|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
231-1471 |
0e+00 |
|
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: 833.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 231 PFSNAGFLSHVSFSWMSPLIVLGNEKIIDSEDVPQVDNSDRAEKLFWIFRSKleWDDGERRITTYK-------------- 296
Cdd:TIGR00957 203 PESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVEN--WKKECKKTRKQPvsavygkkdpskpk 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 297 --------------------------LIKALFFSVWRDILLSTLFAFVYTVSCYVAPYLMDTFVQYLNGQRQYSNQGVVL 350
Cdd:TIGR00957 281 gssqldaneevealivksphkprkpsLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFVNDPMAPDWQGYFY 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 351 VTTFFVAKLVECQARRNWYFRLQKAGIGMRSVLVSMIYEKGLTLPCYSKQGHTSGEIINLMTVDAERISAFSWYMHDPWI 430
Cdd:TIGR00957 361 TGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWS 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 431 LVLQISLALLILYRSLGLGSIAAFAATFLVMLGNIPLAKLEEKFQGNLMESKDNRMKKTSEALLNMRILKLQGWEMKFLH 510
Cdd:TIGR00957 441 APLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLD 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 511 KILDLRGIEAGWLKKFVYnSAAISSVLWAAPSFVSATAFGACMLLKIP---LESGKIIAALATFRILQTPIYKLPDTISM 587
Cdd:TIGR00957 521 KVEGIRQEELKVLKKSAY-LHAVGTFTWVCTPFLVALITFAVYVTVDEnniLDAEKAFVSLALFNILRFPLNILPMVISS 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 588 IVQTKVSLDRIATFLCLDDLQQDGMERLP-SGSSKMDVEVSNGAFSWDDSSPiPTLKDIRFKIPHGMNIAICGTVGSGKS 666
Cdd:TIGR00957 600 IVQASVSLKRLRIFLSHEELEPDSIERRTiKPGEGNSITVHNATFTWARDLP-PTLNGITFSIPEGALVAVVGQVGCGKS 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 667 SLLSSILGEVPKISGNLKVCGRKAYIAQSPWIQSGKVEENILFGKPMQREWYQRVLEACSLNKDLEVFPFRDQTVIGERG 746
Cdd:TIGR00957 679 SLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKG 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 747 INLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEVL--LGLLRNKTVIYVTHQLEFLPEADLILVMKDGR 824
Cdd:TIGR00957 759 VNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGK 838
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 825 ITQAGKYNEILESGTDFMELVGAHTDALAAVDSYEKGSASaQSTTSKESKVSND-------------------------- 878
Cdd:TIGR00957 839 ISEMGSYQELLQRDGAFAEFLRTYAPDEQQGHLEDSWTAL-VSGEGKEAKLIENgmlvtdvvgkqlqrqlsasssdsgdq 917
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 879 -------EEKQEEDLPSPKGQLVQEEEREKGKVGFTVYQKYMKlAYGGALVPIILVVQILFQVLNIGSNYWM-AWVTpvs 950
Cdd:TIGR00957 918 srhhgssAELQKAEAKEETWKLMEADKAQTGQVELSVYWDYMK-AIGLFITFLSIFLFVCNHVSALASNYWLsLWTD--- 993
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 951 kdvKPLVSG-----STLILVYVFLATASSFCILVRAMLSAMTGFKIATELFNQMHFRIFRASMSFFDATPIGRILNRAST 1025
Cdd:TIGR00957 994 ---DPMVNGtqnntSLRLSVYGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSK 1070
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1026 DQSAVDLRLPSQFSNLAIAAVNILGIIGVMGQVAWQVLIVFIPVIAACTWYRQYYISAARELARLSGISRSPLVQHFSET 1105
Cdd:TIGR00957 1071 ELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNET 1150
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1106 LSGITTIRSFDQEPRFRTDIMRLNDCYSRLRFHAISAMEWLCFRLDLLST--VAFAlslVILVSVPEGVINPSFAGLAVT 1183
Cdd:TIGR00957 1151 LLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNciVLFA---ALFAVISRHSLSAGLVGLSVS 1227
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1184 YALNLNSLQATLIWTLCDLENKMISVERMLQYIDIPSEPSLVIESTRPEKSWPCRGEITICNLQVRYGPHLPMVLRGLTC 1263
Cdd:TIGR00957 1228 YSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSGWPPRGRVEFRNYCLRYREDLDLVLRHINV 1307
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1264 TFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSIIPQEPTMFEGTVRSNLDPLEEYA 1343
Cdd:TIGR00957 1308 TIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYS 1387
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1344 DDQIWEALDKCQLGDEIRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLRQH 1423
Cdd:TIGR00957 1388 DEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQ 1467
|
1290 1300 1310 1320
....*....|....*....|....*....|....*....|....*...
gi 30682486 1424 FSGCTVITIAHRISSVIDSDMVLLLDQGLIEEHDSPARLLEDKSSSFS 1471
Cdd:TIGR00957 1468 FEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYS 1515
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
225-1488 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 811.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 225 DDEVVTPFSNAGFLSHVSFSWMSPLIVLGNEKIIDSEDVPQVDNSDRAEKLFWIFRSKleWDDgERRITTYKLIKALFFS 304
Cdd:PLN03130 222 GGEQICPERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKC--WDE-ELKKPKPWLLRALNNS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 305 VWRDILLSTLFAFVYTVSCYVAPYLMDTFVQYLNgQRQYSNQGVVLVTTFFVAKL--VECQARrnwYFR-LQKAGIGMRS 381
Cdd:PLN03130 299 LGGRFWLGGFFKIGNDLSQFVGPLLLNLLLESMQ-NGEPAWIGYIYAFSIFVGVVlgVLCEAQ---YFQnVMRVGFRLRS 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 382 VLVSMIYEKGLTLPCYSKQGHTSGEIINLMTVDAERISAFSWYMHDPWILVLQISLALLILYRSLGLGSIaaFAATFLVM 461
Cdd:PLN03130 375 TLVAAVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASL--IGSLMLVL 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 462 LgnIPLAKL----EEKFQGNLMESKDNRMKKTSEALLNMRILKLQGWEMKFLHKILDLRGIEAGWLKKFVYNSAAISSVL 537
Cdd:PLN03130 453 M--FPIQTFiiskMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSFIL 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 538 WAAPSFVSATAFGACMLLKIPLESGKIIAALATFRILQTPIYKLPDTISMIVQTKVSLDRIATFLCLDdlqqdgmERLPS 617
Cdd:PLN03130 531 NSIPVLVTVVSFGVFTLLGGDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLLAE-------ERVLL 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 618 GSSKMD-----VEVSNGAFSWDDSSPIPTLKDIRFKIPHGMNIAICGTVGSGKSSLLSSILGEVPKIS-GNLKVCGRKAY 691
Cdd:PLN03130 604 PNPPLEpglpaISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGTVAY 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 692 IAQSPWIQSGKVEENILFGKPMQREWYQRVLEACSLNKDLEVFPFRDQTVIGERGINLSGGQKQRIQIARALYQDADIYL 771
Cdd:PLN03130 684 VPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYI 763
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 772 FDDPFSAVDAHTGSHLFKEVLLGLLRNKTVIYVTHQLEFLPEADLILVMKDGRITQAGKYNEILESGTDF---MELVGAH 848
Cdd:PLN03130 764 FDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFqklMENAGKM 843
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 849 TDAlaavdSYEKGSASAQSTTSK--ESKVSNDEEKQEEDLPSPKGQ---LVQEEEREKGKVGFTVYQKYmKLAYGGALVP 923
Cdd:PLN03130 844 EEY-----VEENGEEEDDQTSSKpvANGNANNLKKDSSSKKKSKEGksvLIKQEERETGVVSWKVLERY-KNALGGAWVV 917
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 924 IILVV-QILFQVLNIGSNYWMA-WVTP-VSKDVKPLVsgstLILVYVFLATASSFCILVRAMLSAMTGFKIATELFNQMH 1000
Cdd:PLN03130 918 MILFLcYVLTEVFRVSSSTWLSeWTDQgTPKTHGPLF----YNLIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAML 993
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1001 FRIFRASMSFFDATPIGRILNRASTDQSAVDlRLPSQFSNLAIAAVNIL----GIIGVMGQVA-WQVLIVFIPVIAACTw 1075
Cdd:PLN03130 994 GSILRAPMSFFHTNPLGRIINRFAKDLGDID-RNVAVFVNMFLGQIFQLlstfVLIGIVSTISlWAIMPLLVLFYGAYL- 1071
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1076 yrqYYISAARELARLSGISRSPLVQHFSETLSGITTIRSFDQEPRFRTDIMRLNDCYSRLRFHAISAMEWLCFRLDLLST 1155
Cdd:PLN03130 1072 ---YYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTLVNMSSNRWLAIRLETLGG 1148
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1156 VAFALSLVILVSVPEGVINP-SFA---GLAVTYALNLNSLQATLIWTLCDLENKMISVERMLQYIDIPSEPSLVIESTRP 1231
Cdd:PLN03130 1149 LMIWLTASFAVMQNGRAENQaAFAstmGLLLSYALNITSLLTAVLRLASLAENSLNAVERVGTYIDLPSEAPLVIENNRP 1228
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1232 EKSWPCRGEITICNLQVRYGPHLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGL 1311
Cdd:PLN03130 1229 PPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGL 1308
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1312 HDLRSRLSIIPQEPTMFEGTVRSNLDPLEEYADDQIWEALDKCQLGDEIRKKELKLDSPVSENGQNWSVGQRQLVCLGRV 1391
Cdd:PLN03130 1309 MDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARA 1388
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1392 LLKRSKVLILDEATASVDTATDTLIQETLRQHFSGCTVITIAHRISSVIDSDMVLLLDQGLIEEHDSPARLLEDKSSSFS 1471
Cdd:PLN03130 1389 LLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFS 1468
|
1290
....*....|....*..
gi 30682486 1472 KLVaEYTASSDSRFKRS 1488
Cdd:PLN03130 1469 KMV-QSTGAANAQYLRS 1484
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
34-1474 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 760.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 34 LVMFGSCVYKKRLGWENSDAfTNERFKDMSLTYNKLVVICCETLSALNSVLLLLSCFNLHkngwDRSEL--MILLDLLFT 111
Cdd:PLN03232 44 SVLLGLCFYRIWIILDNAKA-QIYVLRKKYYNCVLGILACYCVVEPVLRLVMGISLFDMD----EETDLppFEVASLMVE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 112 ALSWGAISFYIRSQfTYSHDQKFPILLRvWWVLYFMFSCYRLLvDIALYKKQELVSVHLLLSDVLAVSVGLF----LCYs 187
Cdd:PLN03232 119 AFAWFSMLVLIGLE-TKQYVKEFRWYVR-FGVVYVLVADAVLL-DLVLPLKNSINRTALYLCISSRCCQALFgillLVY- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 188 clqkqgqgerINLLLEEPLLNGAESSAATSVQLDKAEDDEVVTPFSNAGFLSHVSFSWMSPLIVLGNEKIIDSEDVPQVD 267
Cdd:PLN03232 195 ----------IPELDPYPGYHILNNESLDNVEYDALRGGENICPERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 268 NSDRAEKLfwIFRSKLEWDDGERRITTYkLIKALFFSVWRDILLSTLFAFVYTVSCYVAPYLMDTFVQYL-NGQRQYSNQ 346
Cdd:PLN03232 265 QWDQTETL--IKRFQRCWTEESRRPKPW-LLRALNNSLGGRFWLGGIFKIGHDLSQFVGPVILSHLLQSMqEGDPAWVGY 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 347 GVVLVTTFFVAKLVECQARrnWYFRLQKAGIGMRSVLVSMIYEKGLTLPCYSKQGHTSGEIINLMTVDAERISAFSWYMH 426
Cdd:PLN03232 342 VYAFLIFFGVTFGVLCESQ--YFQNVGRVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLH 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 427 DPWILVLQISLALLILYRSLGLGSIaaFAATFLVMLgnIPLAKL----EEKFQGNLMESKDNRMKKTSEALLNMRILKLQ 502
Cdd:PLN03232 420 GLWSAPFRIIVSMVLLYQQLGVASL--FGSLILFLL--IPLQTLivrkMRKLTKEGLQWTDKRVGIINEILASMDTVKCY 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 503 GWEMKFLHKILDLRGIEAGWLKKFVYNSAAISSVLWAAPSFVSATAFGACMLLKIPLESGKIIAALATFRILQTPIYKLP 582
Cdd:PLN03232 496 AWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLP 575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 583 DTISMIVQTKVSLDRIATFLCLDDLQQDGMERLPSGSSKMDVEvsNGAFSWDDSSPIPTLKDIRFKIPHGMNIAICGTVG 662
Cdd:PLN03232 576 NLLSQVVNANVSLQRIEELLLSEERILAQNPPLQPGAPAISIK--NGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTG 653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 663 SGKSSLLSSILGEVPKI-SGNLKVCGRKAYIAQSPWIQSGKVEENILFGKPMQREWYQRVLEACSLNKDLEVFPFRDQTV 741
Cdd:PLN03232 654 EGKTSLISAMLGELSHAeTSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTE 733
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 742 IGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEVLLGLLRNKTVIYVTHQLEFLPEADLILVMK 821
Cdd:PLN03232 734 IGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVS 813
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 822 DGRITQAGKYNEILESGTDFMELVGAHTDALAAVDSYEKGSASAQSTTSKESKVSNDEEKQEEDLPSPKGQLVQEEEREK 901
Cdd:PLN03232 814 EGMIKEEGTFAELSKSGSLFKKLMENAGKMDATQEVNTNDENILKLGPTVTIDVSERNLGSTKQGKRGRSVLVKQEERET 893
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 902 GKVGFTVYQKYMKLAYGGALVPIILVVQILFQVLNIGSNYWMAWVT--PVSKDVKPlvsgSTLILVYVFLATASSFCILV 979
Cdd:PLN03232 894 GIISWNVLMRYNKAVGGLWVVMILLVCYLTTEVLRVSSSTWLSIWTdqSTPKSYSP----GFYIVVYALLGFGQVAVTFT 969
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 980 RAMLSAMTGFKIATELFNQMHFRIFRASMSFFDATPIGRILNRASTDQSAVD---LRLPSQFSNLAIAAVNILGIIGVMG 1056
Cdd:PLN03232 970 NSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDrnvANLMNMFMNQLWQLLSTFALIGTVS 1049
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1057 QVA-WQVLIVFIPVIAACTwyrqYYISAARELARLSGISRSPLVQHFSETLSGITTIRSFDQEPRFRTDIMRLNDCYSRL 1135
Cdd:PLN03232 1050 TISlWAIMPLLILFYAAYL----YYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRF 1125
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1136 RFHAISAMEWLCFRLDLLSTVAFALSLVILV----SVPEGVINPSFAGLAVTYALNLNSLQATLIWTLCDLENKMISVER 1211
Cdd:PLN03232 1126 TLANTSSNRWLTIRLETLGGVMIWLTATFAVlrngNAENQAGFASTMGLLLSYTLNITTLLSGVLRQASKAENSLNSVER 1205
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1212 MLQYIDIPSEPSLVIESTRPEKSWPCRGEITICNLQVRYGPHLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRI 1291
Cdd:PLN03232 1206 VGNYIDLPSEATAIIENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRI 1285
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1292 VEPAAGEIRIDGINILTIGLHDLRSRLSIIPQEPTMFEGTVRSNLDPLEEYADDQIWEALDKCQLGDEIRKKELKLDSPV 1371
Cdd:PLN03232 1286 VELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEV 1365
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1372 SENGQNWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLRQHFSGCTVITIAHRISSVIDSDMVLLLDQG 1451
Cdd:PLN03232 1366 SEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSG 1445
|
1450 1460
....*....|....*....|...
gi 30682486 1452 LIEEHDSPARLLEDKSSSFSKLV 1474
Cdd:PLN03232 1446 QVLEYDSPQELLSRDTSAFFRMV 1468
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
297-1474 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 597.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 297 LIKALFFSVWRDILLSTLFAFVYTVSCYVAPYLMDTFVQYLNGQRQYSNQGVVLVTTFFVAKLVECQARRNWYFRLQKAG 376
Cdd:PTZ00243 234 LLRTLFAALPYYVWWQIPFKLLSDVCTLTLPVLLKYFVKFLDADNATWGRGLGLVLTLFLTQLIQSVCLHRFYYISIRCG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 377 IGMRSVLVSMIYEKGLTLPCYSKQ--GHTSGEIINLMTVDAERISAFSWYMHDPWILVLQISLALLILYRSLGLGSIAAF 454
Cdd:PTZ00243 314 LQYRSALNALIFEKCFTISSKSLAqpDMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWCALMAV 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 455 AATFLVMLGNIPLAKLEEKFQGNLMESKDNRMKKTSEALLNMRILKLQGWEMKFLHKILDLRGIEAGWLKKFVYNSAAIS 534
Cdd:PTZ00243 394 AVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLARVATS 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 535 SVLWAAPSFVSATAFGACMLLKIPLESGKIIAALATFRILQTPIYKLPDTISMIVQTKVSLDRIATFLCLDDLQ----QD 610
Cdd:PTZ00243 474 FVNNATPTLMIAVVFTVYYLLGHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTFLECDNATcstvQD 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 611 GME-----------------------------RLP-----------------------------------------SGSS 620
Cdd:PTZ00243 554 MEEywreqrehstacqlaavlenvdvtafvpvKLPrapkvktsllsralrmlcceqcrptkrhpspsvvvedtdygSPSS 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 621 KMDVEVSNGAFSWDDSSPIPT---------------------LKDIRFKIPHGMNIAICGTVGSGKSSLLSSILGEVPKI 679
Cdd:PTZ00243 634 ASRHIVEGGTGGGHEATPTSErsaktpkmktddffelepkvlLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEIS 713
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 680 SGNLKVCGRKAYIAQSPWIQSGKVEENILFGKPMQREWYQRVLEACSLNKDLEVFPFRDQTVIGERGINLSGGQKQRIQI 759
Cdd:PTZ00243 714 EGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSL 793
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 760 ARALYQDADIYLFDDPFSAVDAHTGSHLFKEVLLGLLRNKTVIYVTHQLEFLPEADLILVMKDGRITQAGKYNEILES-- 837
Cdd:PTZ00243 794 ARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTsl 873
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 838 -------GTDFMELVGAHTDALAAVDSYEKGSASAqSTTSKESKVSNDEEKQEEDLPSPKGQLVQEEEREKGKVGFTVYQ 910
Cdd:PTZ00243 874 yatlaaeLKENKDSKEGDADAEVAEVDAAPGGAVD-HEPPVAKQEGNAEGGDGAALDAAAGRLMTREEKASGSVPWSTYV 952
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 911 KYMKLAYGGALVPIILVVQILFQVLNIGSNYWMA-WVTPVSKdvkplVSGSTLILVYVFLATASSFCILVRAMLSamtgF 989
Cdd:PTZ00243 953 AYLRFCGGLHAAGFVLATFAVTELVTVSSGVWLSmWSTRSFK-----LSAATYLYVYLGIVLLGTFSVPLRFFLS----Y 1023
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 990 KIATELFNQMHFRIFR----ASMSFFDATPIGRILNRASTDQSAVDLRLPSQFSNLAIAAVNILGIIGVMGQVAWQVLIV 1065
Cdd:PTZ00243 1024 EAMRRGSRNMHRDLLRsvsrGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVA 1103
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1066 FIPViaACTWYR--QYYISAARELARLSGISRSPLVQHFSETLSGITTIRSFD------QEPRFRTDIMrlndcysrlrf 1137
Cdd:PTZ00243 1104 LVPC--GYLYYRlmQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGkahlvmQEALRRLDVV----------- 1170
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1138 HAISAME-----WLCFRLDLLSTV---AFALSLVILVSVPEGVINPSFAGLAVTYALNLNslqATLIWTL---CDLENKM 1206
Cdd:PTZ00243 1171 YSCSYLEnvanrWLGVRVEFLSNIvvtVIALIGVIGTMLRATSQEIGLVSLSLTMAMQTT---ATLNWLVrqvATVEADM 1247
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1207 ISVERMLQYID-IPSE--PSL---------------------VIESTRPEKSWP---CRGEITICNLQVRYGPHLPMVLR 1259
Cdd:PTZ00243 1248 NSVERLLYYTDeVPHEdmPELdeevdalerrtgmaadvtgtvVIEPASPTSAAPhpvQAGSLVFEGVQMRYREGLPLVLR 1327
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1260 GLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSIIPQEPTMFEGTVRSNLDPL 1339
Cdd:PTZ00243 1328 GVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPF 1407
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1340 EEYADDQIWEALDKCQLGDEIRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVLIL-DEATASVDTATDTLIQE 1418
Cdd:PTZ00243 1408 LEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQA 1487
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|....*.
