMSQRAMIAMALAGQPKLLIADEPTTALD--------VTVQAqilelllklQQQFQMGLILITHDMGVVAETAQQ 223
Cdd:COG1122 133 HELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDprgrrellELLKR---------LNKEGKTVIIVTHDLDLVAELADR 203
|
250 260
....*....|....*....|..
gi 522049469 224 VVVQYAGQQVEKNSAYELFNHP 245
Cdd:COG1122 204 VIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-225 |
7.27e-36 |
|
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: 128.80 E-value: 7.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSvAMLALMNLL-PPQA-RITCDELVL--DGKNLLQLt 79
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKS-TLLRCINLLeEPDSgTIIIDGLKLtdDKKNINEL- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 80 ateRRRlnggtVAMIFQepmtSLN--PCFTVGYQIDEAVKTHVGGGRKERKEQVLSLLESVGIPDPArryDAYPHQMSGG 157
Cdd:cd03262 75 ---RQK-----VGMVFQ----QFNlfPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKA---DAYPAQLSGG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522049469 158 MSQRAMIAMALAGQPKLLIADEPTTALD---------VTVQAqilelllklqQQFQMGLILITHDMGVVAETAQQVV 225
Cdd:cd03262 140 QQQRVAIARALAMNPKVMLFDEPTSALDpelvgevldVMKDL----------AEEGMTMVVVTHEMGFAREVADRVI 206
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-241 |
8.23e-36 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 129.41 E-value: 8.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQA-RITcdelvLDGKNLLQLTATE 82
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSgEVR-----VLGEDVARDPAEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 RRRlnggtVAMIFQEPmtSLNPCFTVgYQIDEAVKTHVGGGRKERKEQVLSLLESVGIPDPARRYdayPHQMSGGMSQRA 162
Cdd:COG1131 72 RRR-----IGYVPQEP--ALYPDLTV-RENLRFFARLYGLPRKEARERIDELLELFGLTDAADRK---VGTLSGGMKQRL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522049469 163 MIAMALAGQPKLLIADEPTTALDVtVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYEL 241
Cdd:COG1131 141 GLALALLHDPELLILDEPTSGLDP-EARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
23-182 |
2.18e-35 |
|
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: 125.45 E-value: 2.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 23 VEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQAritcDELVLDGKNLLQLTATERRRlnggTVAMIFQEPmtSL 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTE----GTILLDGQDLTDDERKSLRK----EIGYVFQDP--QL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 103 NPCFTVGYQIDEAVKTHvGGGRKERKEQVLSLLESVGIPD-PARRYDAYPHQMSGGMSQRAMIAMALAGQPKLLIADEPT 181
Cdd:pfam00005 71 FPRLTVRENLRLGLLLK-GLSKREKDARAEEALEKLGLGDlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
.
gi 522049469 182 T 182
Cdd:pfam00005 150 A 150
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-226 |
4.17e-35 |
|
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: 126.81 E-value: 4.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 5 SVRNLSVAFPTQNGwfQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQA-RITcdelvLDGKNLLQLTATER 83
Cdd:cd03225 1 ELKNLSFSYPDGAR--PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSgEVL-----VDGKDLTKLSLKEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 84 RRlnggTVAMIFQEPMTSL-NPcfTVGyqiDE---AVKtHVGGGRKERKEQVLSLLESVGIPDPArryDAYPHQMSGGMS 159
Cdd:cd03225 74 RR----KVGLVFQNPDDQFfGP--TVE---EEvafGLE-NLGLPEEEIEERVEEALELVGLEGLR---DRSPFTLSGGQK 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522049469 160 QRAMIAMALAGQPKLLIADEPTTALDvTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVV 226
Cdd:cd03225 141 QRVAIAGVLAMDPDILLLDEPTAGLD-PAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIV 206
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
2-256 |
1.21e-34 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 127.21 E-value: 1.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 2 SLLSVRNLSVAFPTQNGWF-----QAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPqariTCDELVLDGKNLL 76
Cdd:PRK15112 3 TLLEVRNLSKTFRYRTGWFrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEP----TSGELLIDDHPLH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 77 QLTATERRRlnggTVAMIFQEPMTSLNPCFTVGYQIDEAVKTHVGGGRKERKEQVLSLLESVGI-PDPArryDAYPHQMS 155
Cdd:PRK15112 79 FGDYSYRSQ----RIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLlPDHA---SYYPHMLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 156 GGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEK 235
Cdd:PRK15112 152 PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVER 231
|
250 260
....*....|....*....|.
gi 522049469 236 NSAYELFNHPHHPYTAALLSA 256
Cdd:PRK15112 232 GSTADVLASPLHELTKRLIAG 252
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-234 |
4.65e-34 |
|
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: 124.60 E-value: 4.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSV--AMLALMNLLPPQARITcDELVLDGKNL--LQLT 79
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTllRLLNRLNDLIPGAPDE-GEVLLDGKDIydLDVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 80 ATERRRlnggTVAMIFQEPmtslNPcF--TVGYQIDEAVKTHVGGGRKERKEQVLSLLESVGIPDPARRyDAYPHQMSGG 157
Cdd:cd03260 76 VLELRR----RVGMVFQKP----NP-FpgSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKD-RLHALGLSGG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522049469 158 MSQRAMIAMALAGQPKLLIADEPTTALDVTvqAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVE 234
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPI--STAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVE 220
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-250 |
2.80e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 123.10 E-value: 2.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MSLLSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNL--LPPQARITcDELVLDGKNLLQL 78
Cdd:PRK14247 1 MNKIEIRDLKVSF----GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEARVS-GEVYLDGQDIFKM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 79 TATERRRlnggTVAMIFQEPmtslNPC--------FTVGYQIDEAVKThvgggRKERKEQVLSLLESVGIPDPAR-RYDA 149
Cdd:PRK14247 76 DVIELRR----RVQMVFQIP----NPIpnlsifenVALGLKLNRLVKS-----KKELQERVRWALEKAQLWDEVKdRLDA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 150 YPHQMSGGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAqiLELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYA 229
Cdd:PRK14247 143 PAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTA--KIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYK 220
|
250 260
....*....|....*....|.
gi 522049469 230 GQQVEKNSAYELFNHPHHPYT 250
Cdd:PRK14247 221 GQIVEWGPTREVFTNPRHELT 241
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-226 |
3.85e-33 |
|
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: 121.47 E-value: 3.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPqariTCDELVLDGKNLLQLTATER 83
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERP----DSGEILIDGRDVTGVPPERR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 84 RrlnggtVAMIFQEPmtSLNPCFTVGYQIDEAVKtHVGGGRKERKEQVLSLLESVGIPDPARRYdayPHQMSGGMSQRAM 163
Cdd:cd03259 73 N------IGMVFQDY--ALFPHLTVAENIAFGLK-LRGVPKAEIRARVRELLELVGLEGLLNRY---PHELSGGQQQRVA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522049469 164 IAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVV 226
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAV 203
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-226 |
7.16e-33 |
|
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: 122.07 E-value: 7.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFPTQngwfQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQA-RITcdelvLDGKNLLQLTAT 81
Cdd:COG1120 1 MLEAENLSVGYGGR----PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSgEVL-----LDGRDLASLSRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 82 ERRRLnggtVAMIFQEPMTSLNpcFTVGyqidEAVKT----HVGGGRKERKE---QVLSLLESVGIPDPA-RRYDayphQ 153
Cdd:COG1120 72 ELARR----IAYVPQEPPAPFG--LTVR----ELVALgrypHLGLFGRPSAEdreAVEEALERTGLEHLAdRPVD----E 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522049469 154 MSGGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVV 226
Cdd:COG1120 138 LSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVL 210
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-256 |
8.30e-33 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 121.64 E-value: 8.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPtqnGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPqariTCDELVLDGKNLLQLTATER 83
Cdd:cd03295 1 IEFENVTKRYG---GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEP----TSGEIFIDGEDIREQDPVEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 84 RRlnggTVAMIFQEpmTSLNPCFTVGYQIdEAVKTHVGGGRKERKEQVLSLLESVGIPdPARRYDAYPHQMSGGMSQRAM 163
Cdd:cd03295 74 RR----KIGYVIQQ--IGLFPHMTVEENI-ALVPKLLKWPKEKIRERADELLALVGLD-PAEFADRYPHELSGGQQQRVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 164 IAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYELFN 243
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
250
....*....|...
gi 522049469 244 HPHHPYTAALLSA 256
Cdd:cd03295 226 SPANDFVAEFVGA 238
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-255 |
3.53e-31 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 117.54 E-value: 3.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MSLLSVRNLSVAFPTQngwfQAVEGINLTVNPNEILAIVGESGSGKSvAMLALMNLL--PPQARITCDELVLDGKNLLQL 78
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQ----TVLHGIDLEVKPGEVVAIIGPSGSGKT-TLLRCINLLeqPEAGTIRVGDITIDTARSLSQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 79 TATERRRLNGgTVAMIFQEpmTSLNPCFTVGYQIDEAVKTHVGGGRKERKEQVLSLLESVGIpdpARRYDAYPHQMSGGM 158
Cdd:PRK11264 76 QKGLIRQLRQ-HVGFVFQN--FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGL---AGKETSYPRRLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 159 SQRAMIAMALAGQPKLLIADEPTTALD--------VTVQAQILELLLklqqqfqmgLILITHDMGVVAETAQQVVVQYAG 230
Cdd:PRK11264 150 QQRVAIARALAMRPEVILFDEPTSALDpelvgevlNTIRQLAQEKRT---------MVIVTHEMSFARDVADRAIFMDQG 220
|
250 260
....*....|....*....|....*
gi 522049469 231 QQVEKNSAYELFNHPHHPYTAALLS 255
Cdd:PRK11264 221 RIVEQGPAKALFADPQQPRTRQFLE 245
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-254 |
1.18e-30 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 118.33 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MSLlSVRNLSVAFPTqngwFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQA-RItcdelVLDGKNLL-QL 78
Cdd:COG1118 1 MSI-EVRNISKRFGS----FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSgRI-----VLNGRDLFtNL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 79 TATERRrlnggtVAMIFQEPMtsLNPCFTVGyqidEAVK---THVGGGRKERKEQVLSLLESVGIPDPARRYdayPHQMS 155
Cdd:COG1118 71 PPRERR------VGFVFQHYA--LFPHMTVA----ENIAfglRVRPPSKAEIRARVEELLELVQLEGLADRY---PSQLS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 156 GGMSQRAMIAMALAGQPKLLIADEPTTALD-------------------VTVqaqilelllklqqqfqmglILITHDMGV 216
Cdd:COG1118 136 GGQRQRVALARALAVEPEVLLLDEPFGALDakvrkelrrwlrrlhdelgGTT-------------------VFVTHDQEE 196
|
250 260 270
....*....|....*....|....*....|....*...
gi 522049469 217 VAETAQQVVVQYAGQQVEKNSAYELFNHPHHPYTAALL 254
Cdd:COG1118 197 ALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFL 234
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-251 |
1.80e-30 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 117.89 E-value: 1.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MSLLSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQA-RITcdelvLDGKNLLQLT 79
Cdd:COG3842 3 MPALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSgRIL-----LDGRDVTGLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 80 AtERRRlnggtVAMIFQEP-----MTSL-NpcftVGY--QIDeavkthvGGGRKERKEQVLSLLESVGIPDPARRYdayP 151
Cdd:COG3842 74 P-EKRN-----VGMVFQDYalfphLTVAeN----VAFglRMR-------GVPKAEIRARVAELLELVGLEGLADRY---P 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 152 HQMSGGMSQRAMIAMALAGQPKLLIADEPTTALD-------------------VTVqaqilelllklqqqfqmglILITH 212
Cdd:COG3842 134 HQLSGGQQQRVALARALAPEPRVLLLDEPLSALDaklreemreelrrlqrelgITF-------------------IYVTH 194
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 522049469 213 D------MgvvaetAQQVVVQYAGQQVEKNSAYELFNHPHHPYTA 251
Cdd:COG3842 195 DqeealaL------ADRIAVMNDGRIEQVGTPEEIYERPATRFVA 233
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
20-263 |
5.42e-30 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 114.86 E-value: 5.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 20 FQAVEGINLTVNPNEILAIVGESGSGKSvAMLALMN-LLPPQA-RITCDELVL---DGKNLLQLtateRRRlnggtVAMI 94
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKS-TLIQHLNgLLKPTSgTVTIDGRDItakKKKKLKDL----RKK-----VGLV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 95 FQEPMtslnpcftvgYQI-DEAVKTHVGGG-------RKERKEQVLSLLESVGIPDPArrYDAYPHQMSGGMSQRAMIAM 166
Cdd:TIGR04521 88 FQFPE----------HQLfEETVYKDIAFGpknlglsEEEAEERVKEALELVGLDEEY--LERSPFELSGGQMRRVAIAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 167 ALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYELFNHP- 245
Cdd:TIGR04521 156 VLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVd 235
|
250 260
....*....|....*....|....*
gi 522049469 246 ----HH---PYTAALLSALPERALP 263
Cdd:TIGR04521 236 elekIGldvPEITELARKLKEKGLP 260
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-231 |
1.09e-29 |
|
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: 113.30 E-value: 1.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSvamlALMNLLPPQARITCDELVLDGKNLLQLTATER 83
Cdd:cd03219 1 LEVRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKT----TLFNLISGFLRPTSGSVLFDGEDITGLPPHEI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 84 RRLngGtVAMIFQepMTSLNPCFTV------GYQIDEAVKTHVGGGRKERK---EQVLSLLESVGIpdpARRYDAYPHQM 154
Cdd:cd03219 73 ARL--G-IGRTFQ--IPRLFPELTVlenvmvAAQARTGSGLLLARARREERearERAEELLERVGL---ADLADRPAGEL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522049469 155 SGGMSQRAMIAMALAGQPKLLIADEPTTALDVTvQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQ 231
Cdd:cd03219 145 SYGQQRRLEIARALATDPKLLLLDEPAAGLNPE-ETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGR 220
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-226 |
1.23e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 113.26 E-value: 1.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MSLLSVRNLSVAFPTQngwfQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQA-RITcdelvLDGKNLlqlt 79
Cdd:COG1121 4 MPAIELENLTVSYGGR----PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSgTVR-----LFGKPP---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 80 ATERRRlnggtVAMIFQepMTSLNPCF--TVGyqidEAVKT----HVG---GGRKERKEQVLSLLESVGIPDPARRyday 150
Cdd:COG1121 71 RRARRR-----IGYVPQ--RAEVDWDFpiTVR----DVVLMgrygRRGlfrRPSRADREAVDEALERVGLEDLADR---- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 151 P-HQMSGGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAqilelllklqqqFQMGL-----------ILITHDMGVVA 218
Cdd:COG1121 136 PiGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEE------------ALYELlrelrregktiLVVTHDLGAVR 203
|
....*...
gi 522049469 219 ETAQQVVV 226
Cdd:COG1121 204 EYFDRVLL 211
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-234 |
1.42e-29 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 112.91 E-value: 1.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 2 SLLSVRNLSVAFPTQNGWFQAVEGINLTVNPNEILAIVGESGSGKSvAMLALM-NLLPPqariTCDELVLDGKNLLQLTA 80
Cdd:COG4181 7 PIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKS-TLLGLLaGLDRP----TSGTVRLAGQDLFALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 81 TERRRLNGGTVAMIFQE----P-MTSL-NpcftVGYQIDEAvkthvggGRKERKEQVLSLLESVGIpdpARRYDAYPHQM 154
Cdd:COG4181 82 DARARLRARHVGFVFQSfqllPtLTALeN----VMLPLELA-------GRRDARARARALLERVGL---GHRLDHYPAQL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 155 SGGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQyAGQQVE 234
Cdd:COG4181 148 SGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLR-AGRLVE 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-231 |
2.15e-29 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 111.45 E-value: 2.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPTQNGWfqavEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQAritcDELVLDGKNLLQLTATE- 82
Cdd:COG4619 1 LELEGLSFRVGGKPIL----SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTS----GEIYLDGKPLSAMPPPEw 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 RRRlnggtVAMIFQEPmtslnpcftvgYQIDEAVKTHV-----GGGRKERKEQVLSLLESVGIPDPARRYDAypHQMSGG 157
Cdd:COG4619 73 RRQ-----VAYVPQEP-----------ALWGGTVRDNLpfpfqLRERKFDRERALELLERLGLPPDILDKPV--ERLSGG 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522049469 158 MSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQ 231
Cdd:COG4619 135 ERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
7-245 |
5.70e-29 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 111.34 E-value: 5.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 7 RNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSvAMLALMNLLPPqarITCDELVLDGKNLLQLTATERR-R 85
Cdd:PRK09493 5 KNVSKHF----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKS-TLLRCINKLEE---ITSGDLIVDGLKVNDPKVDERLiR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 86 LNGGtvaMIFQE----P-MTSL-NPCFTvgyqideavKTHV-GGGRKERKEQVLSLLESVGIpdpARRYDAYPHQMSGGM 158
Cdd:PRK09493 77 QEAG---MVFQQfylfPhLTALeNVMFG---------PLRVrGASKEEAEKQARELLAKVGL---AERAHHYPSELSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 159 SQRAMIAMALAGQPKLLIADEPTTALDVTVQaQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSA 238
Cdd:PRK09493 142 QQRVAIARALAVKPKLMLFDEPTSALDPELR-HEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDP 220
|
....*..
gi 522049469 239 YELFNHP 245
Cdd:PRK09493 221 QVLIKNP 227
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-185 |
1.13e-28 |
|
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: 110.74 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPtqnGWFQAVEGINLTVNPNEILAIVGESGSGKSvAMLALMNLLppqARITCDELVLDGKNLLQLTATER 83
Cdd:cd03256 1 IEVENLSKTYP---NGKKALKDVSLSINPGEFVALIGPSGAGKS-TLLRCLNGL---VEPTSGSVLIDGTDINKLKGKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 84 RRLNGgTVAMIFQEPmtSLNPCFTVGyqideavkTHVGGGR---------------KERKEQVLSLLESVGIPDPA-RRY 147
Cdd:cd03256 74 RQLRR-QIGMIFQQF--NLIERLSVL--------ENVLSGRlgrrstwrslfglfpKEEKQRALAALERVGLLDKAyQRA 142
|
170 180 190
....*....|....*....|....*....|....*...
gi 522049469 148 DayphQMSGGMSQRAMIAMALAGQPKLLIADEPTTALD 185
Cdd:cd03256 143 D----QLSGGQQQRVAIARALMQQPKLILADEPVASLD 176
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
4-185 |
1.45e-28 |
|
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: 109.72 E-value: 1.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPTQNGWFQAVEGINLTVNPNEILAIVGESGSGKSVaMLALMNLL-PPQAritcDELVLDGKNLLQLTATE 82
Cdd:TIGR02982 2 ISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTT-LLTLIGGLrSVQE----GSLKVLGQELHGASKKQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 R---RRLNGgtvaMIFQEpmTSLNPCFTVGYQIDEAVKTHVGGGRKERKEQVLSLLESVGIPDparRYDAYPHQMSGGMS 159
Cdd:TIGR02982 77 LvqlRRRIG----YIFQA--HNLLGFLTARQNVQMALELQPNLSYQEARERARAMLEAVGLGD---HLNYYPHNLSGGQK 147
|
170 180
....*....|....*....|....*.
gi 522049469 160 QRAMIAMALAGQPKLLIADEPTTALD 185
Cdd:TIGR02982 148 QRVAIARALVHHPKLVLADEPTAALD 173
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-255 |
1.51e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 110.51 E-value: 1.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLAL--MNLLPPQARITcDELVLDGKNLLQLT-- 79
Cdd:COG1117 12 IEVRNLNVYY----GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIPGARVE-GEILLDGEDIYDPDvd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 80 -ATERRRlnggtVAMIFQEPmtslNPcFT------VGYqideAVKTHVGGGRKERKEQVLSLLESVGIPDPAR-RYDAYP 151
Cdd:COG1117 87 vVELRRR-----VGMVFQKP----NP-FPksiydnVAY----GLRLHGIKSKSELDEIVEESLRKAALWDEVKdRLKKSA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 152 HQMSGGMSQRAMIAMALAGQPKLLIADEPTTALD-----------------VTVqaqilelllklqqqfqmglILITHDM 214
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpistakieelilelkkdYTI-------------------VIVTHNM 213
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 522049469 215 GVVAETAQQVVVQYAGQQVEKNSAYELFNHPHHPYTAALLS 255
Cdd:COG1117 214 QQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTEDYIT 254
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
3-231 |
1.85e-28 |
|
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: 109.36 E-value: 1.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFPTQNGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPqariTCDELVLDGKNLLQLTATE 82
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNP----TSGEVLFNGQSLSKLSSNE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 RRRLNGGTVAMIFQepMTSLNPCFTVGYQIdeAVKTHVGG-GRKERKEQVLSLLESVGIPDparRYDAYPHQMSGGMSQR 161
Cdd:TIGR02211 77 RAKLRNKKLGFIYQ--FHHLLPDFTALENV--AMPLLIGKkSVKEAKERAYEMLEKVGLEH---RINHRPSELSGGERQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 162 AMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGvVAETAQQVVVQYAGQ 231
Cdd:TIGR02211 150 VAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLE-LAKKLDRVLEMKDGQ 218
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-225 |
5.08e-28 |
|
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: 108.00 E-value: 5.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 5 SVRNLSVAFPTQNgwfqAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPP-QARITcdelvLDGKNLlqltATER 83
Cdd:cd03235 1 EVEDLTVSYGGHP----VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPtSGSIR-----VFGKPL----EKER 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 84 RRLngGTVAMIFqepmtSLNPCFTVgyQIDEAVKT----HVGGGR---KERKEQVLSLLESVGIPDPA-RRYDayphQMS 155
Cdd:cd03235 68 KRI--GYVPQRR-----SIDRDFPI--SVRDVVLMglygHKGLFRrlsKADKAKVDEALERVGLSELAdRQIG----ELS 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 156 GGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAqILELLLKLQQQFQMGLILITHDMGVVAETAQQVV 225
Cdd:cd03235 135 GGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQE-DIYELLRELRREGMTILVVTHDLGLVLEYFDRVL 203
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-274 |
1.16e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 108.95 E-value: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 2 SLLSVRNLSVAFPTQNGwfQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQA-RITCDELVLDGKNLLQLta 80
Cdd:PRK13635 4 EIIRVEHISFRYPDAAT--YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAgTITVGGMVLSEETVWDV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 81 teRRRlnggtVAMIFQEPMTSLnpcftVGYQIDEAVK---THVGGGRKERKEQVLSLLESVGIPDPARRYdayPHQMSGG 157
Cdd:PRK13635 80 --RRQ-----VGMVFQNPDNQF-----VGATVQDDVAfglENIGVPREEMVERVDQALRQVGMEDFLNRE---PHRLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 158 MSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAEtAQQVVVQYAGQQVEKNS 237
Cdd:PRK13635 145 QKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGT 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 522049469 238 AYELFNHPHH--------PYTAALLSALPER--ALPTGLLpTIPGLV 274
Cdd:PRK13635 224 PEEIFKSGHMlqeigldvPFSVKLKELLKRNgiLLPNTYL-TMESLV 269
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-226 |
1.45e-27 |
|
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: 105.98 E-value: 1.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 5 SVRNLSVAFPTQngwfQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQAritcDELVLDGKNLLQLTATERR 84
Cdd:cd03214 1 EVENLSVGYGGR----TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSS----GEILLDGKDLASLSPKELA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 85 RLnggtvamifqepmtslnpcftVGYqideavkthvgggrkerkeqVLSLLESVGIPDPA-RRYDayphQMSGGMSQRAM 163
Cdd:cd03214 73 RK---------------------IAY--------------------VPQALELLGLAHLAdRPFN----ELSGGERQRVL 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522049469 164 IAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVV 226
Cdd:cd03214 108 LARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVIL 170
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-274 |
1.22e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 108.00 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFPTQNgwfqAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPqariTCDELVLDGKNLLQLTATE 82
Cdd:PRK11607 19 LLEIRNLTKSFDGQH----AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQP----TAGQIMLDGVDLSHVPPYQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 RrrlnggTVAMIFQEpmTSLNPCFTVGYQIDEAVKTHvGGGRKERKEQVLSLLESVGIPDPARRYdayPHQMSGGMSQRA 162
Cdd:PRK11607 91 R------PINMMFQS--YALFPHMTVEQNIAFGLKQD-KLPKAEIASRVNEMLGLVHMQEFAKRK---PHQLSGGQRQRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 163 MIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYELF 242
Cdd:PRK11607 159 ALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY 238
|
250 260 270
....*....|....*....|....*....|....*....
