|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-818 |
1.51e-177 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 551.86 E-value: 1.51e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 2 LRGHVAVRGlskGFGLATQEPWIQFATIRDNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRA 81
Cdd:TIGR00957 691 VEGHVHMKG---SVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQ 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 82 RIALARAVYQEKELYLLDDPLAAVDADVANHLLHRCI--LGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSE 159
Cdd:TIGR00957 768 RVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQE 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 160 ILPLVQAVPK-----AWAENGQESDSATAQSVQNPEKTKEGLE------------------------------------- 197
Cdd:TIGR00957 848 LLQRDGAFAEflrtyAPDEQQGHLEDSWTALVSGEGKEAKLIEngmlvtdvvgkqlqrqlsasssdsgdqsrhhgssael 927
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 198 ---EEQSTSGRLLQEESKKEGAVALHVYQAYWKAVGQGLALAILFSLLLMQATRNAADWWLSHWISQLKAeNSSQEaqps 274
Cdd:TIGR00957 928 qkaEAKEETWKLMEADKAQTGQVELSVYWDYMKAIGLFITFLSIFLFVCNHVSALASNYWLSLWTDDPMV-NGTQN---- 1002
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 275 tspasmglfspqlllfspgnlyipvfplpkaapngssDIRFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLL 354
Cdd:TIGR00957 1003 -------------------------------------NTSLRLSVYGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLL 1045
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 355 HRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHY 434
Cdd:TIGR00957 1046 HNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFY 1125
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 435 RASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSA 514
Cdd:TIGR00957 1126 VASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLF 1205
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 515 IAGIALVQHQQglANPGLVGLSLSYALSLTGLLSGLVSSFTQTEAMLVSVERLEEYTCDLPQEP-QGQPLQLGTGWLTQG 593
Cdd:TIGR00957 1206 AALFAVISRHS--LSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPwQIQETAPPSGWPPRG 1283
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 594 GVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLA 673
Cdd:TIGR00957 1284 RVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKIT 1363
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 674 IIPQEPFLFSGTVRENLDPQGLHKDRALWQALKQCHLSEVITSMGGLDGEL-GEGGRSLSLGQRQLLCLARALLTDAKIL 752
Cdd:TIGR00957 1364 IIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHEcAEGGENLSVGQRQLVCLARALLRKTKIL 1443
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767940955 753 CIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATLRNQ 818
Cdd:TIGR00957 1444 VLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1-815 |
1.34e-161 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 511.59 E-value: 1.34e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 1 MLRGHVAVRGlskGFGLATQEPWIQFATIRDNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQR 80
Cdd:PLN03130 670 RSDASVVIRG---TVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQK 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 81 ARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEI 160
Cdd:PLN03130 747 QRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 161 L---PLVQ-----------AVPKAWAENGQESDSATAQSVQNPEKTKEGLEEEQSTSGR--LLQEESKKEGAVALHVYQA 224
Cdd:PLN03130 827 SnngPLFQklmenagkmeeYVEENGEEEDDQTSSKPVANGNANNLKKDSSSKKKSKEGKsvLIKQEERETGVVSWKVLER 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 225 YWKAVGQGLALAILF-SLLLMQATRNAADWWLSHWISQlkaenssqeaqpsTSPASMGlfspqlllfsPGnlyipvfplp 303
Cdd:PLN03130 907 YKNALGGAWVVMILFlCYVLTEVFRVSSSTWLSEWTDQ-------------GTPKTHG----------PL---------- 953
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 304 kaapngssdirFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVAC 383
Cdd:PLN03130 954 -----------FYNLIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGD 1022
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 384 ADDSLPFILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGL 463
Cdd:PLN03130 1023 IDRNVAVFVNMFLGQIFQLLSTFVLIGIVSTISLWAIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGL 1102
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 464 SVLRATGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQH-----QQGLANpgLVGLSLS 538
Cdd:PLN03130 1103 STIRAYKAYDRMAEINGRSMDNNIRFTLVNMSSNRWLAIRLETLGGLMIWLTASFAVMQNgraenQAAFAS--TMGLLLS 1180
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 539 YALSLTGLLSGLVSSFTQTEAMLVSVERLEEYTcDLPQEPqgqPLQLGT-----GWLTQGGVEFQDVVLAYRPGLPNALD 613
Cdd:PLN03130 1181 YALNITSLLTAVLRLASLAENSLNAVERVGTYI-DLPSEA---PLVIENnrpppGWPSSGSIKFEDVVLRYRPELPPVLH 1256
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 614 GVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENLDPQ 693
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPF 1336
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 694 GLHKDRALWQALKQCHLSEVI-TSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQT 772
Cdd:PLN03130 1337 NEHNDADLWESLERAHLKDVIrRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKT 1416
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 767940955 773 ICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATL 815
Cdd:PLN03130 1417 IREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENL 1459
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
6-815 |
2.32e-157 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 497.58 E-value: 2.32e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 6 VAVRGlskGFGLATQEPWIQFATIRDNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIAL 85
Cdd:PLN03232 675 VVIRG---SVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSM 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 86 ARAVYQEKELYLLDDPLAAVDADVANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEiLPLVQ 165
Cdd:PLN03232 752 ARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAE-LSKSG 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 166 AVPKAWAENGQESDSATAQSVQNPEKTKEGLEEEQSTSGR--------------LLQEESKKEGAVALHVYQAYWKAVGQ 231
Cdd:PLN03232 831 SLFKKLMENAGKMDATQEVNTNDENILKLGPTVTIDVSERnlgstkqgkrgrsvLVKQEERETGIISWNVLMRYNKAVGG 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 232 GLALAILFS-LLLMQATRNAADWWLSHWISQLKAENssqeaqpstspasmglfspqlllFSPGnlyipvfplpkaapngs 310
Cdd:PLN03232 911 LWVVMILLVcYLTTEVLRVSSSTWLSIWTDQSTPKS-----------------------YSPG----------------- 950
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 311 sdirFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPF 390
Cdd:PLN03232 951 ----FYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVAN 1026
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 391 ILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATG 470
Cdd:PLN03232 1027 LMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYK 1106
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 471 ATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQH-----QQGLANpgLVGLSLSYALSLTG 545
Cdd:PLN03232 1107 AYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLRNgnaenQAGFAS--TMGLLLSYTLNITT 1184
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 546 LLSGLVSSFTQTEAMLVSVERLEEYTcDLPQEP-----QGQPLqlgTGWLTQGGVEFQDVVLAYRPGLPNALDGVTFCVQ 620
Cdd:PLN03232 1185 LLSGVLRQASKAENSLNSVERVGNYI-DLPSEAtaiieNNRPV---SGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVS 1260
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 621 PGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENLDPQGLHKDRA 700
Cdd:PLN03232 1261 PSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDAD 1340
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 701 LWQALKQCHLSEVIT-SMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFAN 779
Cdd:PLN03232 1341 LWEALERAHIKDVIDrNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKS 1420
|
810 820 830
....*....|....*....|....*....|....*.
gi 767940955 780 KTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATL 815
Cdd:PLN03232 1421 CTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQEL 1456
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-815 |
7.28e-128 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 418.80 E-value: 7.28e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 20 QEPWIQFATIRDNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLD 99
Cdd:PTZ00243 728 QQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLD 807
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 100 DPLAAVDADVANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL--PLVQAVPKAWAEN--G 175
Cdd:PTZ00243 808 DPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMrtSLYATLAAELKENkdS 887
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 176 QESDS-----------ATAQSVQNPEKTKEGLEEEQ------STSGRLLQEESKKEGAVALHVYQAYWKAVGQGL-ALAI 237
Cdd:PTZ00243 888 KEGDAdaevaevdaapGGAVDHEPPVAKQEGNAEGGdgaaldAAAGRLMTREEKASGSVPWSTYVAYLRFCGGLHaAGFV 967
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 238 LFSLLLMQATRNAADWWLSHWisqlkaenssqeaqpstSPASMGLfspqlllfspgnlyipvfplpkaapngSSDIrfYL 317
Cdd:PTZ00243 968 LATFAVTELVTVSSGVWLSMW-----------------STRSFKL---------------------------SAAT--YL 1001
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 318 TVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFILNILLA 397
Cdd:PTZ00243 1002 YVYLGIVLLGTFSVPLRFFLSYEAMRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQ 1081
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 398 NAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGATYRFEE 477
Cdd:PTZ00243 1082 CLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQ 1161
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 478 ENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGLA--NPGLVGLSLSYALSLTGLLSGLVSSFT 555
Cdd:PTZ00243 1162 EALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIALIGVIGTMLRATsqEIGLVSLSLTMAMQTTATLNWLVRQVA 1241
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 556 QTEAMLVSVERLEEYTCDLPQE--PQ--------------------------GQPLQLGTGWLTQGGVEFQDVVLAYRPG 607
Cdd:PTZ00243 1242 TVEADMNSVERLLYYTDEVPHEdmPEldeevdalerrtgmaadvtgtvviepASPTSAAPHPVQAGSLVFEGVQMRYREG 1321
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 608 LPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVR 687
Cdd:PTZ00243 1322 LPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVR 1401
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 688 ENLDPQGLHKDRALWQALKQCHLSEVITSMGGLDGELGEGGRS-LSLGQRQLLCLARALLT-DAKILCIDEATASVDQKT 765
Cdd:PTZ00243 1402 QNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSnYSVGQRQLMCMARALLKkGSGFILMDEATANIDPAL 1481
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 767940955 766 DQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATL 815
Cdd:PTZ00243 1482 DRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
234-571 |
2.71e-107 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 331.80 E-value: 2.71e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 234 ALAILFSLLLMQATRNAADWWLSHWISQLKAENSSQeaqpstspasmglfspqlllfspgnlyipvfplpkaapnGSSDI 313
Cdd:cd18605 1 LILILLSLILMQASRNLIDFWLSYWVSHSNNSFFNF---------------------------------------INDSF 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 314 RFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFILN 393
Cdd:cd18605 42 NFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILN 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 394 ILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGATY 473
Cdd:cd18605 122 ILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQE 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 474 RFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGL-ANPGLVGLSLSYALSLTGLLSGLVS 552
Cdd:cd18605 202 RFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGVLIVTFVALTAVVQHFFGLsIDAGLIGLALSYALPITGLLSGLLN 281
|
330
....*....|....*....
gi 767940955 553 SFTQTEAMLVSVERLEEYT 571
Cdd:cd18605 282 SFTETEKEMVSVERVRQYF 300
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
593-812 |
2.06e-105 |
|
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: 323.68 E-value: 2.06e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 593 GGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQL 672
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 673 AIIPQEPFLFSGTVRENLDPQGLHKDRALWQALKQCHLSEVITSMGGLDGELGEGGRS-LSLGQRQLLCLARALLTDAKI 751
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGEnLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767940955 752 LCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSP 812
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-818 |
4.86e-93 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 320.32 E-value: 4.86e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 20 QEPWIQFATIRDNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLD 99
Cdd:TIGR01271 494 QTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLD 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 100 DPLAAVDADVANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEI----------LPLVQAVPK 169
Cdd:TIGR01271 574 SPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELqakrpdfsslLLGLEAFDN 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 170 AWAENGQ------------ESDSATA-------QSVQNP-----EKTK------------------------EGLEEEQS 201
Cdd:TIGR01271 654 FSAERRNsiltetlrrvsiDGDSTVFsgpetikQSFKQPppefaEKRKqsiilnpiasarkfsfvqmgpqkaQATTIEDA 733
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 202 TSGRL-----------LQEESKKEGAVALH--VYQAYWK----------AVGQGL--ALAILFSLLLMQATRNAADWWLS 256
Cdd:TIGR01271 734 VREPSerkfslvpedeQGEESLPRGNQYHHglQHQAQRRqsvlqlmthsNRGENRreQLQTSFRKKSSITQQNELASELD 813
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 257 HWISQLKAENS------------------SQEAQPSTSPASMGL---FSPQLLLF---------------SPGNLYI--- 297
Cdd:TIGR01271 814 IYSRRLSKDSVyeiseeineedlkecfadERENVFETTTWNTYLryiTTNRNLVFvlifclviflaevaaSLLGLWLitd 893
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 298 -PVFPL----------------PKAAPNGSSdirfYLTVYATIAGVNSLCTL--LRAVLFAAGTLQAAATLHRRLLHRVL 358
Cdd:TIGR01271 894 nPSAPNyvdqqhanasspdvqkPVIITPTSA----YYIFYIYVGTADSVLALgfFRGLPLVHTLLTVSKRLHEQMLHSVL 969
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 359 MAPVTFFNATPTGRILNRFSSDVACADDSLPFILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASS 438
Cdd:TIGR01271 970 QAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTS 1049
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 439 RELRRLGSLTLSPLYSHLADTLAGLSVLRATGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGI 518
Cdd:TIGR01271 1050 QQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDIIFVFFFIAVTFI 1129
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 519 ALVQHQQGlanPGLVGLSLSYALSLTGLLSGLVSSFTQTEAMLVSVERLEEYTcDLPQEP-----QGQPLQLGTG----- 588
Cdd:TIGR01271 1130 AIGTNQDG---EGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFI-DLPQEEprpsgGGGKYQLSTVlvien 1205
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 589 ------WLTQGGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEpSSGRVLLDGVDTSQ 662
Cdd:TIGR01271 1206 phaqkcWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNS 1284
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 663 LELAQLRSQLAIIPQEPFLFSGTVRENLDPQGLHKDRALWQALKQCHLSEVITSMGGLDGELGEGGRS-LSLGQRQLLCL 741
Cdd:TIGR01271 1285 VTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYvLSNGHKQLMCL 1364
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767940955 742 ARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATLRNQ 818
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNE 1441
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
311-818 |
1.90e-80 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 270.11 E-value: 1.90e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 311 SDIRFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVA----CADD 386
Cdd:COG1132 58 SALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDaveqFLAH 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 387 SLPFILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRlgslTLSPLYSHLADTLAGLSVL 466
Cdd:COG1132 138 GLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQE----ALAELNGRLQESLSGIRVV 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 467 RATGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGLANPGLVGLSLSYALSLTGL 546
Cdd:COG1132 214 KAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGP 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 547 LSGLVSSFTQTEAMLVSVERLEEY---TCDLPQEPQGQPLQLgtgwlTQGGVEFQDVVLAYRPGLPnALDGVTFCVQPGE 623
Cdd:COG1132 294 LRQLANVLNQLQRALASAERIFELldePPEIPDPPGAVPLPP-----VRGEIEFENVSFSYPGDRP-VLKDISLTIPPGE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 624 KLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENL---DPQglHKDRA 700
Cdd:COG1132 368 TVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRPD--ATDEE 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 701 LWQALKQCHLSEVITSM------------GgldgelgeggrSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQL 768
Cdd:COG1132 446 VEEAAKAAQAHEFIEALpdgydtvvgergV-----------NLSGGQRQRIAIARALLKDPPILILDEATSALDTETEAL 514
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 767940955 769 LQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATLRNQ 818
Cdd:COG1132 515 IQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLAR 564
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-150 |
2.41e-78 |
|
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: 251.62 E-value: 2.41e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 2 LRGHVAVRGlskGFGLATQEPWIQFATIRDNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRA 81
Cdd:cd03250 58 LSGSVSVPG---SIAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQ 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 82 RIALARAVYQEKELYLLDDPLAAVDADVANHLLHRCILGMLSYT-TRLLCTHRTEYLERADAVLLMEAGR 150
Cdd:cd03250 135 RISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
589-812 |
6.53e-78 |
|
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: 250.79 E-value: 6.53e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 589 WLTQGGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQL 668
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 669 RSQLAIIPQEPFLFSGTVRENLDPQGLHKDRALWQALKqchLSEvitsmggldgelgeGGRSLSLGQRQLLCLARALLTD 748
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR---VSE--------------GGLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767940955 749 AKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSP 812
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
304-818 |
1.40e-67 |
|
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: 238.19 E-value: 1.40e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 304 KAAPNGSSDIRFYLTVYATIAGV-NSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVA 382
Cdd:COG2274 185 RVLPNQDLSTLWVLAIGLLLALLfEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRDVES 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 383 CAD-----------DSLPFILNILLanaagllgllavlgsglpwlllllpplsIMYYH--------------------VQ 431
Cdd:COG2274 265 IREfltgslltallDLLFVLIFLIV----------------------------LFFYSpplalvvllliplyvllgllFQ 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 432 RHYRASSRELRRLGSLtlspLYSHLADTLAGLSVLRATGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAV 511
Cdd:COG2274 317 PRLRRLSREESEASAK----RQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLA 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 512 VSAI--AGIALVQHQQ-------------GLANPGLVGLslsyalsltgllsglVSSFTQTEAMLVSVERLEEYTcDLPQ 576
Cdd:COG2274 393 TVALlwLGAYLVIDGQltlgqliafnilsGRFLAPVAQL---------------IGLLQRFQDAKIALERLDDIL-DLPP 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 577 EPQGQPLQLGTGWLtQGGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLD 656
Cdd:COG2274 457 EREEGRSKLSLPRL-KGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILID 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 657 GVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENL---DPQglHKDRALWQALKQCHLSEVITSMGG-LDGELGEGGRSLS 732
Cdd:COG2274 536 GIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItlgDPD--ATDEEIIEAARLAGLHDFIEALPMgYDTVVGEGGSNLS 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 733 LGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSP 812
Cdd:COG2274 614 GGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTH 693
|
....*.
gi 767940955 813 ATLRNQ 818
Cdd:COG2274 694 EELLAR 699
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
235-571 |
8.60e-66 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 221.61 E-value: 8.60e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 235 LAILFSLLLMQATRNAADWWLSHWISQlkaenssqeaqpstspasmglfspqlllfspgnlyipvfplpkAAPNGSSDIR 314
Cdd:cd18580 2 LLLLLLLLLLAFLSQFSNIWLDWWSSD-------------------------------------------WSSSPNSSSG 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 315 FYLTVYATIAGVNS-LCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFILN 393
Cdd:cd18580 39 YYLGVYAALLVLASvLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALL 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 394 ILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGATY 473
Cdd:cd18580 119 DFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQE 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 474 RFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQglANPGLVGLSLSYALSLTGLLSGLVSS 553
Cdd:cd18580 199 RFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALLALVVALLAVLLRSS--ISAGLVGLALTYALSLTGSLQWLVRQ 276
|
330
....*....|....*...
gi 767940955 554 FTQTEAMLVSVERLEEYT 571
Cdd:cd18580 277 WTELETSMVSVERILEYT 294
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
593-808 |
5.16e-63 |
|
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: 211.70 E-value: 5.16e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 593 GGVEFQDVVLAYRPGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQL 672
Cdd:cd03254 1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 673 AIIPQEPFLFSGTVRENLDPQGLHKDRALWQ-ALKQCHLSEVITSMGG-LDGELGEGGRSLSLGQRQLLCLARALLTDAK 750
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIeAAKEAGAHDFIMKLPNgYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767940955 751 ILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVE 808
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIE 217
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
595-805 |
5.68e-61 |
|
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: 203.77 E-value: 5.68e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAI 674
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 675 IPQEPFLFSGTVRENLdpqglhkdralwqalkqchlsevitsmggldgelgeggrsLSLGQRQLLCLARALLTDAKILCI 754
Cdd:cd03228 81 VPQDPFLFSGTIRENI----------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767940955 755 DEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGR 805
Cdd:cd03228 121 DEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
303-571 |
1.32e-59 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350047 [Multi-domain] Cd Length: 296 Bit Score: 204.63 E-value: 1.32e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 303 PKAAPNGSSDIR-FYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDV 381
Cdd:cd18603 29 PALNGTQDTEQRdYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 382 ACADDSLPFILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLA 461
Cdd:cd18603 109 DTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQRFYVATSRQLKRLESVSRSPIYSHFSETLQ 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 462 GLSVLRATGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGlaNPGLVGLSLSYAL 541
Cdd:cd18603 189 GASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLIVLFAALFAVLSRDSL--SPGLVGLSISYAL 266
|
250 260 270
....*....|....*....|....*....|
gi 767940955 542 SLTGLLSGLVSSFTQTEAMLVSVERLEEYT 571
Cdd:cd18603 267 QITQTLNWLVRMTSELETNIVSVERIKEYS 296
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
593-818 |
7.79e-57 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 195.90 E-value: 7.79e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 593 GGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQL 672
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 673 AIIPQEPFLFSGTVRENLDPQGLHKDRALWQALKQCHLSEVITSM-GGLDGELGEGGRSLSLGQRQLLCLARALLTDAKI 751
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLpGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767940955 752 LCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATLRNQ 818
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQ 244
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
235-571 |
3.57e-56 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 195.38 E-value: 3.57e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 235 LAILFSLLLMQATRNAADWWLSHWisqlkaenSSQEAQPSTSPASmglfspqlllfspgnlyipvfplpkaapngSSDIR 314
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIW--------ASAYETSSALPPS------------------------------EVSVL 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 315 FYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFILNI 394
Cdd:cd18604 44 YYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSS 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 395 LLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGATYR 474
Cdd:cd18604 124 LLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEER 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 475 FEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQqglANPGLVGLSLSYALSLTGLLSGLVSSF 554
Cdd:cd18604 204 FIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALFSFATAALLVYGPG---IDAGLAGFSLSFALGFSSAILWLVRSY 280
|
330
....*....|....*..
gi 767940955 555 TQTEAMLVSVERLEEYT 571
Cdd:cd18604 281 NELELDMNSVERIQEYL 297
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
576-818 |
1.60e-55 |
|
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: 201.14 E-value: 1.60e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 576 QEPQGQPLQLGTGWLTQGGVEFQDVVLAYrPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLL 655
Cdd:COG4988 318 PEPAAPAGTAPLPAAGPPSIELEDVSFSY-PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILI 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 656 DGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENL---DPQGlhKDRALWQALKQCHLSEVITSMGGLDGELGEGG-RSL 731
Cdd:COG4988 397 NGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLrlgRPDA--SDEELEAALEAAGLDEFVAALPDGLDTPLGEGgRGL 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 732 SLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDS 811
Cdd:COG4988 475 SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGT 554
|
....*..
gi 767940955 812 PATLRNQ 818
Cdd:COG4988 555 HEELLAK 561
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
595-808 |
8.26e-55 |
|
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: 189.36 E-value: 8.26e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAI 674
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 675 IPQEPFLFSGTVRENL---DPQGLHKDraLWQALKQCHLSEVITSMGGLDGELGEGGRS-LSLGQRQLLCLARALLTDAK 750
Cdd:cd03251 81 VSQDVFLFNDTVAENIaygRPGATREE--VEEAARAANAHEFIMELPEGYDTVIGERGVkLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767940955 751 ILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVE 808
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVE 216
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
234-571 |
1.63e-53 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 188.20 E-value: 1.63e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 234 ALAILFSLLLMQATRNAADWWLSHWisqlkaenssQEAQPSTSPASMGLFSPQLLlfspgnlyipvfplpkaapngSSDI 313
Cdd:cd18602 1 VALVLALALLKQGLRVATDFWLADW----------TEANHDVASVVFNITSSSLE---------------------DDEV 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 314 RFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFILN 393
Cdd:cd18602 50 SYYISVYAGLSLGAVILSLVTNLAGELAGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 394 ILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGATY 473
Cdd:cd18602 130 RLLRFLLLCLSAIIVNAIVTPYFLIALIPIIIVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 474 RFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGLANPGLVGLSLSYALSLTGLLSGLVSS 553
Cdd:cd18602 210 RFTQQMLELIDRNNTAFLFLNTANRWLGIRLDYLGAVIVFLAALSSLTAALAGYISPSLVGLAITYALLVPIYLNWVVRN 289
|
330
....*....|....*...
gi 767940955 554 FTQTEAMLVSVERLEEYT 571
Cdd:cd18602 290 LADVEMQMNSVERVLEYT 307
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
235-571 |
4.63e-53 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 186.53 E-value: 4.63e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 235 LAILFSLLLMQATRNAADWWLSHWISQLkaenssqeaqpstspasmglfspqlllfspgnlyipvFPLPKAapngssdir 314
Cdd:cd18606 2 PLLLLLLILSQFAQVFTNLWLSFWTEDF-------------------------------------FGLSQG--------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 315 FYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLP----- 389
Cdd:cd18606 36 FYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPdslrm 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 390 -----------FILNIllanaagllgllavlgSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLAD 458
Cdd:cd18606 116 flytlssiigtFILII----------------IYLPWFAIALPPLLVLYYFIANYYRASSRELKRLESILRSFVYANFSE 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 459 TLAGLSVLRATGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVqhQQGLANPGLVGLSLS 538
Cdd:cd18606 180 SLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLLVLIVALLCVT--RRFSISPSSTGLVLS 257
|
330 340 350
....*....|....*....|....*....|...
gi 767940955 539 YALSLTGLLSGLVSSFTQTEAMLVSVERLEEYT 571
Cdd:cd18606 258 YVLQITQVLSWLVRQFAEVENNMNSVERLLHYA 290
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
595-815 |
1.57e-51 |
|
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: 180.43 E-value: 1.57e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAY--RPGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQL 672
Cdd:cd03249 1 IEFKNVSFRYpsRPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 673 AIIPQEPFLFSGTVRENL---DPQGLHKDRAlwQALKQCHLSEVITSMGGLDGELGEGGRS-LSLGQRQLLCLARALLTD 748
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIrygKPDATDEEVE--EAAKKANIHDFIMSLPDGYDTLVGERGSqLSGGQKQRIAIARALLRN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767940955 749 AKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATL 815
Cdd:cd03249 158 PKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDEL 224
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
323-808 |
4.11e-51 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 188.77 E-value: 4.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 323 IAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDV----ACADDSLPFILNILLAN 398
Cdd:TIGR02203 63 LAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSeqvaSAATDAFIVLVRETLTV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 399 AAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRL-GSLTLSplyshLADTLAGLSVLRATGA----TY 473
Cdd:TIGR02203 143 IGLFIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSmGQVTTV-----AEETLQGYRVVKLFGGqayeTR 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 474 RFEEENLRLLELNQRCQFATSAtmqwLDIRLQLMGAAVVSAIAGIALVQHQQGLANPG-LVGLSLSY-ALSLTGLLSGLV 551
Cdd:TIGR02203 218 RFDAVSNRNRRLAMKMTSAGSI----SSPITQLIASLALAVVLFIALFQAQAGSLTAGdFTAFITAMiALIRPLKSLTNV 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 552 SSFTQTeaMLVSVERLEEYTcDLPQEPQGQPLQLGTgwlTQGGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRT 631
Cdd:TIGR02203 294 NAPMQR--GLAAAESLFTLL-DSPPEKDTGTRAIER---ARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRS 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 632 GSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENL---DPQGLHKDRALwQALKQC 708
Cdd:TIGR02203 368 GSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRTEQADRAEIE-RALAAA 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 709 HLSEVITSMGGLDGELGEGGRS-LSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAH 787
Cdd:TIGR02203 447 YAQDFVDKLPLGLDTPIGENGVlLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAH 526
|
490 500
....*....|....*....|.
gi 767940955 788 RLNTILNSDRVLVLQAGRVVE 808
Cdd:TIGR02203 527 RLSTIEKADRIVVMDDGRIVE 547
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
595-815 |
1.50e-49 |
|
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: 174.73 E-value: 1.50e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAI 674
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 675 IPQEPFLFSGTVRENL---DPQGlhKDRALWQALKQCHLSEVITSMGGLDGELGEGgRSLSL--GQRQLLCLARALLTDA 749
Cdd:cd03253 80 VPQDTVLFNDTIGYNIrygRPDA--TDEEVIEAAKAAQIHDKIMRFPDGYDTIVGE-RGLKLsgGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767940955 750 KILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATL 815
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEEL 222
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
230-571 |
3.63e-49 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 176.21 E-value: 3.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 230 GQGLALAILFSLLLMQATRNAADWWLSHWISQLKAENSSQEAQPSTSPASMglfspqlllfspgnlyipvfplpkaapNG 309
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQGSGNTTNNVDNSTVDSGNI---------------------------SD 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 310 SSDIRFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLP 389
Cdd:cd18599 54 NPDLNFYQLVYGGSILVILLLSLIRGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 390 FILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRAT 469
Cdd:cd18599 134 FTLENFLQNVLLVVFSLIIIAIVFPWFLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAF 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 470 GATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHqqGLANPGLVGLSLSYALSLTGLLSG 549
Cdd:cd18599 214 NKEKEFLSKFKKLLDQNSSAFFLFNCAMRWLAVRLDILAVLITLITALLVVLLK--GSISPAFAGLALSYALQLSGLFQF 291
|
330 340
....*....|....*....|..
gi 767940955 550 LVSSFTQTEAMLVSVERLEEYT 571
Cdd:cd18599 292 TVRLASETEARFTSVERILEYI 313
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
595-815 |
2.38e-46 |
|
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: 165.74 E-value: 2.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAI 674
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 675 IPQEPFLFSGTVRENL---DPqGLHKDRALWQA-LKQCHlsEVITSMGGLDGELGEGG-RSLSLGQRQLLCLARALLTDA 749
Cdd:cd03252 81 VLQENVLFNRSIRDNIalaDP-GMSMERVIEAAkLAGAH--DFISELPEGYDTIVGEQgAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767940955 750 KILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATL 815
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
593-807 |
5.51e-44 |
|
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: 158.52 E-value: 5.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 593 GGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQL 672
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 673 AIIPQEPFLFSGTVRENL---DPqgLHKDRALWQALKQCHLSEVI-TSMGGLDGELGEGGRSLSLGQRQLLCLARALLTD 748
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNItlgAP--LADDERILRAAELAGVTDFVnKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767940955 749 AKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVV 807
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
232-571 |
2.14e-43 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 159.79 E-value: 2.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 232 GLALAILFSLLlMQATRNAADWWLSHWisqlkaeNSSQEAQPSTSPASMGLFSpqlllfspGNLYIPVfplpkaapngsS 311
Cdd:cd18601 4 VFILLVLLNIA-AQVLYVLSDWWLSYW-------ANLEEKLNDTTDRVQGENS--------TNVDIED-----------L 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 312 DIRFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLPFI 391
Cdd:cd18601 57 DRDFNLGIYAGLTAATFVFGFLRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 392 LNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRATGA 471
Cdd:cd18601 137 FLDFLQLLLQVVGVVLLAVVVNPWVLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 472 TYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVqhqqgLA---NPGLVGLSLSYALSLTGLLS 548
Cdd:cd18601 217 QERFQEEFDAHQDLHSEAWFLFLATSRWLAVRLDALCALFVTVVAFGSLF-----LAeslDAGLVGLSLSYALTLMGTFQ 291
|
330 340
....*....|....*....|...
gi 767940955 549 GLVSSFTQTEAMLVSVERLEEYT 571
Cdd:cd18601 292 WCVRQSAEVENLMTSVERVLEYS 314
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
565-819 |
2.75e-43 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 167.98 E-value: 2.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 565 ERLEEYTCDLPQEPQgqPLQLGTGWLtQGGVEFQDVVLAY--RPGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVL 642
Cdd:TIGR00958 452 EKVFEYLDRKPNIPL--TGTLAPLNL-EGLIEFQDVSFSYpnRPDVP-VLKGLTFTLHPGEVVALVGPSGSGKSTVAALL 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 643 FRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENLdPQGLHK--DRALWQALKQCHLSEVITSMGGL 720
Cdd:TIGR00958 528 QNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENI-AYGLTDtpDEEIMAAAKAANAHDFIMEFPNG 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 721 DGELGEGGRS-LSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTicKRFANKTVLTIAHRLNTILNSDRVL 799
Cdd:TIGR00958 607 YDTEVGEKGSqLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIAHRLSTVERADQIL 684
|
250 260
....*....|....*....|
gi 767940955 800 VLQAGRVVELDSPATLRNQP 819
Cdd:TIGR00958 685 VLKKGSVVEMGTHKQLMEDQ 704
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
573-808 |
3.57e-41 |
|
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: 160.37 E-value: 3.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 573 DLPQE----PQGQPLQLgtgwlTQGGVEFQDVVLAYRPGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEP 648
Cdd:COG5265 337 DQPPEvadaPDAPPLVV-----GGGEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDV 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 649 SSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENL---DPQGLHKDraLWQALKQCHLSEVItsmggldgelg 725
Cdd:COG5265 411 TSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIaygRPDASEEE--VEAAARAAQIHDFI----------- 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 726 eggRS---------------LSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLN 790
Cdd:COG5265 478 ---ESlpdgydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLS 554
|
250
....*....|....*...