gi 30682486 1419 TLRQHFSGCTVITIAHRISSVIDSDMVLLLDQGLIEEHDSPARLLEDKSSSFSKLV 1474
Cdd:PTZ00243 1488 TVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMV 1543
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
230-1467 |
2.30e-140 |
|
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: 469.39 E-value: 2.30e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 230 TPFSNAGFLSHVSFSWMSPLIVLGNEKIIDSEDVPQVDNSDRAEKLFWifRSKLEWDdgeRRITTYK----LIKAL---F 302
Cdd:TIGR01271 4 SPVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSE--RLEREWD---RELASAKknpkLLNALrrcF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 303 FsvWRDILLSTLFAFVyTVSCYVAPYLMDTFVQYLNGQRQYS-NQGVVL---VTTFFVAKLVECQARrnwYFRLQKAGIG 378
Cdd:TIGR01271 79 F--WRFVFYGILLYFG-EATKAVQPLLLGRIIASYDPFNAPErEIAYYLalgLCLLFIVRTLLLHPA---IFGLHHLGMQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 379 MRSVLVSMIYEKGLTLPCYSKQGHTSGEIINLMTVDAERISAFSWYMHDPWILVLQISLALLILYRSLGLGSIAAFAatF 458
Cdd:TIGR01271 153 MRIALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLG--F 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 459 LVMLGnIPLAKLEEKfqgnLMESKDNRMKK-------TSEALLNMRILKLQGWEMKFLHKILDLRGIE------AGWLKK 525
Cdd:TIGR01271 231 LILLA-LFQACLGQK----MMPYRDKRAGKiserlaiTSEIIENIQSVKAYCWEEAMEKIIKNIRQDElkltrkIAYLRY 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 526 FvYNSAAISSVLWAAPSFVSATAFGACMLLKiplesgKIIAALATFRILQTPIYK-LPDTISMIVQTKVSLDRIATFLCL 604
Cdd:TIGR01271 306 F-YSSAFFFSGFFVVFLSVVPYALIKGIILR------RIFTTISYCIVLRMTVTRqFPGAIQTWYDSLGAITKIQDFLCK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 605 DDLQQdgmerLPSGSSKMDVEVSNGAFSWDDS-------------------------------SPIPTLKDIRFKIPHGM 653
Cdd:TIGR01271 379 EEYKT-----LEYNLTTTEVEMVNVTASWDEGigelfekikqnnkarkqpngddglffsnfslYVTPVLKNISFKLEKGQ 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 654 NIAICGTVGSGKSSLLSSILGEVPKISGNLKVCGRKAYIAQSPWIQSGKVEENILFGKPMQREWYQRVLEACSLNKDLEV 733
Cdd:TIGR01271 454 LLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIAL 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 734 FPFRDQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEVLLGLLRNKTVIYVTHQLEFLPE 813
Cdd:TIGR01271 534 FPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKK 613
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 814 ADLILVMKDGRITQAGKYNEILESGTDFM-ELVGA-HTDALAA---------------------VDSY------------ 858
Cdd:TIGR01271 614 ADKILLLHEGVCYFYGTFSELQAKRPDFSsLLLGLeAFDNFSAerrnsiltetlrrvsidgdstVFSGpetikqsfkqpp 693
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 859 -------------------------EKGSASAQSTT-------------------------------------------- 869
Cdd:TIGR01271 694 pefaekrkqsiilnpiasarkfsfvQMGPQKAQATTiedavrepserkfslvpedeqgeeslprgnqyhhglqhqaqrrq 773
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 870 ----------------------------------------------SKESKVSNDEEKQEEDLpspKGQLVQEEEREKGK 903
Cdd:TIGR01271 774 svlqlmthsnrgenrreqlqtsfrkkssitqqnelaseldiysrrlSKDSVYEISEEINEEDL---KECFADERENVFET 850
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 904 VGFTVYQKYMKLAYGGALVPIILVVQILFQVLNIGSNYWMAWVTPV---------SKDVKPLV-------SGSTLILVYV 967
Cdd:TIGR01271 851 TTWNTYLRYITTNRNLVFVLIFCLVIFLAEVAASLLGLWLITDNPSapnyvdqqhANASSPDVqkpviitPTSAYYIFYI 930
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 968 FLATASSFCIL--VRAMLSAMTGFKIATELFNQMHFRIFRASMSFFDATPIGRILNRASTDQSAVDLRLPSQFSNLAIAA 1045
Cdd:TIGR01271 931 YVGTADSVLALgfFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLT 1010
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1046 VNILGIIGVMGQVAWQVLIVFIPVIAACTWYRQYYISAARELARLSGISRSPLVQHFSETLSGITTIRSFDQEPRFRTDI 1125
Cdd:TIGR01271 1011 LIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLF 1090
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1126 MRLNDCYSRLRFHAISAMEWLCFRLDLLSTVAFalSLVILVSVPEGVINPSFAGLAVTYALNLNSlqaTLIW---TLCDL 1202
Cdd:TIGR01271 1091 HKALNLHTANWFLYLSTLRWFQMRIDIIFVFFF--IAVTFIAIGTNQDGEGEVGIILTLAMNILS---TLQWavnSSIDV 1165
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1203 ENKMISVERMLQYIDIPSEPS--------------LVIESTRPEKSWPCRGEITICNLQVRYGPHLPMVLRGLTCTFRGG 1268
Cdd:TIGR01271 1166 DGLMRSVSRVFKFIDLPQEEPrpsggggkyqlstvLVIENPHAQKCWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGG 1245
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1269 LKTGIVGRTGCGKSTLIQTLFRIVEpAAGEIRIDGINILTIGLHDLRSRLSIIPQEPTMFEGTVRSNLDPLEEYADDQIW 1348
Cdd:TIGR01271 1246 QRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIW 1324
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1349 EALDKCQLGDEIRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLRQHFSGCT 1428
Cdd:TIGR01271 1325 KVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCT 1404
|
1450 1460 1470
....*....|....*....|....*....|....*....
gi 30682486 1429 VITIAHRISSVIDSDMVLLLDQGLIEEHDSPARLLEDKS 1467
Cdd:TIGR01271 1405 VILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETS 1443
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1239-1459 |
4.00e-118 |
|
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: 369.13 E-value: 4.00e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1239 GEITICNLQVRYGPHLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRL 1318
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1319 SIIPQEPTMFEGTVRSNLDPLEEYADDQIWEALDKCQLGDEIRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKV 1398
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30682486 1399 LILDEATASVDTATDTLIQETLRQHFSGCTVITIAHRISSVIDSDMVLLLDQGLIEEHDSP 1459
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
961-1481 |
1.19e-106 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 351.39 E-value: 1.19e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 961 TLILVYVFLATASSFCILVRAMLSAMTGFKIATELFNQMHFRIFRASMSFFDATPIGRILNRASTDQSAVDLRLPSQFSN 1040
Cdd:COG1132 62 LLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1041 LAIAAVNILGIIGVMGQVAWQ---VLIVFIPVIAACTWY-----RQYYISAARELARLSGisrsplvqHFSETLSGITTI 1112
Cdd:COG1132 142 LVRSVVTLIGALVVLFVIDWRlalIVLLVLPLLLLVLRLfgrrlRKLFRRVQEALAELNG--------RLQESLSGIRVV 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1113 RSFDQEPRFRTDIMRLNDCYSRLRFHAISAMEWLCFRLDLLSTVAFALSLVI-LVSVPEGVINPSFAGLAVTYALNLNSL 1191
Cdd:COG1132 214 KAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVgGLLVLSGSLTVGDLVAFILYLLRLFGP 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1192 QATLIWTLCDLENKMISVERMLQYIDIPSEpslVIESTRPEKSWPCRGEITICNLQVRYGPHLPmVLRGLTCTFRGGLKT 1271
Cdd:COG1132 294 LRQLANVLNQLQRALASAERIFELLDEPPE---IPDPPGAVPLPPVRGEIEFENVSFSYPGDRP-VLKDISLTIPPGETV 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1272 GIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSIIPQEPTMFEGTVRSNL---DPleEYADDQIW 1348
Cdd:COG1132 370 ALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRP--DATDEEVE 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1349 EALDKCQLGDEIRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLRQHFSGCT 1428
Cdd:COG1132 448 EAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRT 527
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 30682486 1429 VITIAHRISSVIDSDMVLLLDQGLIEEHDSPARLLEdKSSSFSKLVAEYTASS 1481
Cdd:COG1132 528 TIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLA-RGGLYARLYRLQFGEE 579
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1235-1459 |
2.96e-93 |
|
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: 299.71 E-value: 2.96e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1235 WPCRGEITICNLQVRYGPHLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDL 1314
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1315 RSRLSIIPQEPTMFEGTVRSNLDPLEEYADDQIWEALDkcqlgdeirkkelkldspVSENGQNWSVGQRQLVCLGRVLLK 1394
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30682486 1395 RSKVLILDEATASVDTATDTLIQETLRQHFSGCTVITIAHRISSVIDSDMVLLLDQGLIEEHDSP 1459
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
624-824 |
1.18e-90 |
|
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: 292.07 E-value: 1.18e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 624 VEVSNGAFSWDD--SSPIPTLKDIRFKIPHGMNIAICGTVGSGKSSLLSSILGEVPKISGNLKVCGRKAYIAQSPWIQSG 701
Cdd:cd03250 1 ISVEDASFTWDSgeQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 702 KVEENILFGKPMQREWYQRVLEACSLNKDLEVFPFRDQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDA 781
Cdd:cd03250 81 TIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 30682486 782 HTGSHLFKEVLLGLLR-NKTVIYVTHQLEFLPEADLILVMKDGR 824
Cdd:cd03250 161 HVGRHIFENCILGLLLnNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
922-1216 |
1.47e-88 |
|
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: 290.17 E-value: 1.47e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 922 VPIILVVQILFQVLNIGSNYWMAWVTPVSKDVKPLVSGSTLILVYVFLATASSFCILVRAMLSAMTGFKIATELFNQMHF 1001
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1002 RIFRASMSFFDATPIGRILNRASTDQSAVDLRLPSQFSNLAIAAVNILGIIGVMGQVAWQVLIVFIPVIAACTWYRQYYI 1081
Cdd:cd18580 81 SVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1082 SAARELARLSGISRSPLVQHFSETLSGITTIRSFDQEPRFRTDIMRLNDCYSRLRFHAISAMEWLCFRLDLLSTVaFALS 1161
Cdd:cd18580 161 RTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGAL-LALV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 30682486 1162 LVILVSVPEGVINPSFAGLAVTYALNLNSLQATLIWTLCDLENKMISVERMLQYI 1216
Cdd:cd18580 240 VALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
949-1476 |
1.02e-87 |
|
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: 302.14 E-value: 1.02e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 949 VSKDVKPLVsgsTLILVYVFLATASSFCILVRAMLSAMTGFKIATELFNQMHFRIFRASMSFFDATPIGRILNRASTDQS 1028
Cdd:COG2274 188 PNQDLSTLW---VLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRDVES 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1029 AVDLrLPSQFSNLAIAAVNILGIIGVMGQVAWQ---VLIVFIPVIAACTWY-RQYYISAARELARLSGISRSPLVqhfsE 1104
Cdd:COG2274 265 IREF-LTGSLLTALLDLLFVLIFLIVLFFYSPPlalVVLLLIPLYVLLGLLfQPRLRRLSREESEASAKRQSLLV----E 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1105 TLSGITTIRSFDQEPRFRTDIMRLNDCYSRLRFHaisaMEWLCFRLDLLSTVAFALSLVILV-----SVPEGVInpSFAG 1179
Cdd:COG2274 340 TLRGIETIKALGAESRFRRRWENLLAKYLNARFK----LRRLSNLLSTLSGLLQQLATVALLwlgayLVIDGQL--TLGQ 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1180 L--AVTYALNLNSLQATLIWTLCDLENKMISVERMLQYIDIPSEPSLVIESTRPEKSwpcRGEITICNLQVRYGPHLPMV 1257
Cdd:COG2274 414 LiaFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRL---KGDIELENVSFRYPGDSPPV 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1258 LRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSIIPQEPTMFEGTVRSNL- 1336
Cdd:COG2274 491 LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENIt 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1337 --DPleEYADDQIWEALDKCQLGDEIRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTATDT 1414
Cdd:COG2274 571 lgDP--DATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEA 648
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30682486 1415 LIQETLRQHFSGCTVITIAHRISSVIDSDMVLLLDQGLIEEHDSPARLLEdKSSSFSKLVAE 1476
Cdd:COG2274 649 IILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLA-RKGLYAELVQQ 709
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
311-598 |
6.14e-87 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)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. ABC transporters typically consist 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: 350023 [Multi-domain] Cd Length: 289 Bit Score: 285.15 E-value: 6.14e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 311 LSTLFAFVYTVSCYVAPYLMDTFVQYLNGQRQYS-NQGVVLVTTFFVAKLVECQARRNWYFRLQKAGIGMRSVLVSMIYE 389
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPlSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 390 KGLTLPCYSKQGHTSGEIINLMTVDAERISAFSWYMHDPWILVLQISLALLILYRSLGLGSIAAFAATFLVMLGNIPLAK 469
Cdd:cd18579 81 KALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 470 LEEKFQGNLMESKDNRMKKTSEALLNMRILKLQGWEMKFLHKILDLRGIEAGWLKKFVYNSAAISSVLWAAPSFVSATAF 549
Cdd:cd18579 161 LISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATF 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 30682486 550 GACMLLKIPLESGKIIAALATFRILQTPIYKLPDTISMIVQTKVSLDRI 598
Cdd:cd18579 241 ATYVLLGNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
926-1466 |
3.36e-71 |
|
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: 249.67 E-value: 3.36e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 926 LVVQILFQV----LNIGSNYWMAW-VTPVSKDVKPLVSGSTLILVYVFLATASSFCILVRAMLSAMTGFKIATELFNQMH 1000
Cdd:COG4988 19 LALAVLLGLlsglLIIAQAWLLASlLAGLIIGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRAAARVKRRLRRRLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1001 FRIFRASMSFFDATPIGRILNRAsTDQsaVDlRLPSQFSN----LAIAAVNILGIIGVMGQVAWQ---VLIVFIPVI--- 1070
Cdd:COG4988 99 EKLLALGPAWLRGKSTGELATLL-TEG--VE-ALDGYFARylpqLFLAALVPLLILVAVFPLDWLsglILLVTAPLIplf 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1071 ------AACTWYRQYYisaaRELARLSGisrsplvqHFSETLSGITTIRSFDQEPRFRTDIMRLNDCYSR-----LR--F 1137
Cdd:COG4988 175 milvgkGAAKASRRQW----RALARLSG--------HFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKrtmkvLRvaF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1138 HAISAMEW------------LCFRLdLLSTVAFALSLVILVSVPEgvinpsfaglavtYALNLNSL----QATLiwtlcd 1201
Cdd:COG4988 243 LSSAVLEFfaslsialvavyIGFRL-LGGSLTLFAALFVLLLAPE-------------FFLPLRDLgsfyHARA------ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1202 leNKMISVERMLQYIDIPSEPSLVIESTRPeksWPCRGEITICNLQVRYGPHLPmVLRGLTCTFRGGLKTGIVGRTGCGK 1281
Cdd:COG4988 303 --NGIAAAEKIFALLDAPEPAAPAGTAPLP---AAGPPSIELEDVSFSYPGGRP-ALDGLSLTIPPGERVALVGPSGAGK 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1282 STLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSIIPQEPTMFEGTVRSNLDPLEEYADD-QIWEALDKCQLGDEI 1360
Cdd:COG4988 377 STLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDeELEAALEAAGLDEFV 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1361 RKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLRQHFSGCTVITIAHRISSVI 1440
Cdd:COG4988 457 AALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLA 536
|
570 580
....*....|....*....|....*.
gi 30682486 1441 DSDMVLLLDQGLIEEHDSPARLLEDK 1466
Cdd:COG4988 537 QADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1239-1474 |
2.01e-70 |
|
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: 236.73 E-value: 2.01e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1239 GEITICNLQVRYGPHLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRL 1318
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1319 SIIPQEPTMFEGTVRSNLDPLEEYADDQIWEALDKCQLGDEIRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKV 1398
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30682486 1399 LILDEATASVDTATDTLIQETLRQHFSGCTVITIAHRISSVIDSDMVLLLDQGLIEEHDSPARLLEDKSSSFSKLV 1474
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLV 253
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
924-1216 |
4.08e-68 |
|
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: 231.59 E-value: 4.08e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 924 IILVVQILFQVLNIGSNYWMA-WVT-PVSKDVKPLVSGSTL--ILVYVFLATASSFCILVRAMLSAMTGFKIATELFNQM 999
Cdd:cd18604 3 LLLLLFVLSQLLSVGQSWWLGiWASaYETSSALPPSEVSVLyyLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHERL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1000 HFRIFRASMSFFDATPIGRILNRASTDQSAVDLRLPSQFSNLAIAAVNILGIIGVMGQVAWQVLIVFIPVIAACTWYRQY 1079
Cdd:cd18604 83 LHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1080 YISAARELARLSGISRSPLVQHFSETLSGITTIRSFDQEPRFRTDIMRLNDCYSRLRFHAISAMEWLCFRLDLLSTVAFA 1159
Cdd:cd18604 163 YLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALFSF 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 30682486 1160 LSLVILVSVPegVINPSFAGLAVTYALNLNSLQATLIWTLCDLENKMISVERMLQYI 1216
Cdd:cd18604 243 ATAALLVYGP--GIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
922-1216 |
9.01e-66 |
|
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: 225.10 E-value: 9.01e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 922 VPIILVVQILFQVLNIGSNYWMA-WVTPVSKDVKPL--VSGSTLILVYVFLATASSFCILVRAMLSAMTGFKIATELFNQ 998
Cdd:cd18605 1 LILILLSLILMQASRNLIDFWLSyWVSHSNNSFFNFinDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 999 MHFRIFRASMSFFDATPIGRILNRASTDQSAVDLRLPSQFSNLAIAAVNILGIIGVMGQVAWQVLIVFIPVIAACTWYRQ 1078
Cdd:cd18605 81 LLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1079 YYISAARELARLSGISRSPLVQHFSETLSGITTIRSFDQEPRFRTDIMRLNDCYSRLRFHAISAMEWLCFRLDLLS--TV 1156
Cdd:cd18605 161 YYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGvlIV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1157 AFALSLVILVSVPEGVINPSFAGLAVTYALNLNSLQATLIWTLCDLENKMISVERMLQYI 1216
Cdd:cd18605 241 TFVALTAVVQHFFGLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
922-1215 |
9.17e-66 |
|
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: 224.66 E-value: 9.17e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 922 VPIILVVQILFQVLNIGSNYWMAWVTpvskDVKPLVSGSTLILVYVFLATASSFCILVRAMLSAMTGFKIATELFNQMHF 1001
Cdd:cd18606 1 LPLLLLLLILSQFAQVFTNLWLSFWT----EDFFGLSQGFYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1002 RIFRASMSFFDATPIGRILNRASTDQSAVDLRLPSQFSNLAIAAVNILGIIGVMGQVAWQVLIVFIPVIAACTWYRQYYI 1081
Cdd:cd18606 77 RVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1082 SAARELARLSGISRSPLVQHFSETLSGITTIRSFDQEPRFRTDIMRLNDCYSRLRFHAISAMEWLCFRLDLLSTVaFALS 1161
Cdd:cd18606 157 ASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSL-LVLI 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 30682486 1162 LVILVSVPEGVINPSFAGLAVTYALNLNSLQATLIWTLCDLENKMISVERMLQY 1215
Cdd:cd18606 236 VALLCVTRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHY 289
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1017-1466 |
5.41e-63 |
|
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: 225.80 E-value: 5.41e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1017 GRILNRASTDQSAVD---LRLpsqFSNLAIAAVNILGIIGVMGQVAWQ----------VLIVFIPVIAactwYRqyyisA 1083
Cdd:COG4987 112 GDLLNRLVADVDALDnlyLRV---LLPLLVALLVILAAVAFLAFFSPAlalvlalgllLAGLLLPLLA----AR-----L 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1084 ARELARLSGISRSPLVQHFSETLSGITTIRSFDQEPRFRTDIMRLNDCYSRLRfHAISAMEWLCfrlDLLSTVAFALS-- 1161
Cdd:COG4987 180 GRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQ-RRLARLSALA---QALLQLAAGLAvv 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1162 LVILVSVP---EGVINPSFAGLAVTYALNLNSLQATLIWTLCDLENKMISVERMLQyidIPSEPSLVIESTRPEKSwPCR 1238
Cdd:COG4987 256 AVLWLAAPlvaAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNE---LLDAPPAVTEPAEPAPA-PGG 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1239 GEITICNLQVRYGPHLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRL 1318
Cdd:COG4987 332 PSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRI 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1319 SIIPQEPTMFEGTVRSNL---DPleEYADDQIWEALDKCQLGDEIRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKR 1395
Cdd:COG4987 412 AVVPQRPHLFDTTLRENLrlaRP--DATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRD 489
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30682486 1396 SKVLILDEATASVDTATDTLIQETLRQHFSGCTVITIAHRISSVIDSDMVLLLDQGLIEEHDSPARLLEDK 1466
Cdd:COG4987 490 APILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQN 560
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
924-1215 |
1.26e-62 |
|
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: 215.81 E-value: 1.26e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 924 IILVVQILFQVLNIGSNYWMA-WVTPVSKDVKPLVSGSTL-ILVYVFLATASSFCILVRAMLSAMTGFKIATELFNQMHF 1001
Cdd:cd18603 3 LILLLYLLSQAFSVGSNIWLSeWSDDPALNGTQDTEQRDYrLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHNKLLH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1002 RIFRASMSFFDATPIGRILNRASTDQSAVDLRLPSQFSNLAIAAVNILGIIGVMGQVAWQVLIVFIPVIAACTWYRQYYI 1081
Cdd:cd18603 83 NILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQRFYV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1082 SAARELARLSGISRSPLVQHFSETLSGITTIRSFDQEPRFRTDIMRLNDCYSRLRFHAISAMEWLCFRLDLL-STVAFAL 1160
Cdd:cd18603 163 ATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLgNLIVLFA 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 30682486 1161 SLVILVSvpEGVINPSFAGLAVTYALNLNslqATLIW---TLCDLENKMISVERMLQY 1215
Cdd:cd18603 243 ALFAVLS--RDSLSPGLVGLSISYALQIT---QTLNWlvrMTSELETNIVSVERIKEY 295
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1239-1466 |
1.32e-62 |
|