gi 522049469 243 NHPHHPYTAALLSA-------LPERaLPTGLLPTIPGLV 274
Cdd:PRK11607 239 EHPTTRYSAEFIGSvnvfegvLKER-QEDGLVIDSPGLV 276
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-231 |
1.50e-26 |
|
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: 102.32 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 5 SVRNLSVAFPTQngwfQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPqariTCDELVLDGKNLLQLTATERR 84
Cdd:cd00267 1 EIENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKP----TSGEILIDGKDIAKLPLEELR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 85 RLnggtVAMIFQepmtslnpcftvgyqideavkthvgggrkerkeqvlsllesvgipdparrydayphqMSGGMSQRAMI 164
Cdd:cd00267 73 RR----IGYVPQ---------------------------------------------------------LSGGQRQRVAL 91
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522049469 165 AMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMgLILITHDMGVVAETAQQVVVQYAGQ 231
Cdd:cd00267 92 ARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRT-VIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-245 |
2.35e-26 |
|
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: 104.24 E-value: 2.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSvamlALMNLLPPQARITCDELVLDGKNLLQLTATER 83
Cdd:cd03300 1 IELENVSKFY----GGFVALDGVSLDIKEGEFFTLLGPSGCGKT----TLLRLIAGFETPTSGEILLDGKDITNLPPHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 84 RrlnggtVAMIFQEpmTSLNPCFTVGYQIDEAVKTHvGGGRKERKEQVLSLLESVGIPDPARRYdayPHQMSGGMSQRAM 163
Cdd:cd03300 73 P------VNTVFQN--YALFPHLTVFENIAFGLRLK-KLPKAEIKERVAEALDLVQLEGYANRK---PSQLSGGQQQRVA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 164 IAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYELFN 243
Cdd:cd03300 141 IARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
..
gi 522049469 244 HP 245
Cdd:cd03300 221 EP 222
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
22-252 |
2.69e-26 |
|
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: 105.03 E-value: 2.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 22 AVEGINLTVNPNEILAIVGESGSGKSVaMLALMN-LLPPqariTCDELVLDGKNLLQLTATERRRLNGGTVAMIFQE--- 97
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKST-LLRCINrLIEP----TSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSfal 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 98 -P-MTSL-NPCFTVGYQideavkthvGGGRKERKEQVLSLLESVGIPDPArryDAYPHQMSGGMSQRAMIAMALAGQPKL 174
Cdd:cd03294 114 lPhRTVLeNVAFGLEVQ---------GVPRAEREERAAEALELVGLEGWE---HKYPDELSGGMQQRVGLARALAVDPDI 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522049469 175 LIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYELFNHPHHPYTAA 252
Cdd:cd03294 182 LLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVRE 259
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-185 |
6.31e-26 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 102.56 E-value: 6.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPTQngwfQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQARITcDELVLDGKNLLQLtATER 83
Cdd:COG4136 2 LSLENLTITLGGR----PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSAS-GEVLLNGRRLTAL-PAEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 84 RRlnggtVAMIFQEPMtsLNPCFTVGYQIDEAVKTHVGggRKERKEQVLSLLESVGIPDparRYDAYPHQMSGGmsQRAM 163
Cdd:COG4136 76 RR-----IGILFQDDL--LFPHLSVGENLAFALPPTIG--RAQRRARVEQALEEAGLAG---FADRDPATLSGG--QRAR 141
|
170 180
....*....|....*....|....
gi 522049469 164 IAM--ALAGQPKLLIADEPTTALD 185
Cdd:COG4136 142 VALlrALLAEPRALLLDEPFSKLD 165
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
7-185 |
6.74e-26 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 102.82 E-value: 6.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 7 RNLSVAFPTQNgwfQAVEGINLTVNPNEILAIVGESGSGKSVamlaLMNLLPPQARITCDELVLDGKNLLQLTATE---- 82
Cdd:COG2884 5 ENVSKRYPGGR---EALSDVSLEIEKGEFVFLTGPSGAGKST----LLKLLYGEERPTSGQVLVNGQDLSRLKRREipyl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 RRRLngGtvaMIFQEpmtslnpcF------TVGYQIdeAVKTHVGG-GRKERKEQVLSLLESVGIPDparRYDAYPHQMS 155
Cdd:COG2884 78 RRRI--G---VVFQD--------FrllpdrTVYENV--ALPLRVTGkSRKEIRRRVREVLDLVGLSD---KAKALPHELS 139
|
170 180 190
....*....|....*....|....*....|
gi 522049469 156 GGMSQRAMIAMALAGQPKLLIADEPTTALD 185
Cdd:COG2884 140 GGEQQRVAIARALVNRPELLLADEPTGNLD 169
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
4-251 |
9.16e-26 |
|
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: 105.12 E-value: 9.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLlppqARITCDELVLDGKNLLQLTATER 83
Cdd:TIGR03265 5 LSIDNIRKRF----GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGL----ERQTAGTIYQGGRDITRLPPQKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 84 rrlnggTVAMIFQEpmTSLNPCFTVGYQIDEAVKTHvGGGRKERKEQVLSLLESVGIPDPARRYdayPHQMSGGMSQRAM 163
Cdd:TIGR03265 77 ------DYGIVFQS--YALFPNLTVADNIAYGLKNR-GMGRAEVAERVAELLDLVGLPGSERKY---PGQLSGGQQQRVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 164 IAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYELFN 243
Cdd:TIGR03265 145 LARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYR 224
|
....*...
gi 522049469 244 HPHHPYTA 251
Cdd:TIGR03265 225 HPATPFVA 232
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
16-256 |
1.11e-25 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 102.57 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 16 QNGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNL-LPPQARITcdelvLDGKNLLQLTATERRrlnggtVAMI 94
Cdd:TIGR00968 9 RFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLeQPDSGRIR-----LNGQDATRVHARDRK------IGFV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 95 FQEpmTSLNPCFTVGYQIDEA--VKTHVGGGRKERKEQVLSLLESVGIPDparrydAYPHQMSGGMSQRAMIAMALAGQP 172
Cdd:TIGR00968 78 FQH--YALFKHLTVRDNIAFGleIRKHPKAKIKARVEELLELVQLEGLGD------RYPNQLSGGQRQRVALARALAVEP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 173 KLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYELFNHPHHPYTAA 252
Cdd:TIGR00968 150 QVLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMS 229
|
....
gi 522049469 253 LLSA 256
Cdd:TIGR00968 230 FLGE 233
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-226 |
1.20e-25 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 102.81 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MSLLSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSvamlALMNLL----PPQA-RITcdelvLDGKNL 75
Cdd:COG0411 2 DPLLEVRGLTKRF----GGLVAVDDVSLEVERGEIVGLIGPNGAGKT----TLFNLItgfyRPTSgRIL-----FDGRDI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 76 LQLTATERRRLngGtVAMIFQepMTSLNPCFTV------------GYQIDEAVKTHVGGGRKERK--EQVLSLLESVGIp 141
Cdd:COG0411 69 TGLPPHRIARL--G-IARTFQ--NPRLFPELTVlenvlvaaharlGRGLLAALLRLPRARREEREarERAEELLERVGL- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 142 dpARRYDAYPHQMSGGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETA 221
Cdd:COG0411 143 --ADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLA 220
|
....*
gi 522049469 222 QQVVV 226
Cdd:COG0411 221 DRIVV 225
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-241 |
3.67e-25 |
|
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: 101.09 E-value: 3.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQAritcDELVLDGKNLLQLTATE 82
Cdd:COG4555 1 MIEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDS----GSILIDGEDVRKEPREA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 RRRLnggtvAMIFQEPMtsLNPCFTVGYQIDEAVKTHvGGGRKERKEQVLSLLESVGIPDPA-RRYdaypHQMSGGMSQR 161
Cdd:COG4555 73 RRQI-----GVLPDERG--LYDRLTVRENIRYFAELY-GLFDEELKKRIEELIELLGLEEFLdRRV----GELSTGMKKK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 162 AMIAMALAGQPKLLIADEPTTALDVTvqAQILELLLKLQQQFQMGLILI-THDMGVVAETAQQVVVQYAGQQVEKNSAYE 240
Cdd:COG4555 141 VALARALVHDPKVLLLDEPTNGLDVM--ARRLLREILRALKKEGKTVLFsSHIMQEVEALCDRVVILHKGKVVAQGSLDE 218
|
.
gi 522049469 241 L 241
Cdd:COG4555 219 L 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-231 |
7.25e-25 |
|
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: 98.62 E-value: 7.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPTqngwFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQAritcDELVLDGKNLLQLTATER 83
Cdd:cd03230 1 IEVRNLSKRYGK----KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDS----GEIKVLGKDIKKEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 84 RRlnggtVAMIFQEPmtSLNPCFTVgyqideavkthvgggrkerkEQVLSLlesvgipdparrydayphqmSGGMSQRAM 163
Cdd:cd03230 73 RR-----IGYLPEEP--SLYENLTV--------------------RENLKL--------------------SGGMKQRLA 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522049469 164 IAMALAGQPKLLIADEPTTALDVTVQAqILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQ 231
Cdd:cd03230 106 LAQALLHDPELLILDEPTSGLDPESRR-EFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
18-241 |
8.20e-25 |
|
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: 99.75 E-value: 8.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 18 GWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPqariTCDELVLDGKNLLQLTATERRRlnggtVAMIFQE 97
Cdd:cd03265 11 GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKP----TSGRATVAGHDVVREPREVRRR-----IGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 98 PmtSLNPCFTvGYQIDEAVKTHVGGGRKERKEQVLSLLESVGIPDPARRYDAYphqMSGGMSQRAMIAMALAGQPKLLIA 177
Cdd:cd03265 82 L--SVDDELT-GWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKT---YSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522049469 178 DEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYEL 241
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-185 |
8.67e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 100.71 E-value: 8.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MSLLSVRNLSVAFPTQNGWFQAVEGINLTVNPNEILAIVGESGSGKSvamlALMNLL-----PPQARITcdelvLDGKnl 75
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKT----TLLNLIagflaPSSGEIT-----LDGV-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 76 lQLTATerrrlnGGTVAMIFQEpmTSLNPCFTV------GYQIDeavkthvGGGRKERKEQVLSLLESVGIPDPARRYda 149
Cdd:COG4525 70 -PVTGP------GADRGVVFQK--DALLPWLNVldnvafGLRLR-------GVPKAERRARAEELLALVGLADFARRR-- 131
|
170 180 190
....*....|....*....|....*....|....*.
gi 522049469 150 yPHQMSGGMSQRAMIAMALAGQPKLLIADEPTTALD 185
Cdd:COG4525 132 -IWQLSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-231 |
1.18e-24 |
|
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: 98.03 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPqariTCDELVLDGKNL---LQLTA 80
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEP----DSGSILIDGEDLtdlEDELP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 81 TERRRlnggtVAMIFQEPmtSLNPCFTVgyqideavkthvgggrkerkeqvlslLESVGIPdparrydayphqMSGGMSQ 160
Cdd:cd03229 73 PLRRR-----IGMVFQDF--ALFPHLTV--------------------------LENIALG------------LSGGQQQ 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522049469 161 RAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQ 231
Cdd:cd03229 108 RVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-256 |
1.38e-24 |
|
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: 99.33 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFptqnGWFQaVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQAritcDELVLDGKNLLQLTATER 83
Cdd:cd03299 1 LKVENLSKDW----KEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDS----GKILLNGKDITNLPPEKR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 84 RrlnggtVAMIFQEpmTSLNPCFTVGYQIDEAVKtHVGGGRKERKEQVLSLLESVGIpdpARRYDAYPHQMSGGMSQRAM 163
Cdd:cd03299 72 D------ISYVPQN--YALFPHMTVYKNIAYGLK-KRKVDKKEIERKVLEIAEMLGI---DHLLNRKPETLSGGEQQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 164 IAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYELFN 243
Cdd:cd03299 140 IARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFK 219
|
250
....*....|...
gi 522049469 244 HPHHPYTAALLSA 256
Cdd:cd03299 220 KPKNEFVAEFLGF 232
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
18-255 |
1.67e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 99.32 E-value: 1.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 18 GWFQAVEGINLTVNPNEILAIVGESGSGKSvAMLALMNLLP-PQAritcDELVLDGK--NLLQLTATERRRLNGGTVAMI 94
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKS-SLLRVLNLLEtPDS----GQLNIAGHqfDFSQKPSEKAIRLLRQKVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 95 FQEpmTSLNPCFTVGYQIDEAVKTHVGGGRKERKEQVLSLLESVGIPDPArryDAYPHQMSGGMSQRAMIAMALAGQPKL 174
Cdd:COG4161 88 FQQ--YNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKA---DRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 175 LIADEPTTALD--VTVQAqilelLLKLQQQFQMGL--ILITHDMGVVAETAQQVVVQYAGQQVEKNSAyELFNHPHHPYT 250
Cdd:COG4161 163 LLFDEPTAALDpeITAQV-----VEIIRELSQTGItqVIVTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQPQTEAF 236
|
....*
gi 522049469 251 AALLS 255
Cdd:COG4161 237 AHYLS 241
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
233-316 |
1.95e-24 |
|
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: 94.74 E-value: 1.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 233 VEKNSAYELFNHPHHPYTAALLSALPERALPTGLLPTIPGLVPGQHNRPQGCLFAPRCAYQQARCQTEVPALAQQQQG-W 311
Cdd:TIGR01727 3 VETGPAEEIFKNPLHPYTKALLSAIPTIKKRDRKLISIPGEVPSLINLPSGCRFYPRCPYAQDECRKEPPALVEIAEGhR 82
|
....*
gi 522049469 312 IRCFY 316
Cdd:TIGR01727 83 VACHL 87
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
18-255 |
6.43e-24 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 98.12 E-value: 6.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 18 GWFQAVEGINLTVNPNEILAIVGESGSGKSVaMLALMNLL--PPQARITCD----ELVLDGKNLLQLTATERRRLNGGTV 91
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKST-FLRCINFLekPSEGSIVVNgqtiNLVRDKDGQLKVADKNQLRLLRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 92 AMIFQEpmTSLNPCFTVGYQIDEAVKTHVGGGRKERKEQVLSLLESVGIPDPARryDAYPHQMSGGMSQRAMIAMALAGQ 171
Cdd:PRK10619 95 TMVFQH--FNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQ--GKYPVHLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 172 PKLLIADEPTTALDVTVQAQILELLLKLQQQFQMgLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYELFNHPHHPYTA 251
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKT-MVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQ 249
|
....
gi 522049469 252 ALLS 255
Cdd:PRK10619 250 QFLK 253
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-226 |
1.11e-23 |
|
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: 95.14 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPTQNGwfQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQA-RITcdelvLDGKNLLQLTATE 82
Cdd:cd03228 1 IEFKNVSFSYPGRPK--PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSgEIL-----IDGVDLRDLDLES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 RRRLnggtVAMIFQEPM---TSLnpcftvgyqideavkthvgggrkerKEQVLsllesvgipdparrydayphqmSGGMS 159
Cdd:cd03228 74 LRKN----IAYVPQDPFlfsGTI-------------------------RENIL----------------------SGGQR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522049469 160 QRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMglILITHDMGVVAEtAQQVVV 226
Cdd:cd03228 103 QRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKGKTV--IVIAHRLSTIRD-ADRIIV 166
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-254 |
1.32e-23 |
|
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: 97.02 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MSLLsVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSvamlALMNLLPPQARITCDELVLDGKNLLQLTA 80
Cdd:cd03296 1 MSIE-VRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKT----TLLRLIAGLERPDSGTILFGGEDATDVPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 81 TERRrlnggtVAMIFQEpmTSLNPCFTVGYQIDEAVKTHVGGGRK---ERKEQVLSLLESVGIPDPARRYdayPHQMSGG 157
Cdd:cd03296 72 QERN------VGFVFQH--YALFRHMTVFDNVAFGLRVKPRSERPpeaEIRAKVHELLKLVQLDWLADRY---PAQLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 158 MSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNS 237
Cdd:cd03296 141 QRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
250
....*....|....*..
gi 522049469 238 AYELFNHPHHPYTAALL 254
Cdd:cd03296 221 PDEVYDHPASPFVYSFL 237
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-250 |
2.99e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 96.65 E-value: 2.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 23 VEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPP-QARITCDELVLD-GKNLLQLTATERRRlnggTVAMIFQEPmt 100
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIyDSKIKVDGKVLYfGKDIFQIDAIKLRK----EVGMVFQQP-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 101 SLNPCFTVGYQIDEAVKTHVGGGRKERKEQVLSLLESVGI-PDPARRYDAYPHQMSGGMSQRAMIAMALAGQPKLLIADE 179
Cdd:PRK14246 100 NPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522049469 180 PTTALDVTvqAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYELFNHPHHPYT 250
Cdd:PRK14246 180 PTSMIDIV--NSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELT 248
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
32-231 |
1.19e-22 |
|
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: 93.90 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 32 PNEILAIVGESGSGKSVAMLALMNLL-PPQARITCDELVL-DGKNLLQLTATERRrlnggtVAMIFQEpmTSLNPCFTVG 109
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEkPDGGTIVLNGTVLfDSRKKINLPPQQRK------IGLVFQQ--YALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 110 YQIDEAVKTHvggGRKERKEQVLSLLESVGIPDPARRYdayPHQMSGGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQ 189
Cdd:cd03297 94 ENLAFGLKRK---RNREDRISVDELLDLLGLDHLLNRY---PAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 522049469 190 AQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQ 231
Cdd:cd03297 168 LQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
16-275 |
1.65e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 96.64 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 16 QNGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPqariTCDELVLDGKNLLQLTATERRRLNGGTVAMIF 95
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP----TRGQVLIDGVDIAKISDAELREVRRKKIAMVF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 96 QEpmTSLNPCFTVgyQIDEAVKTHVGG-GRKERKEQVLSLLESVGIPDPARrydAYPHQMSGGMSQRAMIAMALAGQPKL 174
Cdd:PRK10070 113 QS--FALMPHMTV--LDNTAFGMELAGiNAEERREKALDALRQVGLENYAH---SYPDELSGGMRQRVGLARALAINPDI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 175 LIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYELFNHPHHPYTAALL 254
Cdd:PRK10070 186 LLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF 265
|
250 260 270
....*....|....*....|....*....|.
gi 522049469 255 SALP----------ERALPTGLLPTIPGLVP 275
Cdd:PRK10070 266 RGVDisqvfsakdiARRTPNGLIRKTPGFGP 296
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
21-255 |
3.26e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 93.16 E-value: 3.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 21 QAVEGINLTVNPNEILAIVGESGSGKSvAMLALMNLLP-PQAritcDELVLDGK--NLLQLTATERRRLNGGTVAMIFQE 97
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKS-SLLRVLNLLEmPRS----GTLNIAGNhfDFSKTPSDKAIRELRRNVGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 98 pmTSLNPCFTVGYQIDEAVKTHVGGGRKERKEQVLSLLESVGIPDPArryDAYPHQMSGGMSQRAMIAMALAGQPKLLIA 177
Cdd:PRK11124 91 --YNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYA---DRFPLHLSGGQQQRVAIARALMMEPQVLLF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 178 DEPTTALD--VTVQaqileLLLKLQQQFQMGL--ILITHDMGVVAETAQQVVVQYAGQQVEKNSAyELFNHPHHPYTAAL 253
Cdd:PRK11124 166 DEPTAALDpeITAQ-----IVSIIRELAETGItqVIVTHEVEVARKTASRVVYMENGHIVEQGDA-SCFTQPQTEAFKNY 239
|
..
gi 522049469 254 LS 255
Cdd:PRK11124 240 LS 241
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-186 |
3.26e-22 |
|
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: 92.16 E-value: 3.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQA-RITcdelvLDGKNLLQLTAT 81
Cdd:COG4133 2 MLEAENLSCRR----GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAgEVL-----WNGEPIRDARED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 82 ERRRLnggtvAMIFQEPMtsLNPCFTVGYQIDEAVKTHvggGRKERKEQVLSLLESVGIpdpARRYDAYPHQMSGGMSQR 161
Cdd:COG4133 73 YRRRL-----AYLGHADG--LKPELTVRENLRFWAALY---GLRADREAIDEALEAVGL---AGLADLPVRQLSAGQKRR 139
|
170 180
....*....|....*....|....*
gi 522049469 162 AMIAMALAGQPKLLIADEPTTALDV 186
Cdd:COG4133 140 VALARLLLSPAPLWLLDEPFTALDA 164
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-231 |
1.00e-21 |
|
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: 91.41 E-value: 1.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPtqNGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPqariTCDELVLDGKNLLQLTATER 83
Cdd:cd03263 1 LQIRNLTKTYK--KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRP----TSGTAYINGYSIRTDRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 84 RRlnggtVAMIFQEPMtsLNPCFTVgyqiDEAVKTHV---GGGRKERKEQVLSLLESVGIPDPArryDAYPHQMSGGMSQ 160
Cdd:cd03263 75 QS-----LGYCPQFDA--LFDELTV----REHLRFYArlkGLPKSEIKEEVELLLRVLGLTDKA---NKRARTLSGGMKR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522049469 161 RAMIAMALAGQPKLLIADEPTTALDV--------TVQAQILELllklqqqfqmGLILITHDMGVVAETAQQVVVQYAGQ 231
Cdd:cd03263 141 KLSLAIALIGGPSVLLLDEPTSGLDPasrraiwdLILEVRKGR----------SIILTTHSMDEAEALCDRIAIMSDGK 209
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-185 |
1.62e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 95.18 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 2 SLLSVRNLSVAFPTQNGWFQAVEGINLTVNPNEILAIVGESGSGKSvamlALMNLLPPQARITCDELVLDGKNLLQLTAT 81
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKS----TLMNILGCLDKPTSGTYRVAGQDVATLDAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 82 ERRRLNGGTVAMIFQEpmTSLNPCFTVGYQIdEAVKTHVGGGRKERKEQVLSLLESVGIPDparRYDAYPHQMSGGMSQR 161
Cdd:PRK10535 79 ALAQLRREHFGFIFQR--YHLLSHLTAAQNV-EVPAVYAGLERKQRLLRAQELLQRLGLED---RVEYQPSQLSGGQQQR 152
|
170 180
....*....|....*....|....
gi 522049469 162 AMIAMALAGQPKLLIADEPTTALD 185
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALD 176
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
4-243 |
1.72e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 92.15 E-value: 1.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPTQNGW---FQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQ-ARITCDELVLDGKNLLQLT 79
Cdd:PRK13646 1 MTIRFDNVSYTYQKGTpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTtGTVTVDDITITHKTKDKYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 80 ATERRRlnggtVAMIFQEPMTSLnpcF--TVGYQIDEAVKtHVGGGRKERKEQVLSLLESVGIPDPArrYDAYPHQMSGG 157
Cdd:PRK13646 81 RPVRKR-----IGMVFQFPESQL---FedTVEREIIFGPK-NFKMNLDEVKNYAHRLLMDLGFSRDV--MSQSPFQMSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 158 MSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNS 237
Cdd:PRK13646 150 QMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTS 229
|
....*.