gi 767940955 791 TILNSDRVLVLQAGRVVE 808
Cdd:COG5265 555 TIVDADEILVLEAGRIVE 572
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
18-149 |
2.27e-40 |
|
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: 148.25 E-value: 2.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 18 ATQEPWIQFATIRDNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYL 97
Cdd:cd03290 84 AAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVF 163
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 767940955 98 LDDPLAAVDADVANHLLHRCILGMLSYTTR--LLCTHRTEYLERADAVLLMEAG 149
Cdd:cd03290 164 LDDPFSALDIHLSDHLMQEGILKFLQDDKRtlVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
515-808 |
1.57e-39 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 155.12 E-value: 1.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 515 IAGIALvqHQQGLANPGLVGLSLSYALSLTGLLSGLVSSFTQTeamLVSVERLEEY-----TCDLPQEPQGQPlQLGTgw 589
Cdd:PRK13657 259 VLGAAL--VQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQV---FMAAPKLEEFfevedAVPDVRDPPGAI-DLGR-- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 590 lTQGGVEFQDVVLAYrPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLR 669
Cdd:PRK13657 331 -VKGAVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLR 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 670 SQLAIIPQEPFLFSGTVRENL---DPQGLHKDraLWQALKQCHLSEVI-TSMGGLDGELGEGGRSLSLGQRQLLCLARAL 745
Cdd:PRK13657 409 RNIAVVFQDAGLFNRSIEDNIrvgRPDATDEE--MRAAAERAQAHDFIeRKPDGYDTVVGERGRQLSGGERQRLAIARAL 486
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767940955 746 LTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVE 808
Cdd:PRK13657 487 LKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVE 549
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
593-818 |
1.45e-38 |
|
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: 145.00 E-value: 1.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 593 GGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEpSSGRVLLDGVDTSQLELAQLRSQL 672
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 673 AIIPQEPFLFSGTVRENLDPQGLHKDRALWQALKQCHLSEVITSMGGLDGELGEGGRS-LSLGQRQLLCLARALLTDAKI 751
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCvLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767940955 752 LCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATLRNQ 818
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
592-806 |
2.44e-38 |
|
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: 142.61 E-value: 2.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 592 QGGVEFQDVVLAY--RPGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLR 669
Cdd:cd03248 9 KGIVKFQNVTFAYptRPDTL-VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 670 SQLAIIPQEPFLFSGTVRENLdPQGLHK--DRALWQALKQCHLSEVITSMGGLDGELGEGGRS-LSLGQRQLLCLARALL 746
Cdd:cd03248 88 SKVSLVGQEPVLFARSLQDNI-AYGLQScsFECVKEAAQKAHAHSFISELASGYDTEVGEKGSqLSGGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 747 TDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRV 806
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
596-806 |
8.31e-38 |
|
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: 139.27 E-value: 8.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 596 EFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAII 675
Cdd:cd03246 2 EVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 676 PQEPFLFSGTVRENLdpqglhkdralwqalkqchlsevitsmggldgelgeggrsLSLGQRQLLCLARALLTDAKILCID 755
Cdd:cd03246 82 PQDDELFSGSIAENI----------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767940955 756 EATASVDQKTDQLLQQTICK-RFANKTVLTIAHRLNTILNSDRVLVLQAGRV 806
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAAlKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
595-808 |
2.08e-37 |
|
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: 138.21 E-value: 2.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLElAQLRSQLAI 674
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 675 IPQEPFLFSGTVRENLDpqglhkdralwqalkqchlsevitsmggldgelgeggRSLSLGQRQLLCLARALLTDAKILCI 754
Cdd:cd03247 80 LNQRPYLFDTTLRNNLG-------------------------------------RRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767940955 755 DEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVE 808
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-160 |
1.04e-36 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 139.61 E-value: 1.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 18 ATQEPWIQFATIRDNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYL 97
Cdd:cd03291 103 SSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYL 182
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767940955 98 LDDPLAAVDADVANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEI 160
Cdd:cd03291 183 LDSPFGYLDVFTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
590-818 |
2.28e-36 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 145.35 E-value: 2.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 590 LTQGGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLR 669
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 670 SQLAIIPQEPFLFSGTVRENL---DPQGlhKDRALWQALKQCHLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALL 746
Cdd:PRK11160 414 QAISVVSQRVHLFSATLRDNLllaAPNA--SDEALIEVLQQVGLEKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767940955 747 TDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATLRNQ 818
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQ 563
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
592-818 |
4.04e-36 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 144.78 E-value: 4.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 592 QGGVEFQDVVLAYrPGLPN-ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRS 670
Cdd:PRK11176 339 KGDIEFRNVTFTY-PGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRN 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 671 QLAIIPQEPFLFSGTVRENL--DPQGLHKDRALWQALKQCHLSEVITSMGGLDGELGEGG-RSLSLGQRQLLCLARALLT 747
Cdd:PRK11176 418 QVALVSQNVHLFNDTIANNIayARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENgVLLSGGQRQRIAIARALLR 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767940955 748 DAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATLRNQ 818
Cdd:PRK11176 498 DSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQ 568
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
577-801 |
3.42e-35 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 141.27 E-value: 3.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 577 EPQGQPL--QLGTGWLTQGGVEFQDVVLAYrPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVL 654
Cdd:TIGR02857 302 DAAPRPLagKAPVTAAPASSLEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIA 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 655 LDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENL---DPQGlhKDRALWQALKQCHLSEVITSMGGLDGELG-EGGRS 730
Cdd:TIGR02857 381 VNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIrlaRPDA--SDAEIREALERAGLDEFVAALPQGLDTPIgEGGAG 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767940955 731 LSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVL 801
Cdd:TIGR02857 459 LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
555-808 |
1.42e-34 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 140.24 E-value: 1.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 555 TQTEAML----VSVERLEEYTcDLPQEPQGQPLQLgtgwLTQGGVEFQDVVLAYRPGLPnALDGVTFCVQPGEKLGIVGR 630
Cdd:PRK10790 302 TTQQSMLqqavVAGERVFELM-DGPRQQYGNDDRP----LQSGRIDIDNVSFAYRDDNL-VLQNINLSVPSRGFVALVGH 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 631 TGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENLDpqgLHKD---RALWQALKQ 707
Cdd:PRK10790 376 TGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVT---LGRDiseEQVWQALET 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 708 CHLSEVITSMGGLDGELGEGG-RSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIA 786
Cdd:PRK10790 453 VQLAELARSLPDGLYTPLGEQgNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIA 532
|
250 260
....*....|....*....|..
gi 767940955 787 HRLNTILNSDRVLVLQAGRVVE 808
Cdd:PRK10790 533 HRLSTIVEADTILVLHRGQAVE 554
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
593-818 |
5.00e-34 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 139.49 E-value: 5.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 593 GGVEFQDVVLAYRPGlPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQL 672
Cdd:TIGR01193 472 GDIVINDVSYSYGYG-SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 673 AIIPQEPFLFSGTVRENL---DPQGLHKDRaLWQALKQCHLSEVITSMGG-LDGELGEGGRSLSLGQRQLLCLARALLTD 748
Cdd:TIGR01193 551 NYLPQEPYIFSGSILENLllgAKENVSQDE-IWAACEIAEIKDDIENMPLgYQTELSEEGSSISGGQKQRIALARALLTD 629
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767940955 749 AKILCIDEATASVdqktDQLLQQTICKRFAN---KTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATLRNQ 818
Cdd:TIGR01193 630 SKVLILDESTSNL----DTITEKKIVNNLLNlqdKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
592-819 |
5.29e-34 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 139.32 E-value: 5.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 592 QGGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQ 671
Cdd:TIGR03797 449 SGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQ 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 672 LAIIPQEPFLFSGTVRENL-DPQGLHKDRAlWQALKQCHLSEVITSM-GGLDGELGEGGRSLSLGQRQLLCLARALLTDA 749
Cdd:TIGR03797 529 LGVVLQNGRLMSGSIFENIaGGAPLTLDEA-WEAARMAGLAEDIRAMpMGMHTVISEGGGTLSGGQRQRLLIARALVRKP 607
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 750 KILCIDEATASVDQKTDQLLQQTICKrfANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATLRNQP 819
Cdd:TIGR03797 608 RILLFDEATSALDNRTQAIVSESLER--LKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMARE 675
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
595-819 |
5.67e-33 |
|
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: 134.26 E-value: 5.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGLPN---ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQL 668
Cdd:COG1123 261 LEVRNLSKRYPVRGKGgvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 669 RSQLAIIPQEPF--LFSG-TVRENL-DPQGLH--------KDRALwQALKQCHLSEvitsmggldGELGEGGRSLSLGQR 736
Cdd:COG1123 341 RRRVQMVFQDPYssLNPRmTVGDIIaEPLRLHgllsraerRERVA-ELLERVGLPP---------DLADRYPHELSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 737 QLLCLARALLTDAKILCIDEATASVDQKT-DQLLQ--QTICKRFaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSP 812
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVqAQILNllRDLQREL-GLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPT 489
|
....*..
gi 767940955 813 ATLRNQP 819
Cdd:COG1123 490 EEVFANP 496
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
615-819 |
2.60e-32 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 133.05 E-value: 2.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 615 VTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLePSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENL---D 691
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVllgN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 692 PQGlhKDRALWQALKQCHLSEVITSMGG-LDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQ 770
Cdd:PRK11174 448 PDA--SDEQLQQALENAWVSEFLPLLPQgLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVM 525
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767940955 771 QTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATLRNQP 819
Cdd:PRK11174 526 QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
596-805 |
4.62e-32 |
|
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: 124.12 E-value: 4.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 596 EFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAII 675
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 676 PQEPF--LFSGTVRE----NLDPQGLHKD---RALWQALKQCHLSEvitsmggldgELGEGGRSLSLGQRQLLCLARALL 746
Cdd:cd03225 81 FQNPDdqFFGPTVEEevafGLENLGLPEEeieERVEEALELVGLEG----------LRDRSPFTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767940955 747 TDAKILCIDEATASVDQKTDQLLQQTICK-RFANKTVLTIAHRLNTILN-SDRVLVLQAGR 805
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
435-789 |
3.43e-31 |
|
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: 129.02 E-value: 3.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 435 RASSRELRRLgsltLSPLYSHLADTLAGLSVLRATGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQL-MGAAVVS 513
Cdd:TIGR02868 179 RAAEQALARL----RGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALGAALTLLaAGLAVLG 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 514 AI--AGIALVQHQQG---LANPGLVGLSLSYALSLTGLlsglvsSFTQTEAMLVSVERLEEYTCDLPQEPQGQPLQLGTG 588
Cdd:TIGR02868 255 ALwaGGPAVADGRLApvtLAVLVLLPLAAFEAFAALPA------AAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAV 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 589 WLTQGGVEFQDVVLAYrPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQL 668
Cdd:TIGR02868 329 GLGKPTLELRDLSAGY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 669 RSQLAIIPQEPFLFSGTVRENL---DPQGlhKDRALWQALKQCHLSEVITSMGG-LDGELGEGGRSLSLGQRQLLCLARA 744
Cdd:TIGR02868 408 RRRVSVCAQDAHLFDTTVRENLrlaRPDA--TDEELWAALERVGLADWLRALPDgLDTVLGEGGARLSGGERQRLALARA 485
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 767940955 745 LLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRL 789
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
612-759 |
5.67e-31 |
|
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: 118.90 E-value: 5.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 612 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSG-TVRENL 690
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767940955 691 -------DPQGLHKDRALWQALKQCHLSEVITSmggldgELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATA 759
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEKLGLGDLADR------PVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
595-808 |
1.49e-30 |
|
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: 120.30 E-value: 1.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRP--GLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQL---R 669
Cdd:cd03257 2 LEVKNLSVSFPTggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 670 SQLAIIPQEPFL---FSGTVRENL-DPQGLHKD--------RALWQALKQCHLSEVITSMggldgelgeGGRSLSLGQRQ 737
Cdd:cd03257 82 KEIQMVFQDPMSslnPRMTIGEQIaEPLRIHGKlskkearkEAVLLLLVGVGLPEEVLNR---------YPHELSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767940955 738 LLCLARALLTDAKILCIDEATASVDQKT-DQLLQ--QTICKRFaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVE 808
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVqAQILDllKKLQEEL-GLTLLFITHDLGVVAKiADRVAVMYAGKIVE 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
595-819 |
9.26e-29 |
|
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: 115.37 E-value: 9.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDV--VLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLR 669
Cdd:cd03258 2 IELKNVskVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLsgkELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 670 SQLAIIPQEPFLFSG-TVREN----LDPQGLHKDRALWQA---LKQCHLSEVITSmggldgelgeGGRSLSLGQRQLLCL 741
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENvalpLEIAGVPKAEIEERVlelLELVGLEDKADA----------YPAQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 742 ARALLTDAKILCIDEATASVDQKTDQ----LLQQTICKRfaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLR 816
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQsilaLLRDINREL--GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVF 229
|
...
gi 767940955 817 NQP 819
Cdd:cd03258 230 ANP 232
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
596-805 |
9.82e-29 |
|
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: 112.72 E-value: 9.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 596 EFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAII 675
Cdd:cd00267 1 EIENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 676 PQepflfsgtvrenldpqglhkdralwqalkqchlsevitsmggldgelgeggrsLSLGQRQLLCLARALLTDAKILCID 755
Cdd:cd00267 79 PQ-----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767940955 756 EATASVDQKTDQLLQQTIcKRFA--NKTVLTIAHRLNTILN-SDRVLVLQAGR 805
Cdd:cd00267 106 EPTSGLDPASRERLLELL-RELAeeGRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
565-807 |
2.35e-28 |
|
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: 120.62 E-value: 2.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 565 ERLEEYTCDLPQEPQGQPLQLgtgwlTQGGVEFQDVVLAYrPGLPNA-LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLF 643
Cdd:COG4618 306 RRLNELLAAVPAEPERMPLPR-----PKGRLSVENLTVVP-PGSKRPiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLV 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 644 RLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVREN------LDPQglhkdrALWQALKQCHLSEVITSM 717
Cdd:COG4618 380 GVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENiarfgdADPE------KVVAAAKLAGVHEMILRL 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 718 GGL-DGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICK-RFANKTVLTIAHRLNTILNS 795
Cdd:COG4618 454 PDGyDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAlKARGATVVVITHRPSLLAAV 533
|
250
....*....|..
gi 767940955 796 DRVLVLQAGRVV 807
Cdd:COG4618 534 DKLLVLRDGRVQ 545
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
595-806 |
8.53e-28 |
|
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: 110.57 E-value: 8.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGLpnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQlELAQLRSQLAI 674
Cdd:cd03230 1 IEVRNLSKRYGKKT--ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 675 IPQEPFLFSG-TVRENLDpqglhkdralwqalkqchlsevitsmggldgelgeggrsLSLGQRQLLCLARALLTDAKILC 753
Cdd:cd03230 78 LPEEPSLYENlTVRENLK---------------------------------------LSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767940955 754 IDEATASVDQKTDQLLQQTIcKRFA--NKTVLTIAHRLNTILN-SDRVLVLQAGRV 806
Cdd:cd03230 119 LDEPTSGLDPESRREFWELL-RELKkeGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
11-161 |
1.41e-27 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 118.32 E-value: 1.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 11 LSKGFGLATQEPWIQFATIRDNILFGKTF--DAQLyKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARA 88
Cdd:COG4988 409 WRRQIAWVPQNPYLFAGTIRENLRLGRPDasDEEL-EAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARA 487
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767940955 89 VYQEKELYLLDDPLAAVDADVANHLLHRcILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 161
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAETEAEILQA-LRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELL 559
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
11-161 |
1.67e-27 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 118.33 E-value: 1.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 11 LSKGFGLATQEPWIQFATIRDNILFGK---TfDAQLYkEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALAR 87
Cdd:COG4987 407 LRRRIAVVPQRPHLFDTTLRENLRLARpdaT-DEELW-AALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALAR 484
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767940955 88 AVYQEKELYLLDDPLAAVDADVANHLLHRcILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 161
Cdd:COG4987 485 ALLRDAPILLLDEPTEGLDAATEQALLAD-LLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELL 557
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
15-161 |
2.60e-27 |
|
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: 118.40 E-value: 2.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 15 FGLATQEPWIQFATIRDNILFGKTF--DAQLYkEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQE 92
Cdd:COG2274 551 IGVVLQDVFLFSGTIRENITLGDPDatDEEII-EAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRN 629
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767940955 93 KELYLLDDPLAAVDADVANHLLHRcILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 161
Cdd:COG2274 630 PRILILDEATSALDAETEAIILEN-LRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELL 697
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
595-806 |
3.33e-27 |
|
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: 110.27 E-value: 3.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGLPN--ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLR 669
Cdd:cd03255 1 IELKNLSKTYGGGGEKvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLsekELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 670 -SQLAIIPQE----PFLfsgTVRENL--------DPQGLHKDRALwQALKQCHLSEVITSMggldgelgegGRSLSLGQR 736
Cdd:cd03255 81 rRHIGFVFQSfnllPDL---TALENVelplllagVPKKERRERAE-ELLERVGLGDRLNHY----------PSELSGGQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767940955 737 QLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICK--RFANKTVLTIAHRLNTILNSDRVLVLQAGRV 806
Cdd:cd03255 147 QRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
595-819 |
3.99e-27 |
|
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: 116.54 E-value: 3.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPS---SGRVLLDGVDTSQLELAQLRSQ 671
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 672 LAIIPQEPF--LFSGTVRENLD--------PQGLHKDRALWqALKQCHLSEVITSMGGLdgelgeggrsLSLGQRQLLCL 741
Cdd:COG1123 85 IGMVFQDPMtqLNPVTVGDQIAealenlglSRAEARARVLE-LLEAVGLERRLDRYPHQ----------LSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 742 ARALLTDAKILCIDEATASVDQKTDQLLQQTI--CKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQ 818
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLreLQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
|
.
gi 767940955 819 P 819
Cdd:COG1123 234 P 234
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
595-808 |
4.87e-27 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 110.13 E-value: 4.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGLPN--ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLR 669
Cdd:COG1136 5 LELRNLTKSYGTGEGEvtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLserELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 670 SQ-LAIIPQEPFLFSG-TVREN----LDPQGLHK----DRALwQALKQCHLSEVITSMGgldgelgeggRSLSLGQRQLL 739
Cdd:COG1136 85 RRhIGFVFQFFNLLPElTALENvalpLLLAGVSRkerrERAR-ELLERVGLGDRLDHRP----------SQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767940955 740 CLARALLTDAKILCIDEATASVDQKT-DQLLQ--QTICKRFaNKTVLTIAHRLNTILNSDRVLVLQAGRVVE 808
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTgEEVLEllRELNREL-GTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
595-815 |
1.98e-26 |
|
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: 108.42 E-value: 1.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGlpNALDGVTFCVQPGEKLGIVGRTGSGKSSL-----LLVLFRLLEPSSGRVLLDGVD--TSQLELAQ 667
Cdd:cd03260 1 IELRDLNVYYGDK--HALKDISLDIPKGEITALIGPSGCGKSTLlrllnRLNDLIPGAPDEGEVLLDGKDiyDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 668 LRSQLAIIPQEPFLFSGTVRENLD----PQGLHKDRAL----WQALKQCHLSEvitsmgglDGELGEGGRSLSLGQRQLL 739
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAyglrLHGIKLKEELdervEEALRKAALWD--------EVKDRLHALGLSGGQQQRL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 740 CLARALLTDAKILCIDEATASVD----QKTDQLLQQtICKRFankTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPAT 814
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDpistAKIEELIAE-LKKEY---TIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQ 226
|
.
gi 767940955 815 L 815
Cdd:cd03260 227 I 227
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
595-820 |
5.55e-26 |
|
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: 107.58 E-value: 5.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGLPN--ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQL 672
Cdd:COG1124 2 LEVRNLSVSYGQGGRRvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 673 AIIPQEPFLfS----GTVRENLD-PQGLHK----DRALWQALKQCHLSEvitsmggldGELGEGGRSLSLGQRQLLCLAR 743
Cdd:COG1124 82 QMVFQDPYA-SlhprHTVDRILAePLRIHGlpdrEERIAELLEQVGLPP---------SFLDRYPHQLSGGQRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 744 ALLTDAKILCIDEATASVD---Q-KTDQLLQQTicKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQ 818
Cdd:COG1124 152 ALILEPELLLLDEPTSALDvsvQaEILNLLKDL--REERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLAG 229
|
..
gi 767940955 819 PH 820
Cdd:COG1124 230 PK 231
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
11-155 |
1.17e-25 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 105.75 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 11 LSKGFGLATQEPWIQFATIRDNILFGKTF-DAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAV 89
Cdd:cd03245 76 LRRNIGYVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARAL 155
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767940955 90 YQEKELYLLDDPLAAVDADVANHLLHRcILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAG 155
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKER-LRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
595-813 |
1.55e-25 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 105.52 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLRSQ 671
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 672 LAIIPQE-PFLFSGTVREN----LDPQGLHKD---RALWQALKQCHLSEVITSMggldgelgegGRSLSLGQRQLLCLAR 743
Cdd:COG2884 81 IGVVFQDfRLLPDRTVYENvalpLRVTGKSRKeirRRVREVLDLVGLSDKAKAL----------PHELSGGEQQRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767940955 744 ALLTDAKILCIDEATASVDQKT-DQLLQ--QTICKRfaNKTVLtIA-HRLNtILNS--DRVLVLQAGRVVELDSPA 813
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETsWEIMEllEEINRR--GTTVL-IAtHDLE-LVDRmpKRVLELEDGRLVRDEARG 222
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
595-820 |
5.53e-25 |
|
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: 104.69 E-value: 5.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYrPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAI 674
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 675 IPQEPFLFSG-TVREN--LDPQGLH------KDRALwQALKQCHLSEvitsmgglDGELGEGGRSLSLGQRQLLCLARAL 745
Cdd:cd03295 80 VIQQIGLFPHmTVEENiaLVPKLLKwpkekiRERAD-ELLALVGLDP--------AEFADRYPHELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767940955 746 LTDAKILCIDEATASVDQKTDQLLQQTI--CKRFANKTVLTIAHRLN-TILNSDRVLVLQAGRVVELDSPATLRNQPH 820
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFkrLQQELGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEILRSPA 228
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
611-819 |
6.44e-25 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 110.19 E-value: 6.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 611 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENL 690
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 691 -----DPQGLHKDRALWQA--------LKQCHLSEVitsmggldgelgeGGRS--LSLGQRQLLCLARALLTDAKILCID 755
Cdd:PRK10789 410 algrpDATQQEIEHVARLAsvhddilrLPQGYDTEV-------------GERGvmLSGGQKQRISIARALLLNAEILILD 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767940955 756 EATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATLRNQP 819
Cdd:PRK10789 477 DALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
15-161 |
9.13e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 109.87 E-value: 9.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 15 FGLATQEPWIQFATIRDNILFGK---TfDAQLyKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQ 91
Cdd:COG1132 416 IGVVPQDTFLFSGTIRENIRYGRpdaT-DEEV-EEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLK 493
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 92 EKELYLLDDPLAAVDADVAnHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 161
Cdd:COG1132 494 DPPILILDEATSALDTETE-ALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELL 562
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
611-820 |
1.25e-24 |
|
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: 103.29 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 611 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLElAQLRSQLAI-----IPQepfLFSG- 684
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP-PHEIARLGIgrtfqIPR---LFPEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 685 TVRENL------------------DPQGLHKDRAlWQALKQCHLSEVitsmggldgeLGEGGRSLSLGQRQLLCLARALL 746
Cdd:cd03219 91 TVLENVmvaaqartgsglllararREEREARERA-EELLERVGLADL----------ADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767940955 747 TDAKILCIDEATASV-DQKTDQLLqQTICK-RFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQPH 820
Cdd:cd03219 160 TDPKLLLLDEPAAGLnPEETEELA-ELIRElRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
595-808 |
2.56e-24 |
|
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: 101.78 E-value: 2.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGLPN--ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVdtsqlELAQLRSQL 672
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE-----PVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 673 AIIPQEPFLFS-GTVREN----LDPQGLHK----DRALwQALKQCHLSEVITSMggldgelgegGRSLSLGQRQLLCLAR 743
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNvalgLELQGVPKaearERAE-ELLELVGLSGFENAY----------PHQLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 744 ALLTDAKILCIDEATASVDQKTDQLLQQTICK--RFANKTVLTIAHRLN-TILNSDRVLVLQA--GRVVE 808
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
595-812 |
3.95e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 102.76 E-value: 3.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAI 674
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 675 IPQEP---FLFSgTVRENLdPQGLHKDRalwqaLKQCHLSEVITSMGGLDGELGEGGR---SLSLGQRQLLCLARALLTD 748
Cdd:PRK13632 88 IFQNPdnqFIGA-TVEDDI-AFGLENKK-----VPPKKMKDIIDDLAKKVGMEDYLDKepqNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767940955 749 AKILCIDEATASVDQKTDQLLQQTI--CKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSP 812
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMvdLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKP 226
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
595-820 |
6.47e-24 |
|
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: 101.04 E-value: 6.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLRSQ 671
Cdd:cd03261 1 IELRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseaELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 672 LAIIPQEPFLFSG-TVRENL---------DPQGLHKDRALwQALKQCHLSEVITSMggldgelgegGRSLSLGQRQLLCL 741
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVafplrehtrLSEEEIREIVL-EKLEAVGLRGAEDLY----------PAELSGGMKKRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 742 ARALLTDAKILCIDEATASVDQKTDQLLQQTI--CKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQ 818
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIrsLKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRAS 227
|
..
gi 767940955 819 PH 820
Cdd:cd03261 228 DD 229
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
590-801 |
7.25e-24 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 108.58 E-value: 7.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 590 LTQGGVEFQDVVLAY--RPGLPNALDgVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLE-------------------- 647
Cdd:PTZ00265 1161 DIKGKIEIMDVNFRYisRPNVPIYKD-LTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtne 1239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 648 ----------------------------------PSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENLDpq 693
Cdd:PTZ00265 1240 qdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK-- 1317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 694 gLHKDRALWQALKQ----CHLSEVITSMGGLDGELGEGG-RSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQL 768
Cdd:PTZ00265 1318 -FGKEDATREDVKRackfAAIDEFIESLPNKYDTNVGPYgKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKL 1396
|
250 260 270
....*....|....*....|....*....|....*
gi 767940955 769 LQQTIC--KRFANKTVLTIAHRLNTILNSDRVLVL 801
Cdd:PTZ00265 1397 IEKTIVdiKDKADKTIITIAHRIASIKRSDKIVVF 1431
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
595-805 |
1.17e-23 |
|
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: 99.47 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPG---LPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVlldgvdtsqlelaQLRSQ 671
Cdd:cd03250 1 ISVEDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-------------SVPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 672 LAIIPQEPFLFSGTVREN------LDPQglhkdRaLWQALKQCHLSEVITSMGGLDGELGEGG-RSLSLGQRQLLCLARA 744
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENilfgkpFDEE-----R-YEKVIKACALEPDLEILPDGDLTEIGEKgINLSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767940955 745 LLTDAKILCIDEATASVDQKT-DQLLQQTICKRFA-NKTVLTIAHRLNTILNSDRVLVLQAGR 805
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVgRHIFENCILGLLLnNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
595-815 |
1.76e-23 |
|
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: 100.50 E-value: 1.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGlpNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAI 674
Cdd:COG1120 2 LEAENLSVGYGGR--PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 675 IPQEPFL-FSGTVRE----------NLDPQGLHKDRAL-WQALKQCHLSEvitsmggldgELGEGGRSLSLGQRQLLCLA 742
Cdd:COG1120 80 VPQEPPApFGLTVRElvalgryphlGLFGRPSAEDREAvEEALERTGLEH----------LADRPVDELSGGERQRVLIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 743 RALLTDAKILCIDEATASVD---QKtdQLLQqtICKRFA---NKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATL 815
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDlahQL--EVLE--LLRRLArerGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
602-807 |
1.95e-23 |
|
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: 98.28 E-value: 1.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 602 LAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQepfl 681
Cdd:cd03214 5 LSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 682 fsgtvrenldpqglhkdralwqALKQC---HLSEvitsmggldgelgEGGRSLSLGQRQLLCLARALLTDAKILCIDEAT 758
Cdd:cd03214 81 ----------------------ALELLglaHLAD-------------RPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767940955 759 ASVD----QKTDQLLQQTicKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVV 807
Cdd:cd03214 126 SHLDiahqIELLELLRRL--ARERGKTVVMVLHDLNLAARyADRVILLKDGRIV 177
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
595-820 |
2.55e-23 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 99.78 E-value: 2.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRpGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDtsqleLAQLRSQLAI 674
Cdd:COG1121 7 IELENLTVSYG-GRP-VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP-----PRRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 675 IPQEPFL---FSGTVRE----NLDPQ-GL-----HKDRAL-WQALKQCHLSEVITSMGgldgelgeggRSLSLGQRQLLC 740
Cdd:COG1121 80 VPQRAEVdwdFPITVRDvvlmGRYGRrGLfrrpsRADREAvDEALERVGLEDLADRPI----------GELSGGQQQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 741 LARALLTDAKILCIDEATASVDQKTDQLLQQTICK-RFANKTVLTIAHRLNTIL-NSDRVLVLqAGRVVELDSPATLRNQ 818
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVReYFDRVLLL-NRGLVAHGPPEEVLTP 228
|
..
gi 767940955 819 PH 820
Cdd:COG1121 229 EN 230
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
596-807 |
4.75e-23 |
|
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: 97.99 E-value: 4.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 596 EFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGvdtsqLELAQLRSQLAII 675
Cdd:cd03235 1 EVEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-----KPLEKERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 676 PQE---PFLFSGTVRE----NLDPQG--------LHKDRALwQALKQCHLSEVITSmggldgelgeGGRSLSLGQRQLLC 740
Cdd:cd03235 74 PQRrsiDRDFPISVRDvvlmGLYGHKglfrrlskADKAKVD-EALERVGLSELADR----------QIGELSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767940955 741 LARALLTDAKILCIDEATASVDQKTDQLLQQTICK-RFANKTVLTIAHRLNTILNS-DRVLVLqAGRVV 807
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYfDRVLLL-NRTVV 210
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
611-807 |
7.76e-22 |
|
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: 94.74 E-value: 7.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 611 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQlELAQLRSQLAIIPQEPFLFSG-TVREN 689
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYDRlTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 690 LDP-QGLH--KDRALWQALkqchlsEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTD 766
Cdd:cd03266 99 LEYfAGLYglKGDELTARL------EELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMAT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767940955 767 QLLQQTICK-RFANKTVLTIAHRLNTILN-SDRVLVLQAGRVV 807
Cdd:cd03266 173 RALREFIRQlRALGKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
611-805 |
8.19e-22 |
|
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: 93.41 E-value: 8.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 611 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLE--LAQLRSQLAIIPQEPFLFSG-TVR 687
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGMVFQDFALFPHlTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 688 ENLdpqglhkdrALwqalkqchlsevitsmggldgelgeggrSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQ 767
Cdd:cd03229 95 ENI---------AL----------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 767940955 768 LLQQTICKRFAN--KTVLTIAHRLNTILN-SDRVLVLQAGR 805
Cdd:cd03229 138 EVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
6-161 |
8.61e-22 |
|
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: 95.30 E-value: 8.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 6 VAVRGLSKGFGLATQEPWIQFATIRDNILFGKtFDAQLyKEVLEAC--ALNDDLSI-LPAGDQTEVGEKGVTLSGGQRAR 82
Cdd:cd03249 70 LNLRWLRSQIGLVSQEPVLFDGTIAENIRYGK-PDATD-EEVEEAAkkANIHDFIMsLPDGYDTLVGERGSQLSGGQKQR 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 83 IALARAVYQEKELYLLDDPLAAVDAD---VANHLLHRCILGMlsytTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSE 159
Cdd:cd03249 148 IAIARALLRNPKILLLDEATSALDAEsekLVQEALDRAMKGR----TTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDE 223
|
..
gi 767940955 160 IL 161
Cdd:cd03249 224 LM 225
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
596-807 |
9.46e-22 |
|
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: 94.94 E-value: 9.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 596 EFQDVVLAYrPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLRSQL 672
Cdd:cd03256 2 EVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgkALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 673 AIIPQEPFLFSG-TVREN------------------LDPQglHKDRALwQALKQCHLSEVITSMGGLdgelgeggrsLSL 733
Cdd:cd03256 81 GMIFQQFNLIERlSVLENvlsgrlgrrstwrslfglFPKE--EKQRAL-AALERVGLLDKAYQRADQ----------LSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767940955 734 GQRQLLCLARALLTDAKILCIDEATASVDQKTDQ----LLQQtICKRFaNKTVLTIAHRLNTIL-NSDRVLVLQAGRVV 807
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRqvmdLLKR-INREE-GITVIVSLHQVDLAReYADRIVGLKDGRIV 224
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-155 |
1.26e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 99.92 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 20 QEPWIQFATIRDNILFGKTF--DAQLYkEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYL 97
Cdd:PRK11174 430 QNPQLPHGTLRDNVLLGNPDasDEQLQ-QALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLL 508
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 767940955 98 LDDPLAAVDADVANHLLHRCILGMLSYTTrLLCTHRTEYLERADAVLLMEAGRLIRAG 155
Cdd:PRK11174 509 LDEPTASLDAHSEQLVMQALNAASRRQTT-LMVTHQLEDLAQWDQIWVMQDGQIVQQG 565
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
595-808 |
1.75e-21 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 96.69 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGLPN--ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLR 669
Cdd:COG1135 2 IELENLSKTFPTKGGPvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALserELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 670 SQLAIIPQEPFLFSG-TVREN----------------------LDPQGLhKDRAlwqalkQCHLSEvitsmggldgelge 726
Cdd:COG1135 82 RKIGMIFQHFNLLSSrTVAENvalpleiagvpkaeirkrvaelLELVGL-SDKA------DAYPSQ-------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 727 ggrsLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQ----LLQQtICKRFaNKTVLTIAHRLNTILN-SDRVLVL 801
Cdd:COG1135 141 ----LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRsildLLKD-INREL-GLTIVLITHEMDVVRRiCDRVAVL 214
|
....*..
gi 767940955 802 QAGRVVE 808
Cdd:COG1135 215 ENGRIVE 221
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
611-819 |
2.49e-21 |
|
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: 95.89 E-value: 2.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 611 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEP---SSGRVLLDGVDTSQL---ELAQLR-SQLAIIPQEPF--- 680
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLsekELRKIRgREIQMIFQDPMtsl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 681 --LFsgTVRENL-DPQGLH--------KDRALwQALKQCHLSEVITSMggldgelgeggRS----LSLGQRQLLCLARAL 745
Cdd:COG0444 100 npVM--TVGDQIaEPLRIHgglskaeaRERAI-ELLERVGLPDPERRL-----------DRypheLSGGMRQRVMIARAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 746 LTDAKILCIDEATASVD---QKtdQLLQ--QTICKRFaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQP 819
Cdd:COG0444 166 ALEPKLLIADEPTTALDvtiQA--QILNllKDLQREL-GLAILFITHDLGVVAEiADRVAVMYAGRIVEEGPVEELFENP 242
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
595-811 |
3.99e-21 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 95.64 E-value: 3.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGLP--NALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLR 669
Cdd:PRK11153 2 IELKNISKVFPQGGRtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALsekELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 670 SQLAIIPQEpF--LFSGTVREN----------------------LDPQGL--HKDRALWQalkqchlsevitsmggldge 723
Cdd:PRK11153 82 RQIGMIFQH-FnlLSSRTVFDNvalplelagtpkaeikarvtelLELVGLsdKADRYPAQ-------------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 724 lgeggrsLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQ----LLQQtICKRFaNKTVLTIAHRLNTILN-SDRV 798
Cdd:PRK11153 141 -------LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRsileLLKD-INREL-GLTIVLITHEMDVVKRiCDRV 211
|
250
....*....|...