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: 213.24 E-value: 1.32e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1239 GEITICNLQVRYGPHLPmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRL 1318
Cdd:cd03254 1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1319 SIIPQEPTMFEGTVRSNLDPLEEYADDQIWEALDK-CQLGDEIRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSK 1397
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKeAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30682486 1398 VLILDEATASVDTATDTLIQETLRQHFSGCTVITIAHRISSVIDSDMVLLLDQGLIEEHDSPARLLEDK 1466
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
311-598 |
4.87e-62 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 1 (TMD1) 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: 350039 [Multi-domain] Cd Length: 290 Bit Score: 213.87 E-value: 4.87e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 311 LSTLFAFVYTVSCYVAPYLMDTFVQYLNGQRQYSNQGVVLVTTFFVAKLVECQARRNWYFRLQKAGIGMRSVLVSMIYEK 390
Cdd:cd18595 1 LAALLKLLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 391 GLTLPCYSKQGHTSGEIINLMTVDAERISAFSWYMHDPWILVLQISLALLILYRSLGLGSIAAFAATFLVMLGNIPLAKL 470
Cdd:cd18595 81 ALRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 471 EEKFQGNLMESKDNRMKKTSEALLNMRILKLQGWEMKFLHKILDLRGIEAGWLKKFVYnSAAISSVLW-AAPSFVSATAF 549
Cdd:cd18595 161 IKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAY-LNAVSSFLWtCAPFLVSLATF 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 30682486 550 GACMLL--KIPLESGKIIAALATFRILQTPIYKLPDTISMIVQTKVSLDRI 598
Cdd:cd18595 240 ATYVLSdpDNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
924-1464 |
1.92e-58 |
|
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: 212.65 E-value: 1.92e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 924 IILVVQILFQVLNIGSNYWMAWVtpvskdVKPLVSGS----------TLILVYVFLATASSFCILVRAMLSAMTGFKIAT 993
Cdd:TIGR02203 14 AGLVLAGVAMILVAATESTLAAL------LKPLLDDGfggrdrsvlwWVPLVVIGLAVLRGICSFVSTYLLSWVSNKVVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 994 ELFNQMHFRIFRASMSFFDATPIGRILNRASTDQSAVDLRLPSQFSNLAIAAVNILGIIGVMGQVAWQ---VLIVFIPVI 1070
Cdd:TIGR02203 88 DIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQltlIVVVMLPVL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1071 AactWYRQYYISAARELARLSGISRSPLVQHFSETLSGITTIRSFDQEPRFRTDIMRLNDCYSRLRFHAISAMEWLCFRL 1150
Cdd:TIGR02203 168 S---ILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPIT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1151 DLLSTVAfaLSLVILVSVPEGVINPSFAGLAVTYALNLNSLQATlIWTLCDLENKM----ISVERMLQYIDIPSEPSlvi 1226
Cdd:TIGR02203 245 QLIASLA--LAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRP-LKSLTNVNAPMqrglAAAESLFTLLDSPPEKD--- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1227 ESTRPEKSwpCRGEITICNLQVRYGPHLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINI 1306
Cdd:TIGR02203 319 TGTRAIER--ARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1307 LTIGLHDLRSRLSIIPQEPTMFEGTVRSNL--DPLEEYADDQIWEALDKCQLGDEIRKKELKLDSPVSENGQNWSVGQRQ 1384
Cdd:TIGR02203 397 ADYTLASLRRQVALVSQDVVLFNDTIANNIayGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQ 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1385 LVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLRQHFSGCTVITIAHRISSVIDSDMVLLLDQGLIEEHDSPARLLE 1464
Cdd:TIGR02203 477 RLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLA 556
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
624-823 |
3.02e-58 |
|
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: 200.25 E-value: 3.02e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 624 VEVSNGAFSWddSSPIPTLKDIRFKIPHGMNIAICGTVGSGKSSLLSSILGEVPKISGNL-----------------KVC 686
Cdd:cd03290 1 VQVTNGYFSW--GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 687 GRKAYIAQSPWIQSGKVEENILFGKPMQREWYQRVLEACSLNKDLEVFPFRDQTVIGERGINLSGGQKQRIQIARALYQD 766
Cdd:cd03290 79 YSVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 30682486 767 ADIYLFDDPFSAVDAHTGSHLFKEVLLGLLRN--KTVIYVTHQLEFLPEADLILVMKDG 823
Cdd:cd03290 159 TNIVFLDDPFSALDIHLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
311-598 |
1.62e-57 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) 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: 350040 [Multi-domain] Cd Length: 309 Bit Score: 201.57 E-value: 1.62e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 311 LSTLFAFVYTVSCYVAPYLMDTFVQYL-NGQRQYSNQGVVLVTTFFVAKLVE--CQARRNWYFRlqKAGIGMRSVLVSMI 387
Cdd:cd18596 1 LQALLAVLSSVLSFAPPFFLNRLLRYLeDPGEDATVRPWVWVLLLFLGPLLSslLDQQYLWIGR--RLSVRLRAILTQLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 388 YEKGLTLPCYS-------------------KQGHTSGEIINLMTVDAERISAFSWYMHDPWILVLQISLALLILYRSLGL 448
Cdd:cd18596 79 FEKALRRRDKSgssksseskkkdkeededeKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 449 GSIAAFAATFLVMLGNIPLAKLEEKFQGNLMESKDNRMKKTSEALLNMRILKLQGWEMKFLHKILDLRGIEAGWLKKFVY 528
Cdd:cd18596 159 SALVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFL 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30682486 529 NSAAISSVLWAAPSFVSATAFGA-CMLLKIPLESGKIIAALATFRILQTPIYKLPDTISMIVQTKVSLDRI 598
Cdd:cd18596 239 LDLLLSLLWFLIPILVTVVTFATyTLVMGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1241-1451 |
2.82e-57 |
|
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: 195.68 E-value: 2.82e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSI 1320
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1321 IPQEPTMFEGTVRSNLdpleeyaddqiwealdkcqlgdeirkkelkldspvsengqnWSVGQRQLVCLGRVLLKRSKVLI 1400
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 30682486 1401 LDEATASVDTATDTLIQETLRQHFSGCTVITIAHRISSVIDSDMVLLLDQG 1451
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
289-838 |
7.40e-56 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 205.01 E-value: 7.40e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 289 ERRITTYKLIKALFFSVWRDILLSTLFAFVYTVSCYVAPYLMDTFVQYLNGQRQYS--NQGVVLVTTFFVAKLVecqARR 366
Cdd:COG1132 3 KSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSalLLLLLLLLGLALLRAL---LSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 367 NWYFRLQKAGIGMRSVLVSMIYEKGLTLP--CYSKqgHTSGEIINLMTVDAERIS-AFSWYMHDPWILVLQISLAL-LIL 442
Cdd:COG1132 80 LQRYLLARLAQRVVADLRRDLFEHLLRLPlsFFDR--RRTGDLLSRLTNDVDAVEqFLAHGLPQLVRSVVTLIGALvVLF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 443 YRSLGLGsIAAFAATFLVMLGNIPLAKLEEKFQGNLMESKDNRMKKTSEALLNMRILK---LQGWEMKFLHKIL-DLRGI 518
Cdd:COG1132 158 VIDWRLA-LIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKafgREERELERFREANeELRRA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 519 EAGWLKKFVYNSAAISSVLWAApsFVSATAFGACMLLKIPLESGKIIAALATFRILQTPIYKLPDTISMIVQTKVSLDRI 598
Cdd:COG1132 237 NLRAARLSALFFPLMELLGNLG--LALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 599 ATFLCLDDLQQDGMERLPSGSSKMDVEVSNGAFSWDDSSPIptLKDIRFKIPHGMNIAICG-------TVGsgkssllss 671
Cdd:COG1132 315 FELLDEPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPV--LKDISLTIPPGETVALVGpsgsgksTLV--------- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 672 ilgevpKI--------SGNLKVCG-----------RK--AYIAQSPWIQSGKVEENILFGKP-MQREWYQRVLEACSLNK 729
Cdd:COG1132 384 ------NLllrfydptSGRILIDGvdirdltleslRRqiGVVPQDTFLFSGTIRENIRYGRPdATDEEVEEAAKAAQAHE 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 730 DLEVFPFRDQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFkEVLLGLLRNKTVIYVTHQLE 809
Cdd:COG1132 458 FIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQ-EALERLMKGRTTIVIAHRLS 536
|
570 580
....*....|....*....|....*....
gi 30682486 810 FLPEADLILVMKDGRITQAGKYNEILESG 838
Cdd:COG1132 537 TIRNADRILVLDDGRIVEQGTHEELLARG 565
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
922-1215 |
6.66e-55 |
|
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: 193.97 E-value: 6.66e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 922 VPIILVVQILFQVLNIGSNYWMAWVTPVSKDVKPLVSGSTL-----------ILVYVFLATASSFCILVRAMLSAMTGFK 990
Cdd:cd18602 1 VALVLALALLKQGLRVATDFWLADWTEANHDVASVVFNITSssleddevsyyISVYAGLSLGAVILSLVTNLAGELAGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 991 IATELFNQMHFRIFRASMSFFDATPIGRILNRASTDQSAVDLRLPSQFSNLAIAAVNILGIIGVMGQVAWQVLIVFIPVI 1070
Cdd:cd18602 81 AARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPII 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1071 AACTWYRQYYISAARELARLSGISRSPLVQHFSETLSGITTIRSFDQEPRFRTDIMRL----NDCYSRLRfhaiSAMEWL 1146
Cdd:cd18602 161 IVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELidrnNTAFLFLN----TANRWL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1147 CFRLDLL-STVAFALSLVILVSVPEGVINPSFAGLAVTYALNLNSLQATLIWTLCDLENKMISVERMLQY 1215
Cdd:cd18602 237 GIRLDYLgAVIVFLAALSSLTAALAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEY 306
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
924-1216 |
1.30e-54 |
|
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: 193.55 E-value: 1.30e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 924 IILVVQILFQVLNIGSNYWMAW-------VTPVSKDVKPLVSGSTL--------ILVYVFLATASSFCILVRAMLSAMTG 988
Cdd:cd18599 7 FVLLLFILSVGSTVFSDWWLSYwlkqgsgNTTNNVDNSTVDSGNISdnpdlnfyQLVYGGSILVILLLSLIRGFVFVKVT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 989 FKIATELFNQMHFRIFRASMSFFDATPIGRILNRASTDQSAVDLRLPSQFSNLAIAAVNILGIIGVMGQVAWQVLIVFIP 1068
Cdd:cd18599 87 LRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWFLIALIP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1069 VIAACTWYRQYYISAARELARLSGISRSPLVQHFSETLSGITTIRSFDQEPRFRTDIMRLNDCYSRLRFHAISAMEWLCF 1148
Cdd:cd18599 167 LAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCAMRWLAV 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30682486 1149 RLDLLS---TVAFALSLVILvsvpEGVINPSFAGLAVTYALNLNSL-QATlIWTLCDLENKMISVERMLQYI 1216
Cdd:cd18599 247 RLDILAvliTLITALLVVLL----KGSISPAFAGLALSYALQLSGLfQFT-VRLASETEARFTSVERILEYI 313
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1250-1467 |
5.87e-54 |
|
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: 188.59 E-value: 5.87e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1250 YGPHLPmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSIIPQEPTMFE 1329
Cdd:cd03253 10 YDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDTVLFN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1330 GTVRSNLdpleEYA-----DDQIWEALDKCQLGDEIRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVLILDEA 1404
Cdd:cd03253 89 DTIGYNI----RYGrpdatDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30682486 1405 TASVDTATDTLIQETLRQHFSGCTVITIAHRISSVIDSDMVLLLDQGLIEEHDSPARLLEDKS 1467
Cdd:cd03253 165 TSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGG 227
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1241-1466 |
6.54e-52 |
|
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: 182.82 E-value: 6.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSI 1320
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1321 IPQEPTMFEGTVRSNLD-PLEEYADDQIWEALDKCQLGDEIRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVL 1399
Cdd:cd03251 81 VSQDVFLFNDTVAENIAyGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30682486 1400 ILDEATASVDTATDTLIQETLRQHFSGCTVITIAHRISSVIDSDMVLLLDQGLIEEHDSPARLLEDK 1466
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQG 227
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1005-1466 |
1.50e-49 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 186.85 E-value: 1.50e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1005 RASMSFFDATPIGRILNRASTDQSAV-DLrlpsqFSNLAIAAVNILGIIGVM--------GQVAWQVLIVFIPVIAACTW 1075
Cdd:PRK10790 110 RQPLSAFDTQPVGQLISRVTNDTEVIrDL-----YVTVVATVLRSAALIGAMlvamfsldWRMALVAIMIFPAVLVVMVI 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1076 YRQYYISAAREL-ARLSGISRSplvqhFSETLSGITTIRSFDQEPRFRTDIMRLNdcysrlRFHAISAMEWLcfRLD--- 1151
Cdd:PRK10790 185 YQRYSTPIVRRVrAYLADINDG-----FNEVINGMSVIQQFRQQARFGERMGEAS------RSHYMARMQTL--RLDgfl 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1152 ---LLSTVAfAL---SLVILVSV-PEGVInpsfaGLAVTYAL--NLNSLQATLIwTLCD----LENKMISVERMLQYIDI 1218
Cdd:PRK10790 252 lrpLLSLFS-ALilcGLLMLFGFsASGTI-----EVGVLYAFisYLGRLNEPLI-ELTTqqsmLQQAVVAGERVFELMDG 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1219 PSEPslVIESTRPEKSwpcrGEITICNLQVRYGPHLPmVLR--GLTCTFRGGLktGIVGRTGCGKSTLIQTLFRIVEPAA 1296
Cdd:PRK10790 325 PRQQ--YGNDDRPLQS----GRIDIDNVSFAYRDDNL-VLQniNLSVPSRGFV--ALVGHTGSGKSTLASLLMGYYPLTE 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1297 GEIRIDGINILTIGLHDLRSRLSIIPQEPTMFEGTVRSNLDPLEEYADDQIWEALDKCQLGDEIRKKELKLDSPVSENGQ 1376
Cdd:PRK10790 396 GEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGN 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1377 NWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLRQHFSGCTVITIAHRISSVIDSDMVLLLDQGLIEEH 1456
Cdd:PRK10790 476 NLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQ 555
|
490
....*....|
gi 30682486 1457 DSPARLLEDK 1466
Cdd:PRK10790 556 GTHQQLLAAQ 565
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1241-1474 |
7.34e-49 |
|
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: 174.26 E-value: 7.34e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYgPHLP--MVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRL 1318
Cdd:cd03249 1 IEFKNVSFRY-PSRPdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1319 SIIPQEPTMFEGTVRSNLDPLEEYA-DDQIWEALDKCQLGDEIRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSK 1397
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIRYGKPDAtDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30682486 1398 VLILDEATASVDTATDTLIQETLRQHFSGCTVITIAHRISSVIDSDMVLLLDQGLIEEHDSPARLLEdKSSSFSKLV 1474
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMA-QKGVYAKLV 235
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
314-598 |
5.96e-47 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) 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: 350042 [Multi-domain] Cd Length: 288 Bit Score: 170.43 E-value: 5.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 314 LFAFVYTVSCYVAPYLMDTFVQYLNGQRQYSNQGVV----LVTTFFVAKLveCQARRNWYfrLQKAGIGMRSVLVSMIYE 389
Cdd:cd18598 4 LLKLLADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLyalgLVLSSLLGAL--LSSHYNFQ--MNKVSLKVRAALVTAVYR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 390 KGLTLPCYSKQGHTSGEIINLMTVDAERISAFSWYMHDPWILVLQISLALLILYRSLGLGSIAAFAATFLVMLGNIPLAK 469
Cdd:cd18598 80 KALRVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 470 LEEKFQGNLMESKDNRMKKTSEALLNMRILKLQGWEMKFLHKILDLRGIEAGWLKKFVYNSAAISSvLWAA-PSFVSATA 548
Cdd:cd18598 160 RIGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALCVY-FWATtPVLISILT 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 30682486 549 FGACMLLKIPLESGKIIAALATFRILQTPIYKLPDTISMIVQTKVSLDRI 598
Cdd:cd18598 239 FATYVLMGNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1239-1468 |
9.47e-47 |
|
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: 169.26 E-value: 9.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1239 GEITICNLQVRYGPHLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEpAAGEIRIDGINILTIGLHDLRSRL 1318
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1319 SIIPQEPTMFEGTVRSNLDPLEEYADDQIWEALDKCQLGDEIRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKV 1398
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1399 LILDEATASVDTATDTLIQETLRQHFSGCTVITIAHRISSVIDSDMVLLLDQGLIEEHDSPARLLEDKSS 1468
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSH 229
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
257-845 |
5.12e-46 |
|
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: 178.49 E-value: 5.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 257 IIDSEDVPQVDNSDRAEKLF----WIFRSKLEWDDGERRITTYKLIKALFFSVWRDILLSTLFAFVYTVSCYVAPY---- 328
Cdd:COG2274 102 IADPATGRRKLSLEEFAESWtgvaLLLEPTPEFDKRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLftqv 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 329 LMDTFVQylngqRQYSNQGVVLVTTFFVAKLVEC--QARRNWYFRLQKAGIGMRsvLVSMIYEKGLTLPCYSKQGHTSGE 406
Cdd:COG2274 182 VIDRVLP-----NQDLSTLWVLAIGLLLALLFEGllRLLRSYLLLRLGQRIDLR--LSSRFFRHLLRLPLSFFESRSVGD 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 407 IINLMTvDAERI-SAFSWYMHDPWILVLQ--ISLALLILY-RSLGLGSIAAFAATFLVMLG-NIPLAKLEEKfqgnLMES 481
Cdd:COG2274 255 LASRFR-DVESIrEFLTGSLLTALLDLLFvlIFLIVLFFYsPPLALVVLLLIPLYVLLGLLfQPRLRRLSRE----ESEA 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 482 KDNRMKKTSEALLNMRILKLQGWEMKFLHKIldlRGIEAGWLKKfVYNSAAISSVLWAAPSFVSATAFGACMLLKIPL-E 560
Cdd:COG2274 330 SAKRQSLLVETLRGIETIKALGAESRFRRRW---ENLLAKYLNA-RFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLvI 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 561 SGKI-IAALATFRILQ----TPIYKLPDTISMIVQTKVSLDRIATFLCLDDLQQDGMERLPSGSSKMDVEVSNGAFSWDD 635
Cdd:COG2274 406 DGQLtLGQLIAFNILSgrflAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRLKGDIELENVSFRYPG 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 636 SSPiPTLKDIRFKIPHGMNIAICG-------TVGsgkssllssilgevpKI--------SGNLKVCG-----------RK 689
Cdd:COG2274 486 DSP-PVLDNISLTIKPGERVAIVGrsgsgksTLL---------------KLllglyeptSGRILIDGidlrqidpaslRR 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 690 --AYIAQSPWIQSGKVEENILFGKP-MQREWYQRVLEACSLNKDLEVFPFRDQTVIGERGINLSGGQKQRIQIARALYQD 766
Cdd:COG2274 550 qiGVVLQDVFLFSGTIRENITLGDPdATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRN 629
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30682486 767 ADIYLFDDPFSAVDAHTGSHlFKEVLLGLLRNKTVIYVTHQLEFLPEADLILVMKDGRITQAGKYNEILESGTDFMELV 845
Cdd:COG2274 630 PRILILDEATSALDAETEAI-ILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELV 707
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
887-1475 |
9.09e-46 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 177.44 E-value: 9.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 887 PSPKGQLVQEEEREKGKVGFTVyqkymkLAyGGALVPIILVVQILFQVL--NIGSNYWMAWVTPvskdvkplvsgstLIL 964
Cdd:TIGR03796 139 PSLLRALWRRLRGSRGALLYLL------LA-GLLLVLPGLVIPAFSQIFvdEILVQGRQDWLRP-------------LLL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 965 VYVFLATASSFCILVRAMLSAMTGFKIATELFNQMHFRIFRASMSFFDATPIGRILNRASTDQSAVDLrLPSQFSNLAIA 1044
Cdd:TIGR03796 199 GMGLTALLQGVLTWLQLYYLRRLEIKLAVGMSARFLWHILRLPVRFFAQRHAGDIASRVQLNDQVAEF-LSGQLATTALD 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1045 AVNILGIIGVMGQVAWQVLIVFIPVIAACTWYRQYY--------ISAARELARLSGISRSplvqhfseTLSGITTIRSFD 1116
Cdd:TIGR03796 278 AVMLVFYALLMLLYDPVLTLIGIAFAAINVLALQLVsrrrvdanRRLQQDAGKLTGVAIS--------GLQSIETLKASG 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1117 QEPRFRTdimRLNDCYSRLrFHAISAMEWLCFRLDLLSTVAFALS--LVILVS---VPEGVINpsfAGLAVTYALNLNSL 1191
Cdd:TIGR03796 350 LESDFFS---RWAGYQAKL-LNAQQELGVLTQILGVLPTLLTSLNsaLILVVGglrVMEGQLT---IGMLVAFQSLMSSF 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1192 QA------TLIWTLCDLENKMISVERMLQYidiPSEPSLVIEST---RPEKSWPCRGEITICNLQVRYGPHLPMVLRGLT 1262
Cdd:TIGR03796 423 LEpvnnlvGFGGTLQELEGDLNRLDDVLRN---PVDPLLEEPEGsaaTSEPPRRLSGYVELRNITFGYSPLEPPLIENFS 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1263 CTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSIIPQEPTMFEGTVRSNL---DPl 1339
Cdd:TIGR03796 500 LTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLtlwDP- 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1340 eEYADDQIWEALDKCQLGDEIRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQET 1419
Cdd:TIGR03796 579 -TIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDN 657
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 30682486 1420 LRQHfsGCTVITIAHRISSVIDSDMVLLLDQGLIEEHDSPARLLeDKSSSFSKLVA 1475
Cdd:TIGR03796 658 LRRR--GCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELW-AVGGAYARLIR 710
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1206-1464 |
1.69e-45 |
|
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: 175.01 E-value: 1.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1206 MISVERMLQYIDIPSE-------PSLVIEstrpekswpcRGEITICNLQVRYGPHLPmVLRGLTCTFRGGLKTGIVGRTG 1278
Cdd:COG5265 326 LADMERMFDLLDQPPEvadapdaPPLVVG----------GGEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSG 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1279 CGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSIIPQEPTMFEGTVRSNLdpleEYA-----DDQIWEALDK 1353
Cdd:COG5265 395 AGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNI----AYGrpdasEEEVEAAARA 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1354 CQLGDEIRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLRQHFSGCTVITIA 1433
Cdd:COG5265 471 AQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIA 550
|
250 260 270
....*....|....*....|....*....|.