gi 522049469 238 AYELFN 243
Cdd:PRK13646 230 PKELFK 235
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
18-241 |
1.73e-21 |
|
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: 92.45 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 18 GWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPP---QARITcdelvldGKNLLQLTATERRRlnggtVAMI 94
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPtsgTARVA-------GYDVVREPRKVRRS-----IGIV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 95 FQEPmtSLNPCFTvGYQIDEAVKTHVGGGRKERKEQVLSLLESVGIPDPARRYdayPHQMSGGMSQRAMIAMALAGQPKL 174
Cdd:TIGR01188 72 PQYA--SVDEDLT-GRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRP---VGTYSGGMRRRLDIAASLIHQPDV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522049469 175 LIADEPTTALDVTVQAqILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYEL 241
Cdd:TIGR01188 146 LFLDEPTTGLDPRTRR-AIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-214 |
3.26e-21 |
|
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: 90.22 E-value: 3.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 23 VEGINLTVNPNEILAIVGESGSGKSVamlaLMNLLPPQARITCDELVLDGKnllQLTATERRRLnggtvaMIFQEpmTSL 102
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKST----LLNLISGLAQPTSGGVILEGK---QITEPGPDRM------VVFQN--YSL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 103 NPCFTVGYQIDEAVKTHVGGGRKERKEQVL-SLLESVGIPDPArryDAYPHQMSGGMSQRAMIAMALAGQPKLLIADEPT 181
Cdd:TIGR01184 66 LPWLTVRENIALAVDRVLPDLSKSERRAIVeEHIALVGLTEAA---DKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190
....*....|....*....|....*....|...
gi 522049469 182 TALDVTVQAQILELLLKLQQQFQMGLILITHDM 214
Cdd:TIGR01184 143 GALDALTRGNLQEELMQIWEEHRVTVLMVTHDV 175
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-250 |
4.40e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 90.22 E-value: 4.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFPTQngwfQAVEGINLTVNPNEILAIVGESGSGKSVAMLAL--MNLLPPQARITcDELVLDGKNLLQLTA 80
Cdd:PRK14239 5 ILQVSDLSVYYNKK----KALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEVTIT-GSIVYNGHNIYSPRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 81 --TERRRlnggTVAMIFQEPmtslNPcftVGYQIDEAVkthVGG----GRKERK---EQVLSLLESVGIPDPAR-RYDAY 150
Cdd:PRK14239 80 dtVDLRK----EIGMVFQQP----NP---FPMSIYENV---VYGlrlkGIKDKQvldEAVEKSLKGASIWDEVKdRLHDS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 151 PHQMSGGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMglILITHDMGVVAETAQQVVVQYAG 230
Cdd:PRK14239 146 ALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTM--LLVTRSMQQASRISDRTGFFLDG 223
|
250 260
....*....|....*....|
gi 522049469 231 QQVEKNSAYELFNHPHHPYT 250
Cdd:PRK14239 224 DLIEYNDTKQMFMNPKHKET 243
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
38-254 |
7.54e-21 |
|
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: 91.02 E-value: 7.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 38 IVGESGSGKSVAMLALMNLLPPQAritcDELVLDGKNLLQLTAtERRRLNggtvaMIFQEpmTSLNPCFTVGYQIDEAVK 117
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDS----GSIMLDGEDVTNVPP-HLRHIN-----MVFQS--YALFPHMTVEENVAFGLK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 118 THvGGGRKERKEQVLSLLESVGIPDPARRYdayPHQMSGGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLL 197
Cdd:TIGR01187 69 MR-KVPRAEIKPRVLEALRLVQLEEFADRK---PHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELK 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 522049469 198 KLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYELFNHPHHPYTAALL 254
Cdd:TIGR01187 145 TIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFI 201
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-185 |
7.85e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.77 E-value: 7.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFPTqngwFQAVEGINLTVNPNEILAIVGESGSGKSVamlaLMNLL----PPqaritcD--ELVLDGKNLL 76
Cdd:COG1129 4 LLEMRGISKSFGG----VKALDGVSLELRPGEVHALLGENGAGKST----LMKILsgvyQP------DsgEILLDGEPVR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 77 QLTATERRRLnGgtVAMIFQEPmtSLNPCFTV------GYQIdeavkthVGGG---RKERKEQVLSLLESVGIP-DPARR 146
Cdd:COG1129 70 FRSPRDAQAA-G--IAIIHQEL--NLVPNLSVaeniflGREP-------RRGGlidWRAMRRRARELLARLGLDiDPDTP 137
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 522049469 147 YDAYPhqmsggMSQRAM--IAMALAGQPKLLIADEPTTALD 185
Cdd:COG1129 138 VGDLS------VAQQQLveIARALSRDARVLILDEPTASLT 172
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-184 |
8.59e-21 |
|
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: 88.65 E-value: 8.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQA-RItcdelVLDGKNLLQLTATE 82
Cdd:cd03224 1 LEVENLNAGY----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSgSI-----RFDGRDITGLPPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 RRRLnGgtVAMIFQEPMtsLNPCFTVGYQIDEAVKTHVGGGRKERKEQVLSLLesvgiPDPARRYDAYPHQMSGGmsQRA 162
Cdd:cd03224 72 RARA-G--IGYVPEGRR--IFPELTVEENLLLGAYARRRAKRKARLERVYELF-----PRLKERRKQLAGTLSGG--EQQ 139
|
170 180
....*....|....*....|....
gi 522049469 163 M--IAMALAGQPKLLIADEPTTAL 184
Cdd:cd03224 140 MlaIARALMSRPKLLLLDEPSEGL 163
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-241 |
1.90e-20 |
|
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: 91.75 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPTQNGWfqAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQA-RITcdelvLDGKNLLQLTATE 82
Cdd:COG4987 334 LELEDVSFRYPGAGRP--VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSgSIT-----LGGVDLRDLDEDD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 RRRLnggtVAMIFQEP---MTSL-------NPcftvgyQIDEavkthvgggrkerkEQVLSLLESVGIPDPARR----YD 148
Cdd:COG4987 407 LRRR----IAVVPQRPhlfDTTLrenlrlaRP------DATD--------------EELWAALERVGLGDWLAAlpdgLD 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 149 A----YPHQMSGGMSQRAMIAMALAGQPKLLIADEPTTALD-VTVQAqilELLLKLQQQFQMGLILITHDMgVVAETAQQ 223
Cdd:COG4987 463 TwlgeGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDaATEQA---LLADLLEALAGRTVLLITHRL-AGLERMDR 538
|
250
....*....|....*...
gi 522049469 224 VVVQYAGQQVEKNSAYEL 241
Cdd:COG4987 539 ILVLEDGRIVEQGTHEEL 556
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
25-213 |
2.16e-20 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 87.91 E-value: 2.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 25 GINLTVNPNEILAIVGESGSGKSVamlaLMNLLPPQARITCDELVLDGKNLLQLTATERRRLNGGTVAMIFQEPM--TSL 102
Cdd:PRK10584 28 GVELVVKRGETIALIGESGSGKST----LLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQSFMliPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 103 NPCFTVgyQIDEAVKthvGGGRKERKEQVLSLLESVGIpdpARRYDAYPHQMSGGMSQRAMIAMALAGQPKLLIADEPTT 182
Cdd:PRK10584 104 NALENV--ELPALLR---GESSRQSRNGAKALLEQLGL---GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190
....*....|....*....|....*....|.
gi 522049469 183 ALDVTVQAQILELLLKLQQQFQMGLILITHD 213
Cdd:PRK10584 176 NLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-250 |
2.28e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 88.36 E-value: 2.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNL--LPPQARITcDELVLDGKNLL--QLT 79
Cdd:PRK14267 5 IETVNLRVYY----GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLleLNEEARVE-GEVRLFGRNIYspDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 80 ATERRRlnggTVAMIFQEPmtslNPC--------FTVGYQIDEAVKthvggGRKERKEQVLSLLESVGIPDPAR-RYDAY 150
Cdd:PRK14267 80 PIEVRR----EVGMVFQYP----NPFphltiydnVAIGVKLNGLVK-----SKKELDERVEWALKKAALWDEVKdRLNDY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 151 PHQMSGGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQmgLILITHDMGVVAETAQQVVVQYAG 230
Cdd:PRK14267 147 PSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYT--IVLVTHSPAQAARVSDYVAFLYLG 224
|
250 260
....*....|....*....|
gi 522049469 231 QQVEKNSAYELFNHPHHPYT 250
Cdd:PRK14267 225 KLIEVGPTRKVFENPEHELT 244
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-263 |
2.38e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 89.02 E-value: 2.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MSLLSVRNLSVAFpTQNGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQAritcDELVLDGKNLLQLTA 80
Cdd:PRK13650 2 SNIIEVKNLTFKY-KEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAES----GQIIIDGDLLTEENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 81 TERRRLNGgtvaMIFQEPMTSLnpcftVGYQIDEAVK---THVGGGRKERKEQVLSLLESVGIPDPARRYdayPHQMSGG 157
Cdd:PRK13650 77 WDIRHKIG----MVFQNPDNQF-----VGATVEDDVAfglENKGIPHEEMKERVNEALELVGMQDFKERE---PARLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 158 MSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAeTAQQVVVQYAGQQVEKNS 237
Cdd:PRK13650 145 QKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTST 223
|
250 260 270
....*....|....*....|....*....|....
gi 522049469 238 AYELFNHPHH--------PYTAALLSALPERALP 263
Cdd:PRK13650 224 PRELFSRGNDllqlgldiPFTTSLVQSLRQNGYD 257
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
7-185 |
4.07e-20 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 88.61 E-value: 4.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 7 RNLSVAFPtqnGWFQAVEGINLTVNPNEILAIVGESGSGKSVaMLALMN-LLPPQA-RITcdelvLDGKNLLQLTATERR 84
Cdd:COG1125 5 ENVTKRYP---DGTVAVDDLSLTIPAGEFTVLVGPSGCGKTT-TLRMINrLIEPTSgRIL-----IDGEDIRDLDPVELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 85 RlNGGTVamIfQEpmTSLNPCFTVGYQIdEAVKTHVGGGRKERKEQVLSLLESVGIpDPARRYDAYPHQMSGGMSQRAMI 164
Cdd:COG1125 76 R-RIGYV--I-QQ--IGLFPHMTVAENI-ATVPRLLGWDKERIRARVDELLELVGL-DPEEYRDRYPHELSGGQQQRVGV 147
|
170 180
....*....|....*....|.
gi 522049469 165 AMALAGQPKLLIADEPTTALD 185
Cdd:COG1125 148 ARALAADPPILLMDEPFGALD 168
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-256 |
4.94e-20 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 87.12 E-value: 4.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPTQngWFQAvegiNLTVNPNEILAIVGESGSGKSvamlALMNL----LPPQAritcDELVLDGKNLLQLT 79
Cdd:COG3840 2 LRLDDLTYRYGDF--PLRF----DLTIAAGERVAILGPSGAGKS----TLLNLiagfLPPDS----GRILWNGQDLTALP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 80 ATERrrlnggTVAMIFQEpmTSLNPCFTVgyqideavKTHVGGGR-------KERKEQVLSLLESVGIPDPARRYdayPH 152
Cdd:COG3840 68 PAER------PVSMLFQE--NNLFPHLTV--------AQNIGLGLrpglkltAEQRAQVEQALERVGLAGLLDRL---PG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 153 QMSGGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQ 232
Cdd:COG3840 129 QLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRI 208
|
250 260
....*....|....*....|....
gi 522049469 233 VEKNSAYELFNHPHHPYTAALLSA 256
Cdd:COG3840 209 AADGPTAALLDGEPPPALAAYLGI 232
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-233 |
5.31e-20 |
|
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: 85.17 E-value: 5.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPTqngwFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPqariTCDELVLDGKNLLQLTATER 83
Cdd:cd03216 1 LELRGITKRFGG----VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKP----DSGEILVDGKEVSFASPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 84 RRLngGtVAMIfqepmtslnpcftvgyqideavkthvgggrkerkeqvlsllesvgipdparrydaypHQMSGGMSQRAM 163
Cdd:cd03216 73 RRA--G-IAMV---------------------------------------------------------YQLSVGERQMVE 92
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 164 IAMALAGQPKLLIADEPTTALDVTvQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQV 233
Cdd:cd03216 93 IARALARNARLLILDEPTAALTPA-EVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
22-185 |
5.63e-20 |
|
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: 86.31 E-value: 5.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 22 AVEGINLTVNPNEILAIVGESGSGKSvamlALMNLLPPQARITCDELVLDGKNLLQL----TATERRRLnggtvAMIFQE 97
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKS----TLLKLIYKEELPTSGTIRVNGQDVSDLrgraIPYLRRKI-----GVVFQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 98 pmTSLNPCFTVGYQIDEAVKThVGGGRKERKEQVLSLLESVGIPDparRYDAYPHQMSGGMSQRAMIAMALAGQPKLLIA 177
Cdd:cd03292 87 --FRLLPDRNVYENVAFALEV-TGVPPREIRKRVPAALELVGLSH---KHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
....*...
gi 522049469 178 DEPTTALD 185
Cdd:cd03292 161 DEPTGNLD 168
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
26-278 |
5.84e-20 |
|
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: 89.02 E-value: 5.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 26 INLTVNPNEILAIVGESGSGKSVAMLALMNLL-PPQARITCDELVL-DGKNLLQLTaTERRRlnggtVAMIFQEpmTSLN 103
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTrPDEGEIVLNGRTLfDSRKGIFLP-PEKRR-----IGYVFQE--ARLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 104 PCFTVGYQIDEAVKTHVGGGRKERKEQVLSLLesvGIPDPARRYdayPHQMSGGMSQRAMIAMALAGQPKLLIADEPTTA 183
Cdd:TIGR02142 88 PHLSVRGNLRYGMKRARPSERRISFERVIELL---GIGHLLGRL---PGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 184 LDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYEL-----FNHPHHPYTAALLSALP 258
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVwaspdLPWLAREDQGSLIEGVV 241
|
250 260
....*....|....*....|
gi 522049469 259 ERALPTGLLPTIPglVPGQH 278
Cdd:TIGR02142 242 AEHDQHYGLTALR--LGGGH 259
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
26-186 |
6.84e-20 |
|
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: 88.62 E-value: 6.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 26 INLTVNPNEILAIVGESGSGKSvamlALMNLL-----PPQARITCDELVL-DGKNLLQLtATERRRLnggtvAMIFQEPm 99
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKT----TLLRAIaglerPDSGRIRLGGEVLqDSARGIFL-PPHRRRI-----GYVFQEA- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 100 tSLNPCFTVGYQIDEAVKTHVGGGRKERKEQVLSLLesvGIPDPARRYdayPHQMSGGMSQRAMIAMALAGQPKLLIADE 179
Cdd:COG4148 87 -RLFPHLSVRGNLLYGRKRAPRAERRISFDEVVELL---GIGHLLDRR---PATLSGGERQRVAIGRALLSSPRLLLMDE 159
|
....*..
gi 522049469 180 PTTALDV 186
Cdd:COG4148 160 PLAALDL 166
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-249 |
9.67e-20 |
|
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: 89.89 E-value: 9.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPTQNGWfqAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQA-RITcdelvLDGKNLLQLTATE 82
Cdd:COG2274 474 IELENVSFRYPGDSPP--VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSgRIL-----IDGIDLRQIDPAS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 RRRLnggtVAMIFQEPM---TSL--NpcFTVGY-QIDEavkthvgggrkerkEQVLSLLESVGIPDPARR----YDAY-- 150
Cdd:COG2274 547 LRRQ----IGVVLQDVFlfsGTIreN--ITLGDpDATD--------------EEIIEAARLAGLHDFIEAlpmgYDTVvg 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 151 --PHQMSGGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAqiLELLLKLQQQFQMGLILITHDMGVVAEtAQQVVVQY 228
Cdd:COG2274 607 egGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEA--IILENLRRLLKGRTVIIIAHRLSTIRL-ADRIIVLD 683
|
250 260
....*....|....*....|.
gi 522049469 229 AGQQVEKNSAYELFNHPHHPY 249
Cdd:COG2274 684 KGRIVEDGTHEELLARKGLYA 704
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-184 |
1.35e-19 |
|
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: 85.80 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MSLLSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQA-RITcdelvLDGKNLLQLT 79
Cdd:COG0410 1 MPMLEVENLHAGY----GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSgSIR-----FDGEDITGLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 80 ATERRRLngGtVAM------IFQEpMTslnpcftvgyqIDE-----AVKTHVGGGRKERKEQVLSLLesvgiPDPARRYD 148
Cdd:COG0410 72 PHRIARL--G-IGYvpegrrIFPS-LT-----------VEEnlllgAYARRDRAEVRADLERVYELF-----PRLKERRR 131
|
170 180 190
....*....|....*....|....*....|....*...
gi 522049469 149 AYPHQMSGGmsQRAM--IAMALAGQPKLLIADEPTTAL 184
Cdd:COG0410 132 QRAGTLSGG--EQQMlaIGRALMSRPKLLLLDEPSLGL 167
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
22-242 |
1.44e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 86.68 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 22 AVEGINLTVNPNEILAIVGESGSGKSvAMLALMN--LLPPQARITCDEL-VLDGKNLLQLtateRRRlnggtVAMIFQEP 98
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKS-TIAKHMNalLIPSEGKVYVDGLdTSDEENLWDI----RNK-----AGMVFQNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 99 MTSLnpcftVGYQIDEAVK---THVGGGRKERKEQVLSLLESVGIPDpARRYDayPHQMSGGMSQRAMIAMALAGQPKLL 175
Cdd:PRK13633 95 DNQI-----VATIVEEDVAfgpENLGIPPEEIRERVDESLKKVGMYE-YRRHA--PHLLSGGQKQRVAIAGILAMRPECI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522049469 176 IADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAEtAQQVVVQYAGQQVEKNSAYELF 242
Cdd:PRK13633 167 IFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF 232
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
233-297 |
2.18e-19 |
|
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: 80.52 E-value: 2.18e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522049469 233 VEKNSAYELFNHPHHPYTAALLSALPERALPTGLLPTIPGLVPGQHNRPQGCLFAPRCAYQQARC 297
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPPKRPLYTIPGNVPSLLELPEGCPFAPRCPFATEEC 65
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
20-244 |
2.72e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 86.22 E-value: 2.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 20 FQAVEGINLTVNPNEILAIVGESGSGKSvAMLALMN-LLPPQariTCDELVLDGK---NLLQLTATERRRLNggtVAMIF 95
Cdd:PRK13645 24 FKALNNTSLTFKKNKVTCVIGTTGSGKS-TMIQLTNgLIISE---TGQTIVGDYAipaNLKKIKEVKRLRKE---IGLVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 96 QEPMTSLnpcFTVGYQIDEAV-KTHVGGGRKERKEQVLSLLESVGIP-DPARRYdayPHQMSGGMSQRAMIAMALAGQPK 173
Cdd:PRK13645 97 QFPEYQL---FQETIEKDIAFgPVNLGENKQEAYKKVPELLKLVQLPeDYVKRS---PFELSGGQKRRVALAGIIAMDGN 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522049469 174 LLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYELFNH 244
Cdd:PRK13645 171 TLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-245 |
3.19e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 85.51 E-value: 3.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFPTQNgwfQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPP---QARITCDELVLDGKNLLqlt 79
Cdd:PRK13639 1 ILETRDLKYSYPDGT---EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPtsgEVLIKGEPIKYDKKSLL--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 80 atERRRlnggTVAMIFQEPMTSLnpcFTVGYQIDEAV-KTHVGGGRKERKEQVLSLLESVGIPDPARRYdayPHQMSGGM 158
Cdd:PRK13639 75 --EVRK----TVGIVFQNPDDQL---FAPTVEEDVAFgPLNLGLSKEEVEKRVKEALKAVGMEGFENKP---PHHLSGGQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 159 SQRAMIAMALAGQPKLLIADEPTTALDvTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSA 238
Cdd:PRK13639 143 KKRVAIAGILAMKPEIIVLDEPTSGLD-PMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTP 221
|
....*..
gi 522049469 239 YELFNHP 245
Cdd:PRK13639 222 KEVFSDI 228
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
26-293 |
3.59e-19 |
|
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: 86.97 E-value: 3.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 26 INLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQAriTCDELVLDGKNLLQLTATERrrlnggTVAMIFQEpmTSLNPC 105
Cdd:TIGR03258 24 LSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAG--LTGRIAIADRDLTHAPPHKR------GLALLFQN--YALFPH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 106 FTVgyqideavKTHVGGGRKERK-------EQVLSLLESVGIPDPARRYdayPHQMSGGMSQRAMIAMALAGQPKLLIAD 178
Cdd:TIGR03258 94 LKV--------EDNVAFGLRAQKmpkadiaERVADALKLVGLGDAAAHL---PAQLSGGMQQRIAIARAIAIEPDVLLLD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 179 EPTTALDVTVQAQILELLLKL-QQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYELFNHPHHPYTAALLSA- 256
Cdd:TIGR03258 163 EPLSALDANIRANMREEIAALhEELPELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGAa 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 522049469 257 --LPERALPTGLLPTIPGLVPG----------QHN--------RPQGCLFAPRCAYQ 293
Cdd:TIGR03258 243 niLPAIALGITEAPGLVDVSCGgavifafgdgRHDgrdklaciRPEHLALTPRPAGE 299
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-184 |
4.20e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 87.39 E-value: 4.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFPTqngwFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPqaritcD--ELVLDGKNLLQLTA 80
Cdd:COG3845 5 ALELRGITKRFGG----VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQP------DsgEILIDGKPVRIRSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 81 TERRRLNggtVAMIFQEPMtsLNPCFTV------GYqidEAVKTHVGGGRKERKEqVLSLLESVGIP-DParryDAYPHQ 153
Cdd:COG3845 75 RDAIALG---IGMVHQHFM--LVPNLTVaenivlGL---EPTKGGRLDRKAARAR-IRELSERYGLDvDP----DAKVED 141
|
170 180 190
....*....|....*....|....*....|.
gi 522049469 154 MSGGMSQRAMIAMALAGQPKLLIADEPTTAL 184
Cdd:COG3845 142 LSVGEQQRVEILKALYRGARILILDEPTAVL 172
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-246 |
4.69e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 86.06 E-value: 4.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAF-PTQNGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPP-QARITCDELVLDGKNLLQLTA 80
Cdd:PRK13631 21 ILRVKNLYCVFdEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSkYGTIQVGDIYIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 81 TER--------RRLNGgTVAMIFQEPMTSLnpcFTVGYQIDEAV-KTHVGGGRKERKEQVLSLLESVGIPDPArrYDAYP 151
Cdd:PRK13631 101 TNPyskkiknfKELRR-RVSMVFQFPEYQL---FKDTIEKDIMFgPVALGVKKSEAKKLAKFYLNKMGLDDSY--LERSP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 152 HQMSGGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMgLILITHDMGVVAETAQQVVVQYAGQ 231
Cdd:PRK13631 175 FGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKT-VFVITHTMEHVLEVADEVIVMDKGK 253
|
250
....*....|....*
gi 522049469 232 QVEKNSAYELFNHPH 246
Cdd:PRK13631 254 ILKTGTPYEIFTDQH 268
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-185 |
7.13e-19 |
|
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: 83.08 E-value: 7.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 5 SVRNLSVAFPTQNgwfQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQAritcDELVLDGKNLlqlTATERR 84
Cdd:cd03226 1 RIENISFSYKKGT---EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESS----GSILLNGKPI---KAKERR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 85 RlnggTVAMIFQEPMTSLNPCfTVGYQIDEAVKThvGGGRKERKEQVLSLLesvgipDPARRYDAYPHQMSGGMSQRAMI 164
Cdd:cd03226 71 K----SIGYVMQDVDYQLFTD-SVREELLLGLKE--LDAGNEQAETVLKDL------DLYALKERHPLSLSGGQKQRLAI 137
|
170 180
....*....|....*....|.