gi 767940955 799 LVLQAGRVVELDS 811
Cdd:PRK11153 212 AVIDAGRLVEQGT 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
612-814 |
4.26e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 93.68 E-value: 4.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 612 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFL-FSGTVRE-- 688
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEvv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 689 --NLDPQGLHK---DRALWQALKQC---HLSEvitsmggldgelgEGGRSLSLGQRQLLCLARALL------TDAKILCI 754
Cdd:PRK13548 98 amGRAPHGLSRaedDALVAAALAQVdlaHLAG-------------RDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767940955 755 DEATASVDqktdqLLQQ----TICKRFANK---TVLTIAHRLN-TILNSDRVLVLQAGRVVELDSPAT 814
Cdd:PRK13548 165 DEPTSALD-----LAHQhhvlRLARQLAHErglAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAE 227
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
595-808 |
4.50e-21 |
|
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: 92.20 E-value: 4.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGLpnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRsqLAI 674
Cdd:cd03259 1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRN--IGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 675 IPQEPFLFSG-TVRENL--------DPQGLHKDRALWqALKQCHLSEVITSMggldgelgegGRSLSLGQRQLLCLARAL 745
Cdd:cd03259 77 VFQDYALFPHlTVAENIafglklrgVPKAEIRARVRE-LLELVGLEGLLNRY----------PHELSGGQQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767940955 746 LTDAKILCIDEATASVDQKTDQLLQQTICKRFAN--KTVLTIAHRLNTILN-SDRVLVLQAGRVVE 808
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKELQRElgITTIYVTHDQEEALAlADRIAVMNEGRIVQ 211
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
11-161 |
9.72e-21 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 91.90 E-value: 9.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 11 LSKGFGLATQEPWIQFATIRDNILFGK-TFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAV 89
Cdd:cd03254 75 LRSMIGVVLQDTFLFSGTIMENIRLGRpNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAM 154
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767940955 90 YQEKELYLLDDPLAAVDADVANhLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 161
Cdd:cd03254 155 LRDPKILILDEATSNIDTETEK-LIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
595-813 |
1.08e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 93.16 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAI 674
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 675 IPQEP-FLFSG-TVREN----LDPQGLHKD---RALWQALKQCHLSEVITsmggldgelgEGGRSLSLGQRQLLCLARAL 745
Cdd:PRK13635 86 VFQNPdNQFVGaTVQDDvafgLENIGVPREemvERVDQALRQVGMEDFLN----------REPHRLSGGQKQRVAIAGVL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 746 LTDAKILCIDEATASVDQKTDQLLQQTI--CKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPA 813
Cdd:PRK13635 156 ALQPDIIILDEATSMLDPRGRREVLETVrqLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
563-804 |
1.24e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 96.80 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 563 SVERLEEYTCDLpQEPQGQPLQLGTGWLTQGG-VEFQDVVLAyrpgLPNA---LDGVTFCVQPGEKLGIVGRTGSGKSSl 638
Cdd:COG4178 331 TVDRLAGFEEAL-EAADALPEAASRIETSEDGaLALEDLTLR----TPDGrplLEDLSLSLKPGERLLITGPSGSGKST- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 639 llvlfrllepssgrvLLDGvdtsqleLAQL------------RSQLAIIPQEPFLFSGTVRENL---DPQGLHKDRALWQ 703
Cdd:COG4178 405 ---------------LLRA-------IAGLwpygsgriarpaGARVLFLPQRPYLPLGTLREALlypATAEAFSDAELRE 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 704 ALKQCHLSEVITSMGGLDGELgeggRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVL 783
Cdd:COG4178 463 ALEAVGLGHLAERLDEEADWD----QVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVI 538
|
250 260
....*....|....*....|.
gi 767940955 784 TIAHRLNTILNSDRVLVLQAG 804
Cdd:COG4178 539 SVGHRSTLAAFHDRVLELTGD 559
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
311-567 |
1.33e-20 |
|
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350044 [Multi-domain] Cd Length: 324 Bit Score: 93.71 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 311 SDIRFYLTVYATIAGVNSLCTL--LRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSL 388
Cdd:cd18600 65 TFTSSYYVFYIYVGVADSLLAMgfFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 389 PFILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLRA 468
Cdd:cd18600 145 PLTIFDFIQLFLIVIGAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 469 TGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGlanPGLVGLSLSYALSLTGLLS 548
Cdd:cd18600 225 FGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFTAVTFISIGTTGDG---EGRVGIILTLAMNIMSTLQ 301
|
250
....*....|....*....
gi 767940955 549 GLVSSFTQTEAMLVSVERL 567
Cdd:cd18600 302 WAVNTSIDVDSLMRSVSRI 320
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
10-146 |
1.74e-20 |
|
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: 96.20 E-value: 1.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 10 GLSKGFGLATQEPWIQFATIRDNILFGKTF-DAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARA 88
Cdd:TIGR02857 393 SWRDQIAWVPQHPFLFAGTIAENIRLARPDaSDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARA 472
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 767940955 89 VYQEKELYLLDDPLAAVDADVANHLLHRcILGMLSYTTRLLCTHRTEYLERADAVLLM 146
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEA-LRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
17-151 |
3.30e-20 |
|
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: 90.22 E-value: 3.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 17 LATQEPWIQFATIRDNILFG-KTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKEL 95
Cdd:cd03248 92 LVGQEPVLFARSLQDNIAYGlQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQV 171
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 767940955 96 YLLDDPLAAVDADvANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRL 151
Cdd:cd03248 172 LILDEATSALDAE-SEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
612-819 |
3.58e-20 |
|
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: 90.29 E-value: 3.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 612 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQlRSQLAII--PQEPFLFSG-TVRE 688
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLGIGylPQEASIFRKlTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 689 NLDP--QGLHKDRALWQA-----LKQCHLSEVITSMGGldgelgeggrSLSLGQRQLLCLARALLTDAKILCIDEATASV 761
Cdd:cd03218 95 NILAvlEIRGLSKKEREEkleelLEEFHITHLRKSKAS----------SLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767940955 762 DQKTDQLLQQTIcKRFANKT--VLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQP 819
Cdd:cd03218 165 DPIAVQDIQKII-KILKDRGigVLITDHNVRETLSiTDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
611-807 |
4.48e-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: 87.87 E-value: 4.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 611 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQ-LRSQLAIIPQepflfsgtvren 689
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMVYQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 690 ldpqglhkdralwqalkqchlsevitsmggldgelgeggrsLSLGQRQLLCLARALLTDAKILCIDEATASVDQK-TDQL 768
Cdd:cd03216 83 -----------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAeVERL 121
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767940955 769 LQqtICKRFAN--KTVLTIAHRLNTILN-SDRVLVLQAGRVV 807
Cdd:cd03216 122 FK--VIRRLRAqgVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
596-817 |
4.63e-20 |
|
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: 89.80 E-value: 4.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 596 EFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQ-LRSQLAI 674
Cdd:cd03224 2 EVENLNAGY--GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 675 IPQEPFLFSG-TVRENLD--PQGLHKDRALWQ---------ALKQchlsevitsmggldgELGEGGRSLSLGQRQLLCLA 742
Cdd:cd03224 80 VPEGRRIFPElTVEENLLlgAYARRRAKRKARlervyelfpRLKE---------------RRKQLAGTLSGGEQQMLAIA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 743 RALLTDAKILCIDEATAS-----VDQKTDQLlqQTICKRfaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLR 816
Cdd:cd03224 145 RALMSRPKLLLLDEPSEGlapkiVEEIFEAI--RELRDE--GVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELL 220
|
.
gi 767940955 817 N 817
Cdd:cd03224 221 A 221
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
6-161 |
1.78e-19 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 88.44 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 6 VAVRGLSKGFGLATQEPWIQFATIRDNILFGKtFDAQLyKEVLEA---CALNDDLSILPAGDQTEVGEKGVTLSGGQRAR 82
Cdd:cd03251 69 YTLASLRRQIGLVSQDVFLFNDTVAENIAYGR-PGATR-EEVEEAaraANAHEFIMELPEGYDTVIGERGVKLSGGQRQR 146
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767940955 83 IALARAVYQEKELYLLDDPLAAVDaDVANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 161
Cdd:cd03251 147 IAIARALLKDPPILILDEATSALD-TESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELL 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
611-808 |
2.37e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.39 E-value: 2.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 611 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQ-LRSQLAIIPQEPFLFSG-TVRE 688
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAGIAIIHQELNLVPNlSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 689 NL------------DPQGLHKdRALwQALKQCHLS-----EVitsmggldgelgeggRSLSLGQRQLLCLARALLTDAKI 751
Cdd:COG1129 99 NIflgreprrggliDWRAMRR-RAR-ELLARLGLDidpdtPV---------------GDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767940955 752 LCIDEATASVDQK-TDQLLQqtICKRFANK--TVLTIAHRLNTILN-SDRVLVLQAGRVVE 808
Cdd:COG1129 162 LILDEPTASLTEReVERLFR--IIRRLKAQgvAIIYISHRLDEVFEiADRVTVLRDGRLVG 220
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
612-773 |
4.42e-19 |
|
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: 86.38 E-value: 4.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 612 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLElAQLRSQLAIIPQEPFLFSG-TVRENL 690
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAYLGHADGLKPElTVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 691 D----PQGLHKDRA-LWQALKQCHLSEVITsmggldgelgEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKT 765
Cdd:COG4133 97 RfwaaLYGLRADREaIDEALEAVGLAGLAD----------LPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAG 166
|
....*...
gi 767940955 766 DQLLQQTI 773
Cdd:COG4133 167 VALLAELI 174
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
611-819 |
4.68e-19 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 89.02 E-value: 4.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 611 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLRSQLAIIPQEPFlfsG--- 684
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLsgrELRPLRRRMQMVFQDPY---Asln 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 685 ---TVR----ENLDPQGLH-----KDRALwQALKQCHLSEvitsmggldgelGEGGR---SLSLGQRQLLCLARALLTDA 749
Cdd:COG4608 110 prmTVGdiiaEPLRIHGLAskaerRERVA-ELLELVGLRP------------EHADRyphEFSGGQRQRIGIARALALNP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 750 KILCIDEATASVD---QKtdQ---LLQ--QticKRFaNKTVLTIAHRLNT---IlnSDRVLVLQAGRVVELDSPATLRNQ 818
Cdd:COG4608 177 KLIVCDEPVSALDvsiQA--QvlnLLEdlQ---DEL-GLTYLFISHDLSVvrhI--SDRVAVMYLGKIVEIAPRDELYAR 248
|
.
gi 767940955 819 P 819
Cdd:COG4608 249 P 249
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
595-806 |
7.41e-19 |
|
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: 85.92 E-value: 7.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLRSQ 671
Cdd:cd03292 1 IEFINVTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 672 LAIIPQEPFLFSG-TVREN--LDPQGLHKDRALWQ-----ALKQCHLSEVITSMGGldgelgeggrSLSLGQRQLLCLAR 743
Cdd:cd03292 80 IGVVFQDFRLLPDrNVYENvaFALEVTGVPPREIRkrvpaALELVGLSHKHRALPA----------ELSGGEQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767940955 744 ALLTDAKILCIDEATASVDQKTD----QLLQQtICKRFANKTVLTIAHRL-NTIlnSDRVLVLQAGRV 806
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTweimNLLKK-INKAGTTVVVATHAKELvDTT--RHRVIALERGKL 214
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
612-819 |
8.10e-19 |
|
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: 86.62 E-value: 8.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 612 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSqlELAQLRSQLAIIPQEPFLFSG-TVRENL 690
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYVPQNYALFPHmTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 691 DpQGLHKDRALWQALKQchlsEV--ITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQL 768
Cdd:cd03299 93 A-YGLKKRKVDKKEIER----KVleIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767940955 769 LQQTICK--RFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQP 819
Cdd:cd03299 168 LREELKKirKEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
595-819 |
1.01e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 86.96 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL-ELAQLRSQLA 673
Cdd:PRK13644 2 IRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 674 IIPQEP-FLFSG-TVRENL--DPQGL---------HKDRALWQA--LKQCHLSEvitsmggldgelgeggRSLSLGQRQL 738
Cdd:PRK13644 81 IVFQNPeTQFVGrTVEEDLafGPENLclppieirkRVDRALAEIglEKYRHRSP----------------KTLSGGQGQC 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 739 LCLARALLTDAKILCIDEATASVDQKTDQLLQQTIcKRF--ANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATLR 816
Cdd:PRK13644 145 VALAGILTMEPECLIFDEVTSMLDPDSGIAVLERI-KKLheKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
...
gi 767940955 817 NQP 819
Cdd:PRK13644 224 SDV 226
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
611-819 |
1.10e-18 |
|
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: 86.93 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 611 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLRSQ-LAIIPQEPFLFSG-T 685
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMsrkELRELRRKkISMVFQSFALLPHrT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 686 VREN----LDPQGLHK----DRALwQALKQCHLSEVITSMGgldgelgeggRSLSLGQRQLLCLARALLTDAKILCIDEA 757
Cdd:cd03294 119 VLENvafgLEVQGVPRaereERAA-EALELVGLEGWEHKYP----------DELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767940955 758 TASVD-----QKTDQLLQqtiCKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQP 819
Cdd:cd03294 188 FSALDplirrEMQDELLR---LQAELQKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILTNP 252
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
595-812 |
2.10e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 86.42 E-value: 2.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGLP---NALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG----VDTSQLELAQ 667
Cdd:PRK13641 3 IKFENVDYIYSPGTPmekKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 668 LRSQLAIIPQ--EPFLFSGTVRENLD--PQ--GLHKDRALWQA---LKQCHLSEVITSMGGLdgelgeggrSLSLGQRQL 738
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEfgPKnfGFSEDEAKEKAlkwLKKVGLSEDLISKSPF---------ELSGGQMRR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767940955 739 LCLARALLTDAKILCIDEATASVDQKT-DQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSP 812
Cdd:PRK13641 154 VAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASP 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
611-819 |
3.88e-18 |
|
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: 88.59 E-value: 3.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 611 ALDGVTFCVQPGEKLGIVGRTGSGKSSlLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLRSQLAIIPQEPFlfsG--- 684
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKST-LGLALLRLIPSEGEIRFDGQDLDGLsrrALRPLRRRMQVVFQDPF---Gsls 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 685 -------TVRENLDPQGLHKDRA-----LWQALKQCHLSEvitsmggldgelGEGGR---SLSLGQRQLLCLARALLTDA 749
Cdd:COG4172 377 prmtvgqIIAEGLRVHGPGLSAAerrarVAEALEEVGLDP------------AARHRyphEFSGGQRQRIAIARALILEP 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767940955 750 KILCIDEATASVD---QKtdQLLQ--QTICKRFaNKTVLTIAHRLNTI--LnSDRVLVLQAGRVVELDSPATLRNQP 819
Cdd:COG4172 445 KLLVLDEPTSALDvsvQA--QILDllRDLQREH-GLAYLFISHDLAVVraL-AHRVMVMKDGKVVEQGPTEQVFDAP 517
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
11-161 |
6.32e-18 |
|
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: 84.07 E-value: 6.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 11 LSKGFGLATQEPWIQFATIRDNILFGKTfdAQLYKEVLEACAL---NDDLSILPAGDQTEVGEKGVTLSGGQRARIALAR 87
Cdd:cd03252 74 LRRQVGVVLQENVLFNRSIRDNIALADP--GMSMERVIEAAKLagaHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIAR 151
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767940955 88 AVYQEKELYLLDDPLAAVDADvANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 161
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYE-SEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
612-815 |
7.94e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 84.40 E-value: 7.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 612 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEP-FLFSG-TVREN 689
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPdNQFVGaTVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 690 ----LDPQGL-HKD--RALWQALKQCHLSEVITSMGGldgelgeggrSLSLGQRQLLCLARALLTDAKILCIDEATASVD 762
Cdd:PRK13650 103 vafgLENKGIpHEEmkERVNEALELVGMQDFKEREPA----------RLSGGQKQRVAIAGAVAMRPKIIILDEATSMLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767940955 763 QKTDQLLQQTI--CKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATL 815
Cdd:PRK13650 173 PEGRLELIKTIkgIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
11-150 |
9.66e-18 |
|
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: 81.28 E-value: 9.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 11 LSKGFGLATQEPWIQFATIRDNILfgktfdaqlykevleacalnddlsilpagdqtevgekgvtlSGGQRARIALARAVY 90
Cdd:cd03228 74 LRKNIAYVPQDPFLFSGTIRENIL-----------------------------------------SGGQRQRIAIARALL 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 91 QEKELYLLDDPLAAVDADvANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGR 150
Cdd:cd03228 113 RDPPILILDEATSALDPE-TEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
287-570 |
1.62e-17 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 83.80 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 287 LLLFS-PGNLYIPV-FPLPKAAPngSSDIRFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTF 364
Cdd:cd18559 11 NHVFSgPSNLWLLLwFDDPVNGP--QEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 365 FNATPTGRILNRFSSDVACADDSLPFILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYhVQRHYRASSRELRRL 444
Cdd:cd18559 89 FERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVP-VNRVYAASSRQLKRL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 445 GSLTLSPLYSHLADTLAGLSVLRATGATYRFeEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQ 524
Cdd:cd18559 168 ESVSKDPRYKLFNETLLGISVIKAFEWEEAF-IRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSRH 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 767940955 525 QglaNPGLVGLSLSYALSLTGLLSGLVSSFTQTEAMLVSVERLEEY 570
Cdd:cd18559 247 S---LAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLER 289
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-156 |
2.25e-17 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 86.30 E-value: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 15 FGLATQEPWIQFATIRDNILFGKTfDA--QLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQE 92
Cdd:PRK10789 391 LAVVSQTPFLFSDTVANNIALGRP-DAtqQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLN 469
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767940955 93 KELYLLDDPLAAVDADVANHLLHRcilgmLS----YTTRLLCTHRTEYLERADAVLLMEAGRLIRAGP 156
Cdd:PRK10789 470 AEILILDDALSAVDGRTEHQILHN-----LRqwgeGRTVIISAHRLSALTEASEILVMQHGHIAQRGN 532
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-160 |
3.21e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 86.31 E-value: 3.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 16 GLATQEPWIQFATIRDNILFGKTF--DAQLYKEVLEACAlNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEK 93
Cdd:TIGR00958 558 ALVGQEPVLFSGSVRENIAYGLTDtpDEEIMAAAKAANA-HDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKP 636
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767940955 94 ELYLLDDPLAAVDADVaNHLLH--RCILGMlsytTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEI 160
Cdd:TIGR00958 637 RVLILDEATSALDAEC-EQLLQesRSRASR----TVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQL 700
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
604-803 |
3.57e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 81.30 E-value: 3.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 604 YRPGLPNALDGVTFCVQPGE-KLgIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLF 682
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEfKL-ITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 683 SGTVRENL-----------DPQGLHKDRALWqALKQCHLSEVITsmggldgelgeggrSLSLGQRQLLCLARALLTDAKI 751
Cdd:PRK10247 94 GDTVYDNLifpwqirnqqpDPAIFLDDLERF-ALPDTILTKNIA--------------ELSGGEKQRISLIRNLQFMPKV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767940955 752 LCIDEATASVDQKTDQLLQQTICK--RFANKTVLTIAHRLNTILNSDRVLVLQA 803
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRyvREQNIAVLWVTHDKDEINHADKVITLQP 212
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
604-813 |
4.79e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 82.40 E-value: 4.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 604 YRPGLP---NALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTS--QLELAQLRSQLAIIPQE 678
Cdd:PRK13637 12 YMEGTPfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 679 P--FLFSGTVrenldpqglHKDRALwqALKQCHLSE------VITSMGGLDGELGEGG-RS---LSLGQRQLLCLARALL 746
Cdd:PRK13637 92 PeyQLFEETI---------EKDIAF--GPINLGLSEeeienrVKRAMNIVGLDYEDYKdKSpfeLSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767940955 747 TDAKILCIDEATASVDQKT-DQLLQQ--TICKRFaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPA 813
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGrDEILNKikELHKEY-NMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPR 230
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
610-816 |
6.75e-17 |
|
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: 80.56 E-value: 6.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 610 NALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLRSQ-LAIIPQ-EPFLFSG 684
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALdedARARLRARhVGFVFQsFQLLPTL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 685 TVREN------LDPQGLHKDRALwQALKQCHLSEVITSMggldgelgegGRSLSLGQRQLLCLARALLTDAKILCIDEAT 758
Cdd:COG4181 106 TALENvmlpleLAGRRDARARAR-ALLERVGLGHRLDHY----------PAQLSGGEQQRVALARAFATEPAILFADEPT 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767940955 759 ASVDQKT-----DQLLQQTickRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVElDSPATLR 816
Cdd:COG4181 175 GNLDAATgeqiiDLLFELN---RERGTTLVLVTHDPALAARCDRVLRLRAGRLVE-DTAATAA 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
27-161 |
8.72e-17 |
|
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: 80.35 E-value: 8.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 27 ATIRDNILFGK--TFDAQLYkEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAA 104
Cdd:cd03253 89 DTIGYNIRYGRpdATDEEVI-EAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSA 167
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 767940955 105 VDAdVANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 161
Cdd:cd03253 168 LDT-HTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL 223
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
606-808 |
9.53e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.19 E-value: 9.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 606 PGLpNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTS-QLELAQLRSQLAIIPQE----PF 680
Cdd:PRK11288 15 PGV-KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVAIIYQElhlvPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 681 LfsgTVRENLD----PQ--GLHKDRAL-WQALKQC-HLSEVITSmggldgelGEGGRSLSLGQRQLLCLARALLTDAKIL 752
Cdd:PRK11288 94 M---TVAENLYlgqlPHkgGIVNRRLLnYEAREQLeHLGVDIDP--------DTPLKYLSIGQRQMVEIAKALARNARVI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767940955 753 CIDEATASVDQK-TDQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVE 808
Cdd:PRK11288 163 AFDEPTSSLSAReIEQLFRVIRELRAEGRVILYVSHRMEEIFAlCDAITVFKDGRYVA 220
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
612-807 |
1.16e-16 |
|
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: 79.13 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 612 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLF--RLLEPSSGRVLLDGVdtsQLELAQLRSQLAIIPQEPFLFSG-TVRE 688
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGR---PLDKRSFRKIIGYVPQDDILHPTlTVRE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 689 nldpqglhkdrALWQALKqchlsevitsmggldgelgegGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQL 768
Cdd:cd03213 102 -----------TLMFAAK---------------------LRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767940955 769 LQQTIcKRFA--NKTVLTIAHRL-NTILNS-DRVLVLQAGRVV 807
Cdd:cd03213 150 VMSLL-RRLAdtGRTIICSIHQPsSEIFELfDKLLLLSQGRVI 191
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
28-170 |
1.46e-16 |
|
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: 83.64 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 28 TIRDNI-LFGKTfDAQlykEVLEACALND--DLsI--LPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPL 102
Cdd:COG4618 421 TIAENIaRFGDA-DPE---KVVAAAKLAGvhEM-IlrLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPN 495
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767940955 103 AAVDADVANHLLhRCILGM-LSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEILPLVQAVPKA 170
Cdd:COG4618 496 SNLDDEGEAALA-AAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLARLARPAAA 563
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
595-815 |
5.02e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 79.37 E-value: 5.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAY-RPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLA 673
Cdd:PRK13642 5 LEVENLVFKYeKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 674 IIPQEP-FLFSGTVREN-----LDPQGLHKDRALWQalkqchLSEVITSMGGLDGELGEGGRsLSLGQRQLLCLARALLT 747
Cdd:PRK13642 85 MVFQNPdNQFVGATVEDdvafgMENQGIPREEMIKR------VDEALLAVNMLDFKTREPAR-LSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 748 DAKILCIDEATASVDQKTDQLLQQTI--CKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATL 815
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIheIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
11-133 |
5.94e-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: 81.64 E-value: 5.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 11 LSKGFGLATQEPWIQFATIRDNILFGK--TFDAQLYkEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARA 88
Cdd:TIGR02868 407 VRRRVSVCAQDAHLFDTTVRENLRLARpdATDEELW-AALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARA 485
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 767940955 89 VYQEKELYLLDDPLAAVDADVANHLLHRcILGMLSYTTRLLCTHR 133
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETADELLED-LLAALSGRTVVLITHH 529
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
595-807 |
6.76e-16 |
|
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: 77.32 E-value: 6.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPglPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGvdtSQLELAQlRSQLAI 674
Cdd:cd03269 1 LEVENVTKRFGR--VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLDIAA-RNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 675 IPQEPFLFSG-TVRENL----DPQGLHKDRALWQA---LKQCHLSEvitsmggldgELGEGGRSLSLGQRQLLCLARALL 746
Cdd:cd03269 75 LPEERGLYPKmKVIDQLvylaQLKGLKKEEARRRIdewLERLELSE----------YANKRVEELSKGNQQKVQFIAAVI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767940955 747 TDAKILCIDEATASVDQKTDQLLQQTICK-RFANKTVLTIAHRLNTILN-SDRVLVLQAGRVV 807
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEElCDRVLLLNKGRAV 207
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-157 |
1.08e-15 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 76.76 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 20 QEPWIQFATIRDNI-LFGKTFDAQLYkEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLL 98
Cdd:cd03244 85 QDPVLFSGTIRSNLdPFGEYSDEELW-QALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVL 163
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 767940955 99 DDPLAAVDADVAnHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPP 157
Cdd:cd03244 164 DEATASVDPETD-ALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
595-762 |
1.54e-15 |
|
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: 76.41 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG--VDTSQLELAQLRSQL 672
Cdd:cd03262 1 IEIKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkLTDDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 673 AIIPQEPFLFSG-TVREN--LDP---QGLHKDRAL---WQALKQCHLSEVITSMGgldgelgeggRSLSLGQRQLLCLAR 743
Cdd:cd03262 79 GMVFQQFNLFPHlTVLENitLAPikvKGMSKAEAEeraLELLEKVGLADKADAYP----------AQLSGGQQQRVAIAR 148
|
170
....*....|....*....
gi 767940955 744 ALLTDAKILCIDEATASVD 762
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALD 167
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
605-819 |
1.98e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 79.31 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 605 RPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRS----QLAIIPQEPF 680
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 681 LFSG-TVRENLD--------PQGLHKDRALwQALKQCHLSEVITSMGGldgelgeggrSLSLGQRQLLCLARALLTDAKI 751
Cdd:PRK10070 117 LMPHmTVLDNTAfgmelagiNAEERREKAL-DALRQVGLENYAHSYPD----------ELSGGMRQRVGLARALAINPDI 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767940955 752 LCIDEATASVDQKTDQLLQQTICKRFA--NKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQP 819
Cdd:PRK10070 186 LLMDEAFSALDPLIRTEMQDELVKLQAkhQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNNP 256
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
615-801 |
2.07e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 81.23 E-value: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 615 VTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLL-DGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENL--- 690
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIkys 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 691 ----------------------------------------------DPQGLHKDRALWQALKQCHLSEV---------IT 715
Cdd:PTZ00265 484 lyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttDSNELIEMRKNYQTIKDSEVVDVskkvlihdfVS 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 716 SMGGLDGELGEGGRS-LSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTI--CKRFANKTVLTIAHRLNTI 792
Cdd:PTZ00265 564 ALPDKYETLVGSNASkLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTInnLKGNENRITIIIAHRLSTI 643
|
....*....
gi 767940955 793 LNSDRVLVL 801
Cdd:PTZ00265 644 RYANTIFVL 652
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
594-804 |
2.22e-15 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 81.11 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 594 GVEFQDVVLAYRPGLPNaldgVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGvdtsqlelaqlrsQLA 673
Cdd:TIGR01271 428 GLFFSNFSLYVTPVLKN----ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RIS 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 674 IIPQEPFLFSGTVRENLdPQGLHKDRALWQA-LKQCHLSEVITSMGGLDGELGEGGR-SLSLGQRQLLCLARALLTDAKI 751
Cdd:TIGR01271 491 FSPQTSWIMPGTIKDNI-IFGLSYDEYRYTSvIKACQLEEDIALFPEKDKTVLGEGGiTLSGGQRARISLARAVYKDADL 569
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767940955 752 LCIDEATASVDQKTD-QLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAG 804
Cdd:TIGR01271 570 YLLDSPFTHLDVVTEkEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
594-804 |
2.61e-15 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 77.20 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 594 GVEFQDVVLAYRPGLPNaldgVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGvdtsqlelaqlrsQLA 673
Cdd:cd03291 39 NLFFSNLCLVGAPVLKN----INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RIS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 674 IIPQEPFLFSGTVRENLdPQGLHKDRALWQA-LKQCHLSEVITSMGGLDGELGEGGR-SLSLGQRQLLCLARALLTDAKI 751
Cdd:cd03291 102 FSSQFSWIMPGTIKENI-IFGVSYDEYRYKSvVKACQLEEDITKFPEKDNTVLGEGGiTLSGGQRARISLARAVYKDADL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767940955 752 LCIDEATASVDQKTD-QLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAG 804
Cdd:cd03291 181 YLLDSPFGYLDVFTEkEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
595-815 |
4.70e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 76.33 E-value: 4.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAI 674
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 675 IPQEP---FLFSgTVREN----LDPQGLHKD---RALWQALKQCHLSEVITSmggldgelgeGGRSLSLGQRQLLCLARA 744
Cdd:PRK13648 88 VFQNPdnqFVGS-IVKYDvafgLENHAVPYDemhRRVSEALKQVDMLERADY----------EPNALSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767940955 745 LLTDAKILCIDEATASVDQKTDQLLQQTICKRFANK--TVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATL 815
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
75-161 |
6.39e-15 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 77.11 E-value: 6.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHL------LHRCILGmlsytTRLLCTH-RTEYLERADAVLLME 147
Cdd:COG1118 134 LSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELrrwlrrLHDELGG-----TTVFVTHdQEEALELADRVVVMN 208
|
90
....*....|....
gi 767940955 148 AGRLIRAGPPSEIL 161
Cdd:COG1118 209 QGRIEQVGTPDEVY 222
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
612-813 |
6.98e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 77.57 E-value: 6.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 612 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFL-FSGTVRE-- 688
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRQvv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 689 ---------NLDPQGLHKDRALWQALKQCHLSEVItsmggldgelGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATA 759
Cdd:PRK09536 99 emgrtphrsRFDTWTETDRAAVERAMERTGVAQFA----------DRPVTSLSGGERQRVLLARALAQATPVLLLDEPTA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767940955 760 SVDqKTDQLLQQTICKRFAN--KTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPA 813
Cdd:PRK09536 169 SLD-INHQVRTLELVRRLVDdgKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPA 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
611-819 |
9.50e-15 |
|
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: 74.58 E-value: 9.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 611 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAqlRSQLAIIPQEPFLFSG-TVREN 689
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTVFQNYALFPHlTVFEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 690 ----LDPQGLHKD---RALWQALKQCHLSEVITSMggldgelgegGRSLSLGQRQLLCLARALLTDAKILCIDEATASVD 762
Cdd:cd03300 93 iafgLRLKKLPKAeikERVAEALDLVQLEGYANRK----------PSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767940955 763 QKTDQLLQQTIcKRFANK---TVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQP 819
Cdd:cd03300 163 LKLRKDMQLEL-KRLQKElgiTFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEIYEEP 222
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
308-540 |
1.51e-14 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 74.60 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 308 NGSSDIRFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDS 387
Cdd:pfam00664 35 PETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 388 LPFILNILLANAAGLLGLLAVLGSGLPWLLLLLPPLSIMYYHVQRHYRASSRELRRLGSLTLSPLYSHLADTLAGLSVLR 467
Cdd:pfam00664 115 LGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVK 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767940955 468 ATGATYRFEEENLRLLELNQRCQFATSATMQWLDIRLQLMGAAVVSAIAGIALVQHQQGLANPGLVGLSLSYA 540
Cdd:pfam00664 195 AFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLF 267
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
619-807 |
1.83e-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: 73.30 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 619 VQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAqlRSQLAIIPQEPFLFSG-TVRENLD---PQG 694
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAHlTVEQNVGlglSPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 695 LHKDRALWQALkqchlsEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQ--- 771
Cdd:cd03298 99 LKLTAEDRQAI------EVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDlvl 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 767940955 772 TICKRFANkTVLTIAHRLNTILN-SDRVLVLQAGRVV 807
Cdd:cd03298 173 DLHAETKM-TVLMVTHQPEDAKRlAQRVVFLDNGRIA 208
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
611-807 |
1.90e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 76.75 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 611 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLElAQLRSQL--AIIPQEPFLFSG-TVR 687
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD-HKLAAQLgiGIIYQELSVIDElTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 688 ENLdPQGLHKDRAL-------WQALKQchLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATAS 760
Cdd:PRK09700 99 ENL-YIGRHLTKKVcgvniidWREMRV--RAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767940955 761 VDQK-TDQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVV 807
Cdd:PRK09700 176 LTNKeVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSV 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
611-820 |
1.97e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 73.92 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 611 ALDGVTFCVQPGEKLGIVGRTGSGKSS----------LllvlfrllEPS---SGRVLLDGVD--TSQLELAQLRSQLAII 675
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTllrclnrmndL--------IPGarvEGEILLDGEDiyDPDVDVVELRRRVGMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 676 PQEPFLFSGTVREN----LDPQGLHKDRAL----WQALKQCHL-SEVitsmggldgelgeGGR------SLSLGQRQLLC 740
Cdd:COG1117 98 FQKPNPFPKSIYDNvaygLRLHGIKSKSELdeivEESLRKAALwDEV-------------KDRlkksalGLSGGQQQRLC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 741 LARALLTDAKILCIDEATASVD----QKTDQLLQQtICKRFankTVLTIAH------RLntilnSDRVLVLQAGRVVELD 810
Cdd:COG1117 165 IARALAVEPEVLLMDEPTSALDpistAKIEELILE-LKKDY---TIVIVTHnmqqaaRV-----SDYTAFFYLGELVEFG 235
|
250
....*....|
gi 767940955 811 SPATLRNQPH 820
Cdd:COG1117 236 PTEQIFTNPK 245
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
595-788 |
2.22e-14 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 71.80 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGLPNaLDGVTFCVQPGEKLGIVGRTGSGKSSLLlvlfrllepssgRVL--LDGVDTSQLELAQlRSQL 672
Cdd:cd03223 1 IELENLSLATPDGRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLF------------RALagLWPWGSGRIGMPE-GEDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 673 AIIPQEPFLFSGTVRENLdpqglhkdRALWQalkqchlsevitsmggldgelgeggRSLSLGQRQLLCLARALLTDAKIL 752
Cdd:cd03223 67 LFLPQRPYLPLGTLREQL--------IYPWD-------------------------DVLSGGEQQRLAFARLLLHKPKFV 113
|
170 180 190
....*....|....*....|....*....|....*.