gi 30682486 1434 HRISSVIDSDMVLLLDQGLIEEHDSPARLLE 1464
Cdd:COG5265 551 HRLSTIVDADEILVLEAGRIVERGTHAELLA 581
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
925-1448 |
4.60e-45 |
|
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: 172.09 E-value: 4.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 925 ILVVQILFQVLNIGSNYWMAWVtpVSKDVKPLVSGSTLILVYVFLATASSFCILVRA---MLSAMTGFKIATELFNQMHF 1001
Cdd:TIGR02857 4 ALALLALLGVLGALLIIAQAWL--LARVVDGLISAGEPLAELLPALGALALVLLLRAllgWLQERAAARAAAAVKSQLRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1002 RIFRASMSFFDA----TPIGRILNRASTDQSAVD----LRLPsQFSNLAIAAVNILGIIGVMGQVAWQVLIVFIPVI--- 1070
Cdd:TIGR02857 82 RLLEAVAALGPRwlqgRPSGELATLALEGVEALDgyfaRYLP-QLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIpif 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1071 -AACTWYRQyyiSAARE----LARLSGisrsplvqHFSETLSGITTIRSFDQEPRFRTDIMRLNDCYSRlrfhaiSAMEW 1145
Cdd:TIGR02857 161 mILIGWAAQ---AAARKqwaaLSRLSG--------HFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRE------RTMRV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1146 LcfRLDLLSTvaFALSLVILVSVpegvinpsfAGLAVTYALNLNSLQATL---IWTLC-----------------DLENK 1205
Cdd:TIGR02857 224 L--RIAFLSS--AVLELFATLSV---------ALVAVYIGFRLLAGDLDLatgLFVLLlapefylplrqlgaqyhARADG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1206 MISVERMLQYIDIPSEPSLVIESTRPEKSWPcrgeITICNLQVRYgPHLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLI 1285
Cdd:TIGR02857 291 VAAAEALFAVLDAAPRPLAGKAPVTAAPASS----LEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1286 QTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSIIPQEPTMFEGTVRSNLDPLEEYADD-QIWEALDKCQLGDEIRKKE 1364
Cdd:TIGR02857 366 NLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDaEIREALERAGLDEFVAALP 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1365 LKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLRQHFSGCTVITIAHRISSVIDSDM 1444
Cdd:TIGR02857 446 QGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADR 525
|
....
gi 30682486 1445 VLLL 1448
Cdd:TIGR02857 526 IVVL 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1239-1453 |
8.17e-45 |
|
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: 161.99 E-value: 8.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1239 GEITICNLQVRYGPHLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRL 1318
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1319 SIIPQEPTMFEGTVRSNLDPLEEYADDQ-IWEALDKCQLGDEIRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSK 1397
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDErILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 30682486 1398 VLILDEATASVDTATDTLIQETLRQHFSGCTVITIAHRISSVIDSDMVLLLDQGLI 1453
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
923-1215 |
1.07e-44 |
|
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: 164.80 E-value: 1.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 923 PIILVVQILF----QVLNIGSNYWMA-WVTPVSKD---VKPLVSGSTLIL----------VYVFLATASSFCILvrAMLS 984
Cdd:cd18601 2 VFVFILLVLLniaaQVLYVLSDWWLSyWANLEEKLndtTDRVQGENSTNVdiedldrdfnLGIYAGLTAATFVF--GFLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 985 AMTGFKIA----TELFNQMHFRIFRASMSFFDATPIGRILNRASTDQSAVDLRLPSQFSNLAIAAVNILGIIGVMGQVAW 1060
Cdd:cd18601 80 SLLFFHVAvsasKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1061 QVLIVFIPVIAACTWYRQYYISAARELARLSGISRSPLVQHFSETLSGITTIRSFDQEPRFRTDIMRLNDCYSRLRFHAI 1140
Cdd:cd18601 160 WVLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30682486 1141 SAMEWLCFRLDLLSTVAFALSLVILVSVPEGvINPSFAGLAVTYALNLNslqATLIWTL---CDLENKMISVERMLQY 1215
Cdd:cd18601 240 ATSRWLAVRLDALCALFVTVVAFGSLFLAES-LDAGLVGLSLSYALTLM---GTFQWCVrqsAEVENLMTSVERVLEY 313
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
640-863 |
1.52e-44 |
|
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: 163.49 E-value: 1.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 640 PTLKDIRFKIPHGMNIAICGTVGSGKSSLLSSILGEVPKISGNLKVCGRKAYIAQSPWIQSGKVEENILFGKPMQREWYQ 719
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 720 RVLEACSLNKDLEVFPFRDQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEVLLGLLRNK 799
Cdd:cd03291 131 SVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANK 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30682486 800 TVIYVTHQLEFLPEADLILVMKDGRITQAGKYNEILESGTDFmelvgahTDALAAVDSYEKGSA 863
Cdd:cd03291 211 TRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDF-------SSKLMGYDTFDQFSA 267
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
989-1466 |
6.36e-44 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 171.83 E-value: 6.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 989 FKIATELFN-QMHFRIFRA----SMSFFDATPIGRILNRASTDQSAVDLRLPSQFSNLAIAAVNILGIIGVMGQVAWQ-- 1061
Cdd:TIGR00958 225 FNYTMARINlRIREDLFRSllrqDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRlt 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1062 -VLIVFIP-VIAACTWYRQYYISAAREL----ARLSGISRsplvqhfsETLSGITTIRSFDQE----PRFRTdimRLNDC 1131
Cdd:TIGR00958 305 mVTLINLPlVFLAEKVFGKRYQLLSEELqeavAKANQVAE--------EALSGMRTVRSFAAEegeaSRFKE---ALEET 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1132 YS--RLRFHAISAMEW---LCFRLDLLSTVAFALSLVILVSVPEGVInPSFaglaVTYALNLNSLQATLIWTLCDLENKM 1206
Cdd:TIGR00958 374 LQlnKRKALAYAGYLWttsVLGMLIQVLVLYYGGQLVLTGKVSSGNL-VSF----LLYQEQLGEAVRVLSYVYSGMMQAV 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1207 ISVERMLQYIDipSEPSlvIESTRPEKSWPCRGEITICNLQVRYG--PHLPmVLRGLTCTFRGGLKTGIVGRTGCGKSTL 1284
Cdd:TIGR00958 449 GASEKVFEYLD--RKPN--IPLTGTLAPLNLEGLIEFQDVSFSYPnrPDVP-VLKGLTFTLHPGEVVALVGPSGSGKSTV 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1285 IQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSIIPQEPTMFEGTVRSNLD-PLEEYADDQIWEALDKCQLGDEIRKK 1363
Cdd:TIGR00958 524 AALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAyGLTDTPDEEIMAAAKAANAHDFIMEF 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1364 ELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETlrQHFSGCTVITIAHRISSVIDSD 1443
Cdd:TIGR00958 604 PNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIAHRLSTVERAD 681
|
490 500
....*....|....*....|...
gi 30682486 1444 MVLLLDQGLIEEHDSPARLLEDK 1466
Cdd:TIGR00958 682 QILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
367-598 |
1.55e-42 |
|
Six-transmembrane helical domain 1 (TMD1) 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: 350041 [Multi-domain] Cd Length: 293 Bit Score: 158.00 E-value: 1.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 367 NWYF-RLQKAGIGMRSVLVSMIYEKGLTLPCYSKQGHTSGEIINLMTVDAERISAFSWYMHDPWILVLQISLALLILYRS 445
Cdd:cd18597 61 NHFFyRSMLTGAQVRAALTKAIYRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 446 LGLGSIAAFAATFLVMLGNIPLAKLEEKFQGNLMESKDNRMKKTSEALLNMRILKLQGWEMKFLHKILDLRGIEAGWLKK 525
Cdd:cd18597 141 LGPSALVGIGVLILSIPLQGFLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRK 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30682486 526 FVYNSAAISSVLWAAPSFVSATAFGACMLLKIPLESGKIIAALATFRILQTPIYKLPDTISMIVQTKVSLDRI 598
Cdd:cd18597 221 LQILRSILTAVAFSLPVLASMLSFITYYATGHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
596-838 |
1.88e-41 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 161.85 E-value: 1.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 596 DRIATFLCLDDLQQDGMERLPSGSSKMDVEVSNGAFSWDDSSPIptLKDIRFKIPHGMNIAICG-------TVGSGKSSL 668
Cdd:COG4988 309 EKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPA--LDGLSLTIPPGERVALVGpsgagksTLLNLLLGF 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 669 lssilgeVPKISGNLKVCGRK-------------AYIAQSPWIQSGKVEENILFGKP-MQREWYQRVLEACSLNKDLEVF 734
Cdd:COG4988 387 -------LPPYSGSILINGVDlsdldpaswrrqiAWVPQNPYLFAGTIRENLRLGRPdASDEELEAALEAAGLDEFVAAL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 735 PFRDQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLfKEVLLGLLRNKTVIYVTHQLEFLPEA 814
Cdd:COG4988 460 PDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEI-LQALRRLAKGRTVILITHRLALLAQA 538
|
250 260
....*....|....*....|....
gi 30682486 815 DLILVMKDGRITQAGKYNEILESG 838
Cdd:COG4988 539 DRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1241-1475 |
4.26e-41 |
|
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: 151.87 E-value: 4.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSI 1320
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1321 IPQEPTMFEGTVRSNLDPLEEYAD-DQIWEALDKCQLGDEIRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVL 1399
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSmERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30682486 1400 ILDEATASVDTATDTLIQETLRQHFSGCTVITIAHRISSVIDSDMVLLLDQGLIEEHDSPARLLeDKSSSFSKLVA 1475
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELL-AENGLYAYLYQ 235
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
989-1435 |
5.86e-41 |
|
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: 159.83 E-value: 5.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 989 FKIATELFNQMHFRIFRASMSFFDATPIGRILNRASTDQSAVDLRLPSQFSNLAIAAVNILGIIGVMGQVAWQVLIVFIp 1068
Cdd:TIGR02868 82 LRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILA- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1069 VIAACTWYRQYYISAAreLARLSGISRSPLVQHFS----ETLSGITTIRSFDQEPRFRTDIMRLNDCYSRLRFHAISAME 1144
Cdd:TIGR02868 161 AGLLLAGFVAPLVSLR--AARAAEQALARLRGELAaqltDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1145 WLcfrlDLLSTVAFALSLV--ILVSVP---EGVINPSFAGLAVTYALNLNSLQATLIWTLCDLENKMISVERMLQYIDip 1219
Cdd:TIGR02868 239 LG----AALTLLAAGLAVLgaLWAGGPavaDGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLD-- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1220 sEPSLVIESTRPEKSWPCRGEITICNLQVRYG-PHLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGE 1298
Cdd:TIGR02868 313 -AAGPVAEGSAPAAGAVGLGKPTLELRDLSAGyPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGE 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1299 IRIDGINILTIGLHDLRSRLSIIPQEPTMFEGTVRSNLD-PLEEYADDQIWEALDKCQLGDEIRKKELKLDSPVSENGQN 1377
Cdd:TIGR02868 392 VTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRlARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGAR 471
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 30682486 1378 WSVGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLRQHFSGCTVITIAHR 1435
Cdd:TIGR02868 472 LSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
311-598 |
1.09e-40 |
|
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 1 (TMD1) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and they 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: 350035 [Multi-domain] Cd Length: 309 Bit Score: 153.16 E-value: 1.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 311 LSTLFAFVYTVSCYVAPYLMDTFVQYLNGQRQYSNQ------------------GVVLVTTFFVAKLVECQARRNWYFRL 372
Cdd:cd18591 1 LGGILKLLGDLLGFVGPLCISGIVDYVEENTYSSSNstdklsvsyvtveeffsnGYVLAVILFLALLLQATFSQASYHIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 373 QKAGIGMRSVLVSMIYEKGLTLPCY--SKQGHTSGEIINLMTVDAERISAFSWYMHDPWILVLQISLALLILYRSLGLGS 450
Cdd:cd18591 81 IREGIRLKTALQAMIYEKALRLSSWnlSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 451 IAAFAATFLVMLGNIPLAKLEEKFQGNLMESKDNRMKKTSEALLNMRILKLQGWEMKFLHKILDLRGIEAGWLKKFVYNS 530
Cdd:cd18591 161 LIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYW 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30682486 531 AAISSVLWAAPSFVSATAFGACMLLK-IPLESGKIIAALATFRILQTPIYKLPDTISMIVQTKVSLDRI 598
Cdd:cd18591 241 SLMTFLTQASPILVTLVTFGLYPYLEgEPLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1258-1475 |
2.73e-37 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 149.73 E-value: 2.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1258 LRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSIIPQEPTMFEGTVRSNLD 1337
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1338 PLEEYA-DDQIWEALDKCQLGDEIRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLI 1416
Cdd:PRK13657 431 VGRPDAtDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKV 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 30682486 1417 QETLRQHFSGCTVITIAHRISSVIDSDMVLLLDQGlieehdspaRLLEdkSSSFSKLVA 1475
Cdd:PRK13657 511 KAALDELMKGRTTFIIAHRLSTVRNADRILVFDNG---------RVVE--SGSFDELVA 558
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1252-1453 |
1.41e-35 |
|
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: 135.68 E-value: 1.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1252 PHLPmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSIIPQEPTMFEGT 1331
Cdd:cd03248 25 PDTL-VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFARS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1332 VRSNLD-PLEEYADDQIWEALDKCQLGDEIRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVLILDEATASVDT 1410
Cdd:cd03248 104 LQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 30682486 1411 ATDTLIQETLRQHFSGCTVITIAHRISSVIDSDMVLLLDQGLI 1453
Cdd:cd03248 184 ESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1002-1464 |
1.52e-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: 142.40 E-value: 1.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1002 RIFRASMSFFDATPIGRILNRASTdQSAVDLRLPSQFSNLAIAAVNILGIIGVMGQVAWQ-------VLIVFIPVIAACT 1074
Cdd:TIGR03797 218 RLLRLPVSFFRQYSTGDLASRAMG-ISQIRRILSGSTLTTLLSGIFALLNLGLMFYYSWKlalvavaLALVAIAVTLVLG 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1075 WYRQYYISAAREL-ARLSGIsrspLVQhfseTLSGITTIRSFDQEPRFRTDIMRLndcYSRLRFHAISAMEWLcfrlDLL 1153
Cdd:TIGR03797 297 LLQVRKERRLLELsGKISGL----TVQ----LINGISKLRVAGAENRAFARWAKL---FSRQRKLELSAQRIE----NLL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1154 STVAFAL----SLVI--LVSVPEGVINPSFAG-LAVTYALNLNSLQAT-LIWTLCDLENKMISVERMLQYIDipSEPSLV 1225
Cdd:TIGR03797 362 TVFNAVLpvltSAALfaAAISLLGGAGLSLGSfLAFNTAFGSFSGAVTqLSNTLISILAVIPLWERAKPILE--ALPEVD 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1226 IESTRPEKswpCRGEITICNLQVRYGPHLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGIN 1305
Cdd:TIGR03797 440 EAKTDPGK---LSGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQD 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1306 ILTIGLHDLRSRLSIIPQEPTMFEGTVRSNLDPLEEYADDQIWEALDKCQLGDEIRKKELKLDSPVSENGQNWSVGQRQL 1385
Cdd:TIGR03797 517 LAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQR 596
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30682486 1386 VCLGRVLLKRSKVLILDEATASVDTATDTLIQETLRQhfSGCTVITIAHRISSVIDSDMVLLLDQGLIEEHDSPARLLE 1464
Cdd:TIGR03797 597 LLIARALVRKPRILLFDEATSALDNRTQAIVSESLER--LKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMA 673
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
998-1466 |
4.69e-34 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 139.77 E-value: 4.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 998 QMHFRIFRASM----SFFDATPIGRILNRASTDQSAVdlrlPSQFSNLAIAAV----NILGIIGVMGQVAWQ---VLIVF 1066
Cdd:PRK11176 99 TMRRRLFGHMMgmpvSFFDKQSTGTLLSRITYDSEQV----ASSSSGALITVVregaSIIGLFIMMFYYSWQlslILIVI 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1067 IPVIAactWYRQYYISAARELARLSGISRSPLVQHFSETLSGITTIRSFD-QEprfrTDIMRLNDCYSRLRFHAisamew 1145
Cdd:PRK11176 175 APIVS---IAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGgQE----VETKRFDKVSNRMRQQG------ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1146 lcfrldllstvafaLSLVILVSVPEGVIN--PSFAGLAVTYALNLNSLQATLI-WTLCDLENKMISVERMLQ-------- 1214
Cdd:PRK11176 242 --------------MKMVSASSISDPIIQliASLALAFVLYAASFPSVMDTLTaGTITVVFSSMIALMRPLKsltnvnaq 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1215 -------------YIDIPSEP---SLVIEstrpekswPCRGEITICNLQVRY-GPHLPmVLRGLTCTFRGGLKTGIVGRT 1277
Cdd:PRK11176 308 fqrgmaacqtlfaILDLEQEKdegKRVIE--------RAKGDIEFRNVTFTYpGKEVP-ALRNINFKIPAGKTVALVGRS 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1278 GCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSIIPQEPTMFEGTVRSNLD--PLEEYADDQIWEALDKCQ 1355
Cdd:PRK11176 379 GSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAyaRTEQYSREQIEEAARMAY 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1356 LGDEIRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLRQHFSGCTVITIAHR 1435
Cdd:PRK11176 459 AMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHR 538
|
490 500 510
....*....|....*....|....*....|.
gi 30682486 1436 ISSVIDSDMVLLLDQGLIEEHDSPARLLEDK 1466
Cdd:PRK11176 539 LSTIEKADEILVVEDGEIVERGTHAELLAQN 569
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1258-1406 |
1.35e-33 |
|
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: 126.99 E-value: 1.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1258 LRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSIIPQEPTMF-EGTVRSNL 1336
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30682486 1337 -------DPLEEYADDQIWEALDKCQLGDeirkkelKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVLILDEATA 1406
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEKLGLGD-------LADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1241-1466 |
1.52e-33 |
|
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: 129.76 E-value: 1.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHLPmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSI 1320
Cdd:COG1122 1 IELENLSFSYPGGTP-ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1321 IPQEPT--MFEGTVRS-------NLDPLEEYADDQIWEALDKCQLGDeirkkelKLDSPVSEngqnWSVGQRQLVCLGRV 1391
Cdd:COG1122 80 VFQNPDdqLFAPTVEEdvafgpeNLGLPREEIRERVEEALELVGLEH-------LADRPPHE----LSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30682486 1392 LLKRSKVLILDEATASVDTATDTLIQETLRQ-HFSGCTVITIAHRISSVID-SDMVLLLDQGLIEEHDSPARLLEDK 1466
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
387-836 |
4.63e-33 |
|
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: 136.43 E-value: 4.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 387 IYEKGLTLPCYSKQGHTSGEIINLMTVDAERISAFswYMH---DPWILVLQISLALLILYR-SLGLGsiAAFAATFLVML 462
Cdd:COG4987 94 LYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNL--YLRvllPLLVALLVILAAVAFLAFfSPALA--LVLALGLLLAG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 463 GNIPL--AKLEEKFQGNLMESKDNRMKKTSEALLNMRILKLQGWEMKFLHKILDLrgiEAGWLK------KFVYNSAAIS 534
Cdd:COG4987 170 LLLPLlaARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAA---EARLAAaqrrlaRLSALAQALL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 535 S---------VLWAAPSFVSATAFGACMLLKIPLesgkiiAALATFRILQTpiykLPDTISMIVQTKVSLDRIAtflclD 605
Cdd:COG4987 247 QlaaglavvaVLWLAAPLVAAGALSGPLLALLVL------AALALFEALAP----LPAAAQHLGRVRAAARRLN-----E 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 606 DLQQDGMERLPSGSSKM----DVEVSNGAFSWDDSSPiPTLKDIRFKIPHGMNIAICG-------TVGSGKSSLlssilg 674
Cdd:COG4987 312 LLDAPPAVTEPAEPAPApggpSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGpsgsgksTLLALLLRF------ 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 675 eVPKISGNLKVCGRK-------------AYIAQSPWIQSGKVEENILFGKP------MQRewyqrVLEACSLNKDLEVFP 735
Cdd:COG4987 385 -LDPQSGSITLGGVDlrdldeddlrrriAVVPQRPHLFDTTLRENLRLARPdatdeeLWA-----ALERVGLGDWLAALP 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 736 FRDQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEvLLGLLRNKTVIYVTHQLEFLPEAD 815
Cdd:COG4987 459 DGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLAD-LLEALAGRTVLLITHRLAGLERMD 537
|
490 500
....*....|....*....|.