gi 522049469 165 AMALAGQPKLLIADEPTTALD 185
Cdd:cd03226 138 AAALLSGKDLLIFDEPTSGLD 158
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
22-243 |
8.52e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 84.71 E-value: 8.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 22 AVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQA-RITCDELVLDGKNLlQLTATERRrlnggtVAMIFQEPMt 100
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSgKIIIDGVDITDKKV-KLSDIRKK------VGLVFQYPE- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 101 slnpcftvgYQI-DEAVK-------THVGGGRKERKEQVLSLLESVGIPdparrYDAY----PHQMSGGMSQRAMIAMAL 168
Cdd:PRK13637 94 ---------YQLfEETIEkdiafgpINLGLSEEEIENRVKRAMNIVGLD-----YEDYkdksPFELSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522049469 169 AGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYELFN 243
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-224 |
1.07e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 83.33 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 2 SLLSVRNLSVAFPTQNGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPqariTCDELVLDGKNLLQLTAT 81
Cdd:PRK11629 4 ILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTP----TSGDVIFNGQPMSKLSSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 82 ERRRLNGGTVAMIFQepMTSLNPCFTVGYQIdeAVKTHVGG-GRKERKEQVLSLLESVGIpdpARRYDAYPHQMSGGMSQ 160
Cdd:PRK11629 80 AKAELRNQKLGFIYQ--FHHLLPDFTALENV--AMPLLIGKkKPAEINSRALEMLAAVGL---EHRANHRPSELSGGERQ 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522049469 161 RAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQV 224
Cdd:PRK11629 153 RVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-233 |
1.21e-18 |
|
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: 82.69 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPTQNgwfqAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPqariTCDELVLDGKNLLQLTATER 83
Cdd:cd03301 1 VELENVTKRFGNVT----ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEP----TSGRIYIGGRDVTDLPPKDR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 84 rrlnggTVAMIFQEpmTSLNPCFTVGYQIDEAVKTHvGGGRKERKEQVLSLLESVGIpdpARRYDAYPHQMSGGMSQRAM 163
Cdd:cd03301 73 ------DIAMVFQN--YALYPHMTVYDNIAFGLKLR-KVPKDEIDERVREVAELLQI---EHLLDRKPKQLSGGQRQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522049469 164 IAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMgVVAET-AQQVVVQYAG--QQV 233
Cdd:cd03301 141 LGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQ-VEAMTmADRIAVMNDGqiQQI 212
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-233 |
2.02e-18 |
|
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: 81.94 E-value: 2.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQAritcDELVLDGKnllQLTATER 83
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDS----GEVLFDGK---PLDIAAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 84 RRLnggtvAMIFQEpmTSLNPCFTVGYQIDEAVKTHvGGGRKERKEQVLSLLESVGIPDPA-RRYDayphQMSGGMSQRA 162
Cdd:cd03269 70 NRI-----GYLPEE--RGLYPKMKVIDQLVYLAQLK-GLKKEEARRRIDEWLERLELSEYAnKRVE----ELSKGNQQKV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522049469 163 MIAMALAGQPKLLIADEPTTALDVtVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQV 233
Cdd:cd03269 138 QFIAAVIHDPELLILDEPFSGLDP-VNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-185 |
2.40e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 84.35 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MSLLSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSVamlaLMNLLppqA---RITCDELVLDGKNLLQ 77
Cdd:COG3839 1 MASLELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKST----LLRMI---AgleDPTSGEILIGGRDVTD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 78 LTATERRrlnggtVAMIFQEP-----MTslnpcftvgyqideavkthV-----------GGGRKERKEQVLSLLESVGIP 141
Cdd:COG3839 70 LPPKDRN------IAMVFQSYalyphMT-------------------VyeniafplklrKVPKAEIDRRVREAAELLGLE 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 522049469 142 DPARRYdayPHQMSGGMSQRAMIAMALAGQPKLLIADEPTTALD 185
Cdd:COG3839 125 DLLDRK---PKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLD 165
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-244 |
2.56e-18 |
|
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: 85.58 E-value: 2.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPTQNgwfQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQA-RITcdelvLDGKNLLQLTATE 82
Cdd:COG4988 337 IELEDVSFSYPGGR---PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSgSIL-----INGVDLSDLDPAS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 RRRLnggtVAMIFQEPmtslnpcftvgYQIDEAVKTHVGGGRKER-KEQVLSLLESVGIPDparRYDAYPHQM------- 154
Cdd:COG4988 409 WRRQ----IAWVPQNP-----------YLFAGTIRENLRLGRPDAsDEELEAALEAAGLDE---FVAALPDGLdtplgeg 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 155 ----SGGMSQRAMIAMALAGQPKLLIADEPTTALDVT----VQAQILELLLKLQqqfqmgLILITHDMGVVAEtAQQVVV 226
Cdd:COG4988 471 grglSGGQAQRLALARALLRDAPLLLLDEPTAHLDAEteaeILQALRRLAKGRT------VILITHRLALLAQ-ADRILV 543
|
250
....*....|....*...
gi 522049469 227 QYAGQQVEKNSAYELFNH 244
Cdd:COG4988 544 LDDGRIVEQGTHEELLAK 561
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-185 |
3.03e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 82.51 E-value: 3.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQA-RITcdelvLDGKNLLQLTAT 81
Cdd:PRK13548 2 MLEARNLSVRL----GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSgEVR-----LNGRPLADWSPA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 82 E--RRRlnggtvAMIFQEpmTSLNPCFTVgyqiDEAVK---THVGGGRKERKEQVLSLLESVGIPDPARRYdaYPhQMSG 156
Cdd:PRK13548 73 ElaRRR------AVLPQH--SSLSFPFTV----EEVVAmgrAPHGLSRAEDDALVAAALAQVDLAHLAGRD--YP-QLSG 137
|
170 180 190
....*....|....*....|....*....|....*
gi 522049469 157 GMSQRAMIAMALA------GQPKLLIADEPTTALD 185
Cdd:PRK13548 138 GEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALD 172
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-243 |
3.13e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 82.73 E-value: 3.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 2 SLLSVRNLSVAFPTQNGWfqAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQAritcDELVLDGKNLLQLTAT 81
Cdd:PRK13632 6 VMIKVENVSFSYPNSENN--ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQS----GEIKIDGITISKENLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 82 ERRrlngGTVAMIFQEPMTSLnpcftvgyqIDEAVKTHVGGG-------RKERKEQVLSLLESVGIPDparRYDAYPHQM 154
Cdd:PRK13632 80 EIR----KKIGIIFQNPDNQF---------IGATVEDDIAFGlenkkvpPKKMKDIIDDLAKKVGMED---YLDKEPQNL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 155 SGGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAEtAQQVVVQYAGQQVE 234
Cdd:PRK13632 144 SGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIA 222
|
....*....
gi 522049469 235 KNSAYELFN 243
Cdd:PRK13632 223 QGKPKEILN 231
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
7-245 |
6.45e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 84.39 E-value: 6.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 7 RNLSVAFPTQNGwFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPqariTCDELVLDGKNLLQLTATERRRl 86
Cdd:TIGR00958 482 QDVSFSYPNRPD-VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQP----TGGQVLLDGVPLVQYDHHYLHR- 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 87 nggTVAMIFQEPMTslnpcftvgyqIDEAVKTHVGGG-RKERKEQVLSLLESVG----IPDPARRYDAY--PH--QMSGG 157
Cdd:TIGR00958 556 ---QVALVGQEPVL-----------FSGSVRENIAYGlTDTPDEEIMAAAKAANahdfIMEFPNGYDTEvgEKgsQLSGG 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 158 MSQRAMIAMALAGQPKLLIADEPTTALDVTVQAqileLLLKLQQQFQMGLILITHDMGVVaETAQQVVVQYAGQQVEKNS 237
Cdd:TIGR00958 622 QKQRIAIARALVRKPRVLILDEATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTV-ERADQILVLKKGSVVEMGT 696
|
....*...
gi 522049469 238 AYELFNHP 245
Cdd:TIGR00958 697 HKQLMEDQ 704
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
22-245 |
1.70e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 81.22 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 22 AVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPP---QARITcDELVLDGKNLLQLTATERRrlnggtVAMIFQEP 98
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPtsgTVTIG-ERVITAGKKNKKLKPLRKK------VGIVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 99 MTSLnpcftvgyqIDEAVK-------THVGGGRKERKEQVLSLLESVGIPDPARryDAYPHQMSGGMSQRAMIAMALAGQ 171
Cdd:PRK13634 95 EHQL---------FEETVEkdicfgpMNFGVSEEDAKQKAREMIELVGLPEELL--ARSPFELSGGQMRRVAIAGVLAME 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522049469 172 PKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYELFNHP 245
Cdd:PRK13634 164 PEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-214 |
1.81e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 80.51 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFPTQngwfQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQA-RITCDELVLDGKnllqltAT 81
Cdd:PRK11248 1 MLQISHLYADYGGK----PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHgSITLDGKPVEGP------GA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 82 ERrrlnggtvAMIFQE----PMTSLNPCFTVGYQIdeavkthVGGGRKERKEQVLSLLESVGIPDPARRydaYPHQMSGG 157
Cdd:PRK11248 71 ER--------GVVFQNegllPWRNVQDNVAFGLQL-------AGVEKMQRLEIAHQMLKKVGLEGAEKR---YIWQLSGG 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 522049469 158 MSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDM 214
Cdd:PRK11248 133 QRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-283 |
1.93e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 81.03 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 21 QAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQA--------RITCDElvlDGKNLLQLtateRRRlnggtVA 92
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSgtitiagyHITPET---GNKNLKKL----RKK-----VS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 93 MIFQEPMTSLnpcF--TVGYQIDEAVKtHVGGGRKERKEQVLSLLESVGIPDPArrYDAYPHQMSGGMSQRAMIAMALAG 170
Cdd:PRK13641 89 LVFQFPEAQL---FenTVLKDVEFGPK-NFGFSEDEAKEKALKWLKKVGLSEDL--ISKSPFELSGGQMRRVAIAGVMAY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 171 QPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMgLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYELFNHP----- 245
Cdd:PRK13641 163 EPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHT-VILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKewlkk 241
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 522049469 246 HH---PYTAALLSALPERALPTGLLP-TIPGLVPGQHNRPQG 283
Cdd:PRK13641 242 HYldePATSRFASKLEKGGFKFSEMPlTIDELVDGIKNNLKG 283
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-245 |
2.29e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 80.62 E-value: 2.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MSLLSVRNLSVAFPTQNgwfQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPqariTCDELVLDGKNLLQLTA 80
Cdd:PRK13652 1 MHLIETRDLCYSYSGSK---EALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKP----TSGSVLIRGEPITKENI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 81 TERRRlnggTVAMIFQEPMTSLnpcFTVGYQIDEAV-KTHVGGGRKERKEQVLSLLESVGIPDPARRYdayPHQMSGGMS 159
Cdd:PRK13652 74 REVRK----FVGLVFQNPDDQI---FSPTVEQDIAFgPINLGLDEETVAHRVSSALHMLGLEELRDRV---PHHLSGGEK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 160 QRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAY 239
Cdd:PRK13652 144 KRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVE 223
|
....*.
gi 522049469 240 ELFNHP 245
Cdd:PRK13652 224 EIFLQP 229
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-185 |
2.90e-17 |
|
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: 79.40 E-value: 2.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFP--TQNGW-FQAVEGINLTVNPNEILAIVGESGSGKSVAMLALM-NLLPPQARItcdeLVLDGKNLLQL 78
Cdd:COG4778 4 LLEVENLSKTFTlhLQGGKrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYgNYLPDSGSI----LVRHDGGWVDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 79 -TATERR--RLNGGTVAMIFQ---------------EPMTSLnpcftvgyqideavkthvGGGRKERKEQVLSLLESVGI 140
Cdd:COG4778 80 aQASPREilALRRRTIGYVSQflrviprvsaldvvaEPLLER------------------GVDREEARARARELLARLNL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 522049469 141 PDpaRRYDAYPHQMSGGMSQRAMIAMALAGQPKLLIADEPTTALD 185
Cdd:COG4778 142 PE--RLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLD 184
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-186 |
4.94e-17 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 77.47 E-value: 4.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAfptqngwfQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQARitcdELVLDGKNLLQLTATE 82
Cdd:cd03215 4 VLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASG----EITLDGKPVTRRSPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 RRRLNGGTVAmifqepmtslnpcftvgyqideavkthvgggrKERKEQVLSLLESVgipdparrYD--AYPHQMSGGMSQ 160
Cdd:cd03215 72 AIRAGIAYVP--------------------------------EDRKREGLVLDLSV--------AEniALSSLLSGGNQQ 111
|
170 180
....*....|....*....|....*.
gi 522049469 161 RAMIAMALAGQPKLLIADEPTTALDV 186
Cdd:cd03215 112 KVVLARWLARDPRVLILDEPTRGVDV 137
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-212 |
8.51e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 78.19 E-value: 8.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAfptqngwfqaVE------GINLTVNPNEILAIVGESGSGKSVAMLALMNLlpPQARITCDELVLDGKNLLQ 77
Cdd:COG0396 1 LEIKNLHVS----------VEgkeilkGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGH--PKYEVTSGSILLDGEDILE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 78 LTATERRRLngGtVAMIFQEPM------------TSLNpcftvgyqideAVKTHVGGGRKERKEqVLSLLESVGI-PDPA 144
Cdd:COG0396 69 LSPDERARA--G-IFLAFQYPVeipgvsvsnflrTALN-----------ARRGEELSAREFLKL-LKEKMKELGLdEDFL 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522049469 145 RRYDAYphQMSGGMSQRAMIAMALAGQPKLLIADEPTTALDV--------TVQAqilelllklQQQFQMGLILITH 212
Cdd:COG0396 134 DRYVNE--GFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIdalrivaeGVNK---------LRSPDRGILIITH 198
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-245 |
2.28e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 77.92 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 2 SLLSVRNLSVAFPTQNGwfQAVEGINLTVNPNEILAIVGESGSGKS-VAMLALMNLLP---PQARITCDELVLDGKNLLQ 77
Cdd:PRK13640 4 NIVEFKHVSFTYPDSKK--PALNDISFSIPRGSWTALIGHNGSGKStISKLINGLLLPddnPNSKITVDGITLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 78 LtateRRRlnggtVAMIFQEPMTSLnpcftVGYQIDEAVK---THVGGGRKERKEQVLSLLESVGIPDPArryDAYPHQM 154
Cdd:PRK13640 82 I----REK-----VGIVFQNPDNQF-----VGATVGDDVAfglENRAVPRPEMIKIVRDVLADVGMLDYI---DSEPANL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 155 SGGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGvVAETAQQVVVQYAGQQVE 234
Cdd:PRK13640 145 SGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDID-EANMADQVLVLDDGKLLA 223
|
250
....*....|.
gi 522049469 235 KNSAYELFNHP 245
Cdd:PRK13640 224 QGSPVEIFSKV 234
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-212 |
3.32e-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: 75.64 E-value: 3.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLlpPQARITCDELVLDGKNLLQLTATER 83
Cdd:cd03217 1 LEIKDLHVSV----GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH--PKYEVTEGEILFKGEDITDLPPEER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 84 RRLnGGTVAmiFQEPMtslnpcftvgyQIdEAVKthvgggrkerkeqVLSLLESVGIpdparrydayphQMSGGMSQRAM 163
Cdd:cd03217 75 ARL-GIFLA--FQYPP-----------EI-PGVK-------------NADFLRYVNE------------GFSGGEKKRNE 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 522049469 164 IAMALAGQPKLLIADEPTTALDVtVQAQILELLLKLQQQFQMGLILITH 212
Cdd:cd03217 115 ILQLLLLEPDLAILDEPDSGLDI-DALRLVAEVINKLREEGKSVLIITH 162
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-190 |
4.09e-16 |
|
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: 78.94 E-value: 4.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPTQNgwfQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQAritcDELVLDGKNLLQLTATER 83
Cdd:TIGR02868 335 LELRDLSAGYPGAP---PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQ----GEVTLDGVPVSSLDQDEV 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 84 RRlnggTVAMIFQEPmtslnpcftvgYQIDEAVKTHVGGGRKE-RKEQVLSLLESVGIPDPARR----YDAYPHQM---- 154
Cdd:TIGR02868 408 RR----RVSVCAQDA-----------HLFDTTVRENLRLARPDaTDEELWAALERVGLADWLRAlpdgLDTVLGEGgarl 472
|
170 180 190
....*....|....*....|....*....|....*.
gi 522049469 155 SGGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQA 190
Cdd:TIGR02868 473 SGGERQRLALARALLADAPILLLDEPTEHLDAETAD 508
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-257 |
4.79e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 76.67 E-value: 4.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPTQNgwfqAVEGINLTVNPNEILAIVGESGSGKSVAMLAL--MNLLPPQARITCDeLVLDGKNLLQL-TA 80
Cdd:PRK14271 22 MAAVNLTLGFAGKT----VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrMNDKVSGYRYSGD-VLLGGRSIFNYrDV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 81 TERRRlnggTVAMIFQEPmtslNPC-FTVGYQIDEAVKTHVGGGRKERKEQVLSLLESVGIPDPAR-RYDAYPHQMSGGM 158
Cdd:PRK14271 97 LEFRR----RVGMLFQRP----NPFpMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKdRLSDSPFRLSGGQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 159 SQRAMIAMALAGQPKLLIADEPTTALDVTvqAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSA 238
Cdd:PRK14271 169 QQLLCLARTLAVNPEVLLLDEPTSALDPT--TTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPT 246
|
250
....*....|....*....
gi 522049469 239 YELFNHPHHPYTAALLSAL 257
Cdd:PRK14271 247 EQLFSSPKHAETARYVAGL 265
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-250 |
5.21e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 76.61 E-value: 5.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPTQngwfQAVEGINLTVNPNEILAIVGESGSGKSVAMLAL--MNLLPPQARITcDELVLDGKNLLQltat 81
Cdd:PRK14258 8 IKVNNLSFYYDTQ----KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrMNELESEVRVE-GRVEFFNQNIYE---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 82 erRRLNGG----TVAMIFQEPmtSLNPcFTVGYQIDEAVKthVGGGRKerKEQVLSLLESvGIPDpARRYDAYPHQ---- 153
Cdd:PRK14258 79 --RRVNLNrlrrQVSMVHPKP--NLFP-MSVYDNVAYGVK--IVGWRP--KLEIDDIVES-ALKD-ADLWDEIKHKihks 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 154 ---MSGGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYA- 229
Cdd:PRK14258 148 aldLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGn 227
|
250 260
....*....|....*....|....*
gi 522049469 230 ----GQQVEKNSAYELFNHPHHPYT 250
Cdd:PRK14258 228 enriGQLVEFGLTKKIFNSPHDSRT 252
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-186 |
7.97e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 77.76 E-value: 7.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFPTQNgwfQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQAritcDELVLDGKNLLQLTATE 82
Cdd:COG3845 257 VLEVENLSVRDDRGV---PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPAS----GSIRLDGEDITGLSPRE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 RRRLNggtVAMIFQEPM-TSLNPCFTV------GYQIDEAVkthVGGG---RKERKEQVLSLLESVGI----PD-PARry 147
Cdd:COG3845 330 RRRLG---VAYIPEDRLgRGLVPDMSVaenlilGRYRRPPF---SRGGfldRKAIRAFAEELIEEFDVrtpgPDtPAR-- 401
|
170 180 190
....*....|....*....|....*....|....*....
gi 522049469 148 dayphQMSGGMSQRAMIAMALAGQPKLLIADEPTTALDV 186
Cdd:COG3845 402 -----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDV 435
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-231 |
1.07e-15 |
|
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: 74.54 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPTQngwfQAVEGINLTVnPNEILAIVGESGSGKSVAMLALMNLLPPQAritcDELVLDGKNLLQLTATER 83
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSS----GTIRIDGQDVLKQPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 84 RRLngGTVAmifQEPMTSlnPCFTVGYQIDEAVKTHvGGGRKERKEQVLSLLESVGIPDparRYDAYPHQMSGGMSQRAM 163
Cdd:cd03264 72 RRI--GYLP---QEFGVY--PNFTVREFLDYIAWLK-GIPSKEVKARVDEVLELVNLGD---RAKKKIGSLSGGMRRRVG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 164 IAMALAGQPKLLIADEPTTALD-----------------VTVqaqilelllklqqqfqmglILITHDMGVVAETAQQVVV 226
Cdd:cd03264 141 IAQALVGDPSILIVDEPTAGLDpeerirfrnllselgedRIV-------------------ILSTHIVEDVESLCNQVAV 201
|
....*
gi 522049469 227 QYAGQ 231
Cdd:cd03264 202 LNKGK 206
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-242 |
1.21e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 75.65 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFPTQNgwfQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQA-RITCDELVLD--GKNLLQLT 79
Cdd:PRK13636 5 ILKVEELNYNYSDGT---HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSgRILFDGKPIDysRKGLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 80 ATerrrlnggtVAMIFQEPMTSLnpcFTVG-YQIDEAVKTHVGGGRKERKEQVLSLLESVGIpdpARRYDAYPHQMSGGM 158
Cdd:PRK13636 82 ES---------VGMVFQDPDNQL---FSASvYQDVSFGAVNLKLPEDEVRKRVDNALKRTGI---EHLKDKPTHCLSFGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 159 SQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSA 238
Cdd:PRK13636 147 KKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNP 226
|
....
gi 522049469 239 YELF 242
Cdd:PRK13636 227 KEVF 230
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
6-233 |
1.48e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 75.54 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 6 VRNLSVAFPTQNgwfQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNL-LPPQARITcdelvLDGKNLLQLTATERR 84
Cdd:PRK13647 7 VEDLHFRYKDGT---KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIyLPQRGRVK-----VMGREVNAENEKWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 85 rlngGTVAMIFQEPMTSLnpcFTVGYQIDEAV-KTHVGGGRKERKEQVLSLLESVGIPDPArryDAYPHQMSGGMSQRAM 163
Cdd:PRK13647 79 ----SKVGLVFQDPDDQV---FSSTVWDDVAFgPVNMGLDKDEVERRVEEALKAVRMWDFR---DKPPYHLSYGQKKRVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 164 IAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMgLILITHDMGVVAETAQQVVVQYAGQQV 233
Cdd:PRK13647 149 IAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKT-VIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
21-233 |
1.99e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 75.89 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 21 QAVEGINLTVNPNEILAIVGESGSGKSVaMLALMNLLPPQariTCDELVLDGKNLLQLTATERRrlnggtVAMIFQE--- 97
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTT-LLRIIAGLEHQ---TSGHIRFHGTDVSRLHARDRK------VGFVFQHyal 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 98 --PMTslnpcftvgyqideaVKTHVGGG-----RKER------KEQVLSLLESVGIPDPARRYdayPHQMSGGMSQRAMI 164
Cdd:PRK10851 86 frHMT---------------VFDNIAFGltvlpRRERpnaaaiKAKVTQLLEMVQLAHLADRY---PAQLSGGQKQRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522049469 165 AMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAG--QQV 233
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGniEQA 218
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-185 |
2.45e-15 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 76.36 E-value: 2.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPTQNgwfQAVEGINLTVNPNEILAIVGESGSGKSvamlALMNLLP----PQA-RITcdelvLDGKNLLQL 78
Cdd:COG1132 340 IEFENVSFSYPGDR---PVLKDISLTIPPGETVALVGPSGSGKS----TLVNLLLrfydPTSgRIL-----IDGVDIRDL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 79 TATERRRLnggtVAMIFQEPMtsLnpcF--TVGYQIdeavkthvGGGRKER-KEQVLSLLESVGI-------PDparRYD 148
Cdd:COG1132 408 TLESLRRQ----IGVVPQDTF--L---FsgTIRENI--------RYGRPDAtDEEVEEAAKAAQAhefiealPD---GYD 467
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 522049469 149 AY----PHQMSGGMSQRAMIAMALAGQPKLLIADEPTTALD 185
Cdd:COG1132 468 TVvgerGVNLSGGQRQRIAIARALLKDPPILILDEATSALD 508
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-230 |
2.47e-15 |
|
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: 73.56 E-value: 2.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFPTQNGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLL-PPQARITcdelvLDGKNLLQLTAT 81
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLePDAGFAT-----VDGFDVVKEPAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 82 ERRRLNggtvamiFQEPMTSLNPCFTVGYQIDEAVKTHvGGGRKERKEQVLSLLESVGIPDPARRYDAyphQMSGGMSQR 161
Cdd:cd03266 76 ARRRLG-------FVSDSTGLYDRLTARENLEYFAGLY-GLKGDELTARLEELADRLGMEELLDRRVG---GFSTGMRQK 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522049469 162 AMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMgLILITHDMGVVAETAQQVVVQYAG 230
Cdd:cd03266 145 VAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKC-ILFSTHIMQEVERLCDRVVVLHRG 212
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
7-226 |
2.77e-15 |
|
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: 73.66 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 7 RNLSVAFPTQNGwFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQAritcDELVLDGKnllQLTATERRRL 86
Cdd:cd03248 15 QNVTFAYPTRPD-TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQG----GQVLLDGK---PISQYEHKYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 87 NgGTVAMIFQEPMT---SLNPCFTVGYQ-------IDEAVKTHVGGgrkerkeqVLSLLESvgipDPARRYDAYPHQMSG 156
Cdd:cd03248 87 H-SKVSLVGQEPVLfarSLQDNIAYGLQscsfecvKEAAQKAHAHS--------FISELAS----GYDTEVGEKGSQLSG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 157 GMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQmgLILITHDMGVVaETAQQVVV 226
Cdd:cd03248 154 GQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRT--VLVIAHRLSTV-ERADQILV 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-226 |
2.87e-15 |
|
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: 76.17 E-value: 2.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPtqnGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPqariTCDELVLDGKNLLQLTATER 83
Cdd:TIGR02857 322 LEFSGVSVAYP---GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDP----TEGSIAVNGVPLADADADSW 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 84 RRlnggTVAMIFQEPmtslnpcftvgYQIDEAVKTHVGGGRKERKE-QVLSLLESVGIPDP--------ARRYDAYPHQM 154
Cdd:TIGR02857 395 RD----QIAWVPQHP-----------FLFAGTIAENIRLARPDASDaEIREALERAGLDEFvaalpqglDTPIGEGGAGL 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522049469 155 SGGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQmgLILITHDMGVVAETAQQVVV 226
Cdd:TIGR02857 460 SGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRT--VLLVTHRLALAALADRIVVL 529
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-185 |
2.95e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 75.75 E-value: 2.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MSLLSVRNLSVAFPTQngwfQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPqariTCDELVLDGKNLLQLTA 80
Cdd:PRK09452 12 SPLVELRGISKSFDGK----EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETP----DSGRIMLDGQDITHVPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 81 tERRRLNggTVamiFQEpmTSLNPCFTVGyqidEAV-------KThvggGRKERKEQVLSLLESVGIPDPARRYdayPHQ 153
Cdd:PRK09452 84 -ENRHVN--TV---FQS--YALFPHMTVF----ENVafglrmqKT----PAAEITPRVMEALRMVQLEEFAQRK---PHQ 144
|
170 180 190
....*....|....*....|....*....|..