gi 767940955 753 CIDEATASVDQKTDQLLQQTICKRFAnkTVLTIAHR 788
Cdd:cd03223 114 FLDEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
611-807 |
2.71e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 76.22 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 611 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGvdtsqlELAQLRS-QLAI------IPQEPFLFS 683
Cdd:COG3845 20 ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG------KPVRIRSpRDAIalgigmVHQHFMLVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 684 G-TVRENL-----DPQGLHKDR-ALWQALKQchLSE-----------VitsmggldgelgeggRSLSLGQRQLLCLARAL 745
Cdd:COG3845 94 NlTVAENIvlglePTKGGRLDRkAARARIRE--LSErygldvdpdakV---------------EDLSVGEQQRVEILKAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767940955 746 LTDAKILCIDEATAsV--DQKTDQLLQqtICKRFAN--KTVLTIAHRLNTIL-NSDRVLVLQAGRVV 807
Cdd:COG3845 157 YRGARILILDEPTA-VltPQEADELFE--ILRRLAAegKSIIFITHKLREVMaIADRVTVLRRGKVV 220
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
75-160 |
4.53e-14 |
|
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: 72.76 E-value: 4.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHL------LHRCIlgmlsYTTRLLCTH-RTEYLERADAVLLME 147
Cdd:cd03296 137 LSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELrrwlrrLHDEL-----HVTTVFVTHdQEEALEVADRVVVMN 211
|
90
....*....|...
gi 767940955 148 AGRLIRAGPPSEI 160
Cdd:cd03296 212 KGRIEQVGTPDEV 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
616-815 |
5.39e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 72.09 E-value: 5.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 616 TFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQlRSqLAIIPQEPFLFSG-TVRENLDpQG 694
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-RP-VSMLFQENNLFPHlTVAQNIG-LG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 695 LHKD--------RALWQALKQCHLSEVITSMGgldgelgeggRSLSLGQRQLLCLARALLTDAKILCIDEATASVD---- 762
Cdd:COG3840 96 LRPGlkltaeqrAQVEQALERVGLAGLLDRLP----------GQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalr 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767940955 763 QKTDQLLQQtICKRFANkTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATL 815
Cdd:COG3840 166 QEMLDLVDE-LCRERGL-TVLMVTHDPEDAARiADRVLLVADGRIAADGPTAAL 217
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
595-818 |
7.00e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 72.89 E-value: 7.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGLP---NALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVD----TSQLELAQ 667
Cdd:PRK13646 3 IRFDNVSYTYQKGTPyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithkTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 668 LRSQLAIIPQ--EPFLFSGTV-RENL-DPQGLH------KDRAlWQALKQCHLSEVITSMGGLdgelgeggrSLSLGQRQ 737
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVeREIIfGPKNFKmnldevKNYA-HRLLMDLGFSRDVMSQSPF---------QMSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 738 LLCLARALLTDAKILCIDEATASVDQKT-DQLLqqTICKRFA---NKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSP 812
Cdd:PRK13646 153 KIAIVSILAMNPDIIVLDEPTAGLDPQSkRQVM--RLLKSLQtdeNKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSP 230
|
....*.
gi 767940955 813 ATLRNQ 818
Cdd:PRK13646 231 KELFKD 236
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
8-173 |
8.60e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 75.84 E-value: 8.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 8 VRGLSKGFGLATQEPWIQFATIRDNILFGKTfDAQLyKEVLEAC---ALNDDLSILPAGDQTEVGEKGVTLSGGQRARIA 84
Cdd:PTZ00265 1291 LKDLRNLFSIVSQEPMLFNMSIYENIKFGKE-DATR-EDVKRACkfaAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIA 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 85 LARAVYQEKELYLLDDPLAAVDADvANHLLHRCILGMLSYTTRLLCT--HRTEYLERADAVLLM----EAGRLIRA-GPP 157
Cdd:PTZ00265 1369 IARALLREPKILLLDEATSSLDSN-SEKLIEKTIVDIKDKADKTIITiaHRIASIKRSDKIVVFnnpdRTGSFVQAhGTH 1447
|
170
....*....|....*.
gi 767940955 158 SEILPLVQAVPKAWAE 173
Cdd:PTZ00265 1448 EELLSVQDGVYKKYVK 1463
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
594-819 |
8.84e-14 |
|
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: 71.60 E-value: 8.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 594 GVEFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLElAQLRsQLA 673
Cdd:cd03296 2 SIEVRNVSKRF--GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP-VQER-NVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 674 IIPQEPFLFSG-TVRENL-----------DPQGLHKDRALWQALKQCHLSEVITSMGGldgelgeggrSLSLGQRQLLCL 741
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVafglrvkprseRPPEAEIRAKVHELLKLVQLDWLADRYPA----------QLSGGQRQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 742 ARALLTDAKILCIDEATASVDQKTDQLLQQTIcKRFANKTVLT---IAHRLNTILN-SDRVLVLQAGRVVELDSPATLRN 817
Cdd:cd03296 148 ARALAVEPKVLLLDEPFGALDAKVRKELRRWL-RRLHDELHVTtvfVTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYD 226
|
..
gi 767940955 818 QP 819
Cdd:cd03296 227 HP 228
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
595-812 |
9.42e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 72.43 E-value: 9.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGLPN----ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLE-LAQLR 669
Cdd:PRK13633 5 IKCKNVSYKYESNEESteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 670 SQLAIIPQEP--FLFSGTVR-------ENLDPQGLHKDRALWQALKQCHLSEVitsmggldgeLGEGGRSLSLGQRQLLC 740
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEedvafgpENLGIPPEEIRERVDESLKKVGMYEY----------RRHAPHLLSGGQKQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767940955 741 LARALLTDAKILCIDEATASVDQKTDQLLQQTICK--RFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSP 812
Cdd:PRK13633 155 IAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTP 228
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
551-811 |
1.68e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 74.98 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 551 VSSFTQTEamlVSVERLEEYTCDLPQEPQG---QPLQLGTGWltqgGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGI 627
Cdd:TIGR00957 597 ISSIVQAS---VSLKRLRIFLSHEELEPDSierRTIKPGEGN----SITVHNATFTWARDLPPTLNGITFSIPEGALVAV 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 628 VGRTGSGKSSLLLVLFRLLEPSSGRVLLDGvdtsqlelaqlrsQLAIIPQEPFLFSGTVREN-LDPQGLHKDRaLWQALK 706
Cdd:TIGR00957 670 VGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENiLFGKALNEKY-YQQVLE 735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 707 QCHL---SEVITSMGGLDGELGEGgrSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQ-LLQQTICKR--FANK 780
Cdd:TIGR00957 736 ACALlpdLEILPSGDRTEIGEKGV--NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKhIFEHVIGPEgvLKNK 813
|
250 260 270
....*....|....*....|....*....|.
gi 767940955 781 TVLTIAHRLNTILNSDRVLVLQAGRVVELDS 811
Cdd:TIGR00957 814 TRILVTHGISYLPQVDVIIVMSGGKISEMGS 844
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
595-807 |
2.65e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 71.42 E-value: 2.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGlPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG--VDTSQLELAQLRSQL 672
Cdd:PRK13636 6 LKVEELNYNYSDG-THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 673 AIIPQEP--FLFSGTVRENLD----PQGLHKD---RALWQALKQC---HLSEVITsmggldgelgeggRSLSLGQRQLLC 740
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYQDVSfgavNLKLPEDevrKRVDNALKRTgieHLKDKPT-------------HCLSFGQKKRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767940955 741 LARALLTDAKILCIDEATASVDQK-TDQLLQqtICKRFANKTVLTI---AHRLNTI-LNSDRVLVLQAGRVV 807
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDPMgVSEIMK--LLVEMQKELGLTIiiaTHDIDIVpLYCDNVFVMKEGRVI 221
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
595-818 |
2.92e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 70.92 E-value: 2.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGlPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAI 674
Cdd:PRK13647 5 IEVEDLHFRYKDG-TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 675 IPQEP--FLFSGTVRENL--DPQ--GLHKD---RALWQALKQCHLSEVitsmggldgeLGEGGRSLSLGQRQLLCLARAL 745
Cdd:PRK13647 84 VFQDPddQVFSSTVWDDVafGPVnmGLDKDeveRRVEEALKAVRMWDF----------RDKPPYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767940955 746 LTDAKILCIDEATASVDQKTDQLLqQTICKRFAN--KTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQ 818
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETL-MEILDRLHNqgKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
6-199 |
2.97e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 73.46 E-value: 2.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 6 VAVRGLSKGFGLATQEPWIQFATIRDNILFGKT--FDAQLYkEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARI 83
Cdd:PRK13657 402 VTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPdaTDEEMR-AAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRL 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 84 ALARAVYQEKELYLLDDPLAAVDADVANHlLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEILpl 163
Cdd:PRK13657 481 AIARALLKDPPILILDEATSALDVETEAK-VKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELV-- 557
|
170 180 190
....*....|....*....|....*....|....*.
gi 767940955 164 vqavpkawAENGQESDSATAQSVQNPEKTKEGLEEE 199
Cdd:PRK13657 558 --------ARGGRFAALLRAQGMLQEDERRKQPAAE 585
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
612-807 |
3.35e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.78 E-value: 3.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 612 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRsQLAI--IPQEPFLFSG-TVRE 688
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAH-QLGIylVPQEPLLFPNlSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 689 NL------DPQGLHKDRALWQALkQCHLSevitsmggldgeLGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVD 762
Cdd:PRK15439 106 NIlfglpkRQASMQKMKQLLAAL-GCQLD------------LDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767940955 763 Q-KTDQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVV 807
Cdd:PRK15439 173 PaETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIA 219
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
595-815 |
4.11e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 69.91 E-value: 4.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQ-LRSQLA 673
Cdd:PRK11614 6 LSFDKVSAHY--GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 674 IIPQEPFLFSG-TVRENLDPQGLHKDRALWQAlkqcHLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKIL 752
Cdd:PRK11614 84 IVPEGRRVFSRmTVEENLAMGGFFAERDQFQE----RIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767940955 753 CIDEATASVDQKTDQLLQQTICK-RFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATL 815
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQlREQGMTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDAL 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
594-815 |
5.18e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 70.16 E-value: 5.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 594 GVEFQDVVLAYRPGLP---NALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVD-TSQ---LELA 666
Cdd:PRK13649 2 GINLQNVSYTYQAGTPfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLiTSTsknKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 667 QLRSQLAIIPQ--EPFLFSGTVRENL--DPQ--GLHKDRALWQALKQCHLSEVITSMGGLDGElgeggrSLSLGQRQLLC 740
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEETVLKDVafGPQnfGVSQEEAEALAREKLALVGISESLFEKNPF------ELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767940955 741 LARALLTDAKILCIDEATASVDQKTDQLLqQTICKRF--ANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATL 815
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKEL-MTLFKKLhqSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKDI 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
28-155 |
5.33e-13 |
|
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: 68.70 E-value: 5.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 28 TIRDNILFG----KTFDAQLYKEVLEACALNDDLSILpagdqtevGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLA 103
Cdd:cd03259 88 TVAENIAFGlklrGVPKAEIRARVRELLELVGLEGLL--------NRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 767940955 104 AVDADVANHLLH--RCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAG 155
Cdd:cd03259 160 ALDAKLREELREelKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
595-804 |
5.44e-13 |
|
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: 68.90 E-value: 5.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGLPNaLDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQ--- 671
Cdd:cd03290 1 VQVTNGYFSWGSGLAT-LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnry 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 672 -LAIIPQEPFLFSGTVRENL---DPQGLHKDRALWQAlkqCHLSEVItSMGGLDGELGEGGRSLSL--GQRQLLCLARAL 745
Cdd:cd03290 80 sVAYAAQKPWLLNATVEENItfgSPFNKQRYKAVTDA---CSLQPDI-DLLPFGDQTEIGERGINLsgGQRQRICVARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767940955 746 LTDAKILCIDEATASVD-QKTDQLLQQTICK--RFANKTVLTIAHRLNTILNSDRVLVLQAG 804
Cdd:cd03290 156 YQNTNIVFLDDPFSALDiHLSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
75-151 |
5.65e-13 |
|
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: 67.63 E-value: 5.65e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANHLLHRCILGM-LSYTTRLLCTHRTEYLERADAVLLMEAGRL 151
Cdd:cd03246 97 LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVE-GERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
612-812 |
8.91e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 69.27 E-value: 8.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 612 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSG-TVREnL 690
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRE-L 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 691 DPQGLHKDRALWQALKQCHLSEVITSMGGLDGELGEGGR--SLSLGQRQLLCLARALLTDAKILCIDEATASVD------ 762
Cdd:PRK11231 97 VAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRltDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDinhqve 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767940955 763 -QKTDQLLQQtickrfANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSP 812
Cdd:PRK11231 177 lMRLMRELNT------QGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTP 222
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
604-819 |
1.14e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 69.05 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 604 YRPGL-----PNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGvdtSQLELA--QLRSQ-LAII 675
Cdd:PRK15112 16 YRTGWfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD---HPLHFGdySYRSQrIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 676 PQEPF-----------LFSGTVRENLDPQGLHKDRALWQALKQCHLsevitsmggLDGELGEGGRSLSLGQRQLLCLARA 744
Cdd:PRK15112 93 FQDPStslnprqrisqILDFPLRLNTDLEPEQREKQIIETLRQVGL---------LPDHASYYPHMLAPGQKQRLGLARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 745 LLTDAKILCIDEATASVD-----QKTDQLLQ----QTICKRFANKTVLTIAHRlntilnSDRVLVLQAGRVVELDSPATL 815
Cdd:PRK15112 164 LILRPKVIIADEALASLDmsmrsQLINLMLElqekQGISYIYVTQHLGMMKHI------SDQVLVMHQGEVVERGSTADV 237
|
....
gi 767940955 816 RNQP 819
Cdd:PRK15112 238 LASP 241
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
599-806 |
1.38e-12 |
|
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: 67.07 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 599 DVVLAYRP-GLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQ-LAIIP 676
Cdd:cd03215 2 EPVLEVRGlSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 677 QEPF---LFSG-TVRENLdpqglhkdralwqalkqchlseVITSMggldgelgeggrsLSLGQRQLLCLARALLTDAKIL 752
Cdd:cd03215 82 EDRKregLVLDlSVAENI----------------------ALSSL-------------LSGGNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767940955 753 CIDEATASVDQKTDQLLQQTIcKRFA--NKTVLTIAHRLNTILN-SDRVLVLQAGRV 806
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLI-RELAdaGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
607-813 |
1.77e-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: 70.60 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 607 GLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLL----DGVDTSQ---LELAQLRSQLAIIPQEP 679
Cdd:TIGR03269 295 GVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKpgpDGRGRAKRYIGILHQEY 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 680 FLFS-GTVRENLD-------PQGLHKDRALWqALKQCHLSEvitsmGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKI 751
Cdd:TIGR03269 375 DLYPhRTVLDNLTeaiglelPDELARMKAVI-TLKMVGFDE-----EKAEEILDKYPDELSEGERHRVALAQVLIKEPRI 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767940955 752 LCIDEATASVDQKTDQLLQQTICK--RFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPA 813
Cdd:TIGR03269 449 VILDEPTGTMDPITKVDVTHSILKarEEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPE 513
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
606-819 |
1.83e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 69.22 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 606 PGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDT---SQLELAQLRSQLAIIPQEPFlf 682
Cdd:PRK11308 25 ERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPEAQKLLRQKIQIVFQNPY-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 683 sgtvrENLDP-----QGLHKDRALWQAL-KQCHLSEVITSMGGLDGELGEGGR---SLSLGQRQLLCLARALLTDAKILC 753
Cdd:PRK11308 103 -----GSLNPrkkvgQILEEPLLINTSLsAAERREKALAMMAKVGLRPEHYDRyphMFSGGQRQRIAIARALMLDPDVVV 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767940955 754 IDEATASVD-----QKTDQL--LQQTIckrfaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQP 819
Cdd:PRK11308 178 ADEPVSALDvsvqaQVLNLMmdLQQEL-----GLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
602-816 |
2.36e-12 |
|
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: 67.01 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 602 LAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQlELAQLRSQLAIIPQEPFL 681
Cdd:cd03265 6 LVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 682 FSG-TVRENLDPQG--------LHKDRALwQALKQCHLSEVitsmggldgeLGEGGRSLSLGQRQLLCLARALLTDAKIL 752
Cdd:cd03265 85 DDElTGWENLYIHArlygvpgaERRERID-ELLDFVGLLEA----------ADRLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767940955 753 CIDEATASVDQKT-DQLLQ--QTICKRFaNKTVLTIAHRLNTI-LNSDRVLVLQAGRVVELDSPATLR 816
Cdd:cd03265 154 FLDEPTIGLDPQTrAHVWEyiEKLKEEF-GMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
574-819 |
2.69e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.12 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 574 LPQEPQGQPLQLGTGWLTQGGVEFQDVVLAYRPGL-------PNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLL 646
Cdd:PRK15134 257 LNSEPSGDPVPLPEPASPLLDVEQLQVAFPIRKGIlkrtvdhNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 647 ePSSGRVLLDGVDTSQLELAQL---RSQLAIIPQEPFlfsgtvrENLDPQgLHKDRALWQALK--QCHLS------EVIT 715
Cdd:PRK15134 337 -NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPN-------SSLNPR-LNVLQIIEEGLRvhQPTLSaaqreqQVIA 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 716 SMGGLDGELGEGGR---SLSLGQRQLLCLARALLTDAKILCIDEATASVDqKTDQLLQQTICKRFANKTVLT---IAHRL 789
Cdd:PRK15134 408 VMEEVGLDPETRHRypaEFSGGQRQRIAIARALILKPSLIILDEPTSSLD-KTVQAQILALLKSLQQKHQLAylfISHDL 486
|
250 260 270
....*....|....*....|....*....|.
gi 767940955 790 NTILN-SDRVLVLQAGRVVELDSPATLRNQP 819
Cdd:PRK15134 487 HVVRAlCHQVIVLRQGEVVEQGDCERVFAAP 517
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
612-807 |
5.01e-12 |
|
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: 66.14 E-value: 5.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 612 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPS---SGRVLLDGvdtSQLELAQLRSQLAIIPQEPFLFSG-TVR 687
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNG---QPRKPDQFQKCVAYVRQDDILLPGlTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 688 ENL-----------DPQGLHKDRALWQALKQCHLSEVitsmggldgeLGEGGRSLSLGQRQLLCLARALLTDAKILCIDE 756
Cdd:cd03234 100 ETLtytailrlprkSSDAIRKKRVEDVLLRDLALTRI----------GGNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767940955 757 ATASVDQKTDQLLQQT---ICKRfaNKTVLTIAHRLNTILNS--DRVLVLQAGRVV 807
Cdd:cd03234 170 PTSGLDSFTALNLVSTlsqLARR--NRIVILTIHQPRSDLFRlfDRILLLSSGEIV 223
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
11-161 |
6.86e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 69.62 E-value: 6.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 11 LSKGFGLATQEPWIQFATIRDNI-LFGKTFDAQLYkEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAV 89
Cdd:PLN03232 1308 LRRVLSIIPQSPVLFSGTVRFNIdPFSEHNDADLW-EALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARAL 1386
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767940955 90 YQEKELYLLDDPLAAVDADVaNHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 161
Cdd:PLN03232 1387 LRRSKILVLDEATASVDVRT-DSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELL 1457
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
555-817 |
8.34e-12 |
|
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: 69.27 E-value: 8.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 555 TQTEAMLVSVERLEEYTCDlPQEPQGQPLQLGT----GWLTqgGVEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGR 630
Cdd:TIGR01257 888 TREERALEKTEPLTEEMED-PEHPEGINDSFFErelpGLVP--GVCVKNLVKIFEPSGRPAVDRLNITFYENQITAFLGH 964
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 631 TGSGKSSLLLVLFRLLEPSSGRVLLDGVDTsQLELAQLRSQLAIIPQEPFLFSG-TVRENLDPQGLHKDRALWQAlkQCH 709
Cdd:TIGR01257 965 NGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAEHILFYAQLKGRSWEEA--QLE 1041
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 710 LsEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAHRL 789
Cdd:TIGR01257 1042 M-EAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHM 1120
|
250 260
....*....|....*....|....*....
gi 767940955 790 NTI-LNSDRVLVLQAGRVVELDSPATLRN 817
Cdd:TIGR01257 1121 DEAdLLGDRIAIISQGRLYCSGTPLFLKN 1149
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
611-819 |
1.37e-11 |
|
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: 67.79 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 611 ALDGVTFCVQPGEKLGIVGRTGSGKS----SLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLR----SQLAIIPQEPfLF 682
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRrirgNRIAMIFQEP-MT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 683 SgtvrenLDP---------------QGLHKD----RALwQALKQCHLSEVITSMggldgelgeggRS----LSLGQRQLL 739
Cdd:COG4172 104 S------LNPlhtigkqiaevlrlhRGLSGAaaraRAL-ELLERVGIPDPERRL-----------DAyphqLSGGQRQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 740 CLARALLTDAKILCIDEATASVD---QKtdQLLQ--QTICKRFaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPA 813
Cdd:COG4172 166 MIAMALANEPDLLIADEPTTALDvtvQA--QILDllKDLQREL-GMALLLITHDLGVVRRfADRVAVMRQGEIVEQGPTA 242
|
....*.
gi 767940955 814 TLRNQP 819
Cdd:COG4172 243 ELFAAP 248
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
28-155 |
1.48e-11 |
|
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: 64.62 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 28 TIRDNILFGKTF-----DAQLYKEVLEACALnddlsilpagdqTEVGEKGV-TLSGGQRARIALARAVYQEKELYLLDDP 101
Cdd:cd03297 91 NVRENLAFGLKRkrnreDRISVDELLDLLGL------------DHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEP 158
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 767940955 102 LAAVDADVANHLLH--RCILGMLSYTTrLLCTHRTEYLER-ADAVLLMEAGRLIRAG 155
Cdd:cd03297 159 FSALDRALRLQLLPelKQIKKNLNIPV-IFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
16-161 |
1.56e-11 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 65.08 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 16 GLATQEPWI-QFATIRDNILF-------GKTFDAQLYKEVLEACALNDDLsilpagdqtevGEKGVTLSGGQRARIALAR 87
Cdd:COG1131 76 GYVPQEPALyPDLTVRENLRFfarlyglPRKEARERIDELLELFGLTDAA-----------DRKVGTLSGGMKQRLGLAL 144
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767940955 88 AVYQEKELYLLDDPLAAVDAdVANHLLHRCILGMLSY-TTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 161
Cdd:COG1131 145 ALLHDPELLILDEPTSGLDP-EARRELWELLRELAAEgKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELK 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
612-808 |
1.69e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 65.48 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 612 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRS-----QL-------AIIPQEp 679
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAfrrdiQMvfqdsisAVNPRK- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 680 flfsgTVRENLDPQGLHKDRaLWQALKQCHLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATA 759
Cdd:PRK10419 107 -----TVREIIREPLRHLLS-LDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 760 SVD-----QKTDQL--LQQ---TICkrfanktvLTIAHRLNTILN-SDRVLVLQAGRVVE 808
Cdd:PRK10419 181 NLDlvlqaGVIRLLkkLQQqfgTAC--------LFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
610-819 |
1.81e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 66.78 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 610 NALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQlrSQLAIIPQEPFLFSG-TVRE 688
Cdd:PRK11607 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ--RPINMMFQSYALFPHmTVEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 689 NLdPQGLHKDRalwqaLKQCHLSEVITSMGGLDGELGEGGR---SLSLGQRQLLCLARALLTDAKILCIDEATASVDQKT 765
Cdd:PRK11607 111 NI-AFGLKQDK-----LPKAEIASRVNEMLGLVHMQEFAKRkphQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767940955 766 DQLLQQT---ICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATLRNQP 819
Cdd:PRK11607 185 RDRMQLEvvdILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
595-815 |
1.89e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 66.39 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDT-SQLELAqlRSQLA 673
Cdd:PRK13536 42 IDLAGVSKSY--GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARARLA--RARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 674 IIPQEPFL-FSGTVRENLDPQGLhkdralWQALKQCHLSEVITSM---GGLDGELGEGGRSLSLGQRQLLCLARALLTDA 749
Cdd:PRK13536 118 VVPQFDNLdLEFTVRENLLVFGR------YFGMSTREIEAVIPSLlefARLESKADARVSDLSGGMKRRLTLARALINDP 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767940955 750 KILCIDEATASVDQKTDQLLQQTICKRFA-NKTVLTIAH------RLntilnSDRVLVLQAGRVVELDSPATL 815
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLLArGKTILLTTHfmeeaeRL-----CDRLCVLEAGRKIAEGRPHAL 259
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
595-807 |
1.91e-11 |
|
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: 65.11 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAY--RPglpnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSG---RVLldGVDTSQLELAQLR 669
Cdd:COG1119 4 LELRNVTVRRggKT----ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLF--GERRGGEDVWELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 670 SQLAII-P--QEPFLFSGTVRE--------------NLDPQglHKDRAlWQALKQCHLSEVITsmggldgelgEGGRSLS 732
Cdd:COG1119 78 KRIGLVsPalQLRFPRDETVLDvvlsgffdsiglyrEPTDE--QRERA-RELLELLGLAHLAD----------RPFGTLS 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767940955 733 LGQRQLLCLARALLTDAKILCIDEATASVDQK-TDQLLQ--QTICKRFAnKTVLTIAHRLNTILNS-DRVLVLQAGRVV 807
Cdd:COG1119 145 QGEQRRVLIARALVKDPELLILDEPTAGLDLGaRELLLAllDKLAAEGA-PTLVLVTHHVEEIPPGiTHVLLLKDGRVV 222
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
611-809 |
1.95e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 66.27 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 611 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQL---RSQLAIIPQEPfLFSGTVR 687
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravRSDIQMIFQDP-LASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 688 ENL-----DPQGLHKDRALWQALKQchlsEVITSMGGLDGELGEGGR---SLSLGQRQLLCLARALLTDAKILCIDEATA 759
Cdd:PRK15079 115 MTIgeiiaEPLRTYHPKLSRQEVKD----RVKAMMLKVGLLPNLINRyphEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767940955 760 SVD----QKTDQLLQQTicKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVEL 809
Cdd:PRK15079 191 ALDvsiqAQVVNLLQQL--QREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVEL 243
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
28-161 |
2.04e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 67.35 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 28 TIRDNILF---GKTFDAQLYKEVLEACALnDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAA 104
Cdd:PRK11176 432 TIANNIAYartEQYSREQIEEAARMAYAM-DFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSA 510
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 767940955 105 VDADvANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 161
Cdd:PRK11176 511 LDTE-SERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELL 566
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
20-151 |
2.29e-11 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 64.07 E-value: 2.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 20 QEPWIQFATIRDNILF-----GKTFDAQLYKEVLEACALNDDlsILpagdQTEVGEkgvtLSGGQRARIALARAVYQEKE 94
Cdd:COG4619 81 QEPALWGGTVRDNLPFpfqlrERKFDRERALELLERLGLPPD--IL----DKPVER----LSGGERQRLALIRALLLQPD 150
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 95 LYLLDDPLAAVDADVAnHLLHRCILGMLSY--TTRLLCTHRTEYLER-ADAVLLMEAGRL 151
Cdd:COG4619 151 VLLLDEPTSALDPENT-RRVEELLREYLAEegRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
611-810 |
2.52e-11 |
|
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: 64.09 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 611 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLEL-AQLRSQLaiipqepflfsgTVREN 689
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLgGGFNPEL------------TGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 690 LdpqglhKDRALWQALKQ-------------CHLSEVITSmggldgelgeGGRSLSLGQRQLLCLARALLTDAKILCIDE 756
Cdd:cd03220 105 I------YLNGRLLGLSRkeidekideiiefSELGDFIDL----------PVKTYSSGMKARLAFAIATALEPDILLIDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767940955 757 ATASVD----QKTDQLLQQTICKrfaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELD 810
Cdd:cd03220 169 VLAVGDaafqEKCQRRLRELLKQ---GKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
621-807 |
2.86e-11 |
|
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: 63.85 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 621 PGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGV---DTSQ-LELAQLRSQLAIIPQEPFLFSG-TVRENLDpQGL 695
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRKkINLPPQQRKIGLVFQQYALFPHlNVRENLA-FGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 696 HKDRalwQALKQCHLSEVITSMGGLDGELGEGGRsLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICK 775
Cdd:cd03297 101 KRKR---NREDRISVDELLDLLGLDHLLNRYPAQ-LSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQ 176
|
170 180 190
....*....|....*....|....*....|....*
gi 767940955 776 RFA--NKTVLTIAHRLNTI-LNSDRVLVLQAGRVV 807
Cdd:cd03297 177 IKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQ 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
75-150 |
2.90e-11 |
|
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: 62.26 E-value: 2.90e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVAnHLLHRCILGML-SYTTRLLCTHRTEYLERA-DAVLLMEAGR 150
Cdd:cd00267 81 LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR-ERLLELLRELAeEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-157 |
3.02e-11 |
|
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: 63.59 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 4 GHVAVRGLSKGFGLATQEPWIQFATIRDNI-LFGKTFDAQLYKevleacALnddlsilpagdqtEVGEKGVTLSGGQRAR 82
Cdd:cd03369 73 STIPLEDLRSSLTIIPQDPTLFSGTIRSNLdPFDEYSDEEIYG------AL-------------RVSEGGLNLSQGQRQL 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767940955 83 IALARAVYQEKELYLLDDPLAAVDADvANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPP 157
Cdd:cd03369 134 LCLARALLKRPRVLVLDEATASIDYA-TDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
8-153 |
3.33e-11 |
|
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: 63.64 E-value: 3.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 8 VRGLSKGFGLATQE----PWiqfATIRDNILFGKTF----DAQLYKEVLEACALnddlsilpagdqteVGEKGV------ 73
Cdd:cd03293 68 VTGPGPDRGYVFQQdallPW---LTVLDNVALGLELqgvpKAEARERAEELLEL--------------VGLSGFenayph 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 74 TLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHlLHRCILGMLSYT--TRLLCTHRTE---YLerADAVLLMEA 148
Cdd:cd03293 131 QLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQ-LQEELLDIWRETgkTVLLVTHDIDeavFL--ADRVVVLSA 207
|
....*..
gi 767940955 149 --GRLIR 153
Cdd:cd03293 208 rpGRIVA 214
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
72-155 |
3.96e-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: 62.72 E-value: 3.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 72 GVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLhRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRL 151
Cdd:cd03247 96 GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLL-SLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKI 174
|
....
gi 767940955 152 IRAG 155
Cdd:cd03247 175 IMQG 178
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-161 |
4.04e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 66.39 E-value: 4.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 19 TQEPWIQFATIRDNILFGK--TFDAQLyKEVLEACALnDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELY 96
Cdd:PRK11160 420 SQRVHLFSATLRDNLLLAApnASDEAL-IEVLQQVGL-EKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLL 497
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767940955 97 LLDDPLAAVDADVANHLLhRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 161
Cdd:PRK11160 498 LLDEPTEGLDAETERQIL-ELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELL 561
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
595-819 |
4.13e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 64.44 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEP---SSGRVLLDGVDTSQLELAQLRSQ 671
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 672 LAIIPQEP-FLFSG-TVREN----LDPQGLHKD---RALWQALKQCHLSEVITSmggldgelgeGGRSLSLGQRQLLCLA 742
Cdd:PRK13640 86 VGIVFQNPdNQFVGaTVGDDvafgLENRAVPRPemiKIVRDVLADVGMLDYIDS----------EPANLSGGQKQRVAIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 743 RALLTDAKILCIDEATASVDQK-TDQLLQqtICKRFANK---TVLTIAHRLNTILNSDRVLVLQAGRVVELDSPATLRNQ 818
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAgKEQILK--LIRKLKKKnnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
.
gi 767940955 819 P 819
Cdd:PRK13640 234 V 234
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
602-771 |
4.40e-11 |
|
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: 62.76 E-value: 4.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 602 LAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLelaqlrsqlAIIPQEPFL 681
Cdd:TIGR01189 6 LACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ---------RDEPHENIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 682 FSG---------TVRENLD---PQGLHKDRALWQALKQCHLSEvitsmggldgELGEGGRSLSLGQRQLLCLARALLTDA 749
Cdd:TIGR01189 77 YLGhlpglkpelSALENLHfwaAIHGGAQRTIEDALAAVGLTG----------FEDLPAAQLSAGQQRRLALARLWLSRR 146
|
170 180
....*....|....*....|..