gi 30682486 816 LILVMKDGRITQAGKYNEILE 836
Cdd:COG4987 538 RILVLEDGRIVEQGTHEELLA 558
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1261-1453 |
1.38e-32 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 135.36 E-value: 1.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1261 LTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVePAAGEIRIDGINILTIGLHDLRSRLSIIPQEPTMFEGTVRSNL---D 1337
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVllgN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1338 PleEYADDQIWEALDKCQLGDEIRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQ 1417
Cdd:PRK11174 448 P--DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVM 525
|
170 180 190
....*....|....*....|....*....|....*.
gi 30682486 1418 ETLRQHFSGCTVITIAHRISSVIDSDMVLLLDQGLI 1453
Cdd:PRK11174 526 QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQI 561
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1241-1451 |
1.41e-32 |
|
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: 125.02 E-value: 1.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSI 1320
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1321 IPQEPTMFEGTVRSNLdpleeyaddqiwealdkcqlgdeirkkelkldspvsengqnWSVGQRQLVCLGRVLLKRSKVLI 1400
Cdd:cd03246 81 LPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 30682486 1401 LDEATASVDTATDTLIQETLRQ-HFSGCTVITIAHRISSVIDSDMVLLLDQG 1451
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAAlKAAGATRIVIAHRPETLASADRILVLEDG 171
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
1258-1474 |
3.36e-32 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 134.25 E-value: 3.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1258 LRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSIIPQEPTMFEGTVRSNLD 1337
Cdd:TIGR01192 351 VFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1338 PLEEYA-DDQIWEALDKCQLGDEIRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLI 1416
Cdd:TIGR01192 431 LGREGAtDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARV 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 30682486 1417 QETLRQHFSGCTVITIAHRISSVIDSDMVLLLDQGLIEEHDSPARLLEdKSSSFSKLV 1474
Cdd:TIGR01192 511 KNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQ-KDGRFYKLL 567
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1208-1466 |
4.83e-32 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 133.41 E-value: 4.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1208 SVERMLQYIDIPSEPSLVIESTRPEKswpcRGEITICNLQVRYGPHLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQT 1287
Cdd:PRK11160 310 SARRINEITEQKPEVTFPTTSTAAAD----QVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1288 LFRIVEPAAGEIRIDGINILTIGLHDLRSRLSIIPQEPTMFEGTVRSNLD-PLEEYADDQIWEALDKCQLGDEIRKKElK 1366
Cdd:PRK11160 386 LTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLlAAPNASDEALIEVLQQVGLEKLLEDDK-G 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1367 LDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLRQHFSGCTVITIAHRISSVIDSDMVL 1446
Cdd:PRK11160 465 LNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRIC 544
|
250 260
....*....|....*....|
gi 30682486 1447 LLDQGLIEEHDSPARLLEDK 1466
Cdd:PRK11160 545 VMDNGQIIEQGTHQELLAQQ 564
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
624-844 |
5.10e-32 |
|
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: 125.42 E-value: 5.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 624 VEVSNGAFSWDDSSPIptLKDIRFKIPHGMNIAICG-------TVGsgkssllssilgevpKI--------SGNLKVCG- 687
Cdd:cd03253 1 IEFENVTFAYDPGRPV--LKDVSFTIPAGKKVAIVGpsgsgksTIL---------------RLlfrfydvsSGSILIDGq 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 688 ----------RKA--YIAQSPWIQSGKVEENILFGKPMQREwyQRVLEAC---SLNKDLEVFPFRDQTVIGERGINLSGG 752
Cdd:cd03253 64 direvtldslRRAigVVPQDTVLFNDTIGYNIRYGRPDATD--EEVIEAAkaaQIHDKIMRFPDGYDTIVGERGLKLSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 753 QKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEvLLGLLRNKTVIYVTHQLEFLPEADLILVMKDGRITQAGKYN 832
Cdd:cd03253 142 EKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAA-LRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHE 220
|
250
....*....|..
gi 30682486 833 EILESGTDFMEL 844
Cdd:cd03253 221 ELLAKGGLYAEM 232
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
624-844 |
6.32e-32 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 125.04 E-value: 6.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 624 VEVSNGAFSWDDSSPiPTLKDIRFKIPHGMNIAICG-------TVGSGkssllssilgeVPKI----SGNLKVCG----- 687
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGpsgsgksTLVNL-----------IPRFydvdSGRILIDGhdvrd 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 688 ------RK--AYIAQSPWIQSGKVEENILFGKP-MQREWYQRVLEACSLNKDLEVFPFRDQTVIGERGINLSGGQKQRIQ 758
Cdd:cd03251 69 ytlaslRRqiGLVSQDVFLFNDTVAENIAYGRPgATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 759 IARALYQDADIYLFDDPFSAVDAHTgSHLFKEVLLGLLRNKTVIYVTHQLEFLPEADLILVMKDGRITQAGKYNEILESG 838
Cdd:cd03251 149 IARALLKDPPILILDEATSALDTES-ERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQG 227
|
....*.
gi 30682486 839 TDFMEL 844
Cdd:cd03251 228 GVYAKL 233
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
623-838 |
7.47e-32 |
|
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: 125.03 E-value: 7.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 623 DVEVSNGAFSWDdsSPIPTLKDIRFKIPHGMNIAICG-------TVGSGKSSLLSSILGEVpKISG-NLKVCGRK----- 689
Cdd:cd03254 2 EIEFENVNFSYD--EKKPVLKDINFSIKPGETVAIVGptgagktTLINLLMRFYDPQKGQI-LIDGiDIRDISRKslrsm 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 690 -AYIAQSPWIQSGKVEENILFGKPMQREwyQRVLEAC----------SLNKDLEvfpfrdqTVIGERGINLSGGQKQRIQ 758
Cdd:cd03254 79 iGVVLQDTFLFSGTIMENIRLGRPNATD--EEVIEAAkeagahdfimKLPNGYD-------TVLGENGGNLSQGERQLLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 759 IARALYQDADIYLFDDPFSAVDAHTGShLFKEVLLGLLRNKTVIYVTHQLEFLPEADLILVMKDGRITQAGKYNEILESG 838
Cdd:cd03254 150 IARAMLRDPKILILDEATSNIDTETEK-LIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
387-836 |
7.66e-31 |
|
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: 129.84 E-value: 7.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 387 IYEKGLTLPCYSKQGHTSGEIINLMTVDAERISAfswYMHDPWILVLQ-----ISLALLILYRSLGLGSIAAFAATFLVM 461
Cdd:TIGR02203 93 MFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVAS---AATDAFIVLVRetltvIGLFIVLLYYSWQLTLIVVVMLPVLSI 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 462 LGNIpLAKLEEKFQGNLMESKDNRMKKTSEALLNMRILKLQGWEMKFLHKILDLRGIEAGWLKKFVYNSAAISSVLwaap 541
Cdd:TIGR02203 170 LMRR-VSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPIT---- 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 542 SFVSATAFGACMLLKI------PLESGKIIAALATFRILQTPIYKLPDTISMIVQTKVSLDRIATFLCLDDLQQDGmeRL 615
Cdd:TIGR02203 245 QLIASLALAVVLFIALfqaqagSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKDTG--TR 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 616 PSGSSKMDVEVSNGAFSWDDSSpIPTLKDIRFKIPHGMNIAICGTVGSGKSSLLSSILGEVPKISGNLKVCG-------- 687
Cdd:TIGR02203 323 AIERARGDVEFRNVTFRYPGRD-RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGhdladytl 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 688 ---RK--AYIAQSPWIQSGKVEENILFGKPMQ--REWYQRVLEACSLNKDLEVFPFRDQTVIGERGINLSGGQKQRIQIA 760
Cdd:TIGR02203 402 aslRRqvALVSQDVVLFNDTIANNIAYGRTEQadRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIA 481
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30682486 761 RALYQDADIYLFDDPFSAVDAHTGSHLfKEVLLGLLRNKTVIYVTHQLEFLPEADLILVMKDGRITQAGKYNEILE 836
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESERLV-QAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLA 556
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1242-1451 |
1.77e-30 |
|
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: 118.50 E-value: 1.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1242 TICNLQVRYGPHLpmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSII 1321
Cdd:cd00267 1 EIENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1322 PQeptmfegtvrsnLdpleeyaddqiwealdkcqlgdeirkkelkldspvsengqnwSVGQRQLVCLGRVLLKRSKVLIL 1401
Cdd:cd00267 79 PQ------------L------------------------------------------SGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 30682486 1402 DEATASVDTATDTLIQETLRQHF-SGCTVITIAHRISSVID-SDMVLLLDQG 1451
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELaADRVIVLKDG 156
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
624-824 |
3.67e-30 |
|
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: 117.87 E-value: 3.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 624 VEVSNGAFSWDDSSPiPTLKDIRFKIPHGMNIAICG-------TVGsgkssllssilgevpKI--------SGNLKVCG- 687
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGpsgsgksTLL---------------KLllrlydptSGEILIDGv 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 688 ----------RK--AYIAQSPWIQSGKVEENILfgkpmqrewyqrvleacslnkdlevfpfrdqtvigerginlSGGQKQ 755
Cdd:cd03228 65 dlrdldleslRKniAYVPQDPFLFSGTIRENIL-----------------------------------------SGGQRQ 103
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30682486 756 RIQIARALYQDADIYLFDDPFSAVDAHTgSHLFKEVLLGLLRNKTVIYVTHQLEFLPEADLILVMKDGR 824
Cdd:cd03228 104 RIAIARALLRDPPILILDEATSALDPET-EALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1241-1455 |
4.97e-30 |
|
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: 117.80 E-value: 4.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGlHDLRSRLSI 1320
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1321 IPQEPTMFEGTVRSNLdpleeyaddqiwealdkcqlgdeirkkelkldspvsenGQNWSVGQRQLVCLGRVLLKRSKVLI 1400
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 30682486 1401 LDEATASVDTATDTLIQETLRQHFSGCTVITIAHRISSVIDSDMVLLLDQGLIEE 1455
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
314-598 |
9.37e-30 |
|
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent.
Pssm-ID: 350038 [Multi-domain] Cd Length: 291 Bit Score: 120.82 E-value: 9.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 314 LFAFVYTVSCYVAPYLMDTFVQYLNGQRQYSNQ-------GVVLVTTFFVAklvecqARRNWYFRLQKAGIGMRSVLVSM 386
Cdd:cd18594 4 ILLFLEESLKIVQPLLLGRLVAYFVPDSTVTKTeaylyalGLSLCAFLRVL------LHHPYFFGLHRYGMQLRIALSSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 387 IYEKGLTLPCYSKQGHTSGEIINLMTVDAERISAFSWYMHDPWILVLQISLALLILYRSLGLGSIAAFAATFLVMLGNIP 466
Cdd:cd18594 78 IYKKTLKLSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 467 LAKLEEKFQGNLMESKDNRMKKTSEALLNMRILKLQGWEMKFLHKILDLRGIEAGWLKKFVYNSAAISSVLWAAPSFVSA 546
Cdd:cd18594 158 LGKLFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSF 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 30682486 547 TAFGACMLLKIPLESGKIIAALATFRILQTPI-YKLPDTISMIVQTKVSLDRI 598
Cdd:cd18594 238 ATFVPYVLTGNTLTARKVFTVISLLNALRMTItRFFPESIQTLSESRVSLKRI 290
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1241-1472 |
1.08e-29 |
|
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: 119.14 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGP--HLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRL 1318
Cdd:COG1124 2 LEVRNLSVSYGQggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1319 SIIPQEPtmfegtvRSNLDP-------LEE--------YADDQIWEALDKCQLGDEIRKK---ELkldspvsengqnwSV 1380
Cdd:COG1124 82 QMVFQDP-------YASLHPrhtvdriLAEplrihglpDREERIAELLEQVGLPPSFLDRyphQL-------------SG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1381 GQRQLVCLGRVLLKRSKVLILDEATASVDTATDT----LIQETLRQHfsGCTVITIAHRIsSVID--SDMVLLLDQGLIE 1454
Cdd:COG1124 142 GQRQRVAIARALILEPELLLLDEPTSALDVSVQAeilnLLKDLREER--GLTYLFVSHDL-AVVAhlCDRVAVMQNGRIV 218
|
250
....*....|....*...
gi 30682486 1455 EHDSPARLLEDKSSSFSK 1472
Cdd:COG1124 219 EELTVADLLAGPKHPYTR 236
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1241-1463 |
1.17e-29 |
|
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: 119.38 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHLpmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSI 1320
Cdd:COG1120 2 LEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1321 IPQEPTM-FEGTVR-----------SNLDPLEEYADDQIWEALDKCQLGDeirkkeLKlDSPVSEngqnWSVGQRQLVCL 1388
Cdd:COG1120 80 VPQEPPApFGLTVRelvalgryphlGLFGRPSAEDREAVEEALERTGLEH------LA-DRPVDE----LSGGERQRVLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1389 GRVLLKRSKVLILDEATASVDTATDTLIQETLRQ--HFSGCTVITIAHrissviD-------SDMVLLLDQGLIEEHDSP 1459
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLH------DlnlaaryADRLVLLKDGRIVAQGPP 222
|
....
gi 30682486 1460 ARLL 1463
Cdd:COG1120 223 EEVL 226
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1241-1465 |
4.41e-29 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 117.09 E-value: 4.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHLpmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTiGLHDLRSRLSI 1320
Cdd:COG1131 1 IEVRGLTKRYGDKT--ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1321 IPQEPTMFEG-TVRSNLD--------PLEEyADDQIWEALDKCQLGDeirkkelKLDSPVSengqNWSVGQRQLVCLGRV 1391
Cdd:COG1131 78 VPQEPALYPDlTVRENLRffarlyglPRKE-ARERIDELLELFGLTD-------AADRKVG----TLSGGMKQRLGLALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1392 LLKRSKVLILDEATASVDTATDTLIQETLRQHFS-GCTVItiahrISS-VID-----SDMVLLLDQGLIEEHDSP----A 1460
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLRELAAeGKTVL-----LSThYLEeaerlCDRVAIIDKGRIVADGTPdelkA 220
|
....*
gi 30682486 1461 RLLED 1465
Cdd:COG1131 221 RLLED 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1245-1465 |
6.18e-29 |
|
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: 123.09 E-value: 6.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1245 NLQVRY---GPHLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIG---LHDLRSRL 1318
Cdd:COG1123 265 NLSKRYpvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRELRRRV 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1319 SIIPQEPT------MfegTVRSNL-DPL-------EEYADDQIWEALDKCQLGDEIRKK---ELkldspvsengqnwSVG 1381
Cdd:COG1123 345 QMVFQDPYsslnprM---TVGDIIaEPLrlhgllsRAERRERVAELLERVGLPPDLADRyphEL-------------SGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1382 QRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLR--QHFSGCTVITIAHRISSVID-SDMVLLLDQGLIEEHDS 1458
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGP 488
|
....*..
gi 30682486 1459 PARLLED 1465
Cdd:COG1123 489 TEEVFAN 495
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1241-1465 |
6.41e-29 |
|
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: 123.09 E-value: 6.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAA---GEIRIDGINILTIGLHDLRSR 1317
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1318 LSIIPQEPTmfegtvrSNLDPLeeYADDQIWEALDKCQL-GDEIRKK------ELKLDSPVSENGQNWSVGQRQLVCLGR 1390
Cdd:COG1123 85 IGMVFQDPM-------TQLNPV--TVGDQIAEALENLGLsRAEARARvlelleAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30682486 1391 VLLKRSKVLILDEATASVDTATDTLIQETLR--QHFSGCTVITIAHRISSVID-SDMVLLLDQGLIEEHDSPARLLED 1465
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1241-1464 |
1.05e-28 |
|
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: 116.11 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPhlPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHdLRSRLSI 1320
Cdd:COG4555 2 IEVENLSKKYGK--VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1321 IPQEPTMFEG-TVRSNLDPLEEYADDQIWEALDKCqlgDEIRKKeLKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVL 1399
Cdd:COG4555 79 LPDERGLYDRlTVRENIRYFAELYGLFDEELKKRI---EELIEL-LGLEEFLDRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30682486 1400 ILDEATASVDTATDTLIQETLRQHF-SGCTVITIAHRISSVID-SDMVLLLDQGLIEEHDSPARLLE 1464
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELRE 221
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
597-836 |
2.18e-28 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 122.13 E-value: 2.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 597 RIATFLCLDDLQQDGMERLPSGSSKMDVEVSngAFSWDDSSPiPTLKDIRFKIPHGMNIAICG-------TVGSGKSSLL 669
Cdd:PRK10789 289 RIRAMLAEAPVVKDGSEPVPEGRGELDVNIR--QFTYPQTDH-PALENVNFTLKPGQMLGICGptgsgksTLLSLIQRHF 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 670 SSILGEVPKISGNLKVC------GRKAYIAQSPWIQSGKVEENILFGKP-MQREWYQRVLEACSLNKDLEVFPFRDQTVI 742
Cdd:PRK10789 366 DVSEGDIRFHDIPLTKLqldswrSRLAVVSQTPFLFSDTVANNIALGRPdATQQEIEHVARLASVHDDILRLPQGYDTEV 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 743 GERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEvLLGLLRNKTVIYVTHQLEFLPEADLILVMKD 822
Cdd:PRK10789 446 GERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHN-LRQWGEGRTVIISAHRLSALTEASEILVMQH 524
|
250
....*....|....
gi 30682486 823 GRITQAGKYNEILE 836
Cdd:PRK10789 525 GHIAQRGNHDQLAQ 538
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1241-1462 |
2.83e-28 |
|
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: 114.59 E-value: 2.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHlpMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVE-----PAAGEIRIDGINILTIGLHD-- 1313
Cdd:cd03260 1 IELRDLNVYYGDK--HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1314 LRSRLSIIPQEPTMFEGTVRSNLD--------PLEEYADDQIWEALDKCQLGDEI--RKKELKLdspvsengqnwSVGQR 1383
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAyglrlhgiKLKEELDERVEEALRKAALWDEVkdRLHALGL-----------SGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1384 QLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLRQHFSGCTVITIAH------RIssvidSDMVLLLDQGLIEEHD 1457
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHnmqqaaRV-----ADRTAFLLNGRLVEFG 222
|
....*
gi 30682486 1458 SPARL 1462
Cdd:cd03260 223 PTEQI 227
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
314-598 |
3.28e-28 |
|
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: 116.16 E-value: 3.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 314 LFAFVYTVSCYVAPYLMDTFVQYLNGQRQYSNQGVVLVTTFFVAKLVECQARRNWYFRLQKAGIGMRSVLVSMIYEKGLT 393
Cdd:cd18559 4 LIKLVLCNHVFSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 394 LPCYSKQGHTSGEIINLMTVDAERISAFSWYMHDPWILVLQISLALLILYRSLGLGSIAAFAATFLVMLGNIPLAKLEEK 473
Cdd:cd18559 84 SPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 474 FQGNLMESKDNRMKKTSEALLNMRILKLQGWEMKFLHKILDLRGIEAGWLKKFVYNsAAISSVLWAA-PSFVSATAFGAC 552
Cdd:cd18559 164 LKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYL-RALAVRLWCVgPCIVLFASFFAY 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 30682486 553 MLL--KIPLESGKIIAALATFRILQTPIYKLPDTISMIVQTKVSLDRI 598
Cdd:cd18559 243 VSRhsLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1241-1463 |
4.07e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 114.42 E-value: 4.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHLpmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINIltiglHDLRSRLSI 1320
Cdd:COG1121 7 IELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----RRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1321 IPQEPTM--------FEgTVRSNLDPL---------EEYAddQIWEALDKCQLGDeirkkelKLDSPVSEngqnWSVGQR 1383
Cdd:COG1121 80 VPQRAEVdwdfpitvRD-VVLMGRYGRrglfrrpsrADRE--AVDEALERVGLED-------LADRPIGE----LSGGQQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1384 QLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLRQ-HFSGCTVITIAHRISSVID-SDMVLLLDQGLIeEHDSPAR 1461
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRGLV-AHGPPEE 224
|
..