gi 522049469 154 MSGGMSQRAMIAMALAGQPKLLIADEPTTALD 185
Cdd:PRK09452 145 LSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-234 |
3.33e-15 |
|
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: 75.99 E-value: 3.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAF-PTQNGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQARITCdelVLDGKNLLQLTat 81
Cdd:TIGR03269 279 IIKVRNVSKRYiSVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVN---VRVGDEWVDMT-- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 82 ERRRLNGGTV----AMIFQEpmTSLNPCFTVGYQIDEAVKTHVGGGRKERKeqVLSLLESVGIPDPARR--YDAYPHQMS 155
Cdd:TIGR03269 354 KPGPDGRGRAkryiGILHQE--YDLYPHRTVLDNLTEAIGLELPDELARMK--AVITLKMVGFDEEKAEeiLDKYPDELS 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522049469 156 GGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVE 234
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVK 508
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-242 |
7.55e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 73.59 E-value: 7.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFPTQNGWFQaVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQARItcdeLVLDGKNLLQLTATE 82
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQ-LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGK----VKIDGELLTAENVWN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 RRRlnggTVAMIFQEPMTSLnpcftVGYQIDEAVK---THVGGGRKERKEQVLSLLESVGIPDPARRydaYPHQMSGGMS 159
Cdd:PRK13642 79 LRR----KIGMVFQNPDNQF-----VGATVEDDVAfgmENQGIPREEMIKRVDEALLAVNMLDFKTR---EPARLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 160 QRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAeTAQQVVVQYAGQQVEKNSAY 239
Cdd:PRK13642 147 QRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAA-SSDRILVMKAGEIIKEAAPS 225
|
...
gi 522049469 240 ELF 242
Cdd:PRK13642 226 ELF 228
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-185 |
8.18e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 73.60 E-value: 8.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQA-RITcdelvLDGKnllQLTATE 82
Cdd:COG4152 2 LELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSgEVL-----WDGE---PLDPED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 RRRlnggtvamifqepmtslnpcftVGYQIDE-------AVKTHV-------GGGRKERKEQVLSLLESVGIPDpaRRYD 148
Cdd:COG4152 70 RRR----------------------IGYLPEErglypkmKVGEQLvylarlkGLSKAEAKRRADEWLERLGLGD--RANK 125
|
170 180 190
....*....|....*....|....*....|....*..
gi 522049469 149 AYpHQMSGGMSQRAMIAMALAGQPKLLIADEPTTALD 185
Cdd:COG4152 126 KV-EELSKGNQQKVQLIAALLHDPELLILDEPFSGLD 161
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
21-231 |
9.05e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 72.21 E-value: 9.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 21 QAVEGINLTVNPNEILAIVGESGSGKSVamlaLMNLLPPQARITCDELVLDGKNLLQLTATE----RRRlnggtVAMIFQ 96
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKST----LLKLICGIERPSAGKIWFSGHDITRLKNREvpflRRQ-----IGMIFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 97 EPMTSLnpcftvgyqiDEAVKTHV-------GGGRKERKEQVLSLLESVGIPDPARRYdayPHQMSGGMSQRAMIAMALA 169
Cdd:PRK10908 87 DHHLLM----------DRTVYDNVaipliiaGASGDDIRRRVSAALDKVGLLDKAKNF---PIQLSGGEQQRVGIARAVV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522049469 170 GQPKLLIADEPTTALDvtvQAQILELLLKLQQQFQMG--LILITHDMGVVAETAQQVVVQYAGQ 231
Cdd:PRK10908 154 NKPAVLLADEPTGNLD---DALSEGILRLFEEFNRVGvtVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
28-226 |
2.22e-14 |
|
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: 70.98 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 28 LTVNPNEILAIVGESGSGKSVamlaLMNLLPPQARITCDELVLDGKNLLQLTATERrrlnggTVAMIFQEpmTSLNPCFT 107
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKST----LLNLIAGFETPQSGRVLINGVDVTAAPPADR------PVSMLFQE--NNLFAHLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 108 VGYQIDEAVKTHVGGgRKERKEQVLSLLESVGIPDPARRYdayPHQMSGGMSQRAMIAMALAGQPKLLIADEPTTALDVT 187
Cdd:cd03298 87 VEQNVGLGLSPGLKL-TAEDRQAIEVALARVGLAGLEKRL---PGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 522049469 188 VQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVV 226
Cdd:cd03298 163 LRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVF 201
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-232 |
2.29e-14 |
|
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: 69.94 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPTQNGWfqAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQAritcDELVLDGKNLLQLTATER 83
Cdd:cd03246 1 LEVENVSFRYPGAEPP--VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTS----GRVRLDGADISQWDPNEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 84 RRLnggtvamifqepmtslnpcftVGY--QIDEAVKThvgggrkerkeqvlSLLESVgipdparrydayphqMSGGMSQR 161
Cdd:cd03246 75 GDH---------------------VGYlpQDDELFSG--------------SIAENI---------------LSGGQRQR 104
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522049469 162 AMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMgLILITHDMGVVAEtAQQVVVQYAGQQ 232
Cdd:cd03246 105 LGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGAT-RIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
7-185 |
2.57e-14 |
|
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: 71.03 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 7 RNLSVAFPTQNGwFQAVEGINLTVNPNEILAIVGESGSGKSvamlALMNLL-----PPQARITcdelvLDGKNLLQLTAT 81
Cdd:cd03249 4 KNVSFRYPSRPD-VPILKGLSLTIPPGKTVALVGSSGCGKS----TVVSLLerfydPTSGEIL-----LDGVDIRDLNLR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 82 ERRRLnggtVAMIFQEPMtsLNPC---FTVGYQIDEAVKTHVgggrkerkEQVLSLLES----VGIPDparRYD----AY 150
Cdd:cd03249 74 WLRSQ----IGLVSQEPV--LFDGtiaENIRYGKPDATDEEV--------EEAAKKANIhdfiMSLPD---GYDtlvgER 136
|
170 180 190
....*....|....*....|....*....|....*
gi 522049469 151 PHQMSGGMSQRAMIAMALAGQPKLLIADEPTTALD 185
Cdd:cd03249 137 GSQLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-184 |
6.91e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.88 E-value: 6.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFPTqngwFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPP---QARITCDELVLDGKNLLQlt 79
Cdd:PRK13549 5 LLEMKNITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHgtyEGEIIFEGEELQASNIRD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 80 aTERRrlnggTVAMIFQEPMtsLNPCFTVGYQI---DEAVKthvgGGRKERKEQVL---SLLESVGIP-DPARRYDAYph 152
Cdd:PRK13549 79 -TERA-----GIAIIHQELA--LVKELSVLENIflgNEITP----GGIMDYDAMYLraqKLLAQLKLDiNPATPVGNL-- 144
|
170 180 190
....*....|....*....|....*....|..
gi 522049469 153 qmSGGMSQRAMIAMALAGQPKLLIADEPTTAL 184
Cdd:PRK13549 145 --GLGQQQLVEIAKALNKQARLLILDEPTASL 174
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-255 |
7.51e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 70.20 E-value: 7.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLAL--MNLLPPQARITCDeLVLDGKNLL--QL 78
Cdd:PRK14243 10 VLRTENLNVYY----GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGFRVEGK-VTFHGKNLYapDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 79 TATERRRlnggTVAMIFQEPmtslNPcFTVGYQIDEAVKTHVGGGRKERKEQVLSLLESVGIPDPAR-RYDAYPHQMSGG 157
Cdd:PRK14243 85 DPVEVRR----RIGMVFQKP----NP-FPKSIYDNIAYGARINGYKGDMDELVERSLRQAALWDEVKdKLKQSGLSLSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 158 MSQRAMIAMALAGQPKLLIADEPTTALDVTvqAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYA-------- 229
Cdd:PRK14243 156 QQQRLCIARAIAVQPEVILMDEPCSALDPI--STLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVeltegggr 233
|
250 260
....*....|....*....|....*..
gi 522049469 230 -GQQVEKNSAYELFNHPHHPYTAALLS 255
Cdd:PRK14243 234 yGYLVEFDRTEKIFNSPQQQATRDYVS 260
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
22-244 |
1.45e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 69.77 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 22 AVEGINLTVNPNEILAIVGESGSGKSVAMlALMN--LLPPQARITCDELVLDGKNLLQLTATERRRlnggtVAMIFQEPM 99
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIM-QLLNglHVPTQGSVRVDDTLITSTSKNKDIKQIRKK-----VGLVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 100 TSLnpcftvgyqIDEAVKTHVGGG------RKERKEQV-LSLLESVGIPDPArrYDAYPHQMSGGMSQRAMIAMALAGQP 172
Cdd:PRK13649 96 SQL---------FEETVLKDVAFGpqnfgvSQEEAEALaREKLALVGISESL--FEKNPFELSGGQMRRVAIAGILAMEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522049469 173 KLLIADEPTTALDVTVQaQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYELFNH 244
Cdd:PRK13649 165 KILVLDEPTAGLDPKGR-KELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-189 |
2.02e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 70.26 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MSLLSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPqariTCDELVLDGKNLLQLTA 80
Cdd:PRK09536 1 MPMIDVSDLSVEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTP----TAGTVLVAGDDVEALSA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 81 TERRRLnggtVAMIFQEpmTSLNPCFTVgYQIDEAVKT-HVG--GGRKERKEQVL-SLLESVGIpdpARRYDAYPHQMSG 156
Cdd:PRK09536 73 RAASRR----VASVPQD--TSLSFEFDV-RQVVEMGRTpHRSrfDTWTETDRAAVeRAMERTGV---AQFADRPVTSLSG 142
|
170 180 190
....*....|....*....|....*....|...
gi 522049469 157 GMSQRAMIAMALAGQPKLLIADEPTTALDVTVQ 189
Cdd:PRK09536 143 GERQRVLLARALAQATPVLLLDEPTASLDINHQ 175
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-190 |
2.16e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 68.89 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPTQNgwfqAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQAritcDELVLDGKNLLQLTATER 83
Cdd:PRK11231 3 LRTENLTVGYGTKR----ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQS----GTVFLGDKPISMLSSRQL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 84 RRlnggTVAMIFQEPMTSlnpcftvgyqidEAVKTH--VGGGR-----------KERKEQVLSLLESVGIPDPA-RRYDA 149
Cdd:PRK11231 75 AR----RLALLPQHHLTP------------EGITVRelVAYGRspwlslwgrlsAEDNARVNQAMEQTRINHLAdRRLTD 138
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 522049469 150 yphqMSGGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQA 190
Cdd:PRK11231 139 ----LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQV 175
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
17-242 |
2.19e-13 |
|
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: 68.41 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 17 NGWF------QAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQAritcDELVLDGKNLLQLTATERRRLnggt 90
Cdd:cd03254 7 NVNFsydekkPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQK----GQILIDGIDIRDISRKSLRSM---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 91 VAMIFQEPmtslnpcFTVGYQIDEAVKThvgGGRKERKEQVLSLLESVGIPDPARR----YDAYP----HQMSGGMSQRA 162
Cdd:cd03254 79 IGVVLQDT-------FLFSGTIMENIRL---GRPNATDEEVIEAAKEAGAHDFIMKlpngYDTVLgengGNLSQGERQLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 163 MIAMALAGQPKLLIADEPTTALDV----TVQAQILELLLKLQqqfqmgLILITHDMGVVAEtAQQVVVQYAGQQVEKNSA 238
Cdd:cd03254 149 AIARAMLRDPKILILDEATSNIDTetekLIQEALEKLMKGRT------SIIIAHRLSTIKN-ADKILVLDDGKIIEEGTH 221
|
....
gi 522049469 239 YELF 242
Cdd:cd03254 222 DELL 225
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-242 |
2.70e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 70.52 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPTQNGWFQaveGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQaritCDELVLDGKNLLQLTATER 83
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQ---NINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLT----EGEIRLDGRPLSSLSHSVL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 84 RRlnggTVAMIFQEPMTslnpcftvgyqIDEAVKTHVGGGRKERKEQVLSLLESVGIPDPARRYDAYPHQMSG------G 157
Cdd:PRK10790 414 RQ----GVAMVQQDPVV-----------LADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGeqgnnlS 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 158 MSQRAMIAMA--LAGQPKLLIADEPTTALDV-TVQAQILELLLKLQQQFqmgLILITHDMGVVAEtAQQVVVQYAGQQVE 234
Cdd:PRK10790 479 VGQKQLLALArvLVQTPQILILDEATANIDSgTEQAIQQALAAVREHTT---LVVIAHRLSTIVE-ADTILVLHRGQAVE 554
|
....*...
gi 522049469 235 KNSAYELF 242
Cdd:PRK10790 555 QGTHQQLL 562
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-185 |
3.30e-13 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 67.19 E-value: 3.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFP--TQNGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQAriTCDELVLDGKNLlqltat 81
Cdd:cd03213 4 LSFRNLTVTVKssPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLG--VSGEVLINGRPL------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 82 eRRRLNGGTVAMIFQEPMtsLNPCFTVgyqiDEAVkthvgggrkerkeqvlsllesvgipdparRYDAYPHQMSGGMSQR 161
Cdd:cd03213 76 -DKRSFRKIIGYVPQDDI--LHPTLTV----RETL-----------------------------MFAAKLRGLSGGERKR 119
|
170 180
....*....|....*....|....
gi 522049469 162 AMIAMALAGQPKLLIADEPTTALD 185
Cdd:cd03213 120 VSIALELVSNPSLLFLDEPTSGLD 143
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
11-244 |
3.77e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 68.24 E-value: 3.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 11 VAFPTQ-NGWFqAVEGINLTVNPNEILAIVGESGSGKS-VAMLALMNLLPPQARITCDELVLDGKNLlqltaTERRRlng 88
Cdd:PRK13648 13 VSFQYQsDASF-TLKDVSFNIPKGQWTSIVGHNGSGKStIAKLMIGIEKVKSGEIFYNNQAITDDNF-----EKLRK--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 89 gTVAMIFQEPMTSLnpcftVGyqidEAVKTHVGGG-------RKERKEQVLSLLESVGIPDPArryDAYPHQMSGGMSQR 161
Cdd:PRK13648 84 -HIGIVFQNPDNQF-----VG----SIVKYDVAFGlenhavpYDEMHRRVSEALKQVDMLERA---DYEPNALSGGQKQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 162 AMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAEtAQQVVVQYAGQQVEKNSAYEL 241
Cdd:PRK13648 151 VAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
...
gi 522049469 242 FNH 244
Cdd:PRK13648 230 FDH 232
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-185 |
5.61e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 67.30 E-value: 5.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 27 NLTVNPNEILAIVGESGSGKSvAMLALM-NLLPPqariTCDELVLDGKNLlQLTATERRrlnggTVAMIFQEpmTSLNPC 105
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKS-TLLNLIaGFLTP----ASGSLTLNGQDH-TTTPPSRR-----PVSMLFQE--NNLFSH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 106 FTVGYQI----DEAVK-THvgggrkERKEQVLSLLESVGIPDPARRYdayPHQMSGGMSQRAMIAMALAGQPKLLIADEP 180
Cdd:PRK10771 86 LTVAQNIglglNPGLKlNA------AQREKLHAIARQMGIEDLLARL---PGQLSGGQRQRVALARCLVREQPILLLDEP 156
|
....*
gi 522049469 181 TTALD 185
Cdd:PRK10771 157 FSALD 161
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
6-243 |
5.77e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 68.19 E-value: 5.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 6 VRNLSVAFPTQNGW-FQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPP--------------QARITCDELVL 70
Cdd:PRK13651 5 VKNIVKIFNKKLPTeLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPdtgtiewifkdeknKKKTKEKEKVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 71 DgKNLLQLTATE--------RRRlnggtVAMIFQepmtslnpcFTvGYQIDEAV--------KTHVGGGRKERKEQVLSL 134
Cdd:PRK13651 85 E-KLVIQKTRFKkikkikeiRRR-----VGVVFQ---------FA-EYQLFEQTiekdiifgPVSMGVSKEEAKKRAAKY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 135 LESVGIPDparRY-DAYPHQMSGGMSQRAMIAMALAGQPKLLIADEPTTALDvtvQAQILELLLKLQQQFQMG--LILIT 211
Cdd:PRK13651 149 IELVGLDE---SYlQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLD---PQGVKEILEIFDNLNKQGktIILVT 222
|
250 260 270
....*....|....*....|....*....|..
gi 522049469 212 HDMGVVAETAQQVVVQYAGQQVEKNSAYELFN 243
Cdd:PRK13651 223 HDLDNVLEWTKRTIFFKDGKIIKDGDTYDILS 254
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
21-242 |
6.10e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 68.22 E-value: 6.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 21 QAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLL-PPQARITCDELVLDGKNLLQLTATERRRlnggtVAMIFQEPM 99
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLqPTEGKVTVGDIVVSSTSKQKEIKPVRKK-----VGVVFQFPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 100 TSLnpcFTVGYQIDEAVKTHVGGGRKERKEQVLS-LLESVGIPDpaRRYDAYPHQMSGGMSQRAMIAMALAGQPKLLIAD 178
Cdd:PRK13643 95 SQL---FEETVLKDVAFGPQNFGIPKEKAEKIAAeKLEMVGLAD--EFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522049469 179 EPTTALDVTVQAQILELLLKLQQQFQMgLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYELF 242
Cdd:PRK13643 170 EPTAGLDPKARIEMMQLFESIHQSGQT-VVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
22-241 |
7.34e-13 |
|
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: 67.13 E-value: 7.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 22 AVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPP-QARItcdelVLDGKNLLQLTATERRRlnggTVAMIFQEpmt 100
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPeNGRV-----LVDGHDLALADPAWLRR----QVGVVLQE--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 101 slNPCFTvgYQIDEAVKTHVGGGRKERKEQVLSLLESVG-IPDPARRYDAYPHQ----MSGGMSQRAMIAMALAGQPKLL 175
Cdd:cd03252 85 --NVLFN--RSIRDNIALADPGMSMERVIEAAKLAGAHDfISELPEGYDTIVGEqgagLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522049469 176 IADEPTTALDvtVQAQILELLLKLQQQFQMGLILITHDMGVVaETAQQVVVQYAGQQVEKNSAYEL 241
Cdd:cd03252 161 IFDEATSALD--YESEHAIMRNMHDICAGRTVIIIAHRLSTV-KNADRIIVMEKGRIVEQGSHDEL 223
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-185 |
7.64e-13 |
|
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: 66.84 E-value: 7.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 6 VRNLSVAFPTQNGwfQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQAritcDELVLDGKNLLQLTATERRR 85
Cdd:cd03245 5 FRNVSFSYPNQEI--PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTS----GSVLLDGTDIRQLDPADLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 86 lNGGTVAmifQEPMT---SLNPCFTVGYQIDEavkthvgggrkerKEQVLSLLESVGIPDPARRYdayPH---------- 152
Cdd:cd03245 79 -NIGYVP---QDVTLfygTLRDNITLGAPLAD-------------DERILRAAELAGVTDFVNKH---PNgldlqigerg 138
|
170 180 190
....*....|....*....|....*....|....
gi 522049469 153 -QMSGGMSQRAMIAMALAGQPKLLIADEPTTALD 185
Cdd:cd03245 139 rGLSGGQRQAVALARALLNDPPILLLDEPTSAMD 172
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
22-185 |
8.95e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 65.72 E-value: 8.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 22 AVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPqaritcdelvldgknllqlTATERRRLNGGTVAMIFQEpmTS 101
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRP-------------------TSGTVRRAGGARVAYVPQR--SE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 102 LNPCF--TVgyqiDEAVK----THVGGGRKERKEQVLSL---LESVGIPDPA-RRYDAyphqMSGGMSQRAMIAMALAGQ 171
Cdd:NF040873 66 VPDSLplTV----RDLVAmgrwARRGLWRRLTRDDRAAVddaLERVGLADLAgRQLGE----LSGGQRQRALLAQGLAQE 137
|
170
....*....|....
gi 522049469 172 PKLLIADEPTTALD 185
Cdd:NF040873 138 ADLLLLDEPTTGLD 151
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-243 |
1.05e-12 |
|
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: 68.29 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSVamlaLMNLL-------PPQARIT-----CDE---- 67
Cdd:TIGR03269 1 IEVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSV----LMHVLrgmdqyePTSGRIIyhvalCEKcgyv 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 68 ----------------LVLDGKNLLQLTATERRRLNGgTVAMIFQEP-------------MTSLNpcfTVGYQIDEAVKt 118
Cdd:TIGR03269 73 erpskvgepcpvcggtLEPEEVDFWNLSDKLRRRIRK-RIAIMLQRTfalygddtvldnvLEALE---EIGYEGKEAVG- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 119 hvgggrkerkeQVLSLLESVGIpdpARRYDAYPHQMSGGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLK 198
Cdd:TIGR03269 148 -----------RAVDLIEMVQL---SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEE 213
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 522049469 199 LQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYELFN 243
Cdd:TIGR03269 214 AVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-237 |
1.19e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 67.10 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MSLLSVRNLSVAfptqNGWFQAVEGINLTVNPNEILAIVGESGSGKSVamlaLMNLLPPQARITCDELVLDGKNLLQLTa 80
Cdd:PRK11831 5 ANLVDMRGVSFT----RGNRCIFDNISLTVPRGKITAIMGPSGIGKTT----LLRLIGGQIAPDHGEILFDGENIPAMS- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 81 teRRRLNGG--TVAMIFQEP--MTSLNPCFTVGYQIDEavktHVGGGRKERKEQVLSLLESVGIPDPArryDAYPHQMSG 156
Cdd:PRK11831 76 --RSRLYTVrkRMSMLFQSGalFTDMNVFDNVAYPLRE----HTQLPAPLLHSTVMMKLEAVGLRGAA---KLMPSELSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 157 GMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETA--------QQVVVQY 228
Cdd:PRK11831 147 GMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIAdhayivadKKIVAHG 226
|
....*....