gi 767940955 750 KILCIDEATASVDQKTDQLLQQ 771
Cdd:TIGR01189 147 PLWILDEPTTALDKAGVALLAG 168
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
11-160 |
4.58e-11 |
|
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: 63.35 E-value: 4.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 11 LSKGFGLATQEPWIQFATIRDNILFG--------KTFDAQLYKEVLEACALNDDLSilpagDQTevgeKGVTLSGGQRAR 82
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiklKEELDERVEEALRKAALWDEVK-----DRL----HALGLSGGQQQR 149
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767940955 83 IALARAVYQEKELYLLDDPLAAVDAdVANHLLHRCILGMLSYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEI 160
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDP-ISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
566-810 |
5.56e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.15 E-value: 5.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 566 RLEEYTCDLPQePQGQPlqlgtGWLTqggVEFQDVVLAYrPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRL 645
Cdd:PRK10522 303 ALAPYKAEFPR-PQAFP-----DWQT---LELRNVTFAY-QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGL 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 646 LEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTvrenLDPQGLHKDRALWQA-LKQCHLSEVITsmgglDGEL 724
Cdd:PRK10522 373 YQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQL----LGPEGKPANPALVEKwLERLKMAHKLE-----LEDG 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 725 GEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVD--------QKTDQLLQQtickrfANKTVLTIAHRLNTILNSD 796
Cdd:PRK10522 444 RISNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDphfrrefyQVLLPLLQE------MGKTIFAISHDDHYFIHAD 517
|
250
....*....|....
gi 767940955 797 RVLVLQAGRVVELD 810
Cdd:PRK10522 518 RLLEMRNGQLSELT 531
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
611-807 |
6.09e-11 |
|
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: 63.51 E-value: 6.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 611 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQ----------LELAQlRSQLA--IIPQE 678
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKrrkkflrrigVVFGQ-KTQLWwdLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 679 PFLFSGTVReNLDPQGLHKDRAlwqalkqcHLSEvitsMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEAT 758
Cdd:cd03267 115 SFYLLAAIY-DLPPARFKKRLD--------ELSE----LLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767940955 759 ASVDQKTDQLLQQTIckRFANK----TVLTIAHRLNTILN-SDRVLVLQAGRVV 807
Cdd:cd03267 182 IGLDVVAQENIRNFL--KEYNRergtTVLLTSHYMKDIEAlARRVLVIDKGRLL 233
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
595-807 |
6.55e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 62.97 E-value: 6.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGlPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLRSQ 671
Cdd:PRK10908 2 IRFEHVSKAYLGG-RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrEVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 672 LAIIPQE-PFLFSGTVRENL-------DPQGLHKDRALWQALKQCHLSEVITSMGGldgelgeggrSLSLGQRQLLCLAR 743
Cdd:PRK10908 81 IGMIFQDhHLLMDRTVYDNVaipliiaGASGDDIRRRVSAALDKVGLLDKAKNFPI----------QLSGGEQQRVGIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 744 ALLTDAKILCIDEATASVDQKtdqlLQQTICKRFA--NK---TVLTIAHRLNTILNSD-RVLVLQAGRVV 807
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLDDA----LSEGILRLFEefNRvgvTVLMATHDIGLISRRSyRMLTLSDGHLH 216
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
612-812 |
7.08e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 65.84 E-value: 7.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 612 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPS---SGRVLLDGVdtsQLELAQLRSQLAIIPQ-EPFLFSGTVR 687
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGM---PIDAKEMRAISAYVQQdDLFIPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 688 ENLDPQG-LHKDRALWQALKQCHLSEVITSMGGLDGE-----LGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASV 761
Cdd:TIGR00955 118 EHLMFQAhLRMPRRVTKKEKRERVDEVLQALGLRKCAntrigVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGL 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767940955 762 DQKTDQLLQQTIcKRFANK--TVLTIAHRLNTIL--NSDRVLVLQAGRVVELDSP 812
Cdd:TIGR00955 198 DSFMAYSVVQVL-KGLAQKgkTIICTIHQPSSELfeLFDKIILMAEGRVAYLGSP 251
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
592-808 |
7.90e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 63.39 E-value: 7.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 592 QGGVEFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLE--PS---SGRVLLDGVDTSQLELA 666
Cdd:PRK14247 1 MNKIEIRDLKVSF--GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 667 QLRSQLAIIPQEPFLFSG-TVREN----LDPQGLHKDRA-----LWQALKQCHLSEVITSMGGLDGElgeggrSLSLGQR 736
Cdd:PRK14247 79 ELRRRVQMVFQIPNPIPNlSIFENvalgLKLNRLVKSKKelqerVRWALEKAQLWDEVKDRLDAPAG------KLSGGQQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767940955 737 QLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANKTVLTIAH------RLntilnSDRVLVLQAGRVVE 808
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRI-----SDYVAFLYKGQIVE 225
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
616-818 |
8.53e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 62.68 E-value: 8.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 616 TFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQlrSQLAIIPQEPFLFSG-TVREN----L 690
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR--RPVSMLFQENNLFSHlTVAQNiglgL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 691 DPqGL---HKDRALWQAL-KQCHLSEVITSMGGldgelgeggrSLSLGQRQLLCLARALLTDAKILCIDEATASVD---- 762
Cdd:PRK10771 97 NP-GLklnAAQREKLHAIaRQMGIEDLLARLPG----------QLSGGQRQRVALARCLVREQPILLLDEPFSALDpalr 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767940955 763 QKTDQLLQQtICKRfANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQ 818
Cdd:PRK10771 166 QEMLTLVSQ-VCQE-RQLTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELLSG 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
598-819 |
9.16e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.11 E-value: 9.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 598 QDVVLAYRPG--LPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLePS------SGRVLLDG---VDTSQLELA 666
Cdd:PRK15134 9 ENLSVAFRQQqtVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGeslLHASEQTLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 667 QLR-SQLAIIPQEPFLfsgtvreNLDPqgLHK-DRALWQAL-------KQCHLSEVI-----TSMGGLDGELGEGGRSLS 732
Cdd:PRK15134 88 GVRgNKIAMIFQEPMV-------SLNP--LHTlEKQLYEVLslhrgmrREAARGEILncldrVGIRQAAKRLTDYPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 733 LGQRQLLCLARALLTDAKILCIDEATASVDQKTD----QLLQQTicKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVV 807
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQaqilQLLREL--QQELNMGLLFITHNLSIVRKlADRVAVMQNGRCV 236
|
250
....*....|..
gi 767940955 808 ELDSPATLRNQP 819
Cdd:PRK15134 237 EQNRAATLFSAP 248
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
595-810 |
9.41e-11 |
|
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: 62.27 E-value: 9.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLE-----LAQLR 669
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPpkdrdIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 670 SQLAIIPQEpflfsgTVRENLD-PQGLHK------DRALWQALKQCHLSEVItsmggldgelGEGGRSLSLGQRQLLCLA 742
Cdd:cd03301 79 QNYALYPHM------TVYDNIAfGLKLRKvpkdeiDERVREVAELLQIEHLL----------DRKPKQLSGGQRQRVALG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767940955 743 RALLTDAKILCIDEATASVDQKTDQLLQQTICK--RFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELD 810
Cdd:cd03301 143 RAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHDQVEAMTmADRIAVMNDGQIQQIG 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
74-161 |
9.81e-11 |
|
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: 62.74 E-value: 9.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 74 TLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILGML--SYTTRLLCTHRTEYLER-ADAVLLMEAGR 150
Cdd:COG1122 134 ELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLE--LLKRLnkEGKTVIIVTHDLDLVAElADRVIVLDDGR 211
|
90
....*....|.
gi 767940955 151 LIRAGPPSEIL 161
Cdd:COG1122 212 IVADGTPREVF 222
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
74-160 |
1.13e-10 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 63.96 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 74 TLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHL------LHRcILGmlsyTTRLLCTH-RTEYLERADAVLLM 146
Cdd:COG3842 135 QLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMreelrrLQR-ELG----ITFIYVTHdQEEALALADRIAVM 209
|
90
....*....|....
gi 767940955 147 EAGRLIRAGPPSEI 160
Cdd:COG3842 210 NDGRIEQVGTPEEI 223
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
8-162 |
1.19e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.53 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 8 VRGLSKGFGLATQEPWIQFATIRDNI-LFGKTFDAQLYkEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALA 86
Cdd:PLN03130 1308 LMDLRKVLGIIPQAPVLFSGTVRFNLdPFNEHNDADLW-ESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLA 1386
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767940955 87 RAVYQEKELYLLDDPLAAVDADvANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEILP 162
Cdd:PLN03130 1387 RALLRRSKILVLDEATAAVDVR-TDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLS 1461
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
74-161 |
1.23e-10 |
|
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: 63.97 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 74 TLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILGMLSYTTR---LLCTHRTEYLER-ADAVLLMEAG 149
Cdd:COG4148 133 TLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILP--YLERLRDELDipiLYVSHSLDEVARlADHVVLLEQG 210
|
90
....*....|..
gi 767940955 150 RLIRAGPPSEIL 161
Cdd:COG4148 211 RVVASGPLAEVL 222
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
612-773 |
1.24e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.81 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 612 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTsqlELAQLRSQLAII----PQEPFLfsgTVR 687
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---DDPDVAEACHYLghrnAMKPAL---TVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 688 ENLdpqglhkdrALWQALKQCHLSEVITSMGGL--DGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKT 765
Cdd:PRK13539 92 ENL---------EFWAAFLGGEELDIAAALEAVglAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA 162
|
....*...
gi 767940955 766 DQLLQQTI 773
Cdd:PRK13539 163 VALFAELI 170
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
611-815 |
1.29e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.57 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 611 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLePS---SGRVLLDGvdtSQLELAQLR----SQLAIIPQEPFLFS 683
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEG---EELQASNIRdterAGIAIIHQELALVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 684 G-TVREN------LDPQGLHKDRALWQA----LKQCHLS-EVITSMggldgelgeggRSLSLGQRQLLCLARALLTDAKI 751
Cdd:PRK13549 96 ElSVLENiflgneITPGGIMDYDAMYLRaqklLAQLKLDiNPATPV-----------GNLGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767940955 752 LCIDEATASV-DQKTDQLLqqTICKRFANKTV--LTIAHRLNTILN-SDRVLVLQAGRVVELDSPATL 815
Cdd:PRK13549 165 LILDEPTASLtESETAVLL--DIIRDLKAHGIacIYISHKLNEVKAiSDTICVIRDGRHIGTRPAAGM 230
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
75-160 |
1.30e-10 |
|
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: 62.25 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHL------LHRcILGMlsytTRLLCTH-RTEYLERADAVLLME 147
Cdd:cd03300 131 LSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMqlelkrLQK-ELGI----TFVFVTHdQEEALTMSDRIAVMN 205
|
90
....*....|...
gi 767940955 148 AGRLIRAGPPSEI 160
Cdd:cd03300 206 KGKIQQIGTPEEI 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
611-815 |
1.30e-10 |
|
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: 64.82 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 611 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVL--FRLLEPSSGRVL---------------------------------L 655
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIyhvalcekcgyverpskvgepcpvcggtlepeeV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 656 DGVDTSQLELAQLRSQLAIIPQEPFLFSG--TVREN----LDPQGLHKDRALWQA---LKQCHLSEVITSMGgldgelge 726
Cdd:TIGR03269 95 DFWNLSDKLRRRIRKRIAIMLQRTFALYGddTVLDNvleaLEEIGYEGKEAVGRAvdlIEMVQLSHRITHIA-------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 727 ggRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICKRFANK--TVLTIAHRLNTILN-SDRVLVLQA 803
Cdd:TIGR03269 167 --RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEVIEDlSDKAIWLEN 244
|
250
....*....|..
gi 767940955 804 GRVVELDSPATL 815
Cdd:TIGR03269 245 GEIKEEGTPDEV 256
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
11-161 |
1.90e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 64.35 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 11 LSKGFGLATQEPWIQFATIRDNILFGKTFDAQLYKEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVY 90
Cdd:PRK10790 413 LRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLV 492
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767940955 91 QEKELYLLDDPLAAVDADvANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 161
Cdd:PRK10790 493 QTPQILILDEATANIDSG-TEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLL 562
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
28-161 |
1.96e-10 |
|
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: 61.97 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 28 TIRDNILFG----KTFDAQLYKEVLEacaLNDDLSILPAGDQtevgeKGVTLSGGQRARIALARAVYQEKELYLLDDPLA 103
Cdd:cd03299 87 TVYKNIAYGlkkrKVDKKEIERKVLE---IAEMLGIDHLLNR-----KPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767940955 104 AVDAdvanhLLHRCILGMLSY------TTRLLCTHR-TEYLERADAVLLMEAGRLIRAGPPSEIL 161
Cdd:cd03299 159 ALDV-----RTKEKLREELKKirkefgVTVLHVTHDfEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
75-160 |
2.48e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 63.18 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHL------LHRcilgMLSYTTrLLCTH-RTEYLERADAVLLME 147
Cdd:PRK10851 137 LSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELrrwlrqLHE----ELKFTS-VFVTHdQEEAMEVADRVVVMS 211
|
90
....*....|...
gi 767940955 148 AGRLIRAGPPSEI 160
Cdd:PRK10851 212 QGNIEQAGTPDQV 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
28-155 |
3.29e-10 |
|
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: 60.73 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 28 TIRDNILFG----KTFDAQLYKEVLEACALnddLSIlpagdQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLA 103
Cdd:cd03301 88 TVYDNIAFGlklrKVPKDEIDERVREVAEL---LQI-----EHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 767940955 104 AVDADVANHL------LHRcilgMLSYTTrLLCTH-RTEYLERADAVLLMEAGRLIRAG 155
Cdd:cd03301 160 NLDAKLRVQMraelkrLQQ----RLGTTT-IYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
611-814 |
3.33e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 61.25 E-value: 3.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 611 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAqlrsqLAIIPQepflFSGtvREN- 689
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALLELG-----AGFHPE----LTG--RENi 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 690 ------LdpqGLHKD--RALwqalkqchLSEVI----------TSMggldgelgeggRSLSLGQRQLLCLARALLTDAKI 751
Cdd:COG1134 110 ylngrlL---GLSRKeiDEK--------FDEIVefaelgdfidQPV-----------KTYSSGMRARLAFAVATAVDPDI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767940955 752 LCIDEATASVD----QKTDQLLQQticKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPAT 814
Cdd:COG1134 168 LLVDEVLAVGDaafqKKCLARIRE---LRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEE 232
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
595-813 |
3.92e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 61.67 E-value: 3.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGLP---NALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLL-DGVDTS---QLELAQ 667
Cdd:PRK13643 2 IKFEKVNYTYQPNSPfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgDIVVSStskQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 668 LRSQLAIIPQEP--FLFSGTVRENL--DPQ--GLHKDRALWQAlkqchlSEVITSMGGLDGELGEGGRSLSLGQRQLLCL 741
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVafGPQnfGIPKEKAEKIA------AEKLEMVGLADEFWEKSPFELSGGQMRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767940955 742 ARALLTDAKILCIDEATASVDQKTD-QLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPA 813
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARiEMMQLFESIHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPS 229
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
612-810 |
4.06e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 63.16 E-value: 4.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 612 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGvdtsqlelaQLRsqLAIIPQEPFLFSG-TVRENL 690
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK---------GLR--IGYLPQEPPLDDDlTVLDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 691 dpqgLHKDRALWQALKQchLSEVITSMGGLDGELGEGGR------------------------------------SLSLG 734
Cdd:COG0488 83 ----LDGDAELRALEAE--LEELEAKLAEPDEDLERLAElqeefealggweaearaeeilsglgfpeedldrpvsELSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767940955 735 QRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTIcKRFANkTVLTIAHrlntilnsDRVLvLQ--AGRVVELD 810
Cdd:COG0488 157 WRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL-KNYPG-TVLVVSH--------DRYF-LDrvATRILELD 223
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
28-160 |
4.14e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 62.66 E-value: 4.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 28 TIRDNILFG----KTFDAQLYKEVLEACALN--DDLSilpagdqtevGEKGVTLSGGQRARIALARAVYQEKELYLLDDP 101
Cdd:PRK09452 102 TVFENVAFGlrmqKTPAAEITPRVMEALRMVqlEEFA----------QRKPHQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767940955 102 LAAVDA----DVANHL--LHRcILGMlsytTRLLCTH-RTEYLERADAVLLMEAGRLIRAGPPSEI 160
Cdd:PRK09452 172 LSALDYklrkQMQNELkaLQR-KLGI----TFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
602-819 |
4.44e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 61.14 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 602 LAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG---------------VDTSQLELa 666
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgqlkvADKNQLRL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 667 qLRSQLAIIPQEPFLFSG-TVREN-----LDPQGLHKDRALWQALKqcHLSEV-ITSMGGLDGELgeggrSLSLGQRQLL 739
Cdd:PRK10619 90 -LRTRLTMVFQHFNLWSHmTVLENvmeapIQVLGLSKQEARERAVK--YLAKVgIDERAQGKYPV-----HLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 740 CLARALLTDAKILCIDEATASVDQK-TDQLLQqtICKRFAN--KTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATL 815
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPElVGEVLR--IMQQLAEegKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQL 239
|
....
gi 767940955 816 RNQP 819
Cdd:PRK10619 240 FGNP 243
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
595-807 |
4.57e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 61.64 E-value: 4.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGLP---NALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRV---LLDGVDTSQLELA-- 666
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEKek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 667 -------------------QLRSQLAIIPQ--EPFLFSGTVRENL--DPQ--GLHKDRALWQALKQCHLSEVITSMggld 721
Cdd:PRK13651 83 vleklviqktrfkkikkikEIRRRVGVVFQfaEYQLFEQTIEKDIifGPVsmGVSKEEAKKRAAKYIELVGLDESY---- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 722 gelgeGGRS---LSLGQRQLLCLARALLTDAKILCIDEATASVD-QKTDQLLQqtICKRF--ANKTVLTIAHRLNTILN- 794
Cdd:PRK13651 159 -----LQRSpfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVKEILE--IFDNLnkQGKTIILVTHDLDNVLEw 231
|
250
....*....|...
gi 767940955 795 SDRVLVLQAGRVV 807
Cdd:PRK13651 232 TKRTIFFKDGKII 244
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
607-808 |
4.86e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 62.05 E-value: 4.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 607 GLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPS---SGRVLLDG---VDTSQLELAQLRS-QLAIIPQEP 679
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGreiLNLPEKELNKLRAeQISMIFQDP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 680 FlfsgtvrENLDP---------------QGLHKDRALWQALKQchLSEVitSMGGLDGELGEGGRSLSLGQRQLLCLARA 744
Cdd:PRK09473 107 M-------TSLNPymrvgeqlmevlmlhKGMSKAEAFEESVRM--LDAV--KMPEARKRMKMYPHEFSGGMRQRVMIAMA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 745 LLTDAKILCIDEATASVDQkTDQ-----LLQQTicKRFANKTVLTIAHRLNTILNS-DRVLVLQAGRVVE 808
Cdd:PRK09473 176 LLCRPKLLIADEPTTALDV-TVQaqimtLLNEL--KREFNTAIIMITHDLGVVAGIcDKVLVMYAGRTME 242
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
612-819 |
5.52e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 61.27 E-value: 5.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 612 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSG-----RVLLDGVDT-SQLELAQLRSQLAIIPQEPFLFSGT 685
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfNYRDVLEFRRRVGMLFQRPNPFPMS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 686 VREN-LDPQGLHK--DRALWQALKQCHLSEVITSMGGLDGELGEGGRsLSLGQRQLLCLARALLTDAKILCIDEATASVD 762
Cdd:PRK14271 117 IMDNvLAGVRAHKlvPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFR-LSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767940955 763 QKTDQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQP 819
Cdd:PRK14271 196 PTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSSP 253
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
74-161 |
6.46e-10 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 60.49 E-value: 6.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 74 TLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILGMLS--YTTRLLCTHRTEYLER-ADAVLLMeAGR 150
Cdd:COG1121 139 ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYE--LLRELRreGKTILVVTHDLGAVREyFDRVLLL-NRG 215
|
90
....*....|.
gi 767940955 151 LIRAGPPSEIL 161
Cdd:COG1121 216 LVAHGPPEEVL 226
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
612-819 |
7.00e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 60.45 E-value: 7.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 612 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLE------PSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSG- 684
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPHl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 685 TVREN----LDPQGLHKDRALWQALKQChLSEViTSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATAS 760
Cdd:PRK14246 106 SIYDNiaypLKSHGIKEKREIKKIVEEC-LRKV-GLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 761 VDQKTDQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQP 819
Cdd:PRK14246 184 IDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTSP 243
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
611-819 |
7.23e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 60.39 E-value: 7.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 611 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLElAQLRSQLAIIP--QEPFLF-SGTVR 687
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLP-GHQIARMGVVRtfQHVRLFrEMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 688 ENL-DPQ----------GLHK------------DRAL-WqaLKQCHLSEVITSmggldgelgeGGRSLSLGQRQLLCLAR 743
Cdd:PRK11300 99 ENLlVAQhqqlktglfsGLLKtpafrraesealDRAAtW--LERVGLLEHANR----------QAGNLAYGQQRRLEIAR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767940955 744 ALLTDAKILCIDEATASVDQKTDQLLQQTI--CKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQP 819
Cdd:PRK11300 167 CMVTQPEILMLDEPAAGLNPKETKELDELIaeLRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
74-186 |
9.31e-10 |
|
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: 61.84 E-value: 9.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 74 TLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILGML---SYTTRLLCTHRTEY-LERADAVLLMEAG 149
Cdd:COG1123 142 QLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILD--LLRELqreRGTTVLLITHDLGVvAEIADRVVVMDDG 219
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 767940955 150 RLIRAGPPSEILPLVQ---AVPKAWAENGQESDSATAQSV 186
Cdd:COG1123 220 RIVEDGPPEEILAAPQalaAVPRLGAARGRAAPAAAAAEP 259
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
562-816 |
1.07e-09 |
|
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: 61.74 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 562 VSVERLEEYTCDLPQEPQGQPLQLGTGWLTQ-GGVEFQDVVLAYrpglPNALDGVTFCV-------QPGEKLGIVGRTGS 633
Cdd:COG4615 294 VALRKIEELELALAAAEPAAADAAAPPAPADfQTLELRGVTYRY----PGEDGDEGFTLgpidltiRRGELVFIVGGNGS 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 634 GKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFsgtvRENLDPQGLHKDRALWQALKQCHLSEV 713
Cdd:COG4615 370 GKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF----DRLLGLDGEADPARARELLERLELDHK 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 714 ITsmgglDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATAsvDQktD---------QLLQQTicKRfANKTVLT 784
Cdd:COG4615 446 VS-----VEDGRFSTTDLSQGQRKRLALLVALLEDRPILVFDEWAA--DQ--DpefrrvfytELLPEL--KA-RGKTVIA 513
|
250 260 270
....*....|....*....|....*....|....*..
gi 767940955 785 IAH-----RLntilnSDRVLVLQAGRVVELDSPATLR 816
Cdd:COG4615 514 ISHddryfDL-----ADRVLKMDYGKLVELTGPAALA 545
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
595-815 |
1.51e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 60.20 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQlELAQLRSQLAI 674
Cdd:PRK13537 8 IDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 675 IPQ----EPFLfsgTVRENLDPQGlhkdRALWQALKQCH-LSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDA 749
Cdd:PRK13537 85 VPQfdnlDPDF---TVRENLLVFG----RYFGLSAAAARaLVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767940955 750 KILCIDEATASVDQKTDQLLQQTICKRFAN-KTVLTIAH------RLntilnSDRVLVLQAGRVVELDSPATL 815
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLARgKTILLTTHfmeeaeRL-----CDRLCVIEEGRKIAEGAPHAL 225
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
9-103 |
1.76e-09 |
|
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: 57.27 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 9 RGLSKGFGLATQEPWIQ-FATIRDNILFG--------KTFDAQLYkEVLEACALNDDLSilpagdqTEVGEKGVTLSGGQ 79
Cdd:pfam00005 55 KSLRKEIGYVFQDPQLFpRLTVRENLRLGlllkglskREKDARAE-EALEKLGLGDLAD-------RPVGERPGTLSGGQ 126
|
90 100
....*....|....*....|....
gi 767940955 80 RARIALARAVYQEKELYLLDDPLA 103
Cdd:pfam00005 127 RQRVAIARALLTKPKLLLLDEPTA 150
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
28-160 |
2.08e-09 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 60.09 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 28 TIRDNILFG----KTFDAQLYKEVLEACALnddLSI------LPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYL 97
Cdd:COG3839 91 TVYENIAFPlklrKVPKAEIDRRVREAAEL---LGLedlldrKPK-----------QLSGGQRQRVALGRALVREPKVFL 156
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 98 LDDPLAAVDADVANHL------LHRcilgMLSYTTrLLCTH-RTEYLERADAVLLMEAGRLIRAGPPSEI 160
Cdd:COG3839 157 LDEPLSNLDAKLRVEMraeikrLHR----RLGTTT-IYVTHdQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
595-812 |
2.34e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 59.32 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGlPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG--VDTSQLELAQLRSQL 672
Cdd:PRK13639 2 LETRDLKYSYPDG-TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 673 AIIPQEP--FLFSGTVRE-------NLdpqGLHKD---RALWQALKQCHLSevitsmggldGELGEGGRSLSLGQRQLLC 740
Cdd:PRK13639 81 GIVFQNPddQLFAPTVEEdvafgplNL---GLSKEeveKRVKEALKAVGME----------GFENKPPHHLSGGQKKRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 741 LARALLTDAKILCIDEATASVD----QKTDQLLQQTickrfaNKTVLTI---AHRLNTI-LNSDRVLVLQAGRVVELDSP 812
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDpmgaSQIMKLLYDL------NKEGITIiisTHDVDLVpVYADKVYVMSDGKIIKEGTP 221
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
602-812 |
2.35e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.78 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 602 LAYRPGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQL---------RSQL 672
Cdd:PRK11701 12 LTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 673 AIIPQEP-------FLFSGTVRENLDPQGL-H----KDRAL-WqalkqchLSEVitsmGGLDGELGEGGRSLSLGQRQLL 739
Cdd:PRK11701 92 GFVHQHPrdglrmqVSAGGNIGERLMAVGArHygdiRATAGdW-------LERV----EIDAARIDDLPTTFSGGMQQRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 740 CLARALLTDAKILCIDEATA----SVDQKTDQLLQQTIckRFANKTVLTIAHRLNTI-LNSDRVLVLQAGRVVE------ 808
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGgldvSVQARLLDLLRGLV--RELGLAVVIVTHDLAVArLLAHRLLVMKQGRVVEsgltdq 238
|
....*
gi 767940955 809 -LDSP 812
Cdd:PRK11701 239 vLDDP 243
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
612-771 |
2.36e-09 |
|
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: 57.89 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 612 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENLD 691
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 692 -PQGLHKDRALWQALKQCHLSEVitsmggldgeLGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQ 770
Cdd:cd03231 96 fWHADHSDEQVEEALARVGLNGF----------EDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFA 165
|
.
gi 767940955 771 Q 771
Cdd:cd03231 166 E 166
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
28-161 |
2.52e-09 |
|
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: 58.72 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 28 TIRDNILFgktFdAQLYKEVLEACALNDDlSILPAGDQTEVGEKGV-TLSGGQRARIALARAVYQEKELYLLDDPLAAVD 106
Cdd:COG4555 90 TVRENIRY---F-AELYGLFDEELKKRIE-ELIELLGLEEFLDRRVgELSTGMKKKVALARALVHDPKVLLLDEPTNGLD 164
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 767940955 107 ADvANHLLHRCILGMLSY-TTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 161
Cdd:COG4555 165 VM-ARRLLREILRALKKEgKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELR 220
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
11-160 |
2.53e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 59.48 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 11 LSKGFGLATQEPWIQF--ATIRDNILFG-------KTFDAQLYKEVLEACALNDD-LSILPAGdqtevgekgvtLSGGQR 80
Cdd:PRK13631 114 LRRRVSMVFQFPEYQLfkDTIEKDIMFGpvalgvkKSEAKKLAKFYLNKMGLDDSyLERSPFG-----------LSGGQK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 81 ARIALARAVYQEKELYLLDDPLAAVDADvANHLLHRCIL-GMLSYTTRLLCTHRTEY-LERADAVLLMEAGRLIRAGPPS 158
Cdd:PRK13631 183 RRVAIAGILAIQPEILIFDEPTAGLDPK-GEHEMMQLILdAKANNKTVFVITHTMEHvLEVADEVIVMDKGKILKTGTPY 261
|
..
gi 767940955 159 EI 160
Cdd:PRK13631 262 EI 263
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
611-811 |
3.67e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 60.25 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 611 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG----------VDTSQLELAQLR----SQLAIIP 676
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRhvrgADMAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 677 QEP-------FLFSGTVRENLD-PQGLHKDRALWQA---LKQCHLSEVITSMggldgelGEGGRSLSLGQRQLLCLARAL 745
Cdd:PRK10261 111 QEPmtslnpvFTVGEQIAESIRlHQGASREEAMVEAkrmLDQVRIPEAQTIL-------SRYPHQLSGGMRQRVMIAMAL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767940955 746 LTDAKILCIDEATASVDQKTD-QLLQQ-TICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDS 811
Cdd:PRK10261 184 SCRPAVLIADEPTTALDVTIQaQILQLiKVLQKEMSMGVIFITHDMGVVAEiADRVLVMYQGEAVETGS 252
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
611-811 |
4.04e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 58.25 E-value: 4.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 611 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLE--PS---SGRVLLDGVD--TSQLELAQLRSQLAIIPQEPFLFS 683
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNiySPRTDTVDLRKEIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 684 GTVREN----LDPQGLHK----DRALWQALKQCHL-SEVITSMGGLDGelgeggrSLSLGQRQLLCLARALLTDAKILCI 754
Cdd:PRK14239 100 MSIYENvvygLRLKGIKDkqvlDEAVEKSLKGASIwDEVKDRLHDSAL-------GLSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767940955 755 DEATASVDQKTDQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDS 811
Cdd:PRK14239 173 DEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYND 230
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
8-153 |
4.32e-09 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 58.18 E-value: 4.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 8 VRGLSKGFGLATQE----PWiqfATIRDNILFG-------KTFDAQLYKEVLEACALNDDLSILPAgdqtevgekgvTLS 76
Cdd:COG1116 75 VTGPGPDRGVVFQEpallPW---LTVLDNVALGlelrgvpKAERRERARELLELVGLAGFEDAYPH-----------QLS 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 77 GGQRARIALARAVYQEKELYLLDDPLAAVDADVANHlLHRCILGMLSYT--TRLLCTHRTE---YLerADAVLLMEA--G 149
Cdd:COG1116 141 GGMRQRVAIARALANDPEVLLMDEPFGALDALTRER-LQDELLRLWQETgkTVLFVTHDVDeavFL--ADRVVVLSArpG 217
|
....
gi 767940955 150 RLIR 153
Cdd:COG1116 218 RIVE 221
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
74-161 |
4.83e-09 |
|
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: 57.75 E-value: 4.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 74 TLSGGQRARIALARAVYQEKELYLLDDPLAAVDadvANHLLHrcILGMLSYTTR------LLCTH------RTeylerAD 141
Cdd:COG1120 137 ELSGGERQRVLIARALAQEPPLLLLDEPTSHLD---LAHQLE--VLELLRRLARergrtvVMVLHdlnlaaRY-----AD 206
|
90 100
....*....|....*....|
gi 767940955 142 AVLLMEAGRLIRAGPPSEIL 161
Cdd:COG1120 207 RLVLLKDGRIVAQGPPEEVL 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
557-809 |
4.96e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.87 E-value: 4.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 557 TEAMLVSVERLEEYT-CDLPQ--------EPQGQPLQLGTGWLTQGG--VEFQDVVLAY--RPGLPN-------ALDGVT 616
Cdd:PRK10261 265 TRALLAAVPQLGAMKgLDYPRrfplisleHPAKQEPPIEQDTVVDGEpiLQVRNLVTRFplRSGLLNrvtrevhAVEKVS 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 617 FCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG--VDT-SQLELAQLRSQLAIIPQEPFlfsgtvrENLDP- 692
Cdd:PRK10261 345 FDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqrIDTlSPGKLQALRRDIQFIFQDPY-------ASLDPr 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 693 --------QGLHKDRALWQALKQCHLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVD-- 762
Cdd:PRK10261 418 qtvgdsimEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDvs 497
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 767940955 763 ---QKTDQLLQqtiCKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVEL 809
Cdd:PRK10261 498 irgQIINLLLD---LQRDFGIAYLFISHDMAVVERiSHRVAVMYLGQIVEI 545
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
75-150 |
5.33e-09 |
|
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: 56.43 E-value: 5.33e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHL--LHRCILGMLSYTTrLLCTHRTEYLER-ADAVLLMEAGR 150
Cdd:cd03229 101 LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVraLLKSLQAQLGITV-VLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
73-151 |
8.17e-09 |
|
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: 55.87 E-value: 8.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 73 VTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILGMLS--YTTRLLCTHRTEYLER-ADAVLLMEAG 149
Cdd:cd03230 94 LKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWE--LLRELKkeGKTILLSSHILEEAERlCDRVAILNNG 171
|
..
gi 767940955 150 RL 151
Cdd:cd03230 172 RI 173
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
595-819 |
9.51e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 57.51 E-value: 9.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAI 674
Cdd:PRK13652 4 IETRDLCYSYS-GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 675 IPQEP--FLFSGTVRENL--DPQGLHKDRA-----LWQALKQCHLSEVITSMggldgelgegGRSLSLGQRQLLCLARAL 745
Cdd:PRK13652 83 VFQNPddQIFSPTVEQDIafGPINLGLDEEtvahrVSSALHMLGLEELRDRV----------PHHLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 746 LTDAKILCIDEATASVD-QKTDQLLqqtickRFANK-------TVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLR 816
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDpQGVKELI------DFLNDlpetygmTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIF 226
|
...