gi 30682486 1462 LL 1463
Cdd:COG1121 225 VL 226
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1238-1464 |
7.44e-28 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 120.59 E-value: 7.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1238 RGEITICNLQVRYGPHLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSR 1317
Cdd:PRK10789 311 RGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1318 LSIIPQEPTMFEGTVRSNL---DPleEYADDQIWEALDKCQLGDEIRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLK 1394
Cdd:PRK10789 391 LAVVSQTPFLFSDTVANNIalgRP--DATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLL 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1395 RSKVLILDEATASVDTATDTLIQETLRQHFSGCTVITIAHRISSVIDSDMVLLLDQGLIEEHDSPARLLE 1464
Cdd:PRK10789 469 NAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQ 538
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
734-1474 |
1.06e-27 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 122.45 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 734 FPFRDQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDaHTGSHLFKEVLLGLL--RNKTVIYVTHQLEFL 811
Cdd:PTZ00265 565 LPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINNLKgnENRITIIIAHRLSTI 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 812 PEADLILVM----------------------------------------KDGRITQAGKYneILESGTD----------- 840
Cdd:PTZ00265 644 RYANTIFVLsnrergstvdvdiigedptkdnkennnknnkddnnnnnnnNNNKINNAGSY--IIEQGTHdalmknkngiy 721
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 841 FMELVGAHTDALAAVDSYEKGSASAQSTTSKESKVSND----------EEKQEEDLPSPKGQLVQEEEREKG-KVGF--T 907
Cdd:PTZ00265 722 YTMINNQKVSSKKSSNNDNDKDSDMKSSAYKDSERGYDpdemngnskhENESASNKKSCKMSDENASENNAGgKLPFlrN 801
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 908 VYQKY------MKLAYGGALVPIILVVQILFQVLNIGSNYWM---AWVTPVSK--DVKPLVSGSTLILVYVFLATASSFc 976
Cdd:PTZ00265 802 LFKRKpkapnnLRIVYREIFSYKKDVTIIALSILVAGGLYPVfalLYAKYVSTlfDFANLEANSNKYSLYILVIAIAMF- 880
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 977 ilVRAMLSAMTGFKIATELFNQMHFRIFR----ASMSFFDA---TPiGRILNRASTDqsaVDLRLPSQFSNLAIAAVNIL 1049
Cdd:PTZ00265 881 --ISETLKNYYNNVIGEKVEKTMKRRLFEnilyQEISFFDQdkhAP-GLLSAHINRD---VHLLKTGLVNNIVIFTHFIV 954
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1050 GIIgvmgqVAWQVLIVFIPVIAAC---TWYRQYYISAARelARLS--------GISRSPLVQHFS--------------E 1104
Cdd:PTZ00265 955 LFL-----VSMVMSFYFCPIVAAVltgTYFIFMRVFAIR--ARLTankdvekkEINQPGTVFAYNsddeifkdpsfliqE 1027
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1105 TLSGITTIRSFDQEPRFRTDIMRLNDcYS---RLRFHAISAMEWLCFRLDLLSTVAFALSL--------VILVS-VPEGV 1172
Cdd:PTZ00265 1028 AFYNMNTVIIYGLEDYFCNLIEKAID-YSnkgQKRKTLVNSMLWGFSQSAQLFINSFAYWFgsflirrgTILVDdFMKSL 1106
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1173 INPSFAGlavTYALNLNSLQAtliwtlcDLENKMISVERML------QYIDIPSEPSLVIESTRPEKswpcrGEITICNL 1246
Cdd:PTZ00265 1107 FTFLFTG---SYAGKLMSLKG-------DSENAKLSFEKYYpliirkSNIDVRDNGGIRIKNKNDIK-----GKIEIMDV 1171
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1247 QVRY--GPHLPmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRI--------------------------------- 1291
Cdd:PTZ00265 1172 NFRYisRPNVP-IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtndmtneqdyqgdeeqnv 1250
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1292 ---------------------VEPAAGEIRIDGINILTIGLHDLRSRLSIIPQEPTMFEGTVRSNLDPLEEYADDQIWEA 1350
Cdd:PTZ00265 1251 gmknvnefsltkeggsgedstVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKR 1330
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1351 LDKCQLGDE-IRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLR--QHFSGC 1427
Cdd:PTZ00265 1331 ACKFAAIDEfIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdiKDKADK 1410
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|..
gi 30682486 1428 TVITIAHRISSVIDSDMVLLLDQ-----GLIEEHDSPARLLEDKSSSFSKLV 1474
Cdd:PTZ00265 1411 TIITIAHRIASIKRSDKIVVFNNpdrtgSFVQAHGTHEELLSVQDGVYKKYV 1462
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
596-844 |
6.55e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 117.64 E-value: 6.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 596 DRIATFLCLDDLQQDGMERLPSGSSKMDVEVSN-GAFSWDDSspiPTLKDIRFKIPHGMNIAICGtvgsgkssllssilg 674
Cdd:PRK11174 322 ESLVTFLETPLAHPQQGEKELASNDPVTIEAEDlEILSPDGK---TLAGPLNFTLPAGQRIALVG--------------- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 675 evP----KIS------------GNLKVCG-----------RK--AYIAQSPWIQSGKVEENILFGKP-MQREWYQRVLEA 724
Cdd:PRK11174 384 --PsgagKTSllnallgflpyqGSLKINGielreldpeswRKhlSWVGQNPQLPHGTLRDNVLLGNPdASDEQLQQALEN 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 725 CSLNKDLEVFPFRDQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgSHLFKEVLLGLLRNKTVIYV 804
Cdd:PRK11174 462 AWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS-EQLVMQALNAASRRQTTLMV 540
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 30682486 805 THQLEFLPEADLILVMKDGRITQAGKYNEILESGTDFMEL 844
Cdd:PRK11174 541 THQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1245-1453 |
6.87e-27 |
|
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: 109.93 E-value: 6.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1245 NLQVRYGPHLpmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINIltiglHDLRSRLSIIPQE 1324
Cdd:cd03235 4 DLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-----EKERKRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1325 -------PTMFEGTVRSNLDPL---------EEYADdqIWEALDKCQLGDeirkkelKLDSPVSEngqnWSVGQRQLVCL 1388
Cdd:cd03235 77 rsidrdfPISVRDVVLMGLYGHkglfrrlskADKAK--VDEALERVGLSE-------LADRQIGE----LSGGQQQRVLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30682486 1389 GRVLLKRSKVLILDEATASVDTATDTLIQETLRQ-HFSGCTVITIAHRISSVIDS-DMVLLLDQGLI 1453
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYfDRVLLLNRTVV 210
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
624-845 |
8.18e-27 |
|
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: 110.71 E-value: 8.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 624 VEVSNGAFSWDDSSPIPTLKDIRFKIPHGMNIAICG-------TVGSGKSSLLSSILGEVPkISG----NLKVCGRK--- 689
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGssgcgksTVVSLLERFYDPTSGEIL-LDGvdirDLNLRWLRsqi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 690 AYIAQSPWIQSGKVEENILFGKP-MQREWYQRVLEACSLNKDLEVFPFRDQTVIGERGINLSGGQKQRIQIARALYQDAD 768
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIRYGKPdATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30682486 769 IYLFDDPFSAVDAHTgSHLFKEVLLGLLRNKTVIYVTHQLEFLPEADLILVMKDGRITQAGKYNEILESGTDFMELV 845
Cdd:cd03249 160 ILLLDEATSALDAES-EKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLV 235
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1245-1451 |
1.07e-26 |
|
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: 109.48 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1245 NLQVRYGPHLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSIIPQE 1324
Cdd:cd03225 4 NLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1325 P-TMFEG-TVRS-------NLDPLEEYADDQIWEALDKCQLgdeirkKELKLDSPvsengQNWSVGQRQLVCLGRVLLKR 1395
Cdd:cd03225 84 PdDQFFGpTVEEevafgleNLGLPEEEIEERVEEALELVGL------EGLRDRSP-----FTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 30682486 1396 SKVLILDEATASVDTATDTLIQETLRQ-HFSGCTVITIAHRISSVID-SDMVLLLDQG 1451
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1241-1456 |
1.19e-26 |
|
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: 109.90 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHLPMV--LRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDL---R 1315
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1316 SRLSIIPQEPtmfegtvRSNLDPL---EEyaddQIWEAL--DKCQLGDEIRKKELKLDSPVSENGQNW--------SVGQ 1382
Cdd:cd03257 82 KEIQMVFQDP-------MSSLNPRmtiGE----QIAEPLriHGKLSKKEARKEAVLLLLVGVGLPEEVlnryphelSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30682486 1383 RQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLR--QHFSGCTVITIAHRISSV-IDSDMVLLLDQGLIEEH 1456
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKklQEELGLTLLFITHDLGVVaKIADRVAVMYAGKIVEE 227
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
690-820 |
1.65e-26 |
|
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: 115.85 E-value: 1.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 690 AYIAQSPWIQSGKVEENILFGKPMQ-REWYQRVLEACSLNKDLEVFPFRDQTVIGERGINLSGGQKQRIQIARALYQDAD 768
Cdd:TIGR02857 399 AWVPQHPFLFAGTIAENIRLARPDAsDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAP 478
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 30682486 769 IYLFDDPFSAVDAHTGSHLfKEVLLGLLRNKTVIYVTHQLEFLPEADLILVM 820
Cdd:TIGR02857 479 LLLLDEPTAHLDAETEAEV-LEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1241-1431 |
2.07e-26 |
|
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: 108.34 E-value: 2.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHLpmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINIlTIGLHDLRSRLSI 1320
Cdd:COG4133 3 LEAENLSCRRGERL--LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI-RDAREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1321 IPQEPTMFEG-TVRSNLDPL-----EEYADDQIWEALDKCQLGDEirkkelkLDSPVSengqNWSVGQRQLVCLGRVLLK 1394
Cdd:COG4133 80 LGHADGLKPElTVRENLRFWaalygLRADREAIDEALEAVGLAGL-------ADLPVR----QLSAGQKRRVALARLLLS 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 30682486 1395 RSKVLILDEATASVDTATDTLIQETLRQHFS--GCTVIT 1431
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIAAHLArgGAVLLT 187
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1245-1451 |
3.40e-26 |
|
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: 106.75 E-value: 3.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1245 NLQVRYGPHlpMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSIIPQe 1324
Cdd:cd03214 4 NLSVGYGGR--TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1325 ptmfegtvrsnldpleeyaddqiweALDKCQLGDeirkkelKLDSPVSEngqnWSVGQRQLVCLGRVLLKRSKVLILDEA 1404
Cdd:cd03214 81 -------------------------ALELLGLAH-------LADRPFNE----LSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 30682486 1405 TASVDTATDTLIQETLRQ--HFSGCTVITIAHRISSVID-SDMVLLLDQG 1451
Cdd:cd03214 125 TSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNLAARyADRVILLKDG 174
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
623-825 |
2.39e-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: 2.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 623 DVEVSNGAFSWDDSsPIPTLKDIRFKIPHGMNIAICGTVGSGKSSLLSSILGEVPKISGNLKVCG-----------RK-- 689
Cdd:cd03245 2 RIEFRNVSFSYPNQ-EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlRRni 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 690 AYIAQSPWIQSGKVEENILFGKPMQREwyQRVLEACSL---NKDLEVFPFRDQTVIGERGINLSGGQKQRIQIARALYQD 766
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADD--ERILRAAELagvTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 30682486 767 ADIYLFDDPFSAVDaHTGSHLFKEVLLGLLRNKTVIYVTHQLEFLPEADLILVMKDGRI 825
Cdd:cd03245 159 PPILLLDEPTSAMD-MNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
924-1199 |
5.88e-25 |
|
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: 106.19 E-value: 5.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 924 IILVVQILFQVLNIGSNYWMAWVTPV--SKDVKPLVSGSTLILVYVFLATASSFCILVRAMLSAMTGFKIATELFNQMHF 1001
Cdd:pfam00664 3 LAILLAILSGAISPAFPLVLGRILDVllPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1002 RIFRASMSFFDATPIGRILNRASTDQSAVDLRLPSQFSNLAIAAVNILGIIGVMGQVAWQVLIVFIPVIAACTWYRQYYI 1081
Cdd:pfam00664 83 KILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1082 SAARELARLSGISRSPLVQHFSETLSGITTIRSFDQEPRFRTDIMRLNDCYSRLRFHAISAMEWLCFRLDLLSTVAFALS 1161
Cdd:pfam00664 163 KILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALA 242
|
250 260 270
....*....|....*....|....*....|....*....
gi 30682486 1162 LVILVS-VPEGVINPsfaGLAVTYalnlNSLQATLIWTL 1199
Cdd:pfam00664 243 LWFGAYlVISGELSV---GDLVAF----LSLFAQLFGPL 274
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1238-1453 |
6.48e-25 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 111.29 E-value: 6.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1238 RGEITICNLQVRYGPHLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSR 1317
Cdd:TIGR01842 314 EGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKH 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1318 LSIIPQEPTMFEGTVRSNLDPLEEYADDQ-IWEALDKCQLGDEIRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRS 1396
Cdd:TIGR01842 394 IGYLPQDVELFPGTVAENIARFGENADPEkIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDP 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 30682486 1397 KVLILDEATASVDTATD-TLIQETLRQHFSGCTVITIAHRISSVIDSDMVLLLDQGLI 1453
Cdd:TIGR01842 474 KLVVLDEPNSNLDEEGEqALANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
960-1216 |
6.51e-25 |
|
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: 107.58 E-value: 6.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 960 STLILVYVFLATASSFCIL--VRAMLSAMTGFKIATELFNQMHFRIFRASMSFFDATPIGRILNRASTDQSAVDLRLPSQ 1037
Cdd:cd18600 68 SSYYVFYIYVGVADSLLAMgfFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLT 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1038 FSNLAIAAVNILGIIGVMGQVAWQVLIVFIPVIAACTWYRQYYISAARELARLSGISRSPLVQHFSETLSGITTIRSFDQ 1117
Cdd:cd18600 148 IFDFIQLFLIVIGAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1118 EPRFRTDIMRLNDCYSRLRFHAISAMEWLCFRLDLLSTVAFalSLVILVSVPEGVINPSFAGLAVTYALNLNSlqaTLIW 1197
Cdd:cd18600 228 QPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFF--TAVTFISIGTTGDGEGRVGIILTLAMNIMS---TLQW 302
|
250 260
....*....|....*....|..
gi 30682486 1198 ---TLCDLENKMISVERMLQYI 1216
Cdd:cd18600 303 avnTSIDVDSLMRSVSRIFKFI 324
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1238-1454 |
1.19e-24 |
|
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: 110.61 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1238 RGEITICNLQVRY-GPHLPmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRS 1316
Cdd:COG4618 328 KGRLSVENLTVVPpGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1317 RLSIIPQEPTMFEGTVRSNLDPLEEYADDQIWEALDKCQLGDEIrkkeLKL----DSPVSENGQNWSVGQRQLVCLGRVL 1392
Cdd:COG4618 407 HIGYLPQDVELFDGTIAENIARFGDADPEKVVAAAKLAGVHEMI----LRLpdgyDTRIGEGGARLSGGQRQRIGLARAL 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30682486 1393 LKRSKVLILDEATASVDTATDT-LIQ--ETLRQHfsGCTVITIAHRISSVIDSDMVLLLDQGLIE 1454
Cdd:COG4618 483 YGDPRLVVLDEPNSNLDDEGEAaLAAaiRALKAR--GATVVVITHRPSLLAAVDKLLVLRDGRVQ 545
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
688-845 |
1.38e-24 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 110.56 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 688 RKAYIAQSPWIQSGKVEENILFGKPMQREwyQRVLEACSLNKD---LEVFPFRDQTVIGERGINLSGGQKQRIQIARALY 764
Cdd:TIGR02204 415 RMALVPQDPVLFAASVMENIRYGRPDATD--EEVEAAARAAHAhefISALPEGYDTYLGERGVTLSGGQRQRIAIARAIL 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 765 QDADIYLFDDPFSAVDAHTgSHLFKEVLLGLLRNKTVIYVTHQLEFLPEADLILVMKDGRITQAGKYNEILESGTDFMEL 844
Cdd:TIGR02204 493 KDAPILLLDEATSALDAES-EQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARL 571
|
.
gi 30682486 845 V 845
Cdd:TIGR02204 572 A 572
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1241-1453 |
1.79e-24 |
|
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: 101.71 E-value: 1.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHlpMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGlHDLRSRLSI 1320
Cdd:cd03230 1 IEVRNLSKRYGKK--TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1321 IPQEPTMFEG-TVRSNLDpleeYaddqiwealdkcqlgdeirkkelkldspvsengqnwSVGQRQLVCLGRVLLKRSKVL 1399
Cdd:cd03230 78 LPEEPSLYENlTVRENLK----L------------------------------------SGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 30682486 1400 ILDEATASVDTATDTLIQETLRQH-FSGCTVITIAHRISSVID-SDMVLLLDQGLI 1453
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELkKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1255-1451 |
6.44e-24 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 101.01 E-value: 6.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1255 PMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLfrivepaAGEIRidginiLTIGLHDLRSRLSIIPQEPTMFEGTVRS 1334
Cdd:cd03250 18 SFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL-------LGELE------KLSGSVSVPGSIAYVSQEPWIQNGTIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1335 NLDPLEEYADDQIWEALDKCQLGDEIRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTAT-D 1413
Cdd:cd03250 85 NILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVgR 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 30682486 1414 TLIQETLRQHFSGC-TVITIAHRISSVIDSDMVLLLDQG 1451
Cdd:cd03250 165 HIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1241-1451 |
8.04e-24 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 99.95 E-value: 8.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHLpmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINI--LTIGLHDLRSRL 1318
Cdd:cd03229 1 LELKNVSKRYGQKT--VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdLEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1319 SIIPQEPTMFEG-TVRSNldpleeyaddqIWEALdkcqlgdeirkkelkldspvsengqnwSVGQRQLVCLGRVLLKRSK 1397
Cdd:cd03229 79 GMVFQDFALFPHlTVLEN-----------IALGL---------------------------SGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 30682486 1398 VLILDEATASVDTATDTLIQETLRQHF--SGCTVITIAHRISSVID-SDMVLLLDQG 1451
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQaqLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1241-1464 |
9.86e-24 |
|
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: 101.59 E-value: 9.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHlpMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIG---LHDLRSR 1317
Cdd:COG1127 6 IEVRNLTKSFGDR--VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1318 LSIIPQEPTMFEG-TVRSNLD-PLEEYADdqiweaLDKcqlgDEIRKK-ELKLDS----------PvSEngqnWSVGQRQ 1384
Cdd:COG1127 84 IGMLFQGGALFDSlTVFENVAfPLREHTD------LSE----AEIRELvLEKLELvglpgaadkmP-SE----LSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1385 LVCLGRVLLKRSKVLILDEATASVD----TATDTLIQEtLRQHFsGCTVITIAHRISSVID-SDMVLLLDQGLIEEHDSP 1459
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDpitsAVIDELIRE-LRDEL-GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTP 226
|
....*
gi 30682486 1460 ARLLE 1464
Cdd:COG1127 227 EELLA 231
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
691-845 |
1.47e-23 |
|
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: 101.02 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 691 YIAQSPWIQSGKVEENILFGKP-MQREwyqRVLEACSLNKDLEV---FPFRDQTVIGERGINLSGGQKQRIQIARALYQD 766
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADPgMSME---RVIEAAKLAGAHDFiseLPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30682486 767 ADIYLFDDPFSAVDAHTgSHLFKEVLLGLLRNKTVIYVTHQLEFLPEADLILVMKDGRITQAGKYNEILESGTDFMELV 845
Cdd:cd03252 157 PRILIFDEATSALDYES-EHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLY 234
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
405-845 |
1.47e-23 |
|
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: 107.90 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 405 GEIINLMT-----VDAERISAFSWYMhDPWILVLqISLALLILYRSLGLGSIAAFAATFLVMlgnIPLAKLEEKFQGNLM 479
Cdd:TIGR01193 253 GEIVSRFTdassiIDALASTILSLFL-DMWILVI-VGLFLVRQNMLLFLLSLLSIPVYAVII---ILFKRTFNKLNHDAM 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 480 ESkdNRMKKTS--EALLNMRILKLQGWEMKFLHKILDLRGieaGWLKK-FVYNSA-----AISSVLWAAPSfVSATAFGA 551
Cdd:TIGR01193 328 QA--NAVLNSSiiEDLNGIETIKSLTSEAERYSKIDSEFG---DYLNKsFKYQKAdqgqqAIKAVTKLILN-VVILWTGA 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 552 CMLLKIPLESGKIIAALATFRILQTPIYKLPDTISMIVQTKVSLDRIATFLCLDDLQQDGMERLPSGSSKMDVEVSNGAF 631
Cdd:TIGR01193 402 YLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTELNNLNGDIVINDVSY 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 632 SWDDSSPIptLKDIRFKIPHGMNIAICG-------TVGSGKSSLLSSILGEVPKISGNLKVCGRKA------YIAQSPWI 698
Cdd:TIGR01193 482 SYGYGSNI--LSDISLTIKMNSKTTIVGmsgsgksTLAKLLVGFFQARSGEILLNGFSLKDIDRHTlrqfinYLPQEPYI 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 699 QSGKVEENILFG-KPMQREwyQRVLEACSL---NKDLEVFPFRDQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDD 774
Cdd:TIGR01193 560 FSGSILENLLLGaKENVSQ--DEIWAACEIaeiKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDE 637
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30682486 775 PFSAVDAHTGSHLFKEVLlgLLRNKTVIYVTHQLEFLPEADLILVMKDGRITQAGKYNEILESGTDFMELV 845
Cdd:TIGR01193 638 STSNLDTITEKKIVNNLL--NLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
532-847 |
2.11e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 106.97 E-value: 2.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 532 AISSVLWAAPSFVSATA---FGACMLLKIPLESGKIIA--ALATFRIlqtpiYKLPDTISMIVQTKVSLDRIATFLCLDD 606
Cdd:PRK13657 240 ALASVLNRAASTITMLAilvLGAALVQKGQLRVGEVVAfvGFATLLI-----GRLDQVVAFINQVFMAAPKLEEFFEVED 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 607 LQQDGMER---LPSGSSKMDVEVSNGAFSWDDSSPipTLKDIRFKIPHGMNIAICGTVGSGKSSLLSSILGEVPKISGNL 683
Cdd:PRK13657 315 AVPDVRDPpgaIDLGRVKGAVEFDDVSFSYDNSRQ--GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRI 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 684 KVCG-----------RKAyIA---QSPWIQSGKVEENILFGKP-MQREWYQRVLEACSLNKDLEVFPFRDQTVIGERGIN 748
Cdd:PRK13657 393 LIDGtdirtvtraslRRN-IAvvfQDAGLFNRSIEDNIRVGRPdATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQ 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLfKEVLLGLLRNKTVIYVTHQLEFLPEADLILVMKDGRITQA 828
Cdd:PRK13657 472 LSGGERQRLAIARALLKDPPILILDEATSALDVETEAKV-KAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVES 550
|
330
....*....|....*....