gi 522049469 229 AGQQVEKNS 237
Cdd:PRK11831 227 SAQALQANP 235
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
23-245 |
1.32e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 67.44 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 23 VEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPqariTCDELVLDGKNLLQLTATERrrlnggTVAMIFQEpmTSL 102
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKP----TEGQIFIDGEDVTHRSIQQR------DICMVFQS--YAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 103 NPCFTVGYQIDEAVKThVGGGRKERKEQVLSLLESVgipDPARRYDAYPHQMSGGMSQRAMIAMALAGQPKLLIADEPTT 182
Cdd:PRK11432 90 FPHMSLGENVGYGLKM-LGVPKEERKQRVKEALELV---DLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522049469 183 ALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYELFNHP 245
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-186 |
1.86e-12 |
|
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: 65.88 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MSLLSVRNLSVAFPTQngwfQAVEGINLTVNPNEILAIVGESGSGKSvAMLALMN-LLPPqarITCDELVLDGKNLLQLT 79
Cdd:COG1119 1 DPLLELRNVTVRRGGK----TILDDISWTVKPGEHWAILGPNGAGKS-TLLSLITgDLPP---TYGNDVRLFGERRGGED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 80 ATE-RRRLngGTVAMIFQEPMTSLNPCFTV---GY--------QIDEavkthvgggrkERKEQVLSLLESVGIPDPA-RR 146
Cdd:COG1119 73 VWElRKRI--GLVSPALQLRFPRDETVLDVvlsGFfdsiglyrEPTD-----------EQRERARELLELLGLAHLAdRP 139
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 522049469 147 YdaypHQMSGGMSQRAMIAMALAGQPKLLIADEPTTALDV 186
Cdd:COG1119 140 F----GTLSQGEQRRVLIARALVKDPELLILDEPTAGLDL 175
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-185 |
2.28e-12 |
|
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: 65.64 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPTQngwfQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPP-QARItcdelVLDGKNLLQLTATE 82
Cdd:cd03218 1 LRAENLSKRYGKR----KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPdSGKI-----LLDGQDITKLPMHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 RRRLNGGTVAmifQEPmtSLNPCFTVGYQIDEAVKTHvGGGRKERKEQVLSLLESVGIpDPARRYDAYphQMSGGMSQRA 162
Cdd:cd03218 72 RARLGIGYLP---QEA--SIFRKLTVEENILAVLEIR-GLSKKEREEKLEELLEEFHI-THLRKSKAS--SLSGGERRRV 142
|
170 180
....*....|....*....|...
gi 522049469 163 MIAMALAGQPKLLIADEPTTALD 185
Cdd:cd03218 143 EIARALATNPKFLLLDEPFAGVD 165
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-184 |
3.00e-12 |
|
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: 67.16 E-value: 3.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQariTCD-ELVLDGKnllQLTAT 81
Cdd:TIGR02633 1 LLEMKGIVKTF----GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHG---TWDgEIYWSGS---PLKAS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 82 ERRRLNGGTVAMIFQEPMtsLNPCFTVGYQIDEAVKTHVGGGRKERKEQVL---SLLESVGIP-DPARRYDAyphQMSGG 157
Cdd:TIGR02633 71 NIRDTERAGIVIIHQELT--LVPELSVAENIFLGNEITLPGGRMAYNAMYLrakNLLRELQLDaDNVTRPVG---DYGGG 145
|
170 180
....*....|....*....|....*..
gi 522049469 158 MSQRAMIAMALAGQPKLLIADEPTTAL 184
Cdd:TIGR02633 146 QQQLVEIAKALNKQARLLILDEPSSSL 172
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
7-190 |
3.11e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 67.29 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 7 RNLSVAFPtqnGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQA-RITcdelvLDGKNLLQLTATERRR 85
Cdd:PRK13657 338 DDVSFSYD---NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSgRIL-----IDGTDIRTVTRASLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 86 lNGGTVamiFQEPMTsLNPCFTVGYQIDEAVKTHVGGGRKERKEQVLSLLEsvgipdpaRRYDAYP-------HQMSGGM 158
Cdd:PRK13657 410 -NIAVV---FQDAGL-FNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIE--------RKPDGYDtvvgergRQLSGGE 476
|
170 180 190
....*....|....*....|....*....|..
gi 522049469 159 SQRAMIAMALAGQPKLLIADEPTTALDVTVQA 190
Cdd:PRK13657 477 RQRLAIARALLKDPPILILDEATSALDVETEA 508
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
25-188 |
5.02e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.21 E-value: 5.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 25 GINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQARITCDElVLDGKnllqltaterrrlnggtvamifqepmtslnp 104
Cdd:COG2401 48 DLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-VPDNQ------------------------------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 105 cFTVGYQIDEAVkthvggGRKERKEQVLSLLESVGIPDPA---RRYDayphQMSGGMSQRAMIAMALAGQPKLLIADEPT 181
Cdd:COG2401 96 -FGREASLIDAI------GRKGDFKDAVELLNAVGLSDAVlwlRRFK----ELSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
....*..
gi 522049469 182 TALDVTV 188
Cdd:COG2401 165 SHLDRQT 171
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-186 |
6.42e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.81 E-value: 6.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAfptqngwfQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQAritcDELVLDGKNLLQLTA-- 80
Cdd:COG1129 256 VLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADS----GEIRLDGKPVRIRSPrd 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 81 ---------TERRRLNGgtvamifqepmtsLNPCFTVGYQIDEAV-KTHVGGG---RKERKEQVLSLLESVGI--PDPAR 145
Cdd:COG1129 324 airagiayvPEDRKGEG-------------LVLDLSIRENITLASlDRLSRGGlldRRRERALAEEYIKRLRIktPSPEQ 390
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 522049469 146 RYDayphQMSGGMSQRAMIAMALAGQPKLLIADEPTTALDV 186
Cdd:COG1129 391 PVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDV 427
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
18-241 |
7.53e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 64.62 E-value: 7.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 18 GWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQAritcDELVLDGKNLLQLTATERRRlnggTVAMIFQE 97
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAH----GHVWLDGEHIQHYASKEVAR----RIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 98 PMTSLNpcFTVGYQIDEAVKTH---VGGGRKERKEQVLSLLESVGIPDPARRydaYPHQMSGGMSQRAMIAMALAGQPKL 174
Cdd:PRK10253 90 ATTPGD--ITVQELVARGRYPHqplFTRWRKEDEEAVTKAMQATGITHLADQ---SVDTLSGGQRQRAWIAMVLAQETAI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522049469 175 LIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYEL 241
Cdd:PRK10253 165 MLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
26-186 |
7.89e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 65.28 E-value: 7.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 26 INLTVNPNEILAIVGESGSGKSvamlALMNLL-----PPQARITCDELVL-DGKNLLQLtATERRRlnggtVAMIFQEpm 99
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKT----SLINAIsgltrPQKGRIVLNGRVLfDAEKGICL-PPEKRR-----IGYVFQD-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 100 TSLNPCFTVG----YqideavkthvgGGRKERKEQVLSLLESVGIPDPARRYdayPHQMSGGMSQRAMIAMALAGQPKLL 175
Cdd:PRK11144 85 ARLFPHYKVRgnlrY-----------GMAKSMVAQFDKIVALLGIEPLLDRY---PGSLSGGEKQRVAIGRALLTAPELL 150
|
170
....*....|.
gi 522049469 176 IADEPTTALDV 186
Cdd:PRK11144 151 LMDEPLASLDL 161
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
22-226 |
8.02e-12 |
|
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: 63.89 E-value: 8.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 22 AVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPqariTCDELVLDGknllqLTATERRRLNGGTVAMIFQE---- 97
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQP----TSGEVRVAG-----LVPWKRRKKFLRRIGVVFGQktql 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 98 -----PMTSLNPCFTVgYQIDEAvkthvggGRKERKEQVLSLLESVGIPD-PARrydayphQMSGGMSQRAMIAMALAGQ 171
Cdd:cd03267 107 wwdlpVIDSFYLLAAI-YDLPPA-------RFKKRLDELSELLDLEELLDtPVR-------QLSLGQRMRAEIAAALLHE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 522049469 172 PKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVV 226
Cdd:cd03267 172 PEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLV 226
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-185 |
9.44e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 63.76 E-value: 9.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MSLLSVRNLSVAFPTQngwfQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQA-RITCDElvlDGKNLLQLT 79
Cdd:PRK10895 1 MATLTAKNLAKAYKGR----RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAgNIIIDD---EDISLLPLH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 80 ATERRrlnggTVAMIFQEPmtSLNPCFTVGYQIDEAVKTHVGGGRKERKEQVLSLLESVGIpdpARRYDAYPHQMSGGMS 159
Cdd:PRK10895 74 ARARR-----GIGYLPQEA--SIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHI---EHLRDSMGQSLSGGER 143
|
170 180
....*....|....*....|....*.
gi 522049469 160 QRAMIAMALAGQPKLLIADEPTTALD 185
Cdd:PRK10895 144 RRVEIARALAANPKFILLDEPFAGVD 169
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-185 |
1.08e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 63.95 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAF----PTQNgwfQAVEGINLTVNPNEILAIVGESGSGKSvamlALMNLLPPQARITCDELVLDGKNLLQLT 79
Cdd:COG1101 2 LELKNLSKTFnpgtVNEK---RALDGLNLTIEEGDFVTVIGSNGAGKS----TLLNAIAGSLPPDSGSILIDGKDVTKLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 80 ATERRRLnggtVAMIFQEPMTSLNPCFTvgyqIDE--AVKTHVGGGR-------KERKEQVLSLLESV--GIPDparRYD 148
Cdd:COG1101 75 EYKRAKY----IGRVFQDPMMGTAPSMT----IEEnlALAYRRGKRRglrrgltKKRRELFRELLATLglGLEN---RLD 143
|
170 180 190
....*....|....*....|....*....|....*....
gi 522049469 149 AYPHQMSGGmsQRAMIA--MALAGQPKLLIADEPTTALD 185
Cdd:COG1101 144 TKVGLLSGG--QRQALSllMATLTKPKLLLLDEHTAALD 180
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
25-190 |
1.87e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 62.94 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 25 GINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQARITcdelvLDGKNLLQLTATE--RRRlnggtvAMIFQEPMTSL 102
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQGEIL-----LNGRPLSDWSAAElaRHR------AYLSQQQSPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 103 N-PCF---TVGYQideavkthvGGGRKERKEQVLS-LLESVGIPDPARRydayP-HQMSGGMSQRAMIAMALA------- 169
Cdd:COG4138 83 AmPVFqylALHQP---------AGASSEAVEQLLAqLAEALGLEDKLSR----PlTQLSGGEWQRVRLAAVLLqvwptin 149
|
170 180
....*....|....*....|.
gi 522049469 170 GQPKLLIADEPTTALDVTVQA 190
Cdd:COG4138 150 PEGQLLLLDEPMNSLDVAQQA 170
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-185 |
1.87e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 63.12 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MSLLSVRNLSVAFPTQngwfQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQA-RITcdelvLDGKNLLQLT 79
Cdd:COG1137 1 MMTLEAENLVKSYGKR----TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSgRIF-----LDGEDITHLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 80 ATERRRLNGGTVAmifQEPmtSLnpcF---TVGYQIdEAVKTHVGGGRKERKEQVLSLLESVGIpdpARRYDAYPHQMSG 156
Cdd:COG1137 72 MHKRARLGIGYLP---QEA--SI---FrklTVEDNI-LAVLELRKLSKKEREERLEELLEEFGI---THLRKSKAYSLSG 139
|
170 180
....*....|....*....|....*....
gi 522049469 157 GMSQRAMIAMALAGQPKLLIADEPTTALD 185
Cdd:COG1137 140 GERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
3-245 |
3.53e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 62.31 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSVamlaLMNLLPPQARITCDELVLDGKNLLQLTATE 82
Cdd:PRK11300 5 LLSVSGLMMRF----GGLLAVNNVNLEVREQEIVSLIGPNGAGKTT----VFNCLTGFYKPTGGTILLRGQHIEGLPGHQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 RRRLngGTV-----AMIFQEpMTSLNPCFTVGYQideAVKTHVGGG--------RKERK--EQVLSLLESVGIPDPARRY 147
Cdd:PRK11300 77 IARM--GVVrtfqhVRLFRE-MTVIENLLVAQHQ---QLKTGLFSGllktpafrRAESEalDRAATWLERVGLLEHANRQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 148 D---AYPHQmsggmsQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQV 224
Cdd:PRK11300 151 AgnlAYGQQ------RRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRI 224
|
250 260
....*....|....*....|.
gi 522049469 225 VVQYAGQQVEKNSAYELFNHP 245
Cdd:PRK11300 225 YVVNQGTPLANGTPEEIRNNP 245
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-185 |
3.71e-11 |
|
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: 61.18 E-value: 3.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPTQNGWfqAVEGINLTVNPNEILAIVGESGSGKS-VAMLALMNLLPPQARITcdelvLDGKNLLQLTATE 82
Cdd:cd03247 1 LSINNVSFSYPEQEQQ--VLKNLSLELKQGEKIALLGRSGSGKStLLQLLTGDLKPQQGEIT-----LDGVPVSDLEKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 RRrlnggTVAMIFQEPmtslnpcftvgYQIDEavkthvgggrkerkeqvlSLLESVGIpdparrydayphQMSGGMSQRA 162
Cdd:cd03247 74 SS-----LISVLNQRP-----------YLFDT------------------TLRNNLGR------------RFSGGERQRL 107
|
170 180
....*....|....*....|...
gi 522049469 163 MIAMALAGQPKLLIADEPTTALD 185
Cdd:cd03247 108 ALARILLQDAPIVLLDEPTVGLD 130
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-185 |
4.18e-11 |
|
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: 61.86 E-value: 4.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPTQNGWfqAVEGINLTVNPNEILAIVGESGSGKSVamlaLMNLLPPQARITCDELVLDGKNLLQLTATER 83
Cdd:cd03251 1 VEFKNVTFRYPGDGPP--VLRDISLDIPAGETVALVGPSGSGKST----LVNLIPRFYDVDSGRILIDGHDVRDYTLASL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 84 RRLnggtVAMIFQEPmtslnpcftvgYQIDEAVKTHVGGGRKE-RKEQVLSLLESVGIPDPARR----YDAY----PHQM 154
Cdd:cd03251 75 RRQ----IGLVSQDV-----------FLFNDTVAENIAYGRPGaTREEVEEAARAANAHEFIMElpegYDTVigerGVKL 139
|
170 180 190
....*....|....*....|....*....|.
gi 522049469 155 SGGMSQRAMIAMALAGQPKLLIADEPTTALD 185
Cdd:cd03251 140 SGGQRQRIAIARALLKDPPILILDEATSALD 170
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
25-185 |
6.64e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 61.62 E-value: 6.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 25 GINLTVNPNEILAIVGESGSGKSvamlALMNLLPPQARITCDELvLDGKNLLQlTATERRRlnggtvaMIFQEpmTSLNP 104
Cdd:PRK11247 30 QLDLHIPAGQFVAVVGRSGCGKS----TLLRLLAGLETPSAGEL-LAGTAPLA-EAREDTR-------LMFQD--ARLLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 105 CFTVgyqIDeavktHVGGG-RKERKEQVLSLLESVGIPDparRYDAYPHQMSGGMSQRAMIAMALAGQPKLLIADEPTTA 183
Cdd:PRK11247 95 WKKV---ID-----NVGLGlKGQWRDAALQALAAVGLAD---RANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
..
gi 522049469 184 LD 185
Cdd:PRK11247 164 LD 165
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-185 |
7.86e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 61.54 E-value: 7.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFPTQNgwfQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQAritcdelvldGKNLLQ-LTAT 81
Cdd:PRK13644 1 MIRLENVSYSYPDGT---PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQK----------GKVLVSgIDTG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 82 ERRRLNG--GTVAMIFQEPMTSLnpcftVGYQIDEAVK---THVGGGRKERKEQVLSLLESVGIPDpaRRYDAyPHQMSG 156
Cdd:PRK13644 68 DFSKLQGirKLVGIVFQNPETQF-----VGRTVEEDLAfgpENLCLPPIEIRKRVDRALAEIGLEK--YRHRS-PKTLSG 139
|
170 180
....*....|....*....|....*....
gi 522049469 157 GMSQRAMIAMALAGQPKLLIADEPTTALD 185
Cdd:PRK13644 140 GQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
31-185 |
8.69e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 62.76 E-value: 8.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 31 NPNEILAIVGESGSGKSVAMLALMNLLPPQARITCDeLVLDGKnllQLTATERRRLNggtvAMIFQEPMtsLNPCFTVgy 110
Cdd:TIGR00955 49 KPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGS-VLLNGM---PIDAKEMRAIS----AYVQQDDL--FIPTLTV-- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 111 qiDEA--VKTHVGGGR----KERKEQVLSLLESVGIPDPARRYDAYPHQM---SGGMSQRAMIAMALAGQPKLLIADEPT 181
Cdd:TIGR00955 117 --REHlmFQAHLRMPRrvtkKEKRERVDEVLQALGLRKCANTRIGVPGRVkglSGGERKRLAFASELLTDPPLLFCDEPT 194
|
....
gi 522049469 182 TALD 185
Cdd:TIGR00955 195 SGLD 198
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-242 |
1.43e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 60.79 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 15 TQNGWF-----QAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQAritcDELVLDGKnllQLTATERRRLN-G 88
Cdd:PRK13638 4 TSDLWFryqdePVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQK----GAVLWQGK---PLDYSKRGLLAlR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 89 GTVAMIFQEPMTSLnpcFTVGYQIDEAVK-THVGGGRKE---RKEQVLSLLEsvgipdpARRYDAYPHQ-MSGGMSQRAM 163
Cdd:PRK13638 77 QQVATVFQDPEQQI---FYTDIDSDIAFSlRNLGVPEAEitrRVDEALTLVD-------AQHFRHQPIQcLSHGQKKRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522049469 164 IAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMgLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYELF 242
Cdd:PRK13638 147 IAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNH-VIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-251 |
1.68e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 61.20 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MSLLSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSVamlaLMNLLPPQARITCDELVLDGKNLLQLTA 80
Cdd:PRK11000 1 MASVTLRNVTKAY----GDVVISKDINLDIHEGEFVVFVGPSGCGKST----LLRMIAGLEDITSGDLFIGEKRMNDVPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 81 TERrrlnggTVAMIFQE----PMTSLNPCFTVGYQIDEAVKTHvgggRKERKEQVLSLLESvgipdpARRYDAYPHQMSG 156
Cdd:PRK11000 73 AER------GVGMVFQSyalyPHLSVAENMSFGLKLAGAKKEE----INQRVNQVAEVLQL------AHLLDRKPKALSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 157 GMSQRAMIAMALAGQPKLLIADEPTTALD--VTVQAQILELLLKLQQQFQMglILITHDMgVVAET-AQQVVVQYAGQ-- 231
Cdd:PRK11000 137 GQRQRVAIGRTLVAEPSVFLLDEPLSNLDaaLRVQMRIEISRLHKRLGRTM--IYVTHDQ-VEAMTlADKIVVLDAGRva 213
|
250 260
....*....|....*....|
gi 522049469 232 QVEKnsAYELFNHPHHPYTA 251
Cdd:PRK11000 214 QVGK--PLELYHYPANRFVA 231
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
13-185 |
2.01e-10 |
|
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: 59.98 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 13 FPTQNGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQARITcDELVLDGKNLLQLTATERrrlnggtVA 92
Cdd:cd03234 13 AKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTS-GQILFNGQPRKPDQFQKC-------VA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 93 MIFQEpmTSLNPCFTVGYQIDEAVktHVGGGRKERKEQVLSLLESVGIPDPA--RRYDAYPHQMSGGMSQRAMIAMALAG 170
Cdd:cd03234 85 YVRQD--DILLPGLTVRETLTYTA--ILRLPRKSSDAIRKKRVEDVLLRDLAltRIGGNLVKGISGGERRRVSIAVQLLW 160
|
170
....*....|....*
gi 522049469 171 QPKLLIADEPTTALD 185
Cdd:cd03234 161 DPKVLILDEPTSGLD 175
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
4-185 |
2.48e-10 |
|
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: 61.30 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPTQNGwfQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQA---RitcdelvLDGKNLLQLTA 80
Cdd:COG4618 331 LSVENLTVVPPGSKR--PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAgsvR-------LDGADLSQWDR 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 81 TERRRLNG----------GTVAM-I--FQEPmtslNPcftvgYQIDEAVKT---HvgggrkerkEQVLSLlesvgiPDpa 144
Cdd:COG4618 402 EELGRHIGylpqdvelfdGTIAEnIarFGDA----DP-----EKVVAAAKLagvH---------EMILRL------PD-- 455
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 522049469 145 rRYD----AYPHQMSGGMSQRAMIAMALAGQPKLLIADEPTTALD 185
Cdd:COG4618 456 -GYDtrigEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLD 499
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-185 |
3.17e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 59.64 E-value: 3.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 2 SLLSVRNLSVAFpTQNgwfQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLlppqarITCDELVLDGKNLLQLTAT 81
Cdd:PRK09984 3 TIIRVEKLAKTF-NQH---QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL------ITGDKSAGSHIELLGRTVQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 82 ERRRLNG------GTVAMIFQE-----PMTSLNPCFTVGYQIDEAVKTHVGGGRKERKEQVLSLLESVGIPDparrydaY 150
Cdd:PRK09984 73 REGRLARdirksrANTGYIFQQfnlvnRLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALTRVGMVH-------F 145
|
170 180 190
....*....|....*....|....*....|....*....
gi 522049469 151 PHQ----MSGGMSQRAMIAMALAGQPKLLIADEPTTALD 185
Cdd:PRK09984 146 AHQrvstLSGGQQQRVAIARALMQQAKVILADEPIASLD 184
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
23-185 |
4.48e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 59.82 E-value: 4.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 23 VEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQARIT--CDELVldgknllqltaTERRRLNGGTVAMIFQepMT 100
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSIslCGEPV-----------PSRARHARQRVGVVPQ--FD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 101 SLNPCFTVGYQIdEAVKTHVGGGRKERKEQVLSLLESVGIPDPArryDAYPHQMSGGMSQRAMIAMALAGQPKLLIADEP 180
Cdd:PRK13537 90 NLDPDFTVRENL-LVFGRYFGLSAAAARALVPPLLEFAKLENKA---DAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165
|
....*
gi 522049469 181 TTALD 185
Cdd:PRK13537 166 TTGLD 170
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-186 |
5.73e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.02 E-value: 5.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAfptqngwfqAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPpqarITCDELVLDGKNLLQLTA--- 80
Cdd:PRK10762 258 LKVDNLSGP---------GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALP----RTSGYVTLDGHEVVTRSPqdg 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 81 --------TERRRLNGGTVAMIFQEPM--TSLNPCFTVGYQIDeavkthvgggRKERKEQVLSLLESVGIPDPARryDAY 150
Cdd:PRK10762 325 langivyiSEDRKRDGLVLGMSVKENMslTALRYFSRAGGSLK----------HADEQQAVSDFIRLFNIKTPSM--EQA 392
|
170 180 190
....*....|....*....|....*....|....*.
gi 522049469 151 PHQMSGGMSQRAMIAMALAGQPKLLIADEPTTALDV 186
Cdd:PRK10762 393 IGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDV 428
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-185 |
6.59e-10 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 58.56 E-value: 6.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 5 SVRNLSVAFPTQngwfQAVEGINLTVNPNEILAIVGESGSGKSvAMLALMN-LLPPQA-RITcdelvLDGKNLLQLTATE 82
Cdd:COG4604 3 EIKNVSKRYGGK----VVLDDVSLTIPKGGITALIGPNGAGKS-TLLSMISrLLPPDSgEVL-----VDGLDVATTPSRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 RRRlnggTVAMIFQEPmtSLNPCFTVgyqideavKTHVGGGR---------KERKEQVLSLLESVGIPDPARRY-Dayph 152
Cdd:COG4604 73 LAK----RLAILRQEN--HINSRLTV--------RELVAFGRfpyskgrltAEDREIIDEAIAYLDLEDLADRYlD---- 134
|
170 180 190
....*....|....*....|....*....|...