gi 767940955 817 NQP 819
Cdd:PRK13652 227 LQP 229
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
74-155 |
9.87e-09 |
|
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: 55.52 E-value: 9.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 74 TLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILGMLSY---TTRLLCTHrteYLERA----DAVLLM 146
Cdd:cd03214 97 ELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLE--LLRRLARergKTVVMVLH---DLNLAaryaDRVILL 171
|
....*....
gi 767940955 147 EAGRLIRAG 155
Cdd:cd03214 172 KDGRIVAQG 180
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
75-155 |
9.93e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 56.95 E-value: 9.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILGMLSYT--TRLLCTHRTEYLER-ADAVLLMEAGRL 151
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVS--IIRELAETgiTQVIVTHEVEVARKtASRVVYMENGHI 219
|
....
gi 767940955 152 IRAG 155
Cdd:PRK11124 220 VEQG 223
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
605-807 |
1.02e-08 |
|
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: 56.12 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 605 RPGLPNA--LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPS---SGRVLLDGVDtSQLELAQLRSQLAIIPQEP 679
Cdd:cd03233 14 GKGRSKIpiLKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIP-YKEFAEKYPGEIIYVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 680 FLFSG-TVRENLDpqglhkdralwQALKqCHLSEVItsmggldgelgeggRSLSLGQRQLLCLARALLTDAKILCIDEAT 758
Cdd:cd03233 93 VHFPTlTVRETLD-----------FALR-CKGNEFV--------------RGISGGERKRVSIAEALVSRASVLCWDNST 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767940955 759 ASVDQKTD-QLLQ--QTICKRFANKTVLTIAHRLNTILNS-DRVLVLQAGRVV 807
Cdd:cd03233 147 RGLDSSTAlEILKciRTMADVLKTTTFVSLYQASDEIYDLfDKVLVLYEGRQI 199
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
612-762 |
1.19e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 56.44 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 612 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLEL-AQLRSQLAIIPQEPFLFSG------ 684
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRRlsvydn 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 685 -----TVRENLDPQGlHKDRALwQALKQCHLSEVITSMggldgelgegGRSLSLGQRQLLCLARALLTDAKILCIDEATA 759
Cdd:PRK10895 99 lmavlQIRDDLSAEQ-REDRAN-ELMEEFHIEHLRDSM----------GQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
...
gi 767940955 760 SVD 762
Cdd:PRK10895 167 GVD 169
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
46-170 |
1.29e-08 |
|
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: 58.38 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 46 EVLEACALNDD-LSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVD----ADVANHLLH-RCIL 119
Cdd:COG1123 386 ELLERVGLPPDlADRYPH-----------ELSGGQRQRVAIARALALEPKLLILDEPTSALDvsvqAQILNLLRDlQREL 454
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767940955 120 GmLSYttrLLCTH---RTEYLerADAVLLMEAGRLIRAGPPSEIL--P-------LVQAVPKA 170
Cdd:COG1123 455 G-LTY---LFISHdlaVVRYI--ADRVAVMYDGRIVEDGPTEEVFanPqhpytraLLAAVPSL 511
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
74-155 |
1.58e-08 |
|
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: 55.62 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 74 TLSGGQRARIALARAVYQEKELYLLDDPLAAVD----ADVANHLLHRCILGMlsytTRLLCTH-RTEYLERADAVLLMeA 148
Cdd:cd03235 132 ELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDpktqEDIYELLRELRREGM----TILVVTHdLGLVLEYFDRVLLL-N 206
|
....*..
gi 767940955 149 GRLIRAG 155
Cdd:cd03235 207 RTVVASG 213
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
612-819 |
1.70e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 58.20 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 612 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLRSQ-LAIIPQEPFLFSG-TV 686
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadALAQLRREhFGFIFQRYHLLSHlTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 687 RENLD-PQ---GLHKDRALWQA---LKQCHLSEVItsmggldgelGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATA 759
Cdd:PRK10535 104 AQNVEvPAvyaGLERKQRLLRAqelLQRLGLEDRV----------EYQPSQLSGGQQQRVSIARALMNGGQVILADEPTG 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767940955 760 SVDQKTdqllqqtickrfaNKTVLTIAHRLN------TILNSDRVLVLQAGRVVELDSPATLRNQP 819
Cdd:PRK10535 174 ALDSHS-------------GEEVMAILHQLRdrghtvIIVTHDPQVAAQAERVIEIRDGEIVRNPP 226
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
22-151 |
2.01e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 56.22 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 22 PWiqfATIRDNI---LFGKTFDAQLykEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLL 98
Cdd:PRK11247 94 PW---KKVIDNVglgLKGQWRDAAL--QALAAVGLADRANEWPA-----------ALSGGQKQRVALARALIHRPGLLLL 157
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767940955 99 DDPLAAVDAdvanhlLHRCILGMLSYT-------TRLLCTHR-TEYLERADAVLLMEAGRL 151
Cdd:PRK11247 158 DEPLGALDA------LTRIEMQDLIESlwqqhgfTVLLVTHDvSEAVAMADRVLLIEEGKI 212
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
595-819 |
2.07e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 55.87 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG--VDTSQLELAQLRSQL 672
Cdd:PRK09493 2 IEFKNVSKHF--GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkVNDPKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 673 AIIPQEPFLFSG-TVREN-----LDPQGLHKDRALWQA---LKQCHLSEvitsmggldgELGEGGRSLSLGQRQLLCLAR 743
Cdd:PRK09493 80 GMVFQQFYLFPHlTALENvmfgpLRVRGASKEEAEKQArelLAKVGLAE----------RAHHYPSELSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 744 ALLTDAKILCIDEATASVDQktdQLLQQ--TICKRFANK--TVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQ 818
Cdd:PRK09493 150 ALAVKPKLMLFDEPTSALDP---ELRHEvlKVMQDLAEEgmTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIKN 226
|
.
gi 767940955 819 P 819
Cdd:PRK09493 227 P 227
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
562-808 |
2.38e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.06 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 562 VSVERLEEYTcdLPQE---PQGQPLQLGTGWLTQGGVEFQDVVLAYRPGLPNaldgVTFCVQPGEKLGIVGRTGSGKSSL 638
Cdd:PLN03232 586 VSLQRIEELL--LSEErilAQNPPLQPGAPAISIKNGYFSWDSKTSKPTLSD----INLEIPVGSLVAIVGGTGEGKTSL 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 639 LLVLFRLLEPSSgrvlldgvDTSqlelAQLRSQLAIIPQEPFLFSGTVRENLDPQGLHKDRALWQALKQCHLSEVItSMG 718
Cdd:PLN03232 660 ISAMLGELSHAE--------TSS----VVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDL-DLL 726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 719 GLDGELGEGGR--SLSLGQRQLLCLARALLTDAKILCIDEATASVDQK-TDQLLQQTICKRFANKTVLTIAHRLNTILNS 795
Cdd:PLN03232 727 PGRDLTEIGERgvNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM 806
|
250
....*....|...
gi 767940955 796 DRVLVLQAGRVVE 808
Cdd:PLN03232 807 DRIILVSEGMIKE 819
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
611-812 |
2.39e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 56.88 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 611 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLElAQLRsQLAIIPQEPFLFSG-TVREN 689
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP-AENR-HVNTVFQSYALFPHmTVFEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 690 ----LDPQGLHKD----RALwQALKQCHLSEVITSmggldgelgeGGRSLSLGQRQLLCLARALLTDAKILCIDEATASV 761
Cdd:PRK09452 107 vafgLRMQKTPAAeitpRVM-EALRMVQLEEFAQR----------KPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSAL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767940955 762 DQKTDQLLQQTIcKRFANKTVLT---IAHRLNTILN-SDRVLVLQAGRVVELDSP 812
Cdd:PRK09452 176 DYKLRKQMQNEL-KALQRKLGITfvfVTHDQEEALTmSDRIVVMRDGRIEQDGTP 229
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
20-161 |
2.69e-08 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 55.69 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 20 QEPWIQFATIRDNI-LFGKTFDAQLYkEVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLL 98
Cdd:cd03288 102 QDPILFSGSIRFNLdPECKCTDDRLW-EALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIM 180
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767940955 99 DDPLAAVDADVANhLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 161
Cdd:cd03288 181 DEATASIDMATEN-ILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLL 242
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
612-765 |
2.71e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 55.59 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 612 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLEL---AQLRSQ-LAIIPQEPFLFSG-TV 686
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakAELRNQkLGFIYQFHHLLPDfTA 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767940955 687 RENLDPQGLHKDRALWQALKQCHlsEVITSMGGLDGELGEGGRsLSLGQRQLLCLARALLTDAKILCIDEATASVDQKT 765
Cdd:PRK11629 105 LENVAMPLLIGKKKPAEINSRAL--EMLAAVGLEHRANHRPSE-LSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
28-160 |
2.84e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 56.77 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 28 TIRDNILFGKTFDAQLYKEVleACALNDDLSILPAgdQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDA 107
Cdd:PRK11607 107 TVEQNIAFGLKQDKLPKAEI--ASRVNEMLGLVHM--QEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDK 182
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 767940955 108 DVANHLLHRC--ILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEI 160
Cdd:PRK11607 183 KLRDRMQLEVvdILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
595-812 |
2.88e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 56.18 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRPGLP---NALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLL-DGV---DTSQLELAQ 667
Cdd:PRK13634 3 ITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgERVitaGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 668 LRSQLAIIPQ--EPFLFSGTVRENL--DPQ--GLHKDRALWQA---LKQCHLSEVITSmggldgelgeggRS---LSLGQ 735
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDIcfGPMnfGVSEEDAKQKAremIELVGLPEELLA------------RSpfeLSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 736 RQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQTICK--RFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSP 812
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKlhKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTP 230
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
74-155 |
2.91e-08 |
|
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: 54.81 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 74 TLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLhRCILGMLSYT--TRLLCTHRTEYLER-ADAVLLMEAGR 150
Cdd:cd03298 128 ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML-DLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGR 206
|
....*
gi 767940955 151 LIRAG 155
Cdd:cd03298 207 IAAQG 211
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
611-815 |
3.39e-08 |
|
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: 56.76 E-value: 3.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 611 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSS--GRVLLDGvdtSQLELAQLRSQ----LAIIPQEPFLFSG 684
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSG---SPLKASNIRDTeragIVIIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 685 -TVRENL-------DPQGLHKDRALwqaLKQCHlsEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDE 756
Cdd:TIGR02633 93 lSVAENIflgneitLPGGRMAYNAM---YLRAK--NLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767940955 757 ATASVDQKTDQLLQQTIcKRFANKTV--LTIAHRLNTILN-SDRVLVLQAGRVVELDSPATL 815
Cdd:TIGR02633 168 PSSSLTEKETEILLDII-RDLKAHGVacVYISHKLNEVKAvCDTICVIRDGQHVATKDMSTM 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
75-161 |
3.50e-08 |
|
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: 55.19 E-value: 3.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILGML---SYTTRLLCTHRTEYLER-ADAVLLMEAGR 150
Cdd:COG1124 139 LSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILN--LLKDLreeRGLTYLFVSHDLAVVAHlCDRVAVMQNGR 216
|
90
....*....|.
gi 767940955 151 LIRAGPPSEIL 161
Cdd:COG1124 217 IVEELTVADLL 227
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
612-813 |
3.52e-08 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 54.80 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 612 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEP---SSGRVLLDGVDTSQLElAQLRsQLAIIPQEPFLFSG-TVR 687
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALP-AEQR-RIGILFQDDLLFPHlSVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 688 ENL------DPQGLHKDRALWQALKQCHLSEVITSMGGldgelgeggrSLSLGQRQLLCLARALLTDAKILCIDEATASV 761
Cdd:COG4136 95 ENLafalppTIGRAQRRARVEQALEEAGLAGFADRDPA----------TLSGGQRARVALLRALLAEPRALLLDEPFSKL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767940955 762 DQK-TDQLLQQtickrfanktVLTIAHRLN--TILNS-DRVLVLQAGRVVELDSPA 813
Cdd:COG4136 165 DAAlRAQFREF----------VFEQIRQRGipALLVThDEEDAPAAGRVLDLGNWQ 210
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
74-160 |
3.70e-08 |
|
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: 55.27 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 74 TLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVAN---HLLHRciLGMLSYTTRLLCTHRTEY-LERADAVLLMEAG 149
Cdd:cd03256 144 QLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRqvmDLLKR--INREEGITVIVSLHQVDLaREYADRIVGLKDG 221
|
90
....*....|.
gi 767940955 150 RLIRAGPPSEI 160
Cdd:cd03256 222 RIVFDGPPAEL 232
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
24-151 |
3.97e-08 |
|
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: 54.80 E-value: 3.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 24 IQFATIRDNILFGKTF-------DAQLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELY 96
Cdd:cd03255 94 LPDLTALENVELPLLLagvpkkeRRERAEELLERVGLGDRLNHYPS-----------ELSGGQQQRVAIARALANDPKII 162
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767940955 97 LLDDPLAAVDADVAnhllhRCILGML------SYTTRLLCTHRTEYLERADAVLLMEAGRL 151
Cdd:cd03255 163 LADEPTGNLDSETG-----KEVMELLrelnkeAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
612-812 |
4.46e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 55.40 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 612 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG--VDTSQLELAQLRSQLAIIPQEPflfsgtvren 689
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQDP---------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 690 lDPQGLHKD---------RALWQALKQC--HLSEVITsMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEAT 758
Cdd:PRK13638 87 -EQQIFYTDidsdiafslRNLGVPEAEItrRVDEALT-LVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767940955 759 ASVDQK-TDQLLqqTICKRFANK--TVLTIAHRLNTILN-SDRVLVLQAGRVVELDSP 812
Cdd:PRK13638 165 AGLDPAgRTQMI--AIIRRIVAQgnHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAP 220
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-150 |
4.98e-08 |
|
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: 54.40 E-value: 4.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 8 VRGLSKGFGLATQEPWIQF--ATIRDNILFG-------KTFDAQLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGG 78
Cdd:cd03225 70 LKELRRKVGLVFQNPDDQFfgPTVEEEVAFGlenlglpEEEIEERVEEALELVGLEGLRDRSPF-----------TLSGG 138
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767940955 79 QRARIALARAVYQEKELYLLDDPLAAVD----ADVANHLLHRCILGMlsytTRLLCTHRTEYLER-ADAVLLMEAGR 150
Cdd:cd03225 139 QKQRVAIAGVLAMDPDILLLDEPTAGLDpagrRELLELLKKLKAEGK----TIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
610-818 |
4.98e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 55.48 E-value: 4.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 610 NALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQL---------RSQL-------- 672
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFArrigvvfgqRSQLwwdlpaid 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 673 ------AI--IPQEPFlfsgtvRENLDpqglhkdrALWQALkqcHLSEVITSMggldgelgegGRSLSLGQRQLLCLARA 744
Cdd:COG4586 116 sfrllkAIyrIPDAEY------KKRLD--------ELVELL---DLGELLDTP----------VRQLSLGQRMRCELAAA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767940955 745 LLTDAKILCIDEATASVD----QKTDQLLQQtICKRFaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQ 818
Cdd:COG4586 169 LLHRPKILFLDEPTIGLDvvskEAIREFLKE-YNRER-GTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
610-808 |
5.09e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.40 E-value: 5.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 610 NALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQL---ELAQLRSQLAIIPQEPFLFSGTV 686
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARAKLRAKHVGFVFQSFMLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 687 --RENLDPQGL--------HKDRALwQALKQCHLSEVITSMGGldgelgeggrSLSLGQRQLLCLARALLTDAKILCIDE 756
Cdd:PRK10584 104 naLENVELPALlrgessrqSRNGAK-ALLEQLGLGKRLDHLPA----------QLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767940955 757 ATASVDQKT-DQL--LQQTICKRFANkTVLTIAHRLNTILNSDRVLVLQAGRVVE 808
Cdd:PRK10584 173 PTGNLDRQTgDKIadLLFSLNREHGT-TLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
612-820 |
5.18e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 55.04 E-value: 5.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 612 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSS-----GRVLLDG--VDTSQLELAQLRSQLAIIPQEPFLFSG 684
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNqnIYERRVNLNRLRRQVSMVHPKPNLFPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 685 TVRENL---------DPQgLHKDRALWQALKQCHLSEVITSMGGLDGElgeggrSLSLGQRQLLCLARALLTDAKILCID 755
Cdd:PRK14258 103 SVYDNVaygvkivgwRPK-LEIDDIVESALKDADLWDEIKHKIHKSAL------DLSGGQQQRLCIARALAVKPKVLLMD 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767940955 756 EATASVD----QKTDQLLQQTICKrfANKTVLTIAHRLNTILN-SDRVLVLQA-----GRVVELDSPATLRNQPH 820
Cdd:PRK14258 176 EPCFGLDpiasMKVESLIQSLRLR--SELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLVEFGLTKKIFNSPH 248
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
287-394 |
5.79e-08 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 55.24 E-value: 5.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 287 LLLFSPGNLYIPVFP---LPKAAPNGS-SDIRFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPV 362
Cdd:cd18572 5 LVVAALSELAIPHYTgavIDAVVADGSrEAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDI 84
|
90 100 110
....*....|....*....|....*....|..
gi 767940955 363 TFFNATPTGRILNRFSSDVACADDSLPFILNI 394
Cdd:cd18572 85 AFFDATKTGELTSRLTSDCQKVSDPLSTNLNV 116
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
75-165 |
6.46e-08 |
|
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: 54.43 E-value: 6.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVD---ADVANHLLHRC--ILGMlsytTRLLCTHR-TEYLERADAVLLMEA 148
Cdd:cd03261 137 LSGGMKKRVALARALALDPELLLYDEPTAGLDpiaSGVIDDLIRSLkkELGL----TSIMVTHDlDTAFAIADRIAVLYD 212
|
90 100
....*....|....*....|.
gi 767940955 149 GRLIRAGPPSEIL----PLVQ 165
Cdd:cd03261 213 GKIVAEGTPEELRasddPLVR 233
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
28-155 |
7.35e-08 |
|
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: 55.98 E-value: 7.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 28 TIRDNILFGKTfDAQlYKEVLEA---CALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAA 104
Cdd:COG5265 447 TIAYNIAYGRP-DAS-EEEVEAAaraAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSA 524
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767940955 105 VD-----------ADVANHllhrcilgmlsyTTRLLCTHRTEYLERADAVLLMEAGRLIRAG 155
Cdd:COG5265 525 LDsrteraiqaalREVARG------------RTTLVIAHRLSTIVDADEILVLEAGRIVERG 574
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
621-807 |
7.49e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 56.33 E-value: 7.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 621 PGEKLGIV-GRTGSGKSSLLLVLFRLLEPSSGRVLLDgvdtsqlelaqlRSqLAIIPQEPFLFSGTVRENL------DPQ 693
Cdd:PTZ00243 684 PRGKLTVVlGATGSGKSTLLQSLLSQFEISEGRVWAE------------RS-IAYVPQQAWIMNATVRGNIlffdeeDAA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 694 GLHKdralwqALKQCHLSEVITSMGG-LDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLL-QQ 771
Cdd:PTZ00243 751 RLAD------AVRVSQLEADLAQLGGgLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVvEE 824
|
170 180 190
....*....|....*....|....*....|....*.
gi 767940955 772 TICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVV 807
Cdd:PTZ00243 825 CFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVE 860
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
612-808 |
7.67e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 54.37 E-value: 7.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 612 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGV--DTS------QLELAQLRSQLAIIPQEPFLFS 683
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDItiDTArslsqqKGLIRQLRQHVGFVFQNFNLFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 684 G-TVRENL--DP---QGLHKDRALwqALKQCHLSEVITSmggldGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEA 757
Cdd:PRK11264 99 HrTVLENIieGPvivKGEPKEEAT--ARARELLAKVGLA-----GKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767940955 758 TASVDQKTDQLLQQTIcKRFA--NKTVLTIAHRLNTILN-SDRVLVLQAGRVVE 808
Cdd:PRK11264 172 TSALDPELVGEVLNTI-RQLAqeKRTMVIVTHEMSFARDvADRAIFMDQGRIVE 224
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
75-161 |
1.03e-07 |
|
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: 53.84 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHL------LHRcilgmLSYTTRLLCTHRT-EYLERADAVLLME 147
Cdd:cd03295 136 LSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLqeefkrLQQ-----ELGKTIVFVTHDIdEAFRLADRIAIMK 210
|
90
....*....|....
gi 767940955 148 AGRLIRAGPPSEIL 161
Cdd:cd03295 211 NGEIVQVGTPDEIL 224
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
8-169 |
1.07e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 54.24 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 8 VRGLSKGFGLATQEPWIQF--ATIRDNILFGKTF----DAQLYKEVLEACalndDLSILPagdQTEVGEKGVTLSGGQRA 81
Cdd:PRK13645 85 VKRLRKEIGLVFQFPEYQLfqETIEKDIAFGPVNlgenKQEAYKKVPELL----KLVQLP---EDYVKRSPFELSGGQKR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 82 RIALARAVYQEKELYLLDDPLAAVDADVANHLLHRCILGMLSYTTR-LLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSE 159
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRiIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFE 237
|
170
....*....|
gi 767940955 160 ILPLVQAVPK 169
Cdd:PRK13645 238 IFSNQELLTK 247
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
607-808 |
1.21e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 53.48 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 607 GLPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG------VDTSQLELAQLRSQLAIIPQE-- 678
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQQyn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 679 --PFLfsgTVRENL--DP---QGLHKDRALWQA---LKQCHLSEVITSMGGldgelgeggrSLSLGQRQLLCLARALLTD 748
Cdd:PRK11124 93 lwPHL---TVQQNLieAPcrvLGLSKDQALARAeklLERLRLKPYADRFPL----------HLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767940955 749 AKILCIDEATASVDQK-TDQL------LQQTickrfaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVE 808
Cdd:PRK11124 160 PQVLLFDEPTAALDPEiTAQIvsiireLAET------GITQVIVTHEVEVARKtASRVVYMENGHIVE 221
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
622-816 |
1.24e-07 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 53.57 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 622 GEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSqlelaqLRSQlAIIPQepflFSGTVRENL-DPQGLHKDRA 700
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS------YKPQ-YIKAD----YEGTVRDLLsSITKDFYTHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 701 LWQalkqchlSEVITSMgGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKtDQLLQQTICKRFA-- 778
Cdd:cd03237 94 YFK-------TEIAKPL-QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE-QRLMASKVIRRFAen 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767940955 779 -NKTVLTIAHRLNTI-LNSDRVLVL--QAGRVVELDSPATLR 816
Cdd:cd03237 165 nEKTAFVVEHDIIMIdYLADRLIVFegEPSVNGVANPPQSLR 206
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
611-812 |
1.35e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 53.86 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 611 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLL-DGVDTSQL----ELAQLRSQLAIIPQEP--FLFS 683
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgDYAIPANLkkikEVKRLRKEIGLVFQFPeyQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 684 GTVRENL--DPQGLHKDRAlwQALKQchLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASV 761
Cdd:PRK13645 106 ETIEKDIafGPVNLGENKQ--EAYKK--VPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767940955 762 DQKTDQLLQQTICKRFAN--KTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSP 812
Cdd:PRK13645 182 DPKGEEDFINLFERLNKEykKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSP 235
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
64-161 |
1.46e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 53.43 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 64 DQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILGMLSY--TTRLLCTHRTEYLERAD 141
Cdd:PRK10619 142 DERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR--IMQQLAEegKTMVVVTHEMGFARHVS 219
|
90 100
....*....|....*....|.
gi 767940955 142 A-VLLMEAGRLIRAGPPSEIL 161
Cdd:PRK10619 220 ShVIFLHQGKIEEEGAPEQLF 240
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
606-808 |
1.57e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 53.55 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 606 PGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG--VDTSQLELAQLRSQLAIIPQEPFLfs 683
Cdd:PRK11248 12 GGKP-ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGkpVEGPGAERGVVFQNEGLLPWRNVQ-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 684 GTVRENLDPQGLHKDRAL---WQALKQCHLSEvitsmggldgELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATAS 760
Cdd:PRK11248 89 DNVAFGLQLAGVEKMQRLeiaHQMLKKVGLEG----------AEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767940955 761 VDQKTDQLLQQTICKRFAN--KTVLTIAHRLNTILNSDRVLVLQA---GRVVE 808
Cdd:PRK11248 159 LDAFTREQMQTLLLKLWQEtgKQVLLITHDIEEAVFMATELVLLSpgpGRVVE 211
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
74-161 |
2.02e-07 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 52.83 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 74 TLSGGQRARIALARAVYQEKELYLLDDPLAAVD-------ADVANHLLHRciLGMlsytTRLLCTHRTEYLER-ADAVLL 145
Cdd:COG3840 129 QLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrqemLDLVDELCRE--RGL----TVLMVTHDPEDAARiADRVLL 202
|
90
....*....|....*.
gi 767940955 146 MEAGRLIRAGPPSEIL 161
Cdd:COG3840 203 VADGRIAADGPTAALL 218
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
74-161 |
2.14e-07 |
|
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: 52.78 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 74 TLSGGQRARIALARAVYQEKELYLLDDPLAAVDaDVANHLLHRCI--LGMLSYTTRLLCTHRTEYLERA-DAVLLMEAGR 150
Cdd:COG1119 142 TLSQGEQRRVLIARALVKDPELLILDEPTAGLD-LGARELLLALLdkLAAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGR 220
|
90
....*....|.
gi 767940955 151 LIRAGPPSEIL 161
Cdd:COG1119 221 VVAAGPKEEVL 231
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
611-812 |
2.78e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 53.32 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 611 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLL------DGVDTSQLELA----------QLRSQLAI 674
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigDKKNNHELITNpyskkiknfkELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 675 IPQEP--FLFSGTVRENL--DP--QGLHKDRALWQALKqcHLSEvitsMGGLDGELGEGGRSLSLGQRQLLCLARALLTD 748
Cdd:PRK13631 121 VFQFPeyQLFKDTIEKDImfGPvaLGVKKSEAKKLAKF--YLNK----MGLDDSYLERSPFGLSGGQKRRVAIAGILAIQ 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767940955 749 AKILCIDEATASVDQKTDQLLQQTICKRFA-NKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSP 812
Cdd:PRK13631 195 PEILIFDEPTAGLDPKGEHEMMQLILDAKAnNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTP 260
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
74-161 |
2.94e-07 |
|
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: 54.04 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 74 TLSGGQRARIALARAVYQEKELYLLDDPLAAVD----ADVANHLLH-RCILGmlsyTTRLLCTHRTEY-LERADAVLLME 147
Cdd:TIGR03269 427 ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKaREEME----QTFIIVSHDMDFvLDVCDRAALMR 502
|
90
....*....|....
gi 767940955 148 AGRLIRAGPPSEIL 161
Cdd:TIGR03269 503 DGKIVKIGDPEEIV 516
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
28-161 |
3.09e-07 |
|
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: 52.65 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 28 TIRDNILFG-------KTFDAQLYKEVLEACALNDDLSILPagDQtevgekgvtLSGGQRARIALARAVYQEKELYLLDD 100
Cdd:cd03294 118 TVLENVAFGlevqgvpRAEREERAAEALELVGLEGWEHKYP--DE---------LSGGMQQRVGLARALAVDPDILLMDE 186
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767940955 101 PLAAVD----ADVANHLLHrcILGMLSYTTrLLCTHR-TEYLERADAVLLMEAGRLIRAGPPSEIL 161
Cdd:cd03294 187 AFSALDplirREMQDELLR--LQAELQKTI-VFITHDlDEALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
13-151 |
3.36e-07 |
|
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: 52.55 E-value: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 13 KGFGLATQEPWIQFATIRDNI-LFGKTFDAQLYKeVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQ 91
Cdd:cd03289 77 KAFGVIPQKVFIFSGTFRKNLdPYGKWSDEEIWK-VAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLS 155
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 92 EKELYLLDDPLAAVDAdVANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLMEAGRL 151
Cdd:cd03289 156 KAKILLLDEPSAHLDP-ITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
611-815 |
3.39e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 52.48 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 611 ALDGVTFCVqPGEKL--------------GIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIP 676
Cdd:PRK10575 13 ALRNVSFRV-PGRTLlhplsltfpagkvtGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 677 QE-PFLFSGTVREnLDPQG---LHKDRALWQALKQCHLSEVITsMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKIL 752
Cdd:PRK10575 92 QQlPAAEGMTVRE-LVAIGrypWHGALGRFGAADREKVEEAIS-LVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767940955 753 CIDEATASVD--QKTDQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATL 815
Cdd:PRK10575 170 LLDEPTSALDiaHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAEL 235
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
596-818 |
3.63e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.49 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 596 EFQDVVLAYRPGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQ-LAI 674
Cdd:COG3845 259 EVENLSVRDDRGVP-ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 675 IPQEPFLF----SGTVRENL-----DPQGLHKDRAL-WQALKQcHLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARA 744
Cdd:COG3845 338 IPEDRLGRglvpDMSVAENLilgryRRPPFSRGGFLdRKAIRA-FAEELIEEFDVRTPGPDTPARSLSGGNQQKVILARE 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767940955 745 LLTDAKILCIDEATASVDQK-TDQLLQQTICKRFANKTVLTIAHRLNTILN-SDRVLVLQAGRVV-ELDSPATLRNQ 818
Cdd:COG3845 417 LSRDPKLLIAAQPTRGLDVGaIEFIHQRLLELRDAGAAVLLISEDLDEILAlSDRIAVMYEGRIVgEVPAAEATREE 493
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
75-160 |
4.92e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 52.80 E-value: 4.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADvanhlLHRCI------LGMLSYTTRLLCTH-RTEYLERADAVLLME 147
Cdd:PRK11432 137 ISGGQQQRVALARALILKPKVLLFDEPLSNLDAN-----LRRSMrekireLQQQFNITSLYVTHdQSEAFAVSDTVIVMN 211
|
90
....*....|...
gi 767940955 148 AGRLIRAGPPSEI 160
Cdd:PRK11432 212 KGKIMQIGSPQEL 224
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
610-811 |
5.01e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 51.50 E-value: 5.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 610 NALDGVTFCVQPGEKLGIVGRTGSGKSSLllvlfrllepssGRVLLDgvdtsqLELAQLRSQLAIIPQEPFLFSGTVREN 689
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTL------------LRLLAG------ALKGTPVAGCVDVPDNQFGREASLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 690 LDPQGLHKDRAlwQALKQCHLSEVITsmggldgeLGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLL 769
Cdd:COG2401 106 IGRKGDFKDAV--ELLNAVGLSDAVL--------WLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767940955 770 Q---QTICKRfANKTVLTIAHRLNTI--LNSDRVLVLQAGRVVELDS 811
Cdd:COG2401 176 ArnlQKLARR-AGITLVVATHHYDVIddLQPDLLIFVGYGGVPEEKR 221
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
75-152 |
5.17e-07 |
|
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: 51.35 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVAnhllhRCILGML------SYTTRLLCTHRTEYLER-ADAVLLME 147
Cdd:cd03257 146 LSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQ-----AQILDLLkklqeeLGLTLLFITHDLGVVAKiADRVAVMY 220
|
....*
gi 767940955 148 AGRLI 152
Cdd:cd03257 221 AGKIV 225
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
615-806 |
5.27e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.13 E-value: 5.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 615 VTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQ-LRSQLAIIP---QEPFLF-SGTVREN 689
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPedrQSSGLYlDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 690 LDPQgLHKDRALWQALKQ--CHLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQ 767
Cdd:PRK15439 362 VCAL-THNRRGFWIKPARenAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARN 440
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767940955 768 LLQQTIcKRFA--NKTVLTIAHRLNTILN-SDRVLVLQAGRV 806
Cdd:PRK15439 441 DIYQLI-RSIAaqNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
75-161 |
5.68e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 51.63 E-value: 5.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADvanhLLHRCILGMLSYT----TRLLCTHRTEYLER-ADAVLLMEAG 149
Cdd:PRK09493 137 LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPE----LRHEVLKVMQDLAeegmTMVIVTHEIGFAEKvASRLIFIDKG 212
|
90
....*....|..
gi 767940955 150 RLIRAGPPSEIL 161
Cdd:PRK09493 213 RIAEDGDPQVLI 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
4-160 |
6.13e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 52.14 E-value: 6.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 4 GHVAVRGLSKGFGLATQEPWIQF--ATIRDNILFG-KTFDAQlykevlEACALNDDLS-ILPAGDQTEVGEKG-VTLSGG 78
Cdd:PRK13641 76 GNKNLKKLRKKVSLVFQFPEAQLfeNTVLKDVEFGpKNFGFS------EDEAKEKALKwLKKVGLSEDLISKSpFELSGG 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 79 QRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRCILGMLSYTTRLLCTHRTEYL-ERADAVLLMEAGRLIRAGPP 157
Cdd:PRK13641 150 QMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASP 229
|
...