gi 30682486 829 GKYNEILESGTDFMELVGA 847
Cdd:PRK13657 551 GSFDELVARGGRFAALLRA 569
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1239-1435 |
2.14e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 106.82 E-value: 2.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1239 GEITICNLQVRygphLP---MVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRI-DGINILtiglhdl 1314
Cdd:COG4178 361 GALALEDLTLR----TPdgrPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVL------- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1315 rsrlsIIPQEPTMFEGTVRSNL---DPLEEYADDQIWEALDKCQLGDEIRKkelkLDspvseNGQNW----SVGQRQLVC 1387
Cdd:COG4178 430 -----FLPQRPYLPLGTLREALlypATAEAFSDAELREALEAVGLGHLAER----LD-----EEADWdqvlSLGEQQRLA 495
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 30682486 1388 LGRVLLKRSKVLILDEATASVDTATDTLIQETLRQHFSGCTVITIAHR 1435
Cdd:COG4178 496 FARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
531-808 |
1.51e-22 |
|
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: 103.59 E-value: 1.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 531 AAISSVLWAAPSFVSA-----TAFGACMLLkiplesgkiiaALATFRILqTPiykLPDTISMIVQTKVSLDRIATFLCLD 605
Cdd:TIGR02868 250 LAVLGALWAGGPAVADgrlapVTLAVLVLL-----------PLAAFEAF-AA---LPAAAQQLTRVRAAAERIVEVLDAA 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 606 DLQQDGM--ERLPSGSSKMDVEVSNGAFSWDDSSPIptLKDIRFKIPHGMNIAICGTVGSGKSSLLSSILGEVPKISGNL 683
Cdd:TIGR02868 315 GPVAEGSapAAGAVGLGKPTLELRDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEV 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 684 KVCG-------------RKAYIAQSPWIQSGKVEENILFGKP-MQREWYQRVLEACSLNKDLEVFPFRDQTVIGERGINL 749
Cdd:TIGR02868 393 TLDGvpvssldqdevrrRVSVCAQDAHLFDTTVRENLRLARPdATDEELWAALERVGLADWLRALPDGLDTVLGEGGARL 472
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 30682486 750 SGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFkEVLLGLLRNKTVIYVTHQL 808
Cdd:TIGR02868 473 SGGERQRLALARALLADAPILLLDEPTEHLDAETADELL-EDLLAALSGRTVVLITHHL 530
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
549-844 |
1.84e-22 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 104.44 E-value: 1.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 549 FGACMLLKIPLESGKIIA-ALATFRILQtPIYKLPDTISMIVQTKVSLDRIATFL-CLDDLQQDGMERLPSgsSKMDVEV 626
Cdd:TIGR01846 382 FGAHLVIGGALSPGQLVAfNMLAGRVTQ-PVLRLAQLWQDFQQTGIALERLGDILnSPTEPRSAGLAALPE--LRGAITF 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 627 SNGAFSWDDSSPiPTLKDIRFKIPHGMNIAICGTVGSGKSSLLSSILGEVPKISGNLKVCGRKAYIAQSPWIQ------- 699
Cdd:TIGR01846 459 ENIRFRYAPDSP-EVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRrqmgvvl 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 700 ------SGKVEENILFGKPMQREwyQRVLEACSLNKDLEV---FPFRDQTVIGERGINLSGGQKQRIQIARALYQDADIY 770
Cdd:TIGR01846 538 qenvlfSRSIRDNIALCNPGAPF--EHVIHAAKLAGAHDFiseLPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRIL 615
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30682486 771 LFDDPFSAVDAHTgSHLFKEVLLGLLRNKTVIYVTHQLEFLPEADLILVMKDGRITQAGKYNEILESGTDFMEL 844
Cdd:TIGR01846 616 IFDEATSALDYES-EALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARL 688
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
703-829 |
3.42e-22 |
|
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: 96.43 E-value: 3.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 703 VEENILFG----KPMQREWYQRVLEACSLnkdLEVFPFRDQTVIGerginLSGGQKQRIQIARALYQDADIYLFDDPFSA 778
Cdd:cd03259 89 VAENIAFGlklrGVPKAEIRARVRELLEL---VGLEGLLNRYPHE-----LSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 30682486 779 VDAHTGSHLFKEvLLGLLRN--KTVIYVTH-QLEFLPEADLILVMKDGRITQAG 829
Cdd:cd03259 161 LDAKLREELREE-LKELQRElgITTIYVTHdQEEALALADRIAVMNEGRIVQVG 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
624-837 |
1.35e-21 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 95.54 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 624 VEVSNGAFSWDDSspiPTLKDIRFKIPHGMNIAICG-----------TVGSgkssllssilgEVPKISGNLKVCGRK--- 689
Cdd:COG1121 7 IELENLTVSYGGR---PVLEDVSLTIPPGEFVAIVGpngagkstllkAILG-----------LLPPTSGTVRLFGKPprr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 690 -----AYIAQSPWIQSG---KVEENILFG--------KPMQREWYQRVLEAcsLnKDLEVFPFRDQTvIGErginLSGGQ 753
Cdd:COG1121 73 arrriGYVPQRAEVDWDfpiTVRDVVLMGrygrrglfRRPSRADREAVDEA--L-ERVGLEDLADRP-IGE----LSGGQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 754 KQRIQIARALYQDADIYLFDDPFSAVDAHTgshlfKEVLLGLLR-----NKTVIYVTHQLEFLPE-ADLILVMKDGRITq 827
Cdd:COG1121 145 QQRVLLARALAQDPDLLLLDEPFAGVDAAT-----EEALYELLRelrreGKTILVVTHDLGAVREyFDRVLLLNRGLVA- 218
|
250
....*....|
gi 30682486 828 AGKYNEILES 837
Cdd:COG1121 219 HGPPEEVLTP 228
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1241-1451 |
2.09e-21 |
|
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: 94.18 E-value: 2.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHlpMVLRGLTCTFRGGLkTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINIlTIGLHDLRSRLSI 1320
Cdd:cd03264 1 LQLENLTKRYGKK--RALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV-LKQPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1321 IPQEPTMFEG-TVRSNLDPL-------EEYADDQIWEALDKCQLGDEIRKKELKLdspvsengqnwSVGQRQLVCLGRVL 1392
Cdd:cd03264 77 LPQEFGVYPNfTVREFLDYIawlkgipSKEVKARVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVGIAQAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1393 LKRSKVLILDEATASVDTATDTLIQETLRQHFSGCTVITIAHRISSVIDS-DMVLLLDQG 1451
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLcNQVAVLNKG 205
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1241-1459 |
9.29e-21 |
|
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: 92.95 E-value: 9.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHlpMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILT---IGLHDLRSR 1317
Cdd:cd03261 1 IELRGLTKSFGGR--TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1318 LSIIPQEPTMFEG-TVRSNLD-PLEEYA-------DDQIWEALDKCQLGDEIRKK--ELkldspvsengqnwSVGQRQLV 1386
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVAfPLREHTrlseeeiREIVLEKLEAVGLRGAEDLYpaEL-------------SGGMKKRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30682486 1387 CLGRVLLKRSKVLILDEATASVDTATDTLIQE---TLRQHFsGCTVITIAHRISSVID-SDMVLLLDQGLIEEHDSP 1459
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLDPIASGVIDDlirSLKKEL-GLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTP 221
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
547-835 |
9.75e-21 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 98.19 E-value: 9.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 547 TAFGACMLLKIPLESGKIIAA-LATFRILqTPIYKLPDTISMIVQTKVSLDRIATFLCLDDLQQDGMeRLPSGSSKMDVE 625
Cdd:TIGR01842 243 LGLGAYLAIDGEITPGMMIAGsILVGRAL-APIDGAIGGWKQFSGARQAYKRLNELLANYPSRDPAM-PLPEPEGHLSVE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 626 VSNGAfswddsSPI---PTLKDIRFKIPHGMNIAICGTVGSGKSSLLSSILGEVPKISGNLKVCG-------------RK 689
Cdd:TIGR01842 321 NVTIV------PPGgkkPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGadlkqwdretfgkHI 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 690 AYIAQSPWIQSGKVEENIL-FGKPMQREwyqRVLEACSLNKDLEV---FPFRDQTVIGERGINLSGGQKQRIQIARALYQ 765
Cdd:TIGR01842 395 GYLPQDVELFPGTVAENIArFGENADPE---KIIEAAKLAGVHELilrLPDGYDTVIGPGGATLSGGQRQRIALARALYG 471
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 766 DADIYLFDDPFSAVDAHTGSHLFKEVLLGLLRNKTVIYVTHQLEFLPEADLILVMKDGRITQAGKYNEIL 835
Cdd:TIGR01842 472 DPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVL 541
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
946-1160 |
1.21e-20 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-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. 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. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. 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: 349988 [Multi-domain] Cd Length: 294 Bit Score: 93.99 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 946 VTPVSKDVKPLVsgsTLILVYVFLATASSFCILVRAMLSAMTGFKIATELFNQMHFRIFRASMSFFDATPIGRILNRAST 1025
Cdd:cd18544 30 IVPGQGDLQGLL---LLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1026 DQSAVDLRLPSQFSNLAIAAVNILGIIGVMGQVAWQ---VLIVFIPVIAACTWYRQYYISAARELARLSgISRspLVQHF 1102
Cdd:cd18544 107 DTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRlalISLLVLPLLLLATYLFRKKSRKAYREVREK-LSR--LNAFL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1103 SETLSGITTIRSFDQEPRFRTDIMRLNDCYSRLRFHAISAmeWLCFR--LDLLSTVAFAL 1160
Cdd:cd18544 184 QESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKL--FALFRplVELLSSLALAL 241
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
879-1448 |
1.42e-20 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 99.33 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 879 EEKQEEDLPSPKGQLVQEEEREK---GKVGFTVYQK------------------YMKLAY---------GGALVPIILVV 928
Cdd:PTZ00265 4 DQRQKKDNNSGGGNLSIKDEVEKelnKKGTFELYKKiktqkipfflpfkclpasHRKLLGvsfvcatisGGTLPFFVSVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 929 QILFQVLNIGSNywmawvtpvskdVKPLVSGSTLILVYVF-LATASSFCILVRAMlsamtgfKIATELFNQMHFRIFRAS 1007
Cdd:PTZ00265 84 GVIMKNMNLGEN------------VNDIIFSLVLIGIFQFiLSFISSFCMDVVTT-------KILKTLKLEFLKSVFYQD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1008 MSFFDATPIGRILNRASTDQSAVDLRLPSQFSNLAIAAVNILGI-IGVMGQVAWQVLIV--FIPVIAACTWYRQYYISAA 1084
Cdd:PTZ00265 145 GQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLyIWSLFKNARLTLCItcVFPLIYICGVICNKKVKIN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1085 RELARLSGISRSPLVQhfsETLSGITTIRSFDQEprfRTDIMRLN---DCYSRLRFHAiSAMEWLCFRLD---LLSTVAF 1158
Cdd:PTZ00265 225 KKTSLLYNNNTMSIIE---EALVGIRTVVSYCGE---KTILKKFNlseKLYSKYILKA-NFMESLHIGMIngfILASYAF 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1159 AL---SLVILVSVPEGVINPSFAGLAVTYALnLNSLQATLIWT--LCDLENKMISVERMLQYIDIPSEPSLViESTRPEK 1233
Cdd:PTZ00265 298 GFwygTRIIISDLSNQQPNNDFHGGSVISIL-LGVLISMFMLTiiLPNITEYMKSLEATNSLYEIINRKPLV-ENNDDGK 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1234 SWPCRGEITICNLQVRYGPHLPM-VLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRI-DGINILTIGL 1311
Cdd:PTZ00265 376 KLKDIKKIQFKNVRFHYDTRKDVeIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINL 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1312 HDLRSRLSIIPQEPTMFEGTVRSN----------LDPLEEYADDQIWEALD----------KCQlGD------------- 1358
Cdd:PTZ00265 456 KWWRSKIGVVSQDPLLFSNSIKNNikyslyslkdLEALSNYYNEDGNDSQEnknkrnscraKCA-GDlndmsnttdsnel 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1359 ----------------EIRKKEL----------KLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTAT 1412
Cdd:PTZ00265 535 iemrknyqtikdsevvDVSKKVLihdfvsalpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
650 660 670
....*....|....*....|....*....|....*....
gi 30682486 1413 DTLIQET---LRQHFSGCTVItIAHRISSVIDSDMVLLL 1448
Cdd:PTZ00265 615 EYLVQKTinnLKGNENRITII-IAHRLSTIRYANTIFVL 652
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
676-829 |
1.99e-20 |
|
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: 91.44 E-value: 1.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 676 VPKISGNLKVCGRK--------AYIAQSPWIQSG---KVEENIL--------FGKPMQREWYQRVLEACslnKDLEVFPF 736
Cdd:cd03235 49 LKPTSGSIRVFGKPlekerkriGYVPQRRSIDRDfpiSVRDVVLmglyghkgLFRRLSKADKAKVDEAL---ERVGLSEL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 737 RDQTvIGErginLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgshlfKEVLLGLLR-----NKTVIYVTHQLEFL 811
Cdd:cd03235 126 ADRQ-IGE----LSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKT-----QEDIYELLRelrreGMTILVVTHDLGLV 195
|
170
....*....|....*....
gi 30682486 812 PE-ADLILVMkDGRITQAG 829
Cdd:cd03235 196 LEyFDRVLLL-NRTVVASG 213
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1241-1454 |
2.02e-20 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 92.41 E-value: 2.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHLpmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVE--PAA---GEIRIDGINIL--TIGLHD 1313
Cdd:COG1117 12 IEVRNLNVYYGDKQ--ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGArveGEILLDGEDIYdpDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1314 LRSRLSIIPQEPTMFEGTV---------------RSNLDPLEEyaddqiwEALDKCQLGDEIrKKELKldspvsENGQNW 1378
Cdd:COG1117 90 LRRRVGMVFQKPNPFPKSIydnvayglrlhgiksKSELDEIVE-------ESLRKAALWDEV-KDRLK------KSALGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1379 SVGQRQLVCLGRVLLKRSKVLILDEATASVD-TATDT---LIQEtLRQHFsgcTVITIAH------RIssvidSDMVLLL 1448
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDpISTAKieeLILE-LKKDY---TIVIVTHnmqqaaRV-----SDYTAFF 226
|
....*..
gi 30682486 1449 DQG-LIE 1454
Cdd:COG1117 227 YLGeLVE 233
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1241-1453 |
3.09e-20 |
|
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: 90.67 E-value: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHLpmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINIL--TIGLHDLRSRL 1318
Cdd:cd03262 1 IEIKNLHKSFGDFH--VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1319 SIIPQEPTMFEgtvrsNLDPLEEYADDQIW--------------EALDKCQLGDEIRKKELKLdspvsengqnwSVGQRQ 1384
Cdd:cd03262 79 GMVFQQFNLFP-----HLTVLENITLAPIKvkgmskaeaeeralELLEKVGLADKADAYPAQL-----------SGGQQQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30682486 1385 LVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLRQ--HfSGCTVITIAHRISSVID-SDMVLLLDQGLI 1453
Cdd:cd03262 143 RVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDlaE-EGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
703-834 |
3.18e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 93.98 E-value: 3.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 703 VEENILFGKPMQR----EWYQRVLEACSLnkdLEVFPFRDQTViGErginLSGGQKQRIQIARALYQDADIYLFDDPFSA 778
Cdd:COG3839 92 VYENIAFPLKLRKvpkaEIDRRVREAAEL---LGLEDLLDRKP-KQ----LSGGQRQRVALGRALVREPKVFLLDEPLSN 163
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 30682486 779 VDAHTGSHLFKEvLLGLLR--NKTVIYVTH-QLEFLPEADLILVMKDGRITQAGKYNEI 834
Cdd:COG3839 164 LDAKLRVEMRAE-IKRLHRrlGTTTIYVTHdQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1241-1422 |
3.84e-20 |
|
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: 91.48 E-value: 3.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYgPHLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIG---LHDLRSR 1317
Cdd:cd03256 1 IEVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1318 LSIIPQEPTMFE----------------GTVRS--NLDPLEEYAddQIWEALDKCQLGDEIRKKELKLdspvsengqnwS 1379
Cdd:cd03256 80 IGMIFQQFNLIErlsvlenvlsgrlgrrSTWRSlfGLFPKEEKQ--RALAALERVGLLDKAYQRADQL-----------S 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 30682486 1380 VGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLRQ 1422
Cdd:cd03256 147 GGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKR 189
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1241-1457 |
4.57e-20 |
|
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: 90.27 E-value: 4.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHLpmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHdlRSRLSI 1320
Cdd:cd03259 1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1321 IPQEPTMFEG-TVRSNLD-PL------EEYADDQIWEALDKCQLGDEIRKKELKLdspvsengqnwSVGQRQLVCLGRVL 1392
Cdd:cd03259 77 VFQDYALFPHlTVAENIAfGLklrgvpKAEIRARVRELLELVGLEGLLNRYPHEL-----------SGGQQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30682486 1393 LKRSKVLILDEATASVDTATDTLIQETLR--QHFSGCTVITIAHRISSVID-SDMVLLLDQGLIEEHD 1457
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKelQRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1241-1481 |
4.64e-20 |
|
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: 91.21 E-value: 4.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGpHLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSI 1320
Cdd:cd03295 1 IEFENVTKRYG-GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1321 IPQE----PTMfegTVRSN--LDP-LEEYADDQIWEaldkcqlgdeiRKKEL--KLDSPVSENGQNW----SVGQRQLVC 1387
Cdd:cd03295 80 VIQQiglfPHM---TVEENiaLVPkLLKWPKEKIRE-----------RADELlaLVGLDPAEFADRYphelSGGQQQRVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1388 LGRVLLKRSKVLILDEATASVDTAT-DTLIQETLR-QHFSGCTVITIAHRISSVID-SDMVLLLDQGLIEEHDSPARLLE 1464
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPITrDQLQEEFKRlQQELGKTIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEILR 225
|
250
....*....|....*..
gi 30682486 1465 DKSSSFsklVAEYTASS 1481
Cdd:cd03295 226 SPANDF---VAEFVGAD 239
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1257-1453 |
7.25e-20 |
|
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: 89.86 E-value: 7.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1257 VLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDL----RSRLSIIPQE----PTMf 1328
Cdd:cd03255 19 ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafrRRHIGFVFQSfnllPDL- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1329 egTVRSNLD-PLE------EYADDQIWEALDKCQLGDEIRKKELKLdspvsengqnwSVGQRQLVCLGRVLLKRSKVLIL 1401
Cdd:cd03255 98 --TALENVElPLLlagvpkKERRERAEELLERVGLGDRLNHYPSEL-----------SGGQQQRVAIARALANDPKIILA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 30682486 1402 DEATASVDTATDTLIQETLRQ--HFSGCTVITIAHRISSVIDSDMVLLLDQGLI 1453
Cdd:cd03255 165 DEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
680-825 |
9.42e-20 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 90.53 E-value: 9.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 680 SGNLKVCGRK--------AYIAQS----PWIqsgKVEENILFG-------KPMQREWYQRVLEACSLNKDLEVFPFrdqt 740
Cdd:COG1116 65 SGEVLVDGKPvtgpgpdrGVVFQEpallPWL---TVLDNVALGlelrgvpKAERRERARELLELVGLAGFEDAYPH---- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 741 vigergiNLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLfKEVLLGLLR--NKTVIYVTHQLE---FLpeAD 815
Cdd:COG1116 138 -------QLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERL-QDELLRLWQetGKTVLFVTHDVDeavFL--AD 207
|
170
....*....|..
gi 30682486 816 LILVMKD--GRI 825
Cdd:COG1116 208 RVVVLSArpGRI 219
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
748-846 |
9.66e-20 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 92.52 E-value: 9.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 748 NLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEvLLGLLR--NKTVIYVTH-QLEFLPEADLILVMKDGR 824
Cdd:COG1118 133 QLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRW-LRRLHDelGGTTVFVTHdQEEALELADRVVVMNQGR 211
|
90 100
....*....|....*....|....