gi 522049469 153 QMSGGMSQRAMIAMALAGQPKLLIADEPTTALD 185
Cdd:COG4604 135 ELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLD 167
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
23-185 |
7.45e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 59.07 E-value: 7.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 23 VEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQA-RITcdelvldgknLLQLTATERRRLNGGTVAMIFQepMTS 101
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAgKIT----------VLGVPVPARARLARARIGVVPQ--FDN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 102 LNPCFTVGYQIdEAVKTHVGGGRKERKEQVLSLLESVGIPDPArryDAYPHQMSGGMSQRAMIAMALAGQPKLLIADEPT 181
Cdd:PRK13536 125 LDLEFTVRENL-LVFGRYFGMSTREIEAVIPSLLEFARLESKA---DARVSDLSGGMKRRLTLARALINDPQLLILDEPT 200
|
....
gi 522049469 182 TALD 185
Cdd:PRK13536 201 TGLD 204
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
7-243 |
1.76e-09 |
|
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: 57.24 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 7 RNLSVAFPTQngwFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQA-RITcdelvLDGKNLLQLTATERRR 85
Cdd:cd03253 4 ENVTFAYDPG---RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSgSIL-----IDGQDIREVTLDSLRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 86 lnggTVAMIFQEpmTSLnpcF--TVGYQIdeavkthvGGGR-KERKEQVLSLLESVGIPDPARRY-DAYPHQ-------M 154
Cdd:cd03253 76 ----AIGVVPQD--TVL---FndTIGYNI--------RYGRpDATDEEVIEAAKAAQIHDKIMRFpDGYDTIvgerglkL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 155 SGGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQmgLILITHDMGVVAeTAQQVVVQYAGQQVE 234
Cdd:cd03253 139 SGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRT--TIVIAHRLSTIV-NADKIIVLKDGRIVE 215
|
....*....
gi 522049469 235 KNSAYELFN 243
Cdd:cd03253 216 RGTHEELLA 224
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-100 |
2.89e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 56.57 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 2 SLLSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSVamLALMNLLPPQARITCDELVLDGKNLLQLTAT 81
Cdd:CHL00131 6 PILEIKNLHASV----NENEILKGLNLSINKGEIHAIMGPNGSGKST--LSKVIAGHPAYKILEGDILFKGESILDLEPE 79
|
90
....*....|....*....
gi 522049469 82 ERRRLNggtVAMIFQEPMT 100
Cdd:CHL00131 80 ERAHLG---IFLAFQYPIE 95
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-186 |
3.00e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 56.72 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFPTQngwfQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNllPPQARITCDELVLDGKNLLQLTATE 82
Cdd:PRK09580 1 MLSIKDLHVSVEDK----AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG--REDYEVTGGTVEFKGKDLLELSPED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 RRrlnGGTVAMIFQEPMTslnpcfTVGYQIDEAVKTHVGGGRKERKEQVLSLLESVGIPDPARRYDAYPHQM-------- 154
Cdd:PRK09580 75 RA---GEGIFMAFQYPVE------IPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLltrsvnvg 145
|
170 180 190
....*....|....*....|....*....|...
gi 522049469 155 -SGGMSQRAMIAMALAGQPKLLIADEPTTALDV 186
Cdd:PRK09580 146 fSGGEKKRNDILQMAVLEPELCILDESDSGLDI 178
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-225 |
4.72e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 56.28 E-value: 4.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MSLLSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLL---------PPQARI--TCDELV 69
Cdd:PRK09544 2 TSLVSLENVSVSF----GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVapdegvikrNGKLRIgyVPQKLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 70 LDGKnlLQLTATERRRLNGGTvamifqepmtslnpcftvgyqideavkthvgggrkeRKEQVLSLLESVgipDPARRYDA 149
Cdd:PRK09544 78 LDTT--LPLTVNRFLRLRPGT------------------------------------KKEDILPALKRV---QAGHLIDA 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522049469 150 YPHQMSGGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVV 225
Cdd:PRK09544 117 PMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-184 |
6.43e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 56.72 E-value: 6.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFPTqngwFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPqariTCDELVLDGKNLLQLTATE 82
Cdd:PRK09700 5 YISMAGIGKSFGP----VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEP----TKGTITINNINYNKLDHKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 RRRLNggtVAMIFQEpmtslnpcFTVgyqIDE-AVKTHVGGGR--------------KERKEQVLSLLESVGIpdpARRY 147
Cdd:PRK09700 77 AAQLG---IGIIYQE--------LSV---IDElTVLENLYIGRhltkkvcgvniidwREMRVRAAMMLLRVGL---KVDL 139
|
170 180 190
....*....|....*....|....*....|....*..
gi 522049469 148 DAYPHQMSGGMSQRAMIAMALAGQPKLLIADEPTTAL 184
Cdd:PRK09700 140 DEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
26-275 |
9.75e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 55.18 E-value: 9.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 26 INLTVNPNEILAIVGESGSGKSVAMLALMNLLPPqariTCDELVLDGKNLLQLTATERRRlnggTVAMIFQ-----EPMT 100
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPP----SEGEILLDAQPLESWSSKAFAR----KVAYLPQqlpaaEGMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 101 sLNPCFTVGYQIDEAVKTHVGGGRKERKEQVLSLlesVGI-PDPARRYDAyphqMSGGMSQRAMIAMALAGQPKLLIADE 179
Cdd:PRK10575 102 -VRELVAIGRYPWHGALGRFGAADREKVEEAISL---VGLkPLAHRLVDS----LSGGERQRAWIAMLVAQDSRCLLLDE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 180 PTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVVQYAGQQVEKNSAYELFNhphhpytAALLSALpe 259
Cdd:PRK10575 174 PTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMR-------GETLEQI-- 244
|
250
....*....|....*.
gi 522049469 260 RALPTGLLPTIPGLVP 275
Cdd:PRK10575 245 YGIPMGILPHPAGAAP 260
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-190 |
1.35e-08 |
|
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: 52.84 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPTQngwfQAVEGINLTVNPNEILAIVGESGSGKSvamlALMNLLppqaritcdelvldgknLLQLTATEr 83
Cdd:cd03221 1 IELENLSKTYGGK----LLLKDISLTINPGDRIGLVGRNGAGKS----TLLKLI-----------------AGELEPDE- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 84 rrlngGTVamifqepmtSLNPCFTVGYqideavkthvgggrkerkeqvlsllesvgipdparrydaYPhQMSGGMSQRAM 163
Cdd:cd03221 55 -----GIV---------TWGSTVKIGY---------------------------------------FE-QLSGGEKMRLA 80
|
170 180
....*....|....*....|....*...
gi 522049469 164 IAMALAGQPKLLIADEPTTALDV-TVQA 190
Cdd:cd03221 81 LAKLLLENPNLLLLDEPTNHLDLeSIEA 108
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-185 |
1.40e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 56.18 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 22 AVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPqariTCDELVLDGKNLLQLTATERRRLnggtvAMIFQEPMts 101
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPP----TSGTVLVGGKDIETNLDAVRQSL-----GMCPQHNI-- 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 102 LNPCFTVGYQIDEAVKTHvGGGRKERKEQVLSLLESVGIpdpARRYDAYPHQMSGGMSQRAMIAMALAGQPKLLIADEPT 181
Cdd:TIGR01257 1014 LFHHLTVAEHILFYAQLK-GRSWEEAQLEMEAMLEDTGL---HHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
....
gi 522049469 182 TALD 185
Cdd:TIGR01257 1090 SGVD 1093
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-186 |
1.48e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 55.84 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 6 VRNLSVAFPTQngwfQAVEGINLTVNPNEILAIVGESGSGKSvamlALMNLLppqaritcdelvldgKNLLQLTATERRR 85
Cdd:COG0488 1 LENLSKSFGGR----PLLDDVSLSINPGDRIGLVGRNGAGKS----TLLKIL---------------AGELEPDSGEVSI 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 86 LNGGTVAMIFQEPmtSLNPCFTVgyqIDEAVKTHVGGGRKERKEQVLSLLESVGIPDPAR---------RYDAY------ 150
Cdd:COG0488 58 PKGLRIGYLPQEP--PLDDDLTV---LDTVLDGDAELRALEAELEELEAKLAEPDEDLERlaelqeefeALGGWeaeara 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 522049469 151 ------------PHQ-----MSGGMSQRAMIAMALAGQPKLLIADEPTTALDV 186
Cdd:COG0488 133 eeilsglgfpeeDLDrpvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLDL 185
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-231 |
1.52e-08 |
|
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: 54.08 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPT------------------QNGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPqariTC 65
Cdd:cd03220 1 IELENVSKSYPTykggssslkklgilgrkgEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPP----DS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 66 DELVLDGKnllqltaterrrlnggtVAMIFqEPMTSLNPCFTVgyqIDEAVKTHV--GGGRKERKEQVLSLLESVGIPD- 142
Cdd:cd03220 77 GTVTVRGR-----------------VSSLL-GLGGGFNPELTG---RENIYLNGRllGLSRKEIDEKIDEIIEFSELGDf 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 143 ---PARRYdayphqmSGGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMgLILITHDMGVVAE 219
Cdd:cd03220 136 idlPVKTY-------SSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKT-VILVSHDPSSIKR 207
|
250
....*....|..
gi 522049469 220 TAQQVVVQYAGQ 231
Cdd:cd03220 208 LCDRALVLEKGK 219
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-185 |
1.57e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 55.23 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MSLLSVRNLSVAFPtqnGWFQAVEGINLTVNPNEILAIVGESGSGKS-----VAMLAlmnllppqaRITCDELVLDGKNL 75
Cdd:PRK11650 1 MAGLKLQAVRKSYD---GKTQVIKGIDLDVADGEFIVLVGPSGCGKStllrmVAGLE---------RITSGEIWIGGRVV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 76 LQLTATERrrlnggTVAMIFQEpmTSLNPCFTV------GYQIDEAVKTHvgggRKERKEQVLSLLESVGIPDpaRRyda 149
Cdd:PRK11650 69 NELEPADR------DIAMVFQN--YALYPHMSVrenmayGLKIRGMPKAE----IEERVAEAARILELEPLLD--RK--- 131
|
170 180 190
....*....|....*....|....*....|....*...
gi 522049469 150 yPHQMSGGMSQRamIAM--ALAGQPKLLIADEPTTALD 185
Cdd:PRK11650 132 -PRELSGGQRQR--VAMgrAIVREPAVFLFDEPLSNLD 166
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
22-186 |
1.78e-08 |
|
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: 54.04 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 22 AVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPP-QARITCDELVLDGKNLLQLtateRRRLnggtvAMIFQEPMT 100
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELsSGSILIDGVDISKIGLHDL----RSRI-----SIIPQDPVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 101 -------SLNPCftvGYQIDEAV-----KTHVgggrKERKEQVLSLLESVGIPDPArrydayphQMSGGMSQRAMIAMAL 168
Cdd:cd03244 90 fsgtirsNLDPF---GEYSDEELwqaleRVGL----KEFVESLPGGLDTVVEEGGE--------NLSVGQRQLLCLARAL 154
|
170
....*....|....*...
gi 522049469 169 AGQPKLLIADEPTTALDV 186
Cdd:cd03244 155 LRKSKILVLDEATASVDP 172
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-186 |
1.78e-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: 53.52 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVafptQNGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQAritcDELVLDGKNLLQLTATER 83
Cdd:TIGR01189 1 LAARNLAC----SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDS----GEVRWNGTPLAEQRDEPH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 84 RRLnggtvAMIFQEPmtSLNPCFTVGYQIDEAVKTHVGGGRkerkeQVLSLLESVGIPDPArryDAYPHQMSGGMSQRAM 163
Cdd:TIGR01189 73 ENI-----LYLGHLP--GLKPELSALENLHFWAAIHGGAQR-----TIEDALAAVGLTGFE---DLPAAQLSAGQQRRLA 137
|
170 180
....*....|....*....|...
gi 522049469 164 IAMALAGQPKLLIADEPTTALDV 186
Cdd:TIGR01189 138 LARLWLSRRPLWILDEPTTALDK 160
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-226 |
2.83e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 54.32 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 21 QAVEGINLTVNPNEILAIVGESGSGKS--VAMLAlmNLLPPqariTCDELVLDGknllqLTATERRRLNGGTVAMIF-QE 97
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSttIKMLT--GILVP----TSGEVRVLG-----YVPFKRRKEFARRIGVVFgQR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 98 --------PMTS--LNPCFtvgYQIDEAVkthvgggRKERKEQVLSLLESVGIPD-PARrydayphQMSGGMSQRAMIAM 166
Cdd:COG4586 105 sqlwwdlpAIDSfrLLKAI---YRIPDAE-------YKKRLDELVELLDLGELLDtPVR-------QLSLGQRMRCELAA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 167 ALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVV 226
Cdd:COG4586 168 ALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIV 227
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-190 |
3.12e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 53.78 E-value: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 26 INLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQARITcdelvLDGKNLLQLTATE--RRRlnggtvAMIFQEPMTSLN 103
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQ-----FAGQPLEAWSAAElaRHR------AYLSQQQTPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 104 -PCFTvgY-QIDEAVKTHVGGGRKERKEqvlsLLESVGIPDPARRydaYPHQMSGGMSQRAMIAMAL-----AGQP--KL 174
Cdd:PRK03695 84 mPVFQ--YlTLHQPDKTRTEAVASALNE----VAEALGLDDKLGR---SVNQLSGGEWQRVRLAAVVlqvwpDINPagQL 154
|
170
....*....|....*.
gi 522049469 175 LIADEPTTALDVTVQA 190
Cdd:PRK03695 155 LLLDEPMNSLDVAQQA 170
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
4-185 |
3.65e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 54.43 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPtqNGwfQA-VEGINLTVNPNEILAIVGESGSGKSVAMLALMNL---------LPPQARItcdeLVLdgk 73
Cdd:COG4178 363 LALEDLTLRTP--DG--RPlLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLwpygsgriaRPAGARV----LFL--- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 74 nllqltaTERRRLNGGTV--AMIFqePMTSLnpcftvgyQIDEavkthvgggrkerkEQVLSLLESVGIPDPARRYDA-- 149
Cdd:COG4178 432 -------PQRPYLPLGTLreALLY--PATAE--------AFSD--------------AELREALEAVGLGHLAERLDEea 480
|
170 180 190
....*....|....*....|....*....|....*..
gi 522049469 150 -YPHQMSGGMSQRAMIAMALAGQPKLLIADEPTTALD 185
Cdd:COG4178 481 dWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALD 517
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-184 |
3.98e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.41 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFPtqnGwFQAVEGINLTVNPNEILAIVGESGSGKSVamlaLMNLLP---PQAriTCD-ELVLDGK--NLL 76
Cdd:NF040905 1 ILEMRGITKTFP---G-VKALDDVNLSVREGEIHALCGENGAGKST----LMKVLSgvyPHG--SYEgEILFDGEvcRFK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 77 QLTATERRrlngGTVaMIFQE----PMTSL-------NPCFTVGYqIDeavkthvgggRKERKEQVLSLLESVGIP-DPA 144
Cdd:NF040905 71 DIRDSEAL----GIV-IIHQElaliPYLSIaeniflgNERAKRGV-ID----------WNETNRRARELLAKVGLDeSPD 134
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 522049469 145 RRYDayphQMSGGMSQRAMIAMALAGQPKLLIADEPTTAL 184
Cdd:NF040905 135 TLVT----DIGVGKQQLVEIAKALSKDVKLLILDEPTAAL 170
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-184 |
4.23e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.15 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MSLLSVRNLSVAFPTqngwFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQAritcDELVLDGKNllQLTA 80
Cdd:PRK11288 2 SPYLSFDGIGKTFPG----VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDA----GSILIDGQE--MRFA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 81 TERRRLNGGtVAMIFQEpmTSLNPCFTVGYQIDEAVKTHVGG--GRKERKEQVLSLLESVGIpdparryDAYPHQMSGGM 158
Cdd:PRK11288 72 STTAALAAG-VAIIYQE--LHLVPEMTVAENLYLGQLPHKGGivNRRLLNYEAREQLEHLGV-------DIDPDTPLKYL 141
|
170 180 190
....*....|....*....|....*....|
gi 522049469 159 S--QRAM--IAMALAGQPKLLIADEPTTAL 184
Cdd:PRK11288 142 SigQRQMveIAKALARNARVIAFDEPTSSL 171
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-186 |
5.84e-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: 52.11 E-value: 5.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAfptqNGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQAritcdelvldgknllqltatER 83
Cdd:cd03231 1 LEADELTCE----RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLA--------------------GR 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 84 RRLNGGTVAmiFQEPMTSLNpCFTVGYQidEAVKT-----------HVGGGRkerkEQVLSLLESVGIpdpARRYDAYPH 152
Cdd:cd03231 57 VLLNGGPLD--FQRDSIARG-LLYLGHA--PGIKTtlsvlenlrfwHADHSD----EQVEEALARVGL---NGFEDRPVA 124
|
170 180 190
....*....|....*....|....*....|....
gi 522049469 153 QMSGGMSQRAMIAMALAGQPKLLIADEPTTALDV 186
Cdd:cd03231 125 QLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-185 |
7.63e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 53.70 E-value: 7.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 26 INLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQAritcdELVLDGKNLLQLTATERRRlnggTVAMIFQEPM---TSL 102
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQG-----SLKINGIELRELDPESWRK----HLSWVGQNPQlphGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 103 NPCFTVG-YQIDEavkthvgggrkerkEQVLSLLESVGIPD-PARRYDAYPHQ-------MSGGMSQRAMIAMALAGQPK 173
Cdd:PRK11174 440 RDNVLLGnPDASD--------------EQLQQALENAWVSEfLPLLPQGLDTPigdqaagLSVGQAQRLALARALLQPCQ 505
|
170
....*....|..
gi 522049469 174 LLIADEPTTALD 185
Cdd:PRK11174 506 LLLLDEPTASLD 517
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-261 |
1.01e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.44 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 23 VEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLppqaRITCDELVLDGKNLLQLTATERRRLnggtVAMIFQEPMTSL 102
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIV----ELEKGRIMIDDCDVAKFGLTDLRRV----LSIIPQSPVLFS 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 103 NpcfTVGYQIDeAVKTHVGGGRKERkeqvlslLESVGIPDPARR----YDAYPHQ----MSGGMSQRAMIAMALAGQPKL 174
Cdd:PLN03232 1324 G---TVRFNID-PFSEHNDADLWEA-------LERAHIKDVIDRnpfgLDAEVSEggenFSVGQRQLLSLARALLRRSKI 1392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 175 LIADEPTTALDVTVQAQILELLLKLQQQFQMglILITHDMGVVAEtAQQVVVQYAGQQVEKNSAYELFNHPHHPYTAALL 254
Cdd:PLN03232 1393 LVLDEATASVDVRTDSLIQRTIREEFKSCTM--LVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVH 1469
|
....*..
gi 522049469 255 SALPERA 261
Cdd:PLN03232 1470 STGPANA 1476
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-184 |
1.76e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 51.42 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MSLLSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSVamlaLMNLLPPQARITCDELVLDGKNLLQLTA 80
Cdd:PRK11614 3 KVMLSFDKVSAHY----GKIQALHEVSLHINQGEIVTLIGANGAGKTT----LLGTLCGDPRATSGRIVFDGKDITDWQT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 81 terrrlnggtvAMIFQEPMTSLNPCFTVGYQIDEAVKTHVGGGRKERkEQVLSLLESVgipdparrYDAYP------HQ- 153
Cdd:PRK11614 75 -----------AKIMREAVAIVPEGRRVFSRMTVEENLAMGGFFAER-DQFQERIKWV--------YELFPrlherrIQr 134
|
170 180 190
....*....|....*....|....*....|....
gi 522049469 154 ---MSGGMSQRAMIAMALAGQPKLLIADEPTTAL 184
Cdd:PRK11614 135 agtMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-185 |
2.33e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 51.94 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPTQNGwfQAVEGINLTVNPNEILAIVGESGSGKSVamlaLMNLLPPQARITCDELVLDGKNLLQLTATER 83
Cdd:PRK11176 342 IEFRNVTFTYPGKEV--PALRNINFKIPAGKTVALVGRSGSGKST----IANLLTRFYDIDEGEILLDGHDLRDYTLASL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 84 RRlnggTVAMIFQEPM----TSLNpcfTVGY---------QIDEAVKTHVGGGRKERKEQVL-SLLESVGIpdparryda 149
Cdd:PRK11176 416 RN----QVALVSQNVHlfndTIAN---NIAYarteqysreQIEEAARMAYAMDFINKMDNGLdTVIGENGV--------- 479
|
170 180 190
....*....|....*....|....*....|....*.
gi 522049469 150 yphQMSGGMSQRAMIAMALAGQPKLLIADEPTTALD 185
Cdd:PRK11176 480 ---LLSGGQRQRIAIARALLRDSPILILDEATSALD 512
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
26-190 |
4.30e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.21 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 26 INLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQaritCDELVLDGKNLLQLTAteRRRLNGGTVAM--------IFQE 97
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPAR----GGRIMLNGKEINALST--AQRLARGLVYLpedrqssgLYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 98 PMTSLNPCF----TVGYQIDEAVKTHVgggrKERKEQVLSLLESvGIPDPARRydayphqMSGGMSQRAMIAMALAGQPK 173
Cdd:PRK15439 356 APLAWNVCAlthnRRGFWIKPARENAV----LERYRRALNIKFN-HAEQAART-------LSGGNQQKVLIAKCLEASPQ 423
|
170
....*....|....*..
gi 522049469 174 LLIADEPTTALDVTVQA 190
Cdd:PRK15439 424 LLIVDEPTRGVDVSARN 440
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-226 |
5.29e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 50.08 E-value: 5.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MS-LLSVRNLSVAFPTQN------------------GWFQAVEGINLTVNPNEILAIVGESGSGKSvamlALMNLLppqA 61
Cdd:COG1134 1 MSsMIEVENVSKSYRLYHepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKS----TLLKLI---A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 62 RItcdelvldgknllqLTATE-RRRLNGGTVAMIfqEPMTSLNPCFTvgyqideavkthvggGRkE-----------RKE 129
Cdd:COG1134 74 GI--------------LEPTSgRVEVNGRVSALL--ELGAGFHPELT---------------GR-EniylngrllglSRK 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 130 QVLSLLESV----GIPD----PARRYdayphqmSGGMSQRAMIAMALAGQPKLLIADEpttALDV--------------- 186
Cdd:COG1134 122 EIDEKFDEIvefaELGDfidqPVKTY-------SSGMRARLAFAVATAVDPDILLVDE---VLAVgdaafqkkclarire 191
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 522049469 187 ------TVqaqilelllklqqqfqmglILITHDMGVVAETAQQVVV 226
Cdd:COG1134 192 lresgrTV-------------------IFVSHSMGAVRRLCDRAIW 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-190 |
8.61e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 50.06 E-value: 8.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFPTQngwfQAVEGINLTVNPNEILAIVGESGSGKSvamlALMNLLppqaritCDELvldgknllQLTATE 82
Cdd:COG0488 315 VLELEGLSKSYGDK----TLLDDLSLRIDRGDRIGLIGPNGAGKS----TLLKLL-------AGEL--------EPDSGT 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 RRRlnGGTVamifqepmtslnpcfTVGY------QIDEA--VKTHVGGGRKERKEQ-VLSLLESVGIPdparRYDAY-P- 151
Cdd:COG0488 372 VKL--GETV---------------KIGYfdqhqeELDPDktVLDELRDGAPGGTEQeVRGYLGRFLFS----GDDAFkPv 430
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 522049469 152 HQMSGGMSQRAMIAMALAGQPKLLIADEPTTALDV-TVQA 190
Cdd:COG0488 431 GVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIeTLEA 470
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-219 |
1.36e-06 |
|
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: 47.37 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 32 PNEILAIVGESGSGKSVAMLALMNLLPPQARitcDELVLDGKNLLQLTATERRRLNGGTvamifqepmtslnpcftvgyq 111
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG---GVIYIDGEDILEEVLDQLLLIIVGG--------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 112 ideavkthvgggrkerkeqvlsllesvgipdparrydaYPHQMSGGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQ 191
Cdd:smart00382 57 --------------------------------------KKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEAL 98
|
170 180 190
....*....|....*....|....*....|...