gi 767940955 158 SEI 160
Cdd:PRK13641 230 KEI 232
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
613-819 |
6.25e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 51.62 E-value: 6.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 613 DGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEP----SSGRVLLDGVdtsQLELAQLRSQL-AIIPQEP-------F 680
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGK---PVAPCALRGRKiATIMQNPrsafnplH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 681 LFSGTVRENLDPQGLHKDRA-LWQALKQCHLSEVITSMGGLDGelgeggrSLSLGQRQLLCLARALLTDAKILCIDEATA 759
Cdd:PRK10418 97 TMHTHARETCLALGKPADDAtLTAALEAVGLENAARVLKLYPF-------EMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767940955 760 SVD----QKTDQLLQQTICKRfaNKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQP 819
Cdd:PRK10418 170 DLDvvaqARILDLLESIVQKR--ALGMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFNAP 232
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
8-161 |
6.52e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 51.63 E-value: 6.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 8 VRGLSKGFGLATQEPWIQF--ATIRDNILFGKTFDAQLYKEVLEACalndDLSILPAGDQTEVGEKGVTLSGGQRARIAL 85
Cdd:PRK13642 76 VWNLRRKIGMVFQNPDNQFvgATVEDDVAFGMENQGIPREEMIKRV----DEALLAVNMLDFKTREPARLSGGQKQRVAV 151
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767940955 86 ARAVYQEKELYLLDDPLAAVDADVANHLLhRCILGMLS--YTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEIL 161
Cdd:PRK13642 152 AGIIALRPEIIILDESTSMLDPTGRQEIM-RVIHEIKEkyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
613-806 |
6.95e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.62 E-value: 6.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 613 DGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLE-PSSGRVLLDG--VDTSQLELAqLRSQLAIIPQE-------PFLf 682
Cdd:PRK13549 279 DDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGkpVKIRNPQQA-IAQGIAMVPEDrkrdgivPVM- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 683 sgTVRENLDPQGLH---KDRALWQALKQCHLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATA 759
Cdd:PRK13549 357 --GVGKNITLAALDrftGGSRIDDAAELKTILESIQRLKVKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTR 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767940955 760 SVD--------QKTDQLLQQTICkrfanktVLTIAHRLNTILN-SDRVLVLQAGRV 806
Cdd:PRK13549 435 GIDvgakyeiyKLINQLVQQGVA-------IIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
74-159 |
6.99e-07 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 50.82 E-value: 6.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 74 TLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVAN---HLLHR-CILGmlsyTTRLLCTHRTEYLERADA-VLLMEA 148
Cdd:COG2884 137 ELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWeimELLEEiNRRG----TTVLIATHDLELVDRMPKrVLELED 212
|
90
....*....|.
gi 767940955 149 GRLIRAGPPSE 159
Cdd:COG2884 213 GRLVRDEARGV 223
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
611-818 |
7.63e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.82 E-value: 7.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 611 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG--VDTSQLElAQLR----SQlaiipqepfLFS- 683
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVDAGDIA-TRRRvgymSQ---------AFSl 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 684 -G--TVRENLDpqgLH-------KDRA---LWQALKQCHLSEVITSMGGldgelgeggrSLSLGQRQLLCLARALLTDAK 750
Cdd:NF033858 351 yGelTVRQNLE---LHarlfhlpAAEIaarVAEMLERFDLADVADALPD----------SLPLGIRQRLSLAVAVIHKPE 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767940955 751 ILCIDEATASVD-QKTDQLLQQTIckRFANKTVLTI---AHRLNTILNSDRVLVLQAGRVVELDSPATLRNQ 818
Cdd:NF033858 418 LLILDEPTSGVDpVARDMFWRLLI--ELSREDGVTIfisTHFMNEAERCDRISLMHAGRVLASDTPAALVAA 487
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
612-806 |
7.94e-07 |
|
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: 52.52 E-value: 7.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 612 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPS-SGRVLLDG--VDTSQLELAqLRSQLAIIPQE-------PFL 681
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDIRNPAQA-IRAGIAMVPEDrkrhgivPIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 682 fsgTVRENLDPQGLHKDRALWQ---ALKQCHLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEAT 758
Cdd:TIGR02633 355 ---GVGKNITLSVLKSFCFKMRidaAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767940955 759 ASVD--------QKTDQLLQQTIckrfankTVLTIAHRLNTILN-SDRVLVLQAGRV 806
Cdd:TIGR02633 432 RGVDvgakyeiyKLINQLAQEGV-------AIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
28-161 |
8.15e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 52.14 E-value: 8.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 28 TIRDNIL-FGKTFDAQLyKEVLEACALNDDLSILPAGDQTEVGEkgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVD 106
Cdd:PRK13536 130 TVRENLLvFGRYFGMST-REIEAVIPSLLEFARLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 767940955 107 ADvANHLLHRCILGMLSY-TTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 161
Cdd:PRK13536 205 PH-ARHLIWERLRSLLARgKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALI 260
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
75-160 |
8.96e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 51.28 E-value: 8.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHL------LHRciLGMlsytTRLLCTHRTEYL-ERADAVLLME 147
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELmtlfkkLHQ--SGM----TIVLVTHLMDDVaNYADFVYVLE 219
|
90
....*....|...
gi 767940955 148 AGRLIRAGPPSEI 160
Cdd:PRK13649 220 KGKLVLSGKPKDI 232
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
74-146 |
1.00e-06 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 49.92 E-value: 1.00e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767940955 74 TLSGGQRARIALARAVYQEKELYLLDDPLAAVDA----DVANHLLHRCILGmlsyTTRLLCTHRTEYLERADAVLLM 146
Cdd:NF040873 119 ELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAesreRIIALLAEEHARG----ATVVVVTHDLELVRRADPCVLL 191
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
612-805 |
1.07e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 52.19 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 612 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSS--GRVLLDGVDTSQlelaQLRSQLAIIPQEPFLFSG-TVRE 688
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK----QILKRTGFVTQDDILYPHlTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 689 NLD-------PQGLHKDRALWQAlkQCHLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASV 761
Cdd:PLN03211 160 TLVfcsllrlPKSLTKQEKILVA--ESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGL 237
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767940955 762 DQKTDQLLQQTICKrFAN--KTVLTIAHRLNTILNS--DRVLVLQAGR 805
Cdd:PLN03211 238 DATAAYRLVLTLGS-LAQkgKTIVTSMHQPSSRVYQmfDSVLVLSEGR 284
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
75-166 |
1.12e-06 |
|
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: 50.75 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVD---ADVANHLLHRC--ILGMlsytTRLLCTHRTEYLER-ADAVLLMEA 148
Cdd:COG1127 142 LSGGMRKRVALARALALDPEILLYDEPTAGLDpitSAVIDELIRELrdELGL----TSVVVTHDLDSAFAiADRVAVLAD 217
|
90 100
....*....|....*....|..
gi 767940955 149 GRLIRAGPPSEIL----PLVQA 166
Cdd:COG1127 218 GKIIAEGTPEELLasddPWVRQ 239
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
75-160 |
1.24e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 51.38 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHL------LHRCiLGmlsyTTRLLCTH-RTEYLERADAVLLME 147
Cdd:PRK11650 135 LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMrleiqrLHRR-LK----TTSLYVTHdQVEAMTLADRVVVMN 209
|
90
....*....|...
gi 767940955 148 AGRLIRAGPPSEI 160
Cdd:PRK11650 210 GGVAEQIGTPVEV 222
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
75-160 |
1.26e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 51.57 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHL------LHRcilgmlsyttRLLC-----TH-RTEYLERADA 142
Cdd:PRK11000 134 LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMrieisrLHK----------RLGRtmiyvTHdQVEAMTLADK 203
|
90
....*....|....*...
gi 767940955 143 VLLMEAGRLIRAGPPSEI 160
Cdd:PRK11000 204 IVVLDAGRVAQVGKPLEL 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
74-151 |
1.49e-06 |
|
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: 49.84 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 74 TLSGGQRARIALARAVYQEKELYLLDDPLAAVDA-------DVANHLLHRcilGMlsytTRLLCTHRTEY-LERADAVLL 145
Cdd:cd03262 135 QLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPelvgevlDVMKDLAEE---GM----TMVVVTHEMGFaREVADRVIF 207
|
....*.
gi 767940955 146 MEAGRL 151
Cdd:cd03262 208 MDDGRI 213
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
599-810 |
1.88e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 51.17 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 599 DVVLAYRpGL--PNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQ-LRSQLAII 675
Cdd:COG1129 254 EVVLEVE-GLsvGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYV 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 676 P----QEPFLFSGTVRENLDPQGLHK-------DRALWQALkqchLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARA 744
Cdd:COG1129 333 PedrkGEGLVLDLSIRENITLASLDRlsrggllDRRRERAL----AEEYIKRLRIKTPSPEQPVGNLSGGNQQKVVLAKW 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767940955 745 LLTDAKILCIDEATASVD--QKTD--QLLQQtickrFAN--KTVLTIAHRLNTIL-NSDRVLVLQAGRVV-ELD 810
Cdd:COG1129 409 LATDPKVLILDEPTRGIDvgAKAEiyRLIRE-----LAAegKAVIVISSELPELLgLSDRILVMREGRIVgELD 477
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
75-161 |
1.89e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 50.57 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANHLLHRCILGMLSY-TTRLLCTHRTEYLER-ADAVLLMEAGRLI 152
Cdd:PRK13537 139 LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ-ARHLMWERLRSLLARgKTILLTTHFMEEAERlCDRLCVIEEGRKI 217
|
....*....
gi 767940955 153 RAGPPSEIL 161
Cdd:PRK13537 218 AEGAPHALI 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-161 |
1.97e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 50.37 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 3 RGHVAVRGLSKG-----------FGLATQEPWIQFA--TIRDNILFGKTF----DAQLYKEVleacalndDLSILPAGDQ 65
Cdd:PRK13644 56 KGKVLVSGIDTGdfsklqgirklVGIVFQNPETQFVgrTVEEDLAFGPENlclpPIEIRKRV--------DRALAEIGLE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 66 TEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLL 145
Cdd:PRK13644 128 KYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIV 207
|
170
....*....|....*.
gi 767940955 146 MEAGRLIRAGPPSEIL 161
Cdd:PRK13644 208 MDRGKIVLEGEPENVL 223
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
55-161 |
2.01e-06 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 51.00 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 55 DDLSILPAGDQTEV---GEKGVT-LSGGQRARIALARAVYQEKELYLLDDPLAAVDadvANHLLHrcilgMLSYTTRLLC 130
Cdd:PRK09536 116 DRAAVERAMERTGVaqfADRPVTsLSGGERQRVLLARALAQATPVLLLDEPTASLD---INHQVR-----TLELVRRLVD 187
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 767940955 131 THRTEY-----LERA----DAVLLMEAGRLIRAGPPSEIL 161
Cdd:PRK09536 188 DGKTAVaaihdLDLAarycDELVLLADGRVRAAGPPADVL 227
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
613-801 |
2.14e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 49.42 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 613 DGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLElAQLRSQLaiipqepfLFSG-------- 684
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR-DEYHQDL--------LYLGhqpgikte 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 685 -TVRENLD-PQGLH---KDRALWQALKQCHLSEVitsmggldgeLGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATA 759
Cdd:PRK13538 89 lTALENLRfYQRLHgpgDDEALWEALAQVGLAGF----------EDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767940955 760 SVDQKTDQLLQQTICKRFANK--TVLTIAHRLNTILNSDRVLVL 801
Cdd:PRK13538 159 AIDKQGVARLEALLAQHAEQGgmVILTTHQDLPVASDKVRKLRL 202
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
74-160 |
2.20e-06 |
|
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: 49.68 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 74 TLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLhRCILGMLSY--TTRLLCTHrteYLERADA----VLLME 147
Cdd:cd03265 131 TYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVW-EYIEKLKEEfgMTILLTTH---YMEEAEQlcdrVAIID 206
|
90
....*....|...
gi 767940955 148 AGRLIRAGPPSEI 160
Cdd:cd03265 207 HGRIIAEGTPEEL 219
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
75-161 |
2.25e-06 |
|
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: 49.50 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVAnhllhRCILGMLSYTTR------LLCTHRTEYLER-ADAVLLME 147
Cdd:cd03258 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETT-----QSILALLRDINRelgltiVLITHEMEVVKRiCDRVAVME 215
|
90
....*....|....
gi 767940955 148 AGRLIRAGPPSEIL 161
Cdd:cd03258 216 KGEVVEEGTVEEVF 229
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
8-170 |
2.32e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 50.12 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 8 VRGLSKGFGLATQEPWIQF--ATIRDNILFGKTfDAQLYKEVLEACALnDDLSILpaGDQTEVGEKG-VTLSGGQRARIA 84
Cdd:PRK13643 79 IKPVRKKVGVVFQFPESQLfeETVLKDVAFGPQ-NFGIPKEKAEKIAA-EKLEMV--GLADEFWEKSpFELSGGQMRRVA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 85 LARAVYQEKELYLLDDPLAAVDADVANHLLHRCILGMLSYTTRLLCTH-RTEYLERADAVLLMEAGRLIRAGPPSEILPL 163
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHlMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
|
170
....*....|....
gi 767940955 164 VQ-------AVPKA 170
Cdd:PRK13643 235 VDflkahelGVPKA 248
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
13-167 |
2.40e-06 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 49.64 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 13 KGFGLATQEPWIqFA--TIRDNIL-----FGKTFDAQlyKEVLEAcaLNDDLSILPAGDQtevgeKGVTLSGGQRARIAL 85
Cdd:COG1137 78 LGIGYLPQEASI-FRklTVEDNILavlelRKLSKKER--EERLEE--LLEEFGITHLRKS-----KAYSLSGGERRRVEI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 86 ARAVYQEKELYLLDDPLAAVD----ADVAN---HLLHRCIlGMlsyttrLLCTH--RtEYLERADAVLLMEAGRLIRAGP 156
Cdd:COG1137 148 ARALATNPKFILLDEPFAGVDpiavADIQKiirHLKERGI-GV------LITDHnvR-ETLGICDRAYIISEGKVLAEGT 219
|
170
....*....|...
gi 767940955 157 PSEIL--PLVQAV 167
Cdd:COG1137 220 PEEILnnPLVRKV 232
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
612-812 |
2.58e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 49.68 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 612 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLldgvdTSQLELAQLRSQLAIIPQEPFLFS-GTVREN- 689
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-----AGTAPLAEAREDTRLMFQDARLLPwKKVIDNv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 690 -LDPQGLHKDRALwQALKQCHLSEVITSMGGldgelgeggrSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQL 768
Cdd:PRK11247 103 gLGLKGQWRDAAL-QALAAVGLADRANEWPA----------ALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767940955 769 LQQTICKRFANK--TVLTIAHRLN-TILNSDRVLVLQAGRV-----VELDSP 812
Cdd:PRK11247 172 MQDLIESLWQQHgfTVLLVTHDVSeAVAMADRVLLIEEGKIgldltVDLPRP 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
75-160 |
3.40e-06 |
|
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: 50.57 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANhLLHRCILGML--SYTTRLLCTHRTEYLER-ADAVLLMEAGRL 151
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAK-LVHNALEEAVkaSGISMVLTSHWPEVIEDlSDKAIWLENGEI 247
|
....*....
gi 767940955 152 IRAGPPSEI 160
Cdd:TIGR03269 248 KEEGTPDEV 256
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
75-169 |
4.19e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 49.32 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDA----DVANHLLHrciLGMLSYTTRLLCTHRTEYLERADAVLLMEAGR 150
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPsgrrEVVNTIKE---LNKKYGITIILITHYMEEAVEADRIIVMDSGK 221
|
90
....*....|....*....
gi 767940955 151 LIRAGPPSEILPLVQAVPK 169
Cdd:PRK13633 222 VVMEGTPKEIFKEVEMMKK 240
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
45-211 |
4.44e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.80 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 45 KEVLeacaLNDDLSILPAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDaDVANHLLHRCILGMLSY 124
Cdd:PTZ00265 554 KKVL----IHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINNLKGN 628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 125 TTR--LLCTHRTEYLERADAVLLMeAGRliRAGPPSEILPLVQAVPKAWAENGQESDSATAQSVQNPEKTKEGLEE---- 198
Cdd:PTZ00265 629 ENRitIIIAHRLSTIRYANTIFVL-SNR--ERGSTVDVDIIGEDPTKDNKENNNKNNKDDNNNNNNNNNNKINNAGsyii 705
|
170
....*....|...
gi 767940955 199 EQSTSGRLLQEES 211
Cdd:PTZ00265 706 EQGTHDALMKNKN 718
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
74-160 |
5.01e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 49.49 E-value: 5.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 74 TLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILGMLSYTTR---LLCTHR-TEYLERADAVLLMEAG 149
Cdd:PRK11144 128 SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP--YLERLAREINipiLYVSHSlDEILRLADRVVVLEQG 205
|
90
....*....|.
gi 767940955 150 RLIRAGPPSEI 160
Cdd:PRK11144 206 KVKAFGPLEEV 216
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
11-160 |
5.28e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 48.62 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 11 LSKGFGLATQEPWIQFATIRDNILFGKTFDAQLYKEVLEACALNddlSILPAGDQTEVGEK----GVTLSGGQRARIALA 86
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPMSIYENVVYGLRLKGIKDKQVLDEAVEK---SLKGASIWDEVKDRlhdsALGLSGGQQQRVCIA 160
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767940955 87 RAVYQEKELYLLDDPLAAVDAdVANHLLHRCILGMLSYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEI 160
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDP-ISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQM 234
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
595-805 |
6.01e-06 |
|
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: 46.67 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYrpGLPNALDGVTFCVQPGEKLGIVGRTGSGKSSlllvlfrllepssgrvLLDgvdtsqlelaqlrsqlaI 674
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKST----------------LLK-----------------L 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 675 IPQEPFLFSGTVRENldpqglhkdralwQALKQCHLSEvitsmggldgelgeggrsLSLGQRQLLCLARALLTDAKILCI 754
Cdd:cd03221 46 IAGELEPDEGIVTWG-------------STVKIGYFEQ------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767940955 755 DEATASVDQKTDQLLQQTIcKRFaNKTVLTIAH-R--LNTIlnSDRVLVLQAGR 805
Cdd:cd03221 95 DEPTNHLDLESIEALEEAL-KEY-PGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
11-160 |
6.68e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 48.86 E-value: 6.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 11 LSKGFGLATQEPWIQF--ATIRDNILFG-KTF-----DA-QLYKEVLEACALNDDLSILPAGDqtevgekgvtLSGGQRA 81
Cdd:PRK13634 83 LRKKVGIVFQFPEHQLfeETVEKDICFGpMNFgvseeDAkQKAREMIELVGLPEELLARSPFE----------LSGGQMR 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 82 RIALARAVYQEKELYLLDDPLAAVDADVANHL------LHRcILGMlsytTRLLCTHRTEYLER-ADAVLLMEAGRLIRA 154
Cdd:PRK13634 153 RVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMmemfykLHK-EKGL----TTVLVTHSMEDAARyADQIVVMHKGTVFLQ 227
|
....*.
gi 767940955 155 GPPSEI 160
Cdd:PRK13634 228 GTPREI 233
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
74-108 |
7.41e-06 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 47.86 E-value: 7.41e-06
10 20 30
....*....|....*....|....*....|....*
gi 767940955 74 TLSGGQRARIALARAVYQEKELYLLDDPLAAVDAD 108
Cdd:COG4136 133 TLSGGQRARVALLRALLAEPRALLLDEPFSKLDAA 167
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
75-161 |
7.65e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 48.30 E-value: 7.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDAdVANHLLHRCILGMLSYTTRLLCTHRTEYLER-ADAVLLMEAGRLIR 153
Cdd:PRK14267 150 LSGGQRQRLVIARALAMKPKILLMDEPTANIDP-VGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIE 228
|
....*...
gi 767940955 154 AGPPSEIL 161
Cdd:PRK14267 229 VGPTRKVF 236
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
13-106 |
8.26e-06 |
|
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: 47.92 E-value: 8.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 13 KGFGLATQEPWIqFA--TIRDNIL-----FGKTFDAQlyKEVLEAcaLNDDLSILPAGDQtevgeKGVTLSGGQRARIAL 85
Cdd:cd03218 75 LGIGYLPQEASI-FRklTVEENILavleiRGLSKKER--EEKLEE--LLEEFHITHLRKS-----KASSLSGGERRRVEI 144
|
90 100
....*....|....*....|.
gi 767940955 86 ARAVYQEKELYLLDDPLAAVD 106
Cdd:cd03218 145 ARALATNPKFLLLDEPFAGVD 165
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
75-159 |
8.83e-06 |
|
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: 47.81 E-value: 8.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHllhrcILGML------SYTTRLLCTHRTEYLERADAVLLMEA 148
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQ-----IIDLLfelnreRGTTLVLVTHDPALAARCDRVLRLRA 221
|
90
....*....|.
gi 767940955 149 GRLIRAGPPSE 159
Cdd:COG4181 222 GRLVEDTAATA 232
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
611-806 |
8.88e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 48.09 E-value: 8.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 611 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLfrllepsSGRVLLDGVDTSQLEL----AQLRSQLA------------I 674
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHL-------SGLITGDKSAGSHIELlgrtVQREGRLArdirksrantgyI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 675 IPQEPFLFSGTVRENLDPQGLHKD---RALWQALKQCHLSEVITSMGGLDGELGEGGR--SLSLGQRQLLCLARALLTDA 749
Cdd:PRK09984 92 FQQFNLVNRLSVLENVLIGALGSTpfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRvsTLSGGQQQRVAIARALMQQA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767940955 750 KILCIDEATASVDQKTDQLLQQTIckRFANK----TVLTIAHRLNTILN-SDRVLVLQAGRV 806
Cdd:PRK09984 172 KVILADEPIASLDPESARIVMDTL--RDINQndgiTVVVTLHQVDYALRyCERIVALRQGHV 231
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
612-808 |
8.94e-06 |
|
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: 47.52 E-value: 8.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 612 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLF--RLLEPSSGRVLLDGVDTSQLElAQLRSQLAII--PQEPFLFSGtVR 687
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEILFKGEDITDLP-PEERARLGIFlaFQYPPEIPG-VK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 688 enldpqglhkdralwqalkqchLSEVITSMGGldgelgeggrSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQ 767
Cdd:cd03217 94 ----------------------NADFLRYVNE----------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALR 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767940955 768 LLQQTICK-RFANKTVLTIAHRLNtILN---SDRVLVLQAGRVVE 808
Cdd:cd03217 142 LVAEVINKlREEGKSVLIITHYQR-LLDyikPDRVHVLYDGRIVK 185
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
75-161 |
8.96e-06 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 48.21 E-value: 8.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRCILGMLSYTTRLLCTHRTEYL-ERADAVLLMEAGRLIR 153
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFArDVADRAIFMDQGRIVE 224
|
....*...
gi 767940955 154 AGPPSEIL 161
Cdd:PRK11264 225 QGPAKALF 232
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6-147 |
1.14e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 49.14 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 6 VAVRGLSKGFGLATQEPWIQFATIRDNI-LFGKTFDAQLYKeVLEACALNDDLSILPAGDQTEVGEKGVTLSGGQRARIA 84
Cdd:TIGR01271 1285 VTLQTWRKAFGVIPQKVFIFSGTFRKNLdPYEQWSDEEIWK-VAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMC 1363
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767940955 85 LARAVYQEKELYLLDDPLAAVDAdVANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLME 147
Cdd:TIGR01271 1364 LARSILSKAKILLLDEPSAHLDP-VTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIE 1425
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
603-808 |
1.30e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.97 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 603 AYRPGLPNaldgVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSgrvlldgvDTSqlelAQLRSQLAIIPQEPFLF 682
Cdd:PLN03130 628 AERPTLSN----INLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRS--------DAS----VVIRGTVAYVPQVSWIF 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 683 SGTVRENL---------------DPQGLHKDRALWQALKQCHLSEvitsmggldgelgeGGRSLSLGQRQLLCLARALLT 747
Cdd:PLN03130 692 NATVRDNIlfgspfdperyeraiDVTALQHDLDLLPGGDLTEIGE--------------RGVNISGGQKQRVSMARAVYS 757
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767940955 748 DAKILCIDEATASVD-QKTDQLLQQTICKRFANKTVLTIAHRLNTILNSDRVLVLQAGRVVE 808
Cdd:PLN03130 758 NSDVYIFDDPLSALDaHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKE 819
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
606-810 |
1.43e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.63 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 606 PGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLfrllepS--------SGRVLLDGvdtsqlELAQLRS------- 670
Cdd:NF040905 12 PGVK-ALDDVNLSVREGEIHALCGENGAGKSTLMKVL------SgvyphgsyEGEILFDG------EVCRFKDirdseal 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 671 QLAIIPQE----PFLfsgTVRENL------------D-PQGLHKDRALwqaLKQCHLSE----VITSmggldgelgeggr 729
Cdd:NF040905 79 GIVIIHQElaliPYL---SIAENIflgnerakrgviDwNETNRRAREL---LAKVGLDEspdtLVTD------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 730 sLSLGQRQLLCLARALLTDAKILCIDEATASV-DQKTDQLLQqtICKRFANK--TVLTIAHRLNTILN-SDRVLVLQAGR 805
Cdd:NF040905 140 -IGVGKQQLVEIAKALSKDVKLLILDEPTAALnEEDSAALLD--LLLELKAQgiTSIIISHKLNEIRRvADSITVLRDGR 216
|
....*.
gi 767940955 806 VVE-LD 810
Cdd:NF040905 217 TIEtLD 222
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
310-394 |
1.46e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 47.56 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 310 SSDIRFYLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACADDSLP 389
Cdd:cd18557 32 LDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVT 111
|
....*
gi 767940955 390 FILNI 394
Cdd:cd18557 112 DNLSQ 116
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
6-106 |
1.50e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 47.47 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 6 VAVRglsKGFGLATQEPWIQFATIRDNILFGKTFDA------QLYKEVLEACALNDDLsilpagdQTEVGEKGVTLSGGQ 79
Cdd:PRK14243 87 VEVR---RRIGMVFQKPNPFPKSIYDNIAYGARINGykgdmdELVERSLRQAALWDEV-------KDKLKQSGLSLSGGQ 156
|
90 100
....*....|....*....|....*..
gi 767940955 80 RARIALARAVYQEKELYLLDDPLAAVD 106
Cdd:PRK14243 157 QQRLCIARAIAVQPEVILMDEPCSALD 183
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
75-153 |
1.56e-05 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 46.96 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANH---LLHRCI--LGmlsyTTRLLCTHRTEYLERADAVLLMEAG 149
Cdd:COG1136 145 LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEvleLLRELNreLG----TTIVMVTHDPELAARADRVIRLRDG 220
|
....
gi 767940955 150 RLIR 153
Cdd:COG1136 221 RIVS 224
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
615-807 |
1.58e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 47.23 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 615 VTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLePSSGRVLLDGVDTSQL---ELAQLRSQLAiiPQEPFLFSGTVRENLD 691
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWsaaELARHRAYLS--QQQTPPFAMPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 692 ---PQGLHKDRAlwqalkQCHLSEViTSMGGLDGELGEGGRSLSLGQRQLLCLARALLT-------DAKILCIDEATASV 761
Cdd:PRK03695 92 lhqPDKTRTEAV------ASALNEV-AEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767940955 762 D--QKT--DQLLQQtICKrfANKTVLTIAHRLN-TILNSDRVLVLQAGRVV 807
Cdd:PRK03695 165 DvaQQAalDRLLSE-LCQ--QGIAVVMSSHDLNhTLRHADRVWLLKQGKLL 212
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
323-380 |
1.86e-05 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 47.24 E-value: 1.86e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 767940955 323 IAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSD 380
Cdd:cd18780 51 VVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSD 108
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
75-160 |
2.04e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 47.35 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDA----DVANHL--LHRcilgmlSYT-TRLLCTHRTEYLER-ADAVLLM 146
Cdd:PRK13637 145 LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPkgrdEILNKIkeLHK------EYNmTIILVSHSMEDVAKlADRIIVM 218
|
90
....*....|....
gi 767940955 147 EAGRLIRAGPPSEI 160
Cdd:PRK13637 219 NKGKCELQGTPREV 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
595-810 |
2.32e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 47.75 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYrPGLPnALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLdGVDTsqlelaqlrsQLAI 674
Cdd:COG0488 316 LELEGLSKSY-GDKT-LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 675 IPQEpflfsgtvRENLDPqglhkDRALWQALKQC-------HLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLT 747
Cdd:COG0488 383 FDQH--------QEELDP-----DKTVLDELRDGapggteqEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767940955 748 DAKILCIDEATASVDQKTDQLLQQTIcKRFANkTVLTIAH-R--LNTIlnSDRVLVLQAGRVVELD 810
Cdd:COG0488 450 PPNVLLLDEPTNHLDIETLEALEEAL-DDFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREYP 511
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
612-819 |
2.36e-05 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 47.41 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 612 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQlrSQLAIIPQEPFLFSG-TVREN- 689
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--RDICMVFQSYALFPHmSLGENv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 690 ---LDPQGLHKD---RALWQALKQCHLSevitsmggldGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQ 763
Cdd:PRK11432 100 gygLKMLGVPKEerkQRVKEALELVDLA----------GFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 764 KTDQLLQQTI---CKRFaNKTVLTIAH-RLNTILNSDRVLVLQAGRVVELDSPATLRNQP 819
Cdd:PRK11432 170 NLRRSMREKIrelQQQF-NITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
75-152 |
2.37e-05 |
|
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: 45.50 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILGML--SYTTRLLCTHR-TEYLERADAVLLMEAGRL 151
Cdd:cd03216 83 LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK--VIRRLraQGVAVIFISHRlDEVFEIADRVTVLRDGRV 160
|
.
gi 767940955 152 I 152
Cdd:cd03216 161 V 161
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
28-145 |
2.40e-05 |
|
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: 46.32 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 28 TIRDNILF-----GKTFDAQLYKEVLEACALnDDLSILPAGdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPL 102
Cdd:COG4133 91 TVRENLRFwaalyGLRADREAIDEALEAVGL-AGLADLPVR----------QLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 767940955 103 AAVDADvANHLLHRCIL------GMLsyttrLLCTHRTEYLERADAVLL 145
Cdd:COG4133 160 TALDAA-GVALLAELIAahlargGAV-----LLTTHQPLELAAARVLDL 202
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
75-113 |
2.58e-05 |
|
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: 44.75 E-value: 2.58e-05
10 20 30
....*....|....*....|....*....|....*....
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLaavdadvaNHL 113
Cdd:cd03221 71 LSGGEKMRLALAKLLLENPNLLLLDEPT--------NHL 101
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
612-801 |
2.72e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 46.65 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 612 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGvdtsQLELAQLRSQLAIIPQEPFLFSGTVRenLD 691
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG----KLRIGYVPQKLYLDTTLPLTVNRFLR--LR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 692 PqGLHKDRALwQALKQCHLSEVItsmggldgelGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQ 771
Cdd:PRK09544 94 P-GTKKEDIL-PALKRVQAGHLI----------DAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYD 161
|
170 180 190
....*....|....*....|....*....|...
gi 767940955 772 TI--CKRFANKTVLTIAHRLNTIL-NSDRVLVL 801
Cdd:PRK09544 162 LIdqLRRELDCAVLMVSHDLHLVMaKTDEVLCL 194
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
627-807 |
2.90e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 47.18 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 627 IVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG---VDTSQ-LELAQLRSQLAIIPQEPFLFSG-TVRENLDPQGLHKDRAL 701
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKgICLPPEKRRIGYVFQDARLFPHyKVRGNLRYGMAKSMVAQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 702 WQAlkqchlsevITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVD-QKTDQLLQ--QTICKRFa 778
Cdd:PRK11144 109 FDK---------IVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKRELLPylERLAREI- 178
|
170 180 190
....*....|....*....|....*....|
gi 767940955 779 NKTVLTIAHRLNTILN-SDRVLVLQAGRVV 807
Cdd:PRK11144 179 NIPILYVSHSLDEILRlADRVVVLEQGKVK 208
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
75-169 |
3.45e-05 |
|
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: 47.37 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLL---------HRcilgmLSYttrLLCTH-----RteYLerA 140
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILdllrdlqreHG-----LAY---LFISHdlavvR--AL--A 493
|
90 100 110
....*....|....*....|....*....|....*...
gi 767940955 141 DAVLLMEAGRLIRAGPPSEIL--P-------LVQAVPK 169
Cdd:COG4172 494 HRVMVMKDGKVVEQGPTEQVFdaPqhpytraLLAAAPL 531
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
75-161 |
3.48e-05 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 46.14 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVD-------ADVANHLLHRcilGMlsytTRLLCTH-----RteylERADA 142
Cdd:COG1126 137 LSGGQQQRVAIARALAMEPKVMLFDEPTSALDpelvgevLDVMRDLAKE---GM----TMVVVTHemgfaR----EVADR 205
|
90
....*....|....*....
gi 767940955 143 VLLMEAGRLIRAGPPSEIL 161
Cdd:COG1126 206 VVFMDGGRIVEEGPPEEFF 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
28-161 |
3.89e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 45.73 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 28 TIRDNILFG-----KTFDAQlyKEVLEACA----LNDDLSILPAgdqtevgekgvTLSGGQRARIALARAVYQEKELYLL 98
Cdd:PRK10771 87 TVAQNIGLGlnpglKLNAAQ--REKLHAIArqmgIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLL 153
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 99 DDPLAAVDADVANHllhrcILGMLS------YTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 161
Cdd:PRK10771 154 DEPFSALDPALRQE-----MLTLVSqvcqerQLTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELL 218
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
611-818 |
4.33e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 46.26 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 611 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGvdtSQLELAQlRSQLAIIPQEPFLFSG-TVREn 689
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG---EPLDPED-RRRIGYLPEERGLYPKmKVGE- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 690 ldpQ--------GLHKDRAL-----WqaLKQCHLSEVITSmggldgelgeGGRSLSLGQRQLLCLARALLTDAKILCIDE 756
Cdd:COG4152 91 ---QlvylarlkGLSKAEAKrradeW--LERLGLGDRANK----------KVEELSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767940955 757 ATASVDQKTDQLLQQTIcKRFANK--TVLTIAHRLNTI--LnSDRVLVLQAGRVVELDSPATLRNQ 818
Cdd:COG4152 156 PFSGLDPVNVELLKDVI-RELAAKgtTVIFSSHQMELVeeL-CDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
25-161 |
4.58e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 46.23 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 25 QFA-------TIRDNILFG-------KTFDAQLYKEVLEACALndDLSILPagdqtevgEKGVTLSGGQRARIALARAVY 90
Cdd:PRK13651 112 QFAeyqlfeqTIEKDIIFGpvsmgvsKEEAKKRAAKYIELVGL--DESYLQ--------RSPFELSGGQKRRVALAGILA 181
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767940955 91 QEKELYLLDDPLAAVDADVANHLLHrcILGML--SYTTRLLCTHRTEY-LERADAVLLMEAGRLIRAGPPSEIL 161
Cdd:PRK13651 182 MEPDFLVFDEPTAGLDPQGVKEILE--IFDNLnkQGKTIILVTHDLDNvLEWTKRTIFFKDGKIIKDGDTYDIL 253
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
590-792 |
4.67e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 46.03 E-value: 4.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 590 LTQGGVEFQDVVLAYRPGlPNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQlelAQLR 669
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNG-HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ---ALQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 670 SQLAIIPQ-EPFLFSGTVR-ENLDPQGLHKDRAlWQALKQCHLSEVITSMGGLDGELGEGGRS---LSLGQRQLLCLARA 744
Cdd:PRK15056 78 NLVAYVPQsEEVDWSFPVLvEDVVMMGRYGHMG-WLRRAKKRDRQIVTAALARVDMVEFRHRQigeLSGGQKKRVFLARA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767940955 745 LLTDAKILCIDEATASVDQKTD----QLLQQTickRFANKTVLTIAHRLNTI 792
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEariiSLLREL---RDEGKTMLVSTHNLGSV 205
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
74-160 |
4.95e-05 |
|
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: 45.57 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 74 TLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdVANHLLHRCILGMLSYTTRLLCTHRTEYLER-ADAVLLMEAGRLI 152
Cdd:cd03263 133 TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP-ASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
|
....*...
gi 767940955 153 RAGPPSEI 160
Cdd:cd03263 212 CIGSPQEL 219
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
75-161 |
5.05e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 45.81 E-value: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDAdVANHLLHRCILGMLSYTTRLLCTHRTEYLER-ADAVLLMEAGRLIR 153
Cdd:PRK14246 154 LSGGQQQRLTIARALALKPKVLLMDEPTSMIDI-VNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVE 232
|
....*...
gi 767940955 154 AGPPSEIL 161
Cdd:PRK14246 233 WGSSNEIF 240
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
46-161 |
5.38e-05 |
|
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: 45.51 E-value: 5.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 46 EVLEACALnDDLSILPAGdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRcILGM-LSY 124
Cdd:cd03219 126 ELLERVGL-ADLADRPAG----------ELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAEL-IRELrERG 193
|
90 100 110
....*....|....*....|....*....|....*...
gi 767940955 125 TTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 161
Cdd:cd03219 194 ITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVR 231
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1-155 |
6.39e-05 |
|
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: 45.34 E-value: 6.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 1 MLRGHVAVRG--LSKG-----FGLATQ-EPWIQFATIRDNILFGKTF-----DAQLYKEVLEACALNDDLSILPAGDQTE 67
Cdd:cd03234 62 TTSGQILFNGqpRKPDqfqkcVAYVRQdDILLPGLTVRETLTYTAILrlprkSSDAIRKKRVEDVLLRDLALTRIGGNLV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 68 VGekgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILGMLSYTTRL-LCT-H--RTEYLERADAV 143
Cdd:cd03234 142 KG-----ISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVS--TLSQLARRNRIvILTiHqpRSDLFRLFDRI 214
|
170
....*....|..
gi 767940955 144 LLMEAGRLIRAG 155
Cdd:cd03234 215 LLLSSGEIVYSG 226
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
72-161 |
6.56e-05 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 45.27 E-value: 6.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 72 GVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdVANHLLHRCILGMLSYTTRLLCTHRT--EYLERADAVLLMEAG 149
Cdd:PRK10895 135 GQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP-ISVIDIKRIIEHLRDSGLGVLITDHNvrETLAVCERAYIVSQG 213
|
90
....*....|..
gi 767940955 150 RLIRAGPPSEIL 161
Cdd:PRK10895 214 HLIAHGTPTEIL 225
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
72-163 |
7.12e-05 |
|
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: 44.83 E-value: 7.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 72 GVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDADvANHLLHRCILGMLSYTTR-LLCTHRTEYLE--RADAVLLMEA 148
Cdd:cd03217 102 NEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID-ALRLVAEVINKLREEGKSvLIITHYQRLLDyiKPDRVHVLYD 180
|
90
....*....|....*
gi 767940955 149 GRLIRAGPPSEILPL 163
Cdd:cd03217 181 GRIVKSGDKELALEI 195
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
74-110 |
8.01e-05 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 45.39 E-value: 8.01e-05
10 20 30
....*....|....*....|....*....|....*..
gi 767940955 74 TLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVA 110
Cdd:PRK09984 152 TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESA 188
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
74-155 |
8.06e-05 |
|
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: 44.58 E-value: 8.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 74 TLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdVANHLLHRCILGMLSY-TTRLLCTHRTEYLER-ADAVLLMEAGRL 151
Cdd:cd03269 128 ELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VNVELLKDVIRELARAgKTVILSTHQMELVEElCDRVLLLNKGRA 206
|
....
gi 767940955 152 IRAG 155
Cdd:cd03269 207 VLYG 210
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
75-155 |
8.61e-05 |
|
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: 44.67 E-value: 8.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLL----HRCILGmlsyTTRLLCTHRTEYLER-ADAVLLMEAG 149
Cdd:cd03266 137 FSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALRefirQLRALG----KCILFSTHIMQEVERlCDRVVVLHRG 212
|
....*.
gi 767940955 150 RLIRAG 155
Cdd:cd03266 213 RVVYEG 218
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
16-162 |
9.94e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 45.18 E-value: 9.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 16 GLATQEPWIQF--ATIRDNILFGKTFDA-------QLYKEVLEACALNDDLSILPAgdqtevgekgvTLSGGQRARIALA 86
Cdd:PRK13640 87 GIVFQNPDNQFvgATVGDDVAFGLENRAvprpemiKIVRDVLADVGMLDYIDSEPA-----------NLSGGQKQRVAIA 155
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767940955 87 RAVYQEKELYLLDDPLAAVDADVANHLLHRCI-LGMLSYTTRLLCTHRTEYLERADAVLLMEAGRLIRAGPPSEILP 162
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAGKEQILKLIRkLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
74-137 |
1.05e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 1.05e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767940955 74 TLSGGQRARIALARAVYQEKELYLLDDPlaavdadvANHLLHRCILGMLSYTTR-----LLCTHRTEYL 137
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEP--------TNHLDLHAVLWLETYLLKwpktfIVVSHAREFL 404
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
611-792 |
1.12e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 45.65 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 611 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIpqepflfsgtvrENL 690
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGI------------ENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 691 DPQGlhkdraLWQALKQCHLSEVITSMGGLDGE---LGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQK-TD 766
Cdd:PRK13545 107 ELKG------LMMGLTKEKIKEIIPEIIEFADIgkfIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTfTK 180
|
170 180
....*....|....*....|....*.
gi 767940955 767 QLLQQTICKRFANKTVLTIAHRLNTI 792
Cdd:PRK13545 181 KCLDKMNEFKEQGKTIFFISHSLSQV 206
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
76-160 |
1.20e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 44.96 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 76 SGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrciLGM-------LSYttrLLCTHRTEYLER-ADAVLLME 147
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLN---LMMdlqqelgLSY---VFISHDLSVVEHiADEVMVMY 229
|
90
....*....|...
gi 767940955 148 AGRLIRAGPPSEI 160
Cdd:PRK11308 230 LGRCVEKGTKEQI 242
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
74-117 |
1.21e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 44.02 E-value: 1.21e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 767940955 74 TLSGGQRARIALARAVYQEKELYLLDDPLAAVD----ADVANHLLHRC 117
Cdd:PRK13538 129 QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDkqgvARLEALLAQHA 176
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
627-809 |
1.22e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 44.45 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 627 IVGRTGSGKSSLLLVLFRLLEPS-----SGRVLLDGVD--TSQLELAQLRSQLAIIPQEPFLFSG-TVREN--------- 689
Cdd:PRK14267 35 LMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNiySPDVDPIEVRREVGMVFQYPNPFPHlTIYDNvaigvklng 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 690 -LDPQGLHKDRALWqALKQCHLSEVITSMGGLDGElgeggrSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQL 768
Cdd:PRK14267 115 lVKSKKELDERVEW-ALKKAALWDEVKDRLNDYPS------NLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAK 187
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767940955 769 LQQTICKRFANKTVLTIAHR-LNTILNSDRVLVLQAGRVVEL 809
Cdd:PRK14267 188 IEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEV 229
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
75-170 |
1.69e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 44.30 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILGMLSY--TTRLLCTHRTEYLER-ADAVLLMEAGRL 151
Cdd:PRK13639 138 LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMK--LLYDLNKegITIIISTHDVDLVPVyADKVYVMSDGKI 215
|
90
....*....|....*....
gi 767940955 152 IRAGPPSEILPLVQAVPKA 170
Cdd:PRK13639 216 IKEGTPKEVFSDIETIRKA 234
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
75-107 |
1.77e-04 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 44.08 E-value: 1.77e-04
10 20 30
....*....|....*....|....*....|...
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDA 107
Cdd:COG4525 135 LSGGMRQRVGIARALAADPRFLLMDEPFGALDA 167
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
74-147 |
1.97e-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: 42.91 E-value: 1.97e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767940955 74 TLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRCilgmlsytTRLLCT-----HRTEYLERADAVLLME 147
Cdd:cd03223 91 VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL--------KELGITvisvgHRPSLWKFHDRVLDLD 161
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
75-181 |
2.06e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 44.02 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILGMLSYT---TRLLCTHRTEYL-ERADAVLLMEAGR 150
Cdd:PRK13652 138 LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELID--FLNDLPETygmTVIFSTHQLDLVpEMADYIYVMDKGR 215
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 767940955 151 LIRAGPPSEI-------------LPLVQAVPKAWAENGQESDSA 181
Cdd:PRK13652 216 IVAYGTVEEIflqpdllarvhldLPSLPKLIRSLQAQGIAIDMA 259
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
615-806 |
2.73e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.34 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 615 VTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG---VDTSQLE--------LAQLRSQLAIIPQEPFLFS 683
Cdd:PRK10982 267 VSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGkkiNNHNANEainhgfalVTEERRSTGIYAYLDIGFN 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 684 ---GTVRENLDPQGLHKDRAL-----WqalkqchlseVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCID 755
Cdd:PRK10982 347 sliSNIRNYKNKVGLLDNSRMksdtqW----------VIDSMRVKTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLD 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767940955 756 EATASVDQKTD----QLLQQTICKrfaNKTVLTIAHRLNTILN-SDRVLVLQAGRV 806
Cdd:PRK10982 417 EPTRGIDVGAKfeiyQLIAELAKK---DKGIIIISSEMPELLGiTDRILVMSNGLV 469
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
41-161 |
2.86e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 43.36 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 41 AQLYKEVleacalNDDLSIlPAGdqtevgekgvTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAdVANHLLHRCILG 120
Cdd:PRK14247 130 AQLWDEV------KDRLDA-PAG----------KLSGGQQQRLCIARALAFQPEVLLADEPTANLDP-ENTAKIESLFLE 191
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 767940955 121 MLSYTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAGPPSEIL 161
Cdd:PRK14247 192 LKKDMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWGPTREVF 233
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
75-166 |
2.96e-04 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 43.47 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDA-------DVANHLLHRCILGMLSyttrllCTHRTEYLERADAVLLME 147
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQPDIIILDEATSMLDPrgrrevlETVRQLKEQKGITVLS------ITHDLDEAAQADRVIVMN 214
|
90
....*....|....*....
gi 767940955 148 AGRLIRAGPPSEILPLVQA 166
Cdd:PRK13635 215 KGEILEEGTPEEIFKSGHM 233
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
75-158 |
3.45e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 43.19 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLlhRCILGMLSY--TTRLLCTHRTEY-LERADAVLLMEAGRL 151
Cdd:PRK13647 139 LSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETL--MEILDRLHNqgKTVIVATHDVDLaAEWADQVIVLKEGRV 216
|
....*..
gi 767940955 152 IRAGPPS 158
Cdd:PRK13647 217 LAEGDKS 223
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-149 |
3.47e-04 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 44.03 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 20 QEPWIQFATIRDNILF---GKTFDAQLYKEVLEACALnDDLsilpAGDQTEVGEKGVTLSGGQRARIALARAVYQEKELY 96
Cdd:COG4178 433 QRPYLPLGTLREALLYpatAEAFSDAELREALEAVGL-GHL----AERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWL 507
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 767940955 97 LLDDPLAAVDADVANHLLHRcILGMLSYTTRLLCTHRTEYLERADAVLLMEAG 149
Cdd:COG4178 508 FLDEATSALDEENEAALYQL-LREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
75-151 |
4.30e-04 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 42.88 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILGMLSY---TTRLLCTHRTEYLERADAVLLMEAGRL 151
Cdd:PRK11629 146 LSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQ--LLGELNRlqgTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
67-106 |
4.81e-04 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 42.95 E-value: 4.81e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 767940955 67 EVGEkgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVD 106
Cdd:PRK15056 139 QIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
621-812 |
5.50e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.20 E-value: 5.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 621 PGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGtvrenldpqglhkdra 700
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 701 lwqalkqchlsevitsmggldgelgeggrslsLGQRQLlcLARALLTDAKILCIDEATASVDQKTDQLLQQTIC------ 774
Cdd:smart00382 65 --------------------------------LRLRLA--LALARKLKPDVLILDEITSLLDAEQEALLLLLEElrllll 110
|
170 180 190
....*....|....*....|....*....|....*....
gi 767940955 775 -KRFANKTVLTIAHRLNTILnsDRVLVLQAGRVVELDSP 812
Cdd:smart00382 111 lKSEKNLTVILTTNDEKDLG--PALLRRRFDRRIVLLLI 147
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
75-161 |
5.53e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 42.78 E-value: 5.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHlLHRCILGMLSYTTRLLCTHRTEYLER-ADAVLLMEAGRLIR 153
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEK-IEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVE 242
|
....*...
gi 767940955 154 AGPPSEIL 161
Cdd:PRK14271 243 EGPTEQLF 250
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
306-388 |
5.74e-04 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 42.89 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 306 APNGSSDIRFYLTVyATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVACAD 385
Cdd:cd18573 34 EIFGLSLKTFALAL-LGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVG 112
|
...
gi 767940955 386 DSL 388
Cdd:cd18573 113 KSL 115
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
622-812 |
6.18e-04 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 42.67 E-value: 6.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 622 GEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTVRENLDPQGLHKDRAL 701
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQELVARGRYPHQPL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 702 WQALKQCHLSEVITSMGGL--DGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVD--QKTDQLLQQTICKRF 777
Cdd:PRK10253 113 FTRWRKEDEEAVTKAMQATgiTHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDisHQIDLLELLSELNRE 192
|
170 180 190
....*....|....*....|....*....|....*.
gi 767940955 778 ANKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSP 812
Cdd:PRK10253 193 KGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAP 228
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
595-808 |
6.53e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 42.81 E-value: 6.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 595 VEFQDVVLAYRpglpnALDGVTFCVQPGEKLGIVGRTGSGKS-SLLLVLFRLLEPssGRVL-----LDGVDTSQLELAQL 668
Cdd:PRK11022 11 VHFGDESAPFR-----AVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMaekleFNGQDLQRISEKER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 669 R----SQLAIIPQEPFlfsgtvrENLDP---------------QG----LHKDRALwQALKQCHLSEVITSMggldgelG 725
Cdd:PRK11022 84 RnlvgAEVAMIFQDPM-------TSLNPcytvgfqimeaikvhQGgnkkTRRQRAI-DLLNQVGIPDPASRL-------D 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 726 EGGRSLSLGQRQLLCLARALLTDAKILCIDEATASVD-----QKTDQLLQqtiCKRFANKTVLTIAHRLNTILNS-DRVL 799
Cdd:PRK11022 149 VYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDvtiqaQIIELLLE---LQQKENMALVLITHDLALVAEAaHKII 225
|
....*....
gi 767940955 800 VLQAGRVVE 808
Cdd:PRK11022 226 VMYAGQVVE 234
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
74-155 |
6.61e-04 |
|
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: 41.79 E-value: 6.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 74 TLSGGQRARIALARAVYQEKELYLLDDPLAAVdaDVANHLLHRCILGMLSYT-TRLLCTHRTEYLER-ADAVLLMEAGRL 151
Cdd:cd03264 130 SLSGGMRRRVGIAQALVGDPSILIVDEPTAGL--DPEERIRFRNLLSELGEDrIVILSTHIVEDVESlCNQVAVLNKGKL 207
|
....
gi 767940955 152 IRAG 155
Cdd:cd03264 208 VFEG 211
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
51-107 |
7.31e-04 |
|
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: 41.71 E-value: 7.31e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767940955 51 CALNDDLSILPAGDQteVGEKGV------TLSGGQRARIALARAVYQEKELYLLDDPLAAVDA 107
Cdd:cd03231 98 HADHSDEQVEEALAR--VGLNGFedrpvaQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
71-161 |
7.47e-04 |
|
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: 42.04 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 71 KGVTLSGGQRARIALARAVYQEKELYLLDDP---LA-AVDADVANHLLHRCILGMlsytTRLLCTHR-TEYLERADAVLL 145
Cdd:cd03224 129 LAGTLSGGEQQMLAIARALMSRPKLLLLDEPsegLApKIVEEIFEAIRELRDEGV----TILLVEQNaRFALEIADRAYV 204
|
90
....*....|....*.
gi 767940955 146 MEAGRLIRAGPPSEIL 161
Cdd:cd03224 205 LERGRVVLEGTAAELL 220
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
75-161 |
8.08e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 42.71 E-value: 8.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRCI-LGMLSYTTRLLCTHR-TEYLERADAVLLMEAGRLI 152
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVkLQAKHQRTIVFISHDlDEAMRIGDRIAIMQNGEVV 244
|
....*....
gi 767940955 153 RAGPPSEIL 161
Cdd:PRK10070 245 QVGTPDEIL 253
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
606-807 |
8.20e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.79 E-value: 8.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 606 PGLpNALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG--VDTSQLELAqLRSQLAIIPQEPFLF- 682
Cdd:PRK10982 9 PGV-KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeIDFKSSKEA-LENGISMVHQELNLVl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 683 SGTVRENL-----DPQGLHKDRAlwqalKQCHLSEVITSMGGLDGELGEGGRSLSLGQRQLLCLARALLTDAKILCIDEA 757
Cdd:PRK10982 87 QRSVMDNMwlgryPTKGMFVDQD-----KMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767940955 758 TASVDQK-TDQLLqqTICKRFANK--TVLTIAHRLNTILN-SDRVLVLQAGRVV 807
Cdd:PRK10982 162 TSSLTEKeVNHLF--TIIRKLKERgcGIVYISHKMEEIFQlCDEITILRDGQWI 213
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
75-170 |
9.45e-04 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 41.92 E-value: 9.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLH--RCILGMLSYTtrLLCTHRTEYL-ERADAVLLMEAGRL 151
Cdd:PRK13638 137 LSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAiiRRIVAQGNHV--IISSHDIDLIyEISDAVYVLRQGQI 214
|
90
....*....|....*....
gi 767940955 152 IRAGPPSEILPLVQAVPKA 170
Cdd:PRK13638 215 LTHGAPGEVFACTEAMEQA 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
74-113 |
9.93e-04 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 42.74 E-value: 9.93e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 767940955 74 TLSGGQRARIALARAVYQEKELYLLDDPlaavdadvANHL 113
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEP--------TNHL 183
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
75-107 |
1.01e-03 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 41.61 E-value: 1.01e-03
10 20 30
....*....|....*....|....*....|...
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDA 107
Cdd:PRK11248 129 LSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
27-155 |
1.14e-03 |
|
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: 41.36 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 27 ATIRDNILFG-------KTFDAQLYKEVLEACALNDDLSiLPAGdqtevgekgvTLSGGQRARIALARAVYQEKELYLLD 99
Cdd:cd03220 99 LTGRENIYLNgrllglsRKEIDEKIDEIIEFSELGDFID-LPVK----------TYSSGMKARLAFAIATALEPDILLID 167
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767940955 100 DPLAAVDAdvanHLLHRC---ILGMLS-YTTRLLCTHRTEYLER-ADAVLLMEAGRLIRAG 155
Cdd:cd03220 168 EVLAVGDA----AFQEKCqrrLRELLKqGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
606-807 |
1.14e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 42.21 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 606 PGLPNAldgVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDG--VDTSQLELA---------QLRSQLAI 674
Cdd:PRK11288 266 PGLREP---ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRDAiragimlcpEDRKAEGI 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 675 IPqepflfSGTVRENLD--------PQGLHKDRALWQALKQCHlsevITSMGGLDGELGEGGRSLSLGQRQLLCLARALL 746
Cdd:PRK11288 343 IP------VHSVADNINisarrhhlRAGCLINNRWEAENADRF----IRSLNIKTPSREQLIMNLSGGNQQKAILGRWLS 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 747 TDAKILCIDEATASVD--QKTD------QLLQQTIckrfankTVLTIAHRLNTILN-SDRVLVLQAGRVV 807
Cdd:PRK11288 413 EDMKVILLDEPTRGIDvgAKHEiynviyELAAQGV-------AVLFVSSDLPEVLGvADRIVVMREGRIA 475
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
60-113 |
1.36e-03 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 42.23 E-value: 1.36e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 767940955 60 LPAGDQtevgeKGVTLSGGQRARIALARAVYQEKELYLLDDPLAAVDAD-VA---NHL 113
Cdd:TIGR03719 152 CPPWDA-----DVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAEsVAwleRHL 204
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
76-114 |
1.55e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 42.00 E-value: 1.55e-03
10 20 30
....*....|....*....|....*....|....*....
gi 767940955 76 SGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLL 114
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQIL 465
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
611-820 |
1.63e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 41.71 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 611 ALDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEP----SSGRVLLDGVDTSQLELAQLRS----QLAIIPQEPflf 682
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPRERRKlvghNVSMIFQEP--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 683 sgtvRENLDP---------QGL----HKDRaLWQALKQCHLSEVITSMGGLDGELGEGGRS----LSLGQRQLLCLARAL 745
Cdd:PRK15093 99 ----QSCLDPservgrqlmQNIpgwtYKGR-WWQRFGWRKRRAIELLHRVGIKDHKDAMRSfpyeLTEGECQKVMIAIAL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 746 LTDAKILCIDEATASVDQKTdqllQQTICKRFA------NKTVLTIAHRLNTILN-SDRVLVLQAGRVVELDSPATLRNQ 818
Cdd:PRK15093 174 ANQPRLLIADEPTNAMEPTT----QAQIFRLLTrlnqnnNTTILLISHDLQMLSQwADKINVLYCGQTVETAPSKELVTT 249
|
..
gi 767940955 819 PH 820
Cdd:PRK15093 250 PH 251
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
316-382 |
1.77e-03 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 41.38 E-value: 1.77e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767940955 316 YLTVYATIAGVNSLCTLLRAVLFAAGTLQAAATLHRRLLHRVLMAPVTFFNATPTGRILNRFSSDVA 382
Cdd:cd07346 41 IALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVD 107
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
612-813 |
2.48e-03 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 40.58 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 612 LDGVTFCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPS--------SGRVLLDGVDTSQLE---LAQLRSQLAIIPQEPF 680
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDaprLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 681 LFSgtVRE----------NLDPQGLHKDRAL-WQALkqchlsevitSMGGLDGELGEGGRSLSLGQRQLLCLARAL---- 745
Cdd:PRK13547 97 AFS--AREivllgryphaRRAGALTHRDGEIaWQAL----------ALAGATALVGRDVTTLSGGELARVQFARVLaqlw 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767940955 746 -----LTDAKILCIDEATASVDQKTDQLLQQTI--CKRFANKTVLTIAHRLN-TILNSDRVLVLQAGRVVELDSPA 813
Cdd:PRK13547 165 pphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVrrLARDWNLGVLAIVHDPNlAARHADRIAMLADGAIVAHGAPA 240
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
45-163 |
2.55e-03 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 41.19 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 45 KEVLEacalndDLSILPAGDqTEVGEKGVT--LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLhRCILGML 122
Cdd:TIGR00955 142 DEVLQ------ALGLRKCAN-TRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVV-QVLKGLA 213
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 767940955 123 SYTTRLLCT-HR--TEYLERADAVLLMEAGRLIRAGPPSEILPL 163
Cdd:TIGR00955 214 QKGKTIICTiHQpsSELFELFDKIILMAEGRVAYLGSPDQAVPF 257
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
75-155 |
2.73e-03 |
|
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: 39.84 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHrcILGMLSYTTR-LLCT-H--RTEYLERADAVLLMEAGR 150
Cdd:cd03213 112 LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS--LLRRLADTGRtIICSiHqpSSEIFELFDKLLLLSQGR 189
|
....*
gi 767940955 151 LIRAG 155
Cdd:cd03213 190 VIYFG 194
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
74-161 |
2.95e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 40.30 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 74 TLSGGQRARIALARAVYQ-------EKELYLLDDPLAAVD-ADVA--NHLLHR-CILGMlsytTRLLCTH---RTeyLER 139
Cdd:PRK03695 126 QLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDvAQQAalDRLLSElCQQGI----AVVMSSHdlnHT--LRH 199
|
90 100
....*....|....*....|..
gi 767940955 140 ADAVLLMEAGRLIRAGPPSEIL 161
Cdd:PRK03695 200 ADRVWLLKQGKLLASGRRDEVL 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
45-151 |
3.00e-03 |
|
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: 40.08 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 45 KEVLEACALNDDLSILPAGdqtevgekgvtLSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLHRCILGMLSY 124
Cdd:cd03292 118 PAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAG 186
|
90 100
....*....|....*....|....*...
gi 767940955 125 TTRLLCTHRTEYLERADA-VLLMEAGRL 151
Cdd:cd03292 187 TTVVVATHAKELVDTTRHrVIALERGKL 214
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
74-106 |
3.28e-03 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 40.08 E-value: 3.28e-03
10 20 30
....*....|....*....|....*....|...
gi 767940955 74 TLSGGQRARIALARAVYQEKELYLLDDPLAAVD 106
Cdd:cd03237 115 ELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
75-161 |
3.52e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 40.22 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLhRCILGMLSYT--TRLLCTHRTEYLE-RADAVLLMEAGRL 151
Cdd:PRK13636 142 LSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIM-KLLVEMQKELglTIIIATHDIDIVPlYCDNVFVMKEGRV 220
|
90
....*....|
gi 767940955 152 IRAGPPSEIL 161
Cdd:PRK13636 221 ILQGNPKEVF 230
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
28-106 |
4.86e-03 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 39.63 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 28 TIRDNILFG--------KTFDAQLYKEVLEACALNDdlsilpagdqtEV----GEKGVTLSGGQRARIALARAVYQEKEL 95
Cdd:COG1117 107 SIYDNVAYGlrlhgiksKSELDEIVEESLRKAALWD-----------EVkdrlKKSALGLSGGQQQRLCIARALAVEPEV 175
|
90
....*....|.
gi 767940955 96 YLLDDPLAAVD 106
Cdd:COG1117 176 LLMDEPTSALD 186
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
20-117 |
5.81e-03 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 40.12 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 20 QEPWIQFATIRDNIL--------FGKTFDAQLYKEVLEACALNDDLsilpagdQTEVGEKGV-----TLSGGQRARIALA 86
Cdd:TIGR00954 522 QRPYMTLGTLRDQIIypdssedmKRRGLSDKDLEQILDNVQLTHIL-------EREGGWSAVqdwmdVLSGGEKQRIAMA 594
|
90 100 110
....*....|....*....|....*....|.
gi 767940955 87 RAVYQEKELYLLDDPLAAVDADVANHLLHRC 117
Cdd:TIGR00954 595 RLFYHKPQFAILDECTSAVSVDVEGYMYRLC 625
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
75-106 |
6.00e-03 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 39.71 E-value: 6.00e-03
10 20 30
....*....|....*....|....*....|..
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVD 106
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
651-806 |
6.07e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 39.38 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 651 GRVLLDGVD--TSQLELAQLRSQLAIIPQEPFLFSGTVRENL-------DPQGlHKDRALWQALKQCHL-SEVITSMGGL 720
Cdd:PRK14243 70 GKVTFHGKNlyAPDVDPVEVRRRIGMVFQKPNPFPKSIYDNIaygarinGYKG-DMDELVERSLRQAALwDEVKDKLKQS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 721 DGelgeggrSLSLGQRQLLCLARALLTDAKILCIDEATASVDQ----KTDQLLQQtICKRFankTVLTIAHRLNtilnsd 796
Cdd:PRK14243 149 GL-------SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPistlRIEELMHE-LKEQY---TIIIVTHNMQ------ 211
|
170
....*....|
gi 767940955 797 rvlvlQAGRV 806
Cdd:PRK14243 212 -----QAARV 216
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
619-800 |
6.08e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 40.15 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 619 VQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDgvdtsqlelaqLRsqLAIIPQ--EPFlFSGTVRENLDpqGLH 696
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-----------LK--ISYKPQyiSPD-YDGTVEEFLR--SAN 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 697 KDR---ALWQA-------LKQCHLSEVitsmggldgelgeggRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKtD 766
Cdd:COG1245 427 TDDfgsSYYKTeiikplgLEKLLDKNV---------------KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE-Q 490
|
170 180 190
....*....|....*....|....*....|....*...
gi 767940955 767 QLLQQTICKRFA---NKTVLTIAHRLNTI-LNSDRVLV 800
Cdd:COG1245 491 RLAVAKAIRRFAenrGKTAMVVDHDIYLIdYISDRLMV 528
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
618-807 |
6.15e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 40.48 E-value: 6.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 618 CVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPS----SGRVLLDGVDTSQLElAQLRSQLAIIPQE----PFLfsgTVREN 689
Cdd:TIGR00956 83 LIKPGELTVVLGRPGSGCSTLLKTIASNTDGFhigvEGVITYDGITPEEIK-KHYRGDVVYNAETdvhfPHL---TVGET 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 690 LD-----------PQGLHKD------RALWQA---LKQCHLSEVITSMGgldgelgeggRSLSLGQRQLLCLARALLTDA 749
Cdd:TIGR00956 159 LDfaarcktpqnrPDGVSREeyakhiADVYMAtygLSHTRNTKVGNDFV----------RGVSGGERKRVSIAEASLGGA 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767940955 750 KILCIDEATASVDQKTD----QLLQqtICKRFANKTVLTIAHRL--NTILNSDRVLVLQAGRVV 807
Cdd:TIGR00956 229 KIQCWDNATRGLDSATAlefiRALK--TSANILDTTPLVAIYQCsqDAYELFDKVIVLYEGYQI 290
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
75-152 |
7.07e-03 |
|
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: 38.85 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDAdVANHLLHRCI--LGMLSYTTRLLCTHRTEYLER-ADAVLLMEAGRL 151
Cdd:cd03267 154 LSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV-VAQENIRNFLkeYNRERGTTVLLTSHYMKDIEAlARRVLVIDKGRL 232
|
.
gi 767940955 152 I 152
Cdd:cd03267 233 L 233
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
28-108 |
7.15e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 38.70 E-value: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 28 TIRDNILFGKTFDAQLYKEVLEA-CALN-DDLSILPAGDqtevgekgvtLSGGQRARIALARAVYQEKELYLLDDPLAAV 105
Cdd:PRK13539 89 TVAENLEFWAAFLGGEELDIAAAlEAVGlAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
...
gi 767940955 106 DAD 108
Cdd:PRK13539 159 DAA 161
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
75-160 |
8.08e-03 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 39.40 E-value: 8.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVAnhllhRCILGMLSYTTR------LLCTHRTEYLER-ADAVLLME 147
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPKVLLCDEATSALDPATT-----RSILELLKDINRelgltiVLITHEMDVVKRiCDRVAVID 215
|
90
....*....|...
gi 767940955 148 AGRLIRAGPPSEI 160
Cdd:PRK11153 216 AGRLVEQGTVSEV 228
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
73-146 |
8.25e-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: 38.11 E-value: 8.25e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767940955 73 VTLSGGQRARIALARAV----YQEKELYLLDDPLAAVDADVANHLLHRCILGMLSYTTRLLCTHRTEYLERADAVLLM 146
Cdd:cd03227 76 LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHI 153
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
617-773 |
8.62e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 38.68 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 617 FCVQPGEKLGIVGRTGSGKSSLLLVLFRLLEPSSGRVLLDGVDTSQLELAQLRSQLAIIPQEPFLFSGTvrENLD----P 692
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTL--ENLHflcgL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 693 QGLHKDRALWQALKQCHLSEVITSMggldgelgegGRSLSLGQRQLLCLARALLTDAKILCIDEATASVDQKTDQLLQQT 772
Cdd:PRK13543 110 HGRRAKQMPGSALAIVGLAGYEDTL----------VRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRM 179
|
.
gi 767940955 773 I 773
Cdd:PRK13543 180 I 180
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
75-170 |
9.01e-03 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 39.71 E-value: 9.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDPLAAVDADVANHLLhrCILGMLSYT--TRLLCTHRTEYLERADAVLLMEAGRLI 152
Cdd:PRK10535 145 LSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVM--AILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
90
....*....|....*...
gi 767940955 153 RaGPPSEILPLVQAVPKA 170
Cdd:PRK10535 223 R-NPPAQEKVNVAGGTEP 239
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
75-151 |
9.15e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 39.57 E-value: 9.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767940955 75 LSGGQRARIALARAVYQEKELYLLDDplAAVDAD-VANHLLHRCILGMLSYT--TRLLCTHRTEYLERADAVLLMEAGRL 151
Cdd:PRK10522 450 LSKGQKKRLALLLALAEERDILLLDE--WAADQDpHFRREFYQVLLPLLQEMgkTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
74-108 |
9.96e-03 |
|
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: 38.11 E-value: 9.96e-03
10 20 30
....*....|....*....|....*....|....*
gi 767940955 74 TLSGGQRARIALARAVYQEKELYLLDDPLAAVDAD 108
Cdd:TIGR01189 127 QLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
|
| |