gi 522049469 192 ILELLLKLQQQFQM-----GLILITHDMGVVAE 219
Cdd:smart00382 99 LLLLEELRLLLLLKseknlTVILTTNDEKDLGP 131
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-184 |
1.92e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 49.28 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFptqngwfQAVE---GINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQAritcDELVLDGKNLLQLT 79
Cdd:PRK15439 11 LLCARSISKQY-------SGVEvlkGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDS----GTLEIGGNPCARLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 80 ATERRRLNggtVAMIFQEPMtsLNPCFTVGYQIdeAVKTHVGGGRKERKEQVLSLLESVGIPD-PARRYDAYPHQMsggm 158
Cdd:PRK15439 80 PAKAHQLG---IYLVPQEPL--LFPNLSVKENI--LFGLPKRQASMQKMKQLLAALGCQLDLDsSAGSLEVADRQI---- 148
|
170 180
....*....|....*....|....*.
gi 522049469 159 sqrAMIAMALAGQPKLLIADEPTTAL 184
Cdd:PRK15439 149 ---VEILRGLMRDSRILILDEPTASL 171
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-186 |
2.13e-06 |
|
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: 49.05 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFPTqNGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQ--ARITCDELVLDGKNLLQLTA 80
Cdd:TIGR02633 257 ILEARNLTCWDVI-NPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfeGNVFINGKPVDIRNPAQAIR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 81 T------ERRRLNGGTVAMIFQEPMT--SLNPcFTVGYQIDEAVKTH-VGGGRKERKEQVLSLLESVGipdparrydayp 151
Cdd:TIGR02633 336 AgiamvpEDRKRHGIVPILGVGKNITlsVLKS-FCFKMRIDAAAELQiIGSAIQRLKVKTASPFLPIG------------ 402
|
170 180 190
....*....|....*....|....*....|....*
gi 522049469 152 hQMSGGMSQRAMIAMALAGQPKLLIADEPTTALDV 186
Cdd:TIGR02633 403 -RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-185 |
2.36e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.58 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQARITCDELV-LDGKNLLQLTATE 82
Cdd:NF000106 14 VEVRGLVKHF----GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*TwCANRRALRRTIG* 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 RRRLNGGTvamifQEPMTSLNPCFTVGYQIDEAvkthvgggRKERKEQVLSLLESVGIPDPARRYDAyphQMSGGMSQRA 162
Cdd:NF000106 90 HRPVR*GR-----RESFSGRENLYMIGR*LDLS--------RKDARARADELLERFSLTEAAGRAAA---KYSGGMRRRL 153
|
170 180
....*....|....*....|...
gi 522049469 163 MIAMALAGQPKLLIADEPTTALD 185
Cdd:NF000106 154 DLAASMIGRPAVLYLDEPTTGLD 176
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-185 |
2.41e-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: 47.64 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MSLLSVRNLSVAFPTQNGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQARITCDeLVLDGKNLLQLTA 80
Cdd:cd03233 1 ASTLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGD-IHYNGIPYKEFAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 81 TERRRLnggtvamIFQEPMTSLNPCFTVGYQIDEAVKThvgggrkerkeqvlsllesvgipdparRYDAYPHQMSGGMSQ 160
Cdd:cd03233 80 KYPGEI-------IYVSEEDVHFPTLTVRETLDFALRC---------------------------KGNEFVRGISGGERK 125
|
170 180
....*....|....*....|....*
gi 522049469 161 RAMIAMALAGQPKLLIADEPTTALD 185
Cdd:cd03233 126 RVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-245 |
2.51e-06 |
|
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: 47.41 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPTQNGwfQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPP-QARITcdelvLDGKNLLQLTATE 82
Cdd:cd03369 7 IEVENLSVRYAPDLP--PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAeEGKIE-----IDGIDISTIPLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 RRRlnggTVAMIFQEPM-------TSLNPcftvgY------QIDEAVKTHVGGgrkerkeqvlsllesvgipdparryda 149
Cdd:cd03369 80 LRS----SLTIIPQDPTlfsgtirSNLDP-----FdeysdeEIYGALRVSEGG--------------------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 150 ypHQMSGGMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMglILITHDMGVVAETAqQVVVQYA 229
Cdd:cd03369 124 --LNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTI--LTIAHRLRTIIDYD-KILVMDA 198
|
250
....*....|....*.
gi 522049469 230 GQQVEknsayelFNHP 245
Cdd:cd03369 199 GEVKE-------YDHP 207
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-188 |
2.54e-06 |
|
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: 47.46 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAF-PTQNGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNllppqaritcdelvldgknllQLTATE 82
Cdd:cd03250 1 ISVEDASFTWdSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLG---------------------ELEKLS 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 RRRLNGGTVAMIFQEPM---TSL--NPCFtvGYQIDEavkthvgggrkERKEQVLSL--LEsvgiPDparrYDAYPHQ-- 153
Cdd:cd03250 60 GSVSVPGSIAYVSQEPWiqnGTIreNILF--GKPFDE-----------ERYEKVIKAcaLE----PD----LEILPDGdl 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 522049469 154 ---------MSGGMSQRAMIAMALAGQPKLLIADEPTTALDVTV 188
Cdd:cd03250 119 teigekginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHV 162
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-186 |
2.72e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.77 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPTqNGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLP--PQARITCDELVLDGKNLLQLTA- 80
Cdd:PRK13549 260 LEVRNLTAWDPV-NPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgrWEGEIFIDGKPVKIRNPQQAIAq 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 81 -----TERRRLNGGTVAMIFQEPMT--SLNPcFTVGYQIDEAVKTHVGGgrkerkEQVLSLleSVGIPDPARRYDayphQ 153
Cdd:PRK13549 339 giamvPEDRKRDGIVPVMGVGKNITlaALDR-FTGGSRIDDAAELKTIL------ESIQRL--KVKTASPELAIA----R 405
|
170 180 190
....*....|....*....|....*....|...
gi 522049469 154 MSGGMSQRAMIAMALAGQPKLLIADEPTTALDV 186
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDV 438
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-190 |
2.78e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.47 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 27 NLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQA--------RITcdelVLDGKNLLQLTATERRRLN----------- 87
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSgerqsqfsHIT----RLSFEQLQKLVSDEWQRNNtdmlspgeddt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 88 GGTVAMIFQEPMTSLNPCFTVGYQIdeavkthvgggrkerkeQVLSLLEsvgipdpaRRYDayphQMSGGMSQRAMIAMA 167
Cdd:PRK10938 99 GRTTAEIIQDEVKDPARCEQLAQQF-----------------GITALLD--------RRFK----YLSTGETRKTLLCQA 149
|
170 180
....*....|....*....|...
gi 522049469 168 LAGQPKLLIADEPTTALDVTVQA 190
Cdd:PRK10938 150 LMSEPDLLILDEPFDGLDVASRQ 172
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-187 |
3.54e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.41 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 1 MSLLSVRNLSVAFptqnGWFQAVEGINLTVNPNEILAIVGESGSGKSVAMlalmnllppqaRITCDELVLD-GKNLLQLT 79
Cdd:PRK11147 1 MSLISIHGAWLSF----SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLM-----------KILNGEVLLDdGRIIYEQD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 80 ATERR------RLNGGTV----------------------AMIFQEPMTS-LNPCFTVGYQIDeavktHVGGGRKE-RKE 129
Cdd:PRK11147 66 LIVARlqqdppRNVEGTVydfvaegieeqaeylkryhdisHLVETDPSEKnLNELAKLQEQLD-----HHNLWQLEnRIN 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 522049469 130 QVLSLLESvgipDParryDAYPHQMSGGMSQRAMIAMALAGQPKLLIADEPTTALDVT 187
Cdd:PRK11147 141 EVLAQLGL----DP----DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIE 190
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
26-185 |
4.48e-06 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 47.02 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 26 INLTVNPNEILAIVGESGSGKSVAMLALMNLLPPqariTCDELVLDGKNLLQLTATERRRlnggTVAMIFQEPM---TSL 102
Cdd:PRK10247 26 ISFSLRAGEFKLITGPSGCGKSTLLKIVASLISP----TSGTLLFEGEDISTLKPEIYRQ----QVSYCAQTPTlfgDTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 103 NPCFTVGYQIdeavkthvgggRKERKE--QVLSLLESVGIPDPArrYDAYPHQMSGGMSQRAMIAMALAGQPKLLIADEP 180
Cdd:PRK10247 98 YDNLIFPWQI-----------RNQQPDpaIFLDDLERFALPDTI--LTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
....*
gi 522049469 181 TTALD 185
Cdd:PRK10247 165 TSALD 169
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
26-226 |
5.46e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.13 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 26 INLTVNPNEILAIVGESGSGKSVAMLALMNLL-----PPQARITCDeLVLDGKNLLQLTATERRRLNggtvAMIFQEPmt 100
Cdd:PRK13547 20 LSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaPRGARVTGD-VTLNGEPLAAIDAPRLARLR----AVLPQAA-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 101 slNPCFTvgYQIDEAV------KTHVGGGRKERKEQVLSLLESVGIPDPARRYDAYphQMSGGMSQRAMIAMALA----- 169
Cdd:PRK13547 93 --QPAFA--FSAREIVllgrypHARRAGALTHRDGEIAWQALALAGATALVGRDVT--TLSGGELARVQFARVLAqlwpp 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522049469 170 ----GQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLILITHDMGVVAETAQQVVV 226
Cdd:PRK13547 167 hdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAM 227
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
25-185 |
5.99e-06 |
|
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: 47.89 E-value: 5.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 25 GINLTVNPNEILAIVGESGSGKSvamlALMNLL-----PPQARITcdelvLDGKNLLQLTATERRRlnggTVAMIFQEpm 99
Cdd:COG5265 376 GVSFEVPAGKTVAIVGPSGAGKS----TLARLLfrfydVTSGRIL-----IDGQDIRDVTQASLRA----AIGIVPQD-- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 100 TSLnpcF--TVGY------------QIDEAVK----------------THVGggrkERKeqvLSLlesvgipdparryda 149
Cdd:COG5265 441 TVL---FndTIAYniaygrpdaseeEVEAAARaaqihdfieslpdgydTRVG----ERG---LKL--------------- 495
|
170 180 190
....*....|....*....|....*....|....*.
gi 522049469 150 yphqmSGGMSQRAMIAMALAGQPKLLIADEPTTALD 185
Cdd:COG5265 496 -----SGGEKQRVAIARTLLKNPPILIFDEATSALD 526
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
4-75 |
1.61e-05 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 46.33 E-value: 1.61e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522049469 4 LSVRNLSVAFPTQNG--WFqAVEGINLTVNPNEILAIVGESGSGKS-VAMLaLMNLLPPQA-RITCDELVLDGKNL 75
Cdd:COG4615 328 LELRGVTYRYPGEDGdeGF-TLGPIDLTIRRGELVFIVGGNGSGKStLAKL-LTGLYRPESgEILLDGQPVTADNR 401
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
2-185 |
2.22e-05 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 44.54 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 2 SLLSVRNLSVAFPTQNGWFQAVEGINLTVNPNEILAIVGESGSGKSVamlaLMNLLPPQ--ARITCDELVLDGKnllQLT 79
Cdd:cd03232 2 SVLTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTT----LLDVLAGRktAGVITGEILINGR---PLD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 80 ATERRRLNggtvamiFQEPMTSLNPCFTVgyqiDEAVkthvgggrkerkeqvlsllesvgipdparRYDAYPHQMSGGMS 159
Cdd:cd03232 75 KNFQRSTG-------YVEQQDVHSPNLTV----REAL-----------------------------RFSALLRGLSVEQR 114
|
170 180
....*....|....*....|....*.
gi 522049469 160 QRAMIAMALAGQPKLLIADEPTTALD 185
Cdd:cd03232 115 KRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
121-185 |
3.20e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.50 E-value: 3.20e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522049469 121 GGGRKERKEQVLSLLESVGI---PD-PARrydayphQMSGGMSQRAMIAMALAGQPKLLIADEPTTALD 185
Cdd:NF033858 107 GQDAAERRRRIDELLRATGLapfADrPAG-------KLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
31-185 |
4.25e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.41 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 31 NPNEiLAIVGESGSGKSVAMLAlmnllppqariTCDELVLDGKNLLQLTATERRRLnggtVAMIFQEPMT-SLNPCFTVG 109
Cdd:PTZ00265 1254 NVNE-FSLTKEGGSGEDSTVFK-----------NSGKILLDGVDICDYNLKDLRNL----FSIVSQEPMLfNMSIYENIK 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 110 YQIDEAVKTHVGggRKERKEQVLSLLESvgIPDparRYDA----YPHQMSGGMSQRAMIAMALAGQPKLLIADEPTTALD 185
Cdd:PTZ00265 1318 FGKEDATREDVK--RACKFAAIDEFIES--LPN---KYDTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-186 |
4.56e-05 |
|
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: 43.86 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 17 NGWFQ------AVEGINLTVNPNEILAIVGESGSGKSVAMLALMNllppQARITCDELVLDGKNLLQLTATERRRLNGGT 90
Cdd:cd03290 5 NGYFSwgsglaTLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILG----EMQTLEGKVHWSNKNESEPSFEATRSRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 91 VAMIFQEPmtslnpcftvgYQIDEAVKTHVGGGRKERKEQVLSLLESVGI-PDparrYDAYPH-----------QMSGGM 158
Cdd:cd03290 81 VAYAAQKP-----------WLLNATVEENITFGSPFNKQRYKAVTDACSLqPD----IDLLPFgdqteigergiNLSGGQ 145
|
170 180
....*....|....*....|....*...
gi 522049469 159 SQRAMIAMALAGQPKLLIADEPTTALDV 186
Cdd:cd03290 146 RQRICVARALYQNTNIVFLDDPFSALDI 173
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-185 |
7.42e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 44.43 E-value: 7.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFPTQNgwFQAVEGINLTVNPNEILAIVGESGSGKSvamlALMNLLPPQARITCDELVLDGKNLLQLTATE 82
Cdd:PRK11160 338 SLTLNNVSFTYPDQP--QPVLKGLSLQIKAGEKVALLGRTGCGKS----TLLQLLTRAWDPQQGEILLNGQPIADYSEAA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 RRRlnggtvamifqepmtslnpCFTVGYQideavKTHVGGGR----------KERKEQVLSLLESVGIP---DPARRYDA 149
Cdd:PRK11160 412 LRQ-------------------AISVVSQ-----RVHLFSATlrdnlllaapNASDEALIEVLQQVGLEkllEDDKGLNA 467
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 522049469 150 Y----PHQMSGGMSQRAMIAMALAGQPKLLIADEPTTALD 185
Cdd:PRK11160 468 WlgegGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLD 507
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-184 |
7.97e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.22 E-value: 7.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVAFPTqngwFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQAritcDELVLDGKNllqltate 82
Cdd:PRK10762 4 LLQLKGIDKAFPG----VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDA----GSILYLGKE-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 rRRLNG------GTVAMIFQEpmtsLN--PCFTVGYQI---DEAVKTHVGGGRKERKEQVLSLLESVGIPDPARRYDAyp 151
Cdd:PRK10762 68 -VTFNGpkssqeAGIGIIHQE----LNliPQLTIAENIflgREFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVG-- 140
|
170 180 190
....*....|....*....|....*....|...
gi 522049469 152 hQMSGGMSQRAMIAMALAGQPKLLIADEPTTAL 184
Cdd:PRK10762 141 -ELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-190 |
1.45e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 43.23 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 20 FQAVEGINLTVNPNEILAIVGESGSGKSvamlALMNLLPPQARITCDELVLDGKNLL---QLTA--------TERRRLNG 88
Cdd:PRK09700 276 RKKVRDISFSVCRGEILGFAGLVGSGRT----ELMNCLFGVDKRAGGEIRLNGKDISprsPLDAvkkgmayiTESRRDNG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 89 GTVAMIFQEPMTSLNPCFTVGYQIDEAVKTHVGGGRKERKEQVLSLLESVGIpdparryDAYPHQMSGGMSQRAMIAMAL 168
Cdd:PRK09700 352 FFPNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLALKCHSV-------NQNITELSGGNQQKVLISKWL 424
|
170 180
....*....|....*....|..
gi 522049469 169 AGQPKLLIADEPTTALDVTVQA 190
Cdd:PRK09700 425 CCCPEVIIFDEPTRGIDVGAKA 446
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-190 |
1.47e-04 |
|
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: 41.76 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFPTQNgwfQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLP-PQARITCDElvldgknllqltate 82
Cdd:cd03223 1 IELENLSLATPDGR---VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPwGSGRIGMPE--------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 rrrlnGGTVAMIFQEPMtslnpcFTVGyqideavkthvgggrkerkeqvlSLLESVgipdparrydAYP--HQMSGGMSQ 160
Cdd:cd03223 63 -----GEDLLFLPQRPY------LPLG-----------------------TLREQL----------IYPwdDVLSGGEQQ 98
|
170 180 190
....*....|....*....|....*....|
gi 522049469 161 RAMIAMALAGQPKLLIADEPTTALDVTVQA 190
Cdd:cd03223 99 RLAFARLLLHKPKFVFLDEATSALDEESED 128
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
4-219 |
3.25e-04 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 41.79 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFptQNGwFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLppqaRITCDELVLdgknllqLTATER 83
Cdd:PRK15056 7 IVVNDVTVTW--RNG-HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFV----RLASGKISI-------LGQPTR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 84 RRLNGGTVAMIFQEpmTSLNPCFTVgyQIDEAVKT----HVGGGR---KERKEQVLSLLESVGIPDPARRYDAyphQMSG 156
Cdd:PRK15056 73 QALQKNLVAYVPQS--EEVDWSFPV--LVEDVVMMgrygHMGWLRrakKRDRQIVTAALARVDMVEFRHRQIG---ELSG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522049469 157 GMSQRAMIAMALAGQPKLLIADEPTTALDVTVQAQILELLLKLQQQFQMGLIlITHDMGVVAE 219
Cdd:PRK15056 146 GQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLV-STHNLGSVTE 207
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-73 |
3.88e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 41.88 E-value: 3.88e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522049469 4 LSVRNLSVAFPTQNgwFqAVEGINLTVNPNEILAIVGESGSGKS-VAMLaLMNLLPPQAritcDELVLDGK 73
Cdd:PRK10522 323 LELRNVTFAYQDNG--F-SVGPINLTIKRGELLFLIGGNGSGKStLAML-LTGLYQPQS----GEILLDGK 385
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
3-186 |
5.21e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 40.56 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 3 LLSVRNLSVafptQNGWFQAVEGINLTVNPNEILAIVGESGSGKSvamlALMNLLPPQARITCDELVLDGKNLLQ----- 77
Cdd:PRK13538 1 MLEARNLAC----ERDERILFSGLSFTLNAGELVQIEGPNGAGKT----SLLRILAGLARPDAGEVLWQGEPIRRqrdey 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 78 ----------------LTATERRRLNggtvAMIFQEPmtslnpcftvgyqideavkthvgggrkeRKEQVLSLLESVGIp 141
Cdd:PRK13538 73 hqdllylghqpgikteLTALENLRFY----QRLHGPG----------------------------DDEALWEALAQVGL- 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 522049469 142 dpARRYDAYPHQMSGGmsQRAMIAMA--LAGQPKLLIADEPTTALDV 186
Cdd:PRK13538 120 --AGFEDVPVRQLSAG--QQRRVALArlWLTRAPLWILDEPFTAIDK 162
|
|
| VirB11 |
COG0630 |
Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell ... |
38-93 |
5.43e-04 |
|
Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440395 [Multi-domain] Cd Length: 462 Bit Score: 41.60 E-value: 5.43e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522049469 38 IVGESGSGKSVAMLALMNLLPPQARI-----TcDELVLDGKNLLQLTATERRRLNGGTVAM 93
Cdd:COG0630 295 VAGGTASGKTTLLNALLSFIPPDAKIvtiedT-RELNLPHENWISLVTRESFGGEEGDVTM 354
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-184 |
6.79e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.25 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 7 RNLSVAFPTqngwFQAVEGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQAritcDELVLDGKNlLQLTATERRRL 86
Cdd:PRK10982 2 SNISKSFPG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDS----GSILFQGKE-IDFKSSKEALE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 87 NGgtVAMIFQEpmtsLNpcftvgyQIDE-AVKTHVGGGRKERK----------EQVLSLLESVGIP-DPARRYDAYPhqm 154
Cdd:PRK10982 73 NG--ISMVHQE----LN-------LVLQrSVMDNMWLGRYPTKgmfvdqdkmyRDTKAIFDELDIDiDPRAKVATLS--- 136
|
170 180 190
....*....|....*....|....*....|..
gi 522049469 155 sggMSQRAM--IAMALAGQPKLLIADEPTTAL 184
Cdd:PRK10982 137 ---VSQMQMieIAKAFSYNAKIVIMDEPTSSL 165
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
25-187 |
9.72e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 41.02 E-value: 9.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 25 GINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQArITCDELVLDGKnllqLTATERRRlnggtVAMIFQEPMtsLNP 104
Cdd:PLN03211 86 GVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNN-FTGTILANNRK----PTKQILKR-----TGFVTQDDI--LYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 105 CFTVGYQIDEAVKTHVGggRKERKEQVLSLLESV----GIPDPARRY--DAYPHQMSGGMSQRAMIAMALAGQPKLLIAD 178
Cdd:PLN03211 154 HLTVRETLVFCSLLRLP--KSLTKQEKILVAESViselGLTKCENTIigNSFIRGISGGERKRVSIAHEMLINPSLLILD 231
|
....*....
gi 522049469 179 EPTTALDVT 187
Cdd:PLN03211 232 EPTSGLDAT 240
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
28-63 |
1.22e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 36.42 E-value: 1.22e-03
10 20 30
....*....|....*....|....*....|....*.
gi 522049469 28 LTVNPNEILAIVGESGSGKSVAMLALMNLLPPQARI 63
Cdd:pfam13555 17 IPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPAKRA 52
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-189 |
1.33e-03 |
|
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: 39.84 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 4 LSVRNLSVAFpTQNGwfQAV-EGINLTVNPNEILAIVGESGSGKSVAMLALMNLLPPQARITcdelvLDGKNLLQLTATE 82
Cdd:cd03289 3 MTVKDLTAKY-TEGG--NAVlENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQ-----IDGVSWNSVPLQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 83 RRRLNG--GTVAMIFQEPM-TSLNPcftvgYQideavkthvgggrKERKEQVLSLLESVGIpdpARRYDAYPHQ------ 153
Cdd:cd03289 75 WRKAFGviPQKVFIFSGTFrKNLDP-----YG-------------KWSDEEIWKVAEEVGL---KSVIEQFPGQldfvlv 133
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 522049469 154 -----MSGGMSQRAMIAMALAGQPKLLIADEPTTALD-VTVQ 189
Cdd:cd03289 134 dggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDpITYQ 175
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
152-213 |
1.35e-03 |
|
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: 38.88 E-value: 1.35e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522049469 152 HQMSGGMSQRAMIAMALAGQPK----LLIADEPTTALDVTVQAQILELLLKLQQQFQMgLILITHD 213
Cdd:cd03227 76 LQLSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQ-VIVITHL 140
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
153-185 |
1.77e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.01 E-value: 1.77e-03
10 20 30
....*....|....*....|....*....|...
gi 522049469 153 QMSGGMSQRAMIAMALAGQPKLLIADEPTTALD 185
Cdd:PTZ00265 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-185 |
9.65e-03 |
|
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: 38.07 E-value: 9.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 22 AVEGINLTVNPNEILAIVGESGSGKSVAMlalmNLLPPQARITCDELVLDGKNLLqlTATERRRLNGGTVamifqepmts 101
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTF----KMLTGDTTVTSGDATVAGKSIL--TNISDVHQNMGYC---------- 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522049469 102 lnPCFTVgyqIDEAV--KTHV------GGGRKERKEQVLSL-LESVGIPDPArryDAYPHQMSGGMSQRAMIAMALAGQP 172
Cdd:TIGR01257 2018 --PQFDA---IDDLLtgREHLylyarlRGVPAEEIEKVANWsIQSLGLSLYA---DRLAGTYSGGNKRKLSTAIALIGCP 2089
|
170
....*....|...
gi 522049469 173 KLLIADEPTTALD 185
Cdd:TIGR01257 2090 PLVLLDEPTTGMD 2102
|
|
| |