gi 30682486 825 ITQAGKYNEILES-GTDF-MELVG 846
Cdd:COG1118 212 IEQVGTPDEVYDRpATPFvARFLG 235
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
702-843 |
1.20e-19 |
|
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: 90.05 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 702 KVEENI-----LFGKPMQREwYQRVLEACSLnKDLEVFPFRDQTViGErginLSGGQKQRIQIARALYQDADIYLFDDPF 776
Cdd:cd03295 91 TVEENIalvpkLLKWPKEKI-RERADELLAL-VGLDPAEFADRYP-HE----LSGGQQQRVGVARALAADPPLLLMDEPF 163
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 777 SAVDAHTGSHLFKEVL-LGLLRNKTVIYVTHQL-EFLPEADLILVMKDGRITQAGKYNEILES-GTDFME 843
Cdd:cd03295 164 GALDPITRDQLQEEFKrLQQELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRSpANDFVA 233
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1241-1455 |
2.36e-19 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 88.56 E-value: 2.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRY--GPHLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDL---- 1314
Cdd:COG1136 5 LELRNLTKSYgtGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1315 RSRLSIIPQE----PTMfegTVRSNLD-PLE------EYADDQIWEALDKCQLGDEIRKK--ELkldspvsengqnwSVG 1381
Cdd:COG1136 85 RRHIGFVFQFfnllPEL---TALENVAlPLLlagvsrKERRERARELLERVGLGDRLDHRpsQL-------------SGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30682486 1382 QRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLRQ--HFSGCTVITIAH--RISSVidSDMVLLLDQGLIEE 1455
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHdpELAAR--ADRVIRLRDGRIVS 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1241-1466 |
3.04e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 89.28 E-value: 3.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSI 1320
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1321 IPQEP-TMFEG-TVRS---------NLDPLEeyADDQIWEALDKCQLgDEIRKKElkldsPvsengQNWSVGQRQLVCLG 1389
Cdd:PRK13632 88 IFQNPdNQFIGaTVEDdiafglenkKVPPKK--MKDIIDDLAKKVGM-EDYLDKE-----P-----QNLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30682486 1390 RVLLKRSKVLILDEATASVDTATDTLIQETLRQ-HFSGC-TVITIAHRISSVIDSDMVLLLDQGLIEEHDSPARLLEDK 1466
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDlRKTRKkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
749-824 |
3.25e-19 |
|
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: 86.14 E-value: 3.25e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGsHLFKEVLLGLL-RNKTVIYVTHQLEFLPEA-DLILVMKDGR 824
Cdd:cd00267 81 LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR-ERLLELLRELAeEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1245-1465 |
3.56e-19 |
|
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: 87.87 E-value: 3.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1245 NLQVRYGP-HlpmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDlRSRLSI--I 1321
Cdd:cd03224 5 NLNAGYGKsQ---ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE-RARAGIgyV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1322 PQEPTMFEG-TVRSNLDpLEEYA--DDQIWEALdkcqlgDEI-----RKKElKLDSPvsenGQNWSVGQRQLVCLGRVLL 1393
Cdd:cd03224 81 PEGRRIFPElTVEENLL-LGAYArrRAKRKARL------ERVyelfpRLKE-RRKQL----AGTLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1394 KRSKVLILDEATAS-----VDTATDTLiqETLRQhfSGCTVITI---AHRISSVidSDMVLLLDQGLIEEHDSPARLLED 1465
Cdd:cd03224 149 SRPKLLLLDEPSEGlapkiVEEIFEAI--RELRD--EGVTILLVeqnARFALEI--ADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
952-1164 |
3.92e-19 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the 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 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. 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. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. 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: 349990 [Multi-domain] Cd Length: 292 Bit Score: 89.47 E-value: 3.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 952 DVKPLVsgsTLILVYVFLATASSFCILVRAMLSAMTG----FKIATELFNQMHfrifRASMSFFDATPIGRILNRASTDQ 1027
Cdd:cd18546 34 DLGVLL---LAAAAYLAVVLAGWVAQRAQTRLTGRTGerllYDLRLRVFAHLQ----RLSLDFHERETSGRIMTRMTSDI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1028 SAVDLRLPSQFSNLAIAAVNILGIIGVMGQVAWQ----VLIVFIPVIAACTWYRQY----YiSAARELarlsgISRspLV 1099
Cdd:cd18546 107 DALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRlalvALAALPPLALATRWFRRRssraY-RRARER-----IAA--VN 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30682486 1100 QHFSETLSGITTIRSFDQEPRFRTDIMRLNDCYSRLRFHAISAMEWLCFRLDLLSTVAFALSLVI 1164
Cdd:cd18546 179 ADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLV 243
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1245-1451 |
4.07e-19 |
|
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: 88.26 E-value: 4.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1245 NLQVRYGPHLpmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDlRSRLSIIP-- 1322
Cdd:cd03219 5 GLTKRFGGLV--ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHE-IARLGIGRtf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1323 QEPTMFEG-TVRSNLD-----------------PLEEYADDQIWEALDKCQLGDeirkkelKLDSPVSengqNWSVGQRQ 1384
Cdd:cd03219 82 QIPRLFPElTVLENVMvaaqartgsglllararREEREARERAEELLERVGLAD-------LADRPAG----ELSYGQQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30682486 1385 LVCLGRVLLKRSKVLILDEATASVDTA-TDTLIQ--ETLRQHfsGCTVITIAHRISSVID-SDMVLLLDQG 1451
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAAGLNPEeTEELAEliRELRER--GITVLLVEHDMDVVMSlADRVTVLDQG 219
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1241-1439 |
4.12e-19 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 87.81 E-value: 4.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHLPMV--LRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLhDLRSRL 1318
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPA-EARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1319 SIIPQEPTMFEG-TVRSNLdplEEYAD------DQIWEALDKcqLGDEIRKKELkLDSPVSEngqnWSVGQRQLVCLGRV 1391
Cdd:cd03266 81 GFVSDSTGLYDRlTARENL---EYFAGlyglkgDELTARLEE--LADRLGMEEL-LDRRVGG----FSTGMRQKVAIARA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 30682486 1392 LLKRSKVLILDEATASVD-TATDTLIQETLRQHFSGCTVITIAHRISSV 1439
Cdd:cd03266 151 LVHDPPVLLLDEPTTGLDvMATRALREFIRQLRALGKCILFSTHIMQEV 199
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
680-825 |
4.21e-19 |
|
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: 87.53 E-value: 4.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 680 SGNLKVCGRK--------AYIAQS----PWIqsgKVEENILFGKPMQ----REWYQRV---LEACSLNKDLEVFPFRdqt 740
Cdd:cd03293 58 SGEVLVDGEPvtgpgpdrGYVFQQdallPWL---TVLDNVALGLELQgvpkAEARERAeelLELVGLSGFENAYPHQ--- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 741 vigerginLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLfKEVLLGLLR--NKTVIYVTHQLE---FLpeAD 815
Cdd:cd03293 132 --------LSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQL-QEELLDIWRetGKTVLLVTHDIDeavFL--AD 200
|
170
....*....|..
gi 30682486 816 LILVM--KDGRI 825
Cdd:cd03293 201 RVVVLsaRPGRI 212
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1241-1430 |
5.22e-19 |
|
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: 87.56 E-value: 5.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTiGLHDLRSRLSI 1320
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1321 IPQEPTMFEG-TVRSNLD--------PLEEyADDQIWEALDKCQLGDeirkkelKLDSPVSengqNWSVGQRQLVCLGRV 1391
Cdd:cd03263 80 CPQFDALFDElTVREHLRfyarlkglPKSE-IKEEVELLLRVLGLTD-------KANKRAR----TLSGGMKRKLSLAIA 147
|
170 180 190
....*....|....*....|....*....|....*....
gi 30682486 1392 LLKRSKVLILDEATASVDTATDTLIQETLRQHFSGCTVI 1430
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSII 186
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1238-1455 |
5.92e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 88.05 E-value: 5.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1238 RGEITICNLQVRYGPhlPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVE--PAA---GEIRIDGINILTIGLH 1312
Cdd:PRK14247 1 MNKIEIRDLKVSFGQ--VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEArvsGEVYLDGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1313 DLRSRLSIIPQEP------TMFE----GTVRSNLDPLEEYADDQIWEALDKCQLGDEIRKkelKLDSPVSEngqnWSVGQ 1382
Cdd:PRK14247 79 ELRRRVQMVFQIPnpipnlSIFEnvalGLKLNRLVKSKKELQERVRWALEKAQLWDEVKD---RLDAPAGK----LSGGQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30682486 1383 RQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLRQHFSGCTVITIAH------RIssvidSDMVLLLDQGLIEE 1455
Cdd:PRK14247 152 QQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRI-----SDYVAFLYKGQIVE 225
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
680-846 |
6.36e-19 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 87.43 E-value: 6.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 680 SGNLKVCGRK------------AYIAQSPWIQSG-KVEENI-----LFGKPMQ--REWYQRVLEACSLNkdlevfPFRDQ 739
Cdd:COG1131 54 SGEVRVLGEDvardpaevrrriGYVPQEPALYPDlTVRENLrffarLYGLPRKeaRERIDELLELFGLT------DAADR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 740 TVIgergiNLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHtGSHLFKEVLLGLL-RNKTVIYVTHQLEflpEA---- 814
Cdd:COG1131 128 KVG-----TLSGGMKQRLGLALALLHDPELLILDEPTSGLDPE-ARRELWELLRELAaEGKTVLLSTHYLE---EAerlc 198
|
170 180 190
....*....|....*....|....*....|....
gi 30682486 815 DLILVMKDGRITQAGKYNEILESGTD--FMELVG 846
Cdd:COG1131 199 DRVAIIDKGRIVADGTPDELKARLLEdvFLELTG 232
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
311-598 |
7.31e-19 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 1 (TMD1) 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: 350036 [Multi-domain] Cd Length: 287 Bit Score: 88.77 E-value: 7.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 311 LSTLFAFVYTVSCYVAP-YLMDTFVQYLNGQRQYSNQGVVLVTTFFVaklveCQARRNWYFRL-----QKAGIGMRSVLV 384
Cdd:cd18592 1 FSILLLLISLIFGFIGPtILIRKLLEYLEDSDSSVWYGILLVLGLFL-----TELLRSLFFSLtwaisYRTGIRLRGAVL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 385 SMIYEKGLTLPcySKQGHTSGEIINLMTVDAERI----SAFSWYMHDPWILVLQISLALLILYRSLGLGsIAAFAATFLV 460
Cdd:cd18592 76 GLLYKKILRLR--SLGDKSVGELINIFSNDGQRLfdaaVFGPLVIGGPVVLILGIVYSTYLLGPWALLG-MLVFLLFYPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 461 MLGnipLAKLEEKFQGNLMESKDNRMKKTSEALLNMRILKLQGWEMKFLHKILDLRGIEAGWLKKFVYNSAAISSVLWAA 540
Cdd:cd18592 153 QAF---IAKLTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIV 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 30682486 541 PSFVSATAFGACMLLKIPLESGKIIAALATFRILQTPIYKLPDTISMIVQTKVSLDRI 598
Cdd:cd18592 230 PVIASVVTFLAHVALGNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1245-1493 |
8.53e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 88.35 E-value: 8.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1245 NLQVRYGPHLPMVLRGLT-CTF--RGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINIL----TIGLHDLRSR 1317
Cdd:PRK13641 7 NVDYIYSPGTPMEKKGLDnISFelEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKKLRKK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1318 LSIIPQ--EPTMFEGTVRS-------NLDPLEEYADDQIWEALDKCQLGDEIRKKelkldSPVSENGqnwsvGQRQLVCL 1388
Cdd:PRK13641 87 VSLVFQfpEAQLFENTVLKdvefgpkNFGFSEDEAKEKALKWLKKVGLSEDLISK-----SPFELSG-----GQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1389 GRVLLKRSKVLILDEATASVDTATdtliQETLRQHF-----SGCTVITIAHRISSVID-SDMVLLLDQGLIEEHDSPARL 1462
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEG----RKEMMQLFkdyqkAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEI 232
|
250 260 270
....*....|....*....|....*....|.
gi 30682486 1463 LEDKSSSFSKLVAEYTAssdSRFKRSSMKTN 1493
Cdd:PRK13641 233 FSDKEWLKKHYLDEPAT---SRFASKLEKGG 260
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
623-829 |
9.10e-19 |
|
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: 86.78 E-value: 9.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 623 DVEVSNGAFSWDDSSPiPTLKDIRFKIPHGMNIAICG-------TVGSGKSSLLSSILGEVpKISG-NLKVCGRKAY--- 691
Cdd:cd03244 2 DIEFKNVSLRYRPNLP-PVLKNISFSIKPGEKVGIVGrtgsgksSLLLALFRLVELSSGSI-LIDGvDISKIGLHDLrsr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 692 ---IAQSPWIQSGKVEENI-LFGKPMQREWYQrVLEACSLNKDLEVFPFRDQTVIGERGINLSGGQKQRIQIARALYQDA 767
Cdd:cd03244 80 isiIPQDPVLFSGTIRSNLdPFGEYSDEELWQ-ALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30682486 768 DIYLFDDPFSAVDAHTGSHLfKEVLLGLLRNKTVIYVTHQLEFLPEADLILVMKDGRITQAG 829
Cdd:cd03244 159 KILVLDEATASVDPETDALI-QKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFD 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
703-837 |
1.16e-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: 87.70 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 703 VEENILFGKPMQ-------REWYQRVLEACSLNKDLEVFPfrDQtvigerginLSGGQKQRIQIARALYQDADIYLFDDP 775
Cdd:cd03294 119 VLENVAFGLEVQgvpraerEERAAEALELVGLEGWEHKYP--DE---------LSGGMQQRVGLARALAVDPDILLMDEA 187
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30682486 776 FSAVDAhtgshLFK----EVLLGLLRN--KTVIYVTHQL-EFLPEADLILVMKDGRITQAGKYNEILES 837
Cdd:cd03294 188 FSALDP-----LIRremqDELLRLQAElqKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1257-1436 |
1.26e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 91.23 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1257 VLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDG--INILTIgLHDLRSRLSIIPQEPTMFEG-TVR 1333
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSP-RDAQAAGIAIIHQELNLVPNlSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1334 SNldpleeyaddqIWealdkcqLGDEIRKK---------------------ELKLDSPVSEngqnWSVGQRQLVCLGRVL 1392
Cdd:COG1129 98 EN-----------IF-------LGREPRRGglidwramrrrarellarlglDIDPDTPVGD----LSVAQQQLVEIARAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 30682486 1393 LKRSKVLILDEATASVDTA-TDTLIQ--ETLRQHfsGCTVITIAHRI 1436
Cdd:COG1129 156 SRDARVLILDEPTASLTEReVERLFRiiRRLKAQ--GVAIIYISHRL 200
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
740-836 |
1.51e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 91.23 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 740 TVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDahTGS-HLFKEVLLGLLRNKTVIYVTHQLEFLPEADLIL 818
Cdd:PRK11176 472 TVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALD--TESeRAIQAALDELQKNRTSLVIAHRLSTIEKADEIL 549
|
90
....*....|....*...
gi 30682486 819 VMKDGRITQAGKYNEILE 836
Cdd:PRK11176 550 VVEDGEIVERGTHAELLA 567
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1241-1463 |
1.62e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 86.35 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGpHLPMvlrGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDlrsR-LS 1319
Cdd:COG3840 2 LRLDDLTYRYG-DFPL---RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE---RpVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1320 IIPQEPTMFEG-TVRSN----LDP---LEEYADDQIWEALDKCQLGDEIRKKELKLdspvsengqnwSVGQRQLVCLGRV 1391
Cdd:COG3840 75 MLFQENNLFPHlTVAQNiglgLRPglkLTAEQRAQVEQALERVGLAGLLDRLPGQL-----------SGGQRQRVALARC 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30682486 1392 LLKRSKVLILDEATASVDTATD----TLIQETLRQHfsGCTVITIAHRISSVID-SDMVLLLDQGLIEEHDSPARLL 1463
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPALRqemlDLVDELCRER--GLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1241-1460 |
1.78e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 87.41 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHLPM---VLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINIL--TIGLHDLR 1315
Cdd:PRK13637 3 IKIENLTHIYMEGTPFekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1316 SRLSIIPQEP--TMFEGTVR-------SNLDPLEEYADDQIWEALDKCQLGDEirkkELKLDSPVSENGqnwsvGQRQLV 1386
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEkdiafgpINLGLSEEEIENRVKRAMNIVGLDYE----DYKDKSPFELSG-----GQKRRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30682486 1387 CLGRVLLKRSKVLILDEATASVD-TATDTLIQE--TLRQHFsGCTVITIAHRISSVID-SDMVLLLDQGLIEEHDSPA 1460
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDpKGRDEILNKikELHKEY-NMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPR 230
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
625-824 |
1.85e-18 |
|
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: 85.60 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 625 EVSNGAFSWDDSSPiPTLKDIRFKIPHGMNIAICG-------TVGSGKSSLLssilgevPKISGNLKVCGRKayIAQSPW 697
Cdd:cd03225 1 ELKNLSFSYPDGAR-PALDDISLTIKKGEFVLIVGpngsgksTLLRLLNGLL-------GPTSGEVLVDGKD--LTKLSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 698 IQSGK-----------------VEENILFG---KPMQREW-YQRV---LEACSLNKDLEVFPFrdqtvigergiNLSGGQ 753
Cdd:cd03225 71 KELRRkvglvfqnpddqffgptVEEEVAFGlenLGLPEEEiEERVeeaLELVGLEGLRDRSPF-----------TLSGGQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30682486 754 KQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFkEVLLGLLR-NKTVIYVTHQLEFLPE-ADLILVMKDGR 824
Cdd:cd03225 140 KQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELL-ELLKKLKAeGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
624-829 |
2.27e-18 |
|
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: 84.29 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 624 VEVSNGAFSWDDSSPiPTLKDIRFKIPHGMNIAICGTvgsgkssllssilgevpkiSGnlkvCGrKAYIAQ------SPw 697
Cdd:cd03247 1 LSINNVSFSYPEQEQ-QVLKNLSLELKQGEKIALLGR-------------------SG----SG-KSTLLQlltgdlKP- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 698 iQSGKVeenILFGKPMQRewYQRVLEA--CSLNKDLEVFpfrDQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDP 775
Cdd:cd03247 55 -QQGEI---TLDGVPVSD--LEKALSSliSVLNQRPYLF---DTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 30682486 776 FSAVDAHTGSHLFkEVLLGLLRNKTVIYVTHQLEFLPEADLILVMKDGRITQAG 829
Cdd:cd03247 126 TVGLDPITERQLL-SLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
400-845 |
3.34e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 90.55 E-value: 3.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 400 QGHTSGEIINLMTVDAERISafSWymhdpwilvlqISLALLILYRSL--GLGSIA-----AFAATFLVMLgNIPLAKLEE 472
Cdd:TIGR00958 253 DENKTGELTSRLSSDTQTMS--RS-----------LSLNVNVLLRNLvmLLGLLGfmlwlSPRLTMVTLI-NLPLVFLAE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 473 KFQG----NLMESKDNRMKKTS----EALLNMRILKLQGWE-------MKFLHKILDLrgieaGWLKKFVYNSAAISSVL 537
Cdd:TIGR00958 319 KVFGkryqLLSEELQEAVAKANqvaeEALSGMRTVRSFAAEegeasrfKEALEETLQL-----NKRKALAYAGYLWTTSV 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 538 WAAPSFVSATAFGACMLLKIPLESGKIIAALATFRILQTPIYKLPDTISMIVQTKVSLDRIatFLCLD---DLQQDGMER 614
Cdd:TIGR00958 394 LGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKV--FEYLDrkpNIPLTGTLA 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 615 LPSGSSKmdVEVSNGAFSWDDSSPIPTLKDIRFKIPHGMNIAICG-------TVGSGKSSLLSSILGEV-----PKISGN 682
Cdd:TIGR00958 472 PLNLEGL--IEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGpsgsgksTVAALLQNLYQPTGGQVlldgvPLVQYD 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 683 LKVCGRK-AYIAQSPWIQSGKVEENILFG---KPMqrEWYQRVLEACSLNKDLEVFPFRDQTVIGERGINLSGGQKQRIQ 758
Cdd:TIGR00958 550 HHYLHRQvALVGQEPVLFSGSVRENIAYGltdTPD--EEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIA 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 759 IARALYQDADIYLFDDPFSAVDAHTgshlfkEVLLGLLRN---KTVIYVTHQLEFLPEADLILVMKDGRITQAGKYNEIL 835
Cdd:TIGR00958 628 IARALVRKPRVLILDEATSALDAEC------EQLLQESRSrasRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLM 701
|
490
....*....|
gi 30682486 836 ESGTDFMELV 845
Cdd:TIGR00958 702 EDQGCYKHLV 711
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
739-838 |
3.42e-18 |
|
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: 90.26 E-value: 3.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 739 QTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgSHLFKEVLLGLLRNKTVIYVTHQLEFLPEADLIL 818
Cdd:COG5265 485 DTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRT-ERAIQAALREVARGRTTLVIAHRLSTIVDADEIL 563
|
90 100
....*....|....*....|
gi 30682486 819 VMKDGRITQAGKYNEILESG 838
Cdd:COG5265 564 VLEAGRIVERGTHAELLAQG 583
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
368-598 |
3.43e-18 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) 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: 350037 [Multi-domain] Cd Length: 291 Bit Score: 86.89 E-value: 3.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 368 WYF-RLQKAGIGMRSVLVSMIYEKGLTLPCYSKQGHTSGEIINLMTVDAERISAFSWYMHDPWILVLQISLALLILYRSL 446
Cdd:cd18593 59 PYFfGMQRIGMRLRVACSSLIYRKALRLSQAALGKTTVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLQLIAVIYILWFEI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 447 GLGSIAAFAatFLVMLgnIPL----AKLEEKFQGNLMESKDNRMKKTSEALLNMRILKLQGWEMKFLHKILDLRGIEAGW 522
Cdd:cd18593 139 GWSCLAGLA--VLLIL--IPLqsffGKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKK 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30682486 523 LKKFVYNSAAISSVLWAAPSFVSATAFGACMLLKIPLESGKIIAALATFRILQTPI-YKLPDTISMIVQTKVSLDRI 598
Cdd:cd18593 215 VRRTSFLRALNMGLFFVSSKLILFLTFLAYILLGNILTAERVFVTMALYNAVRLTMtLFFPFAIQFGSELSVSIRRI 291
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
690-825 |
3.63e-18 |
|
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: 85.22 E-value: 3.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 690 AYIAQSPWIQSGKVEENILFGkpMQREWYQRVLEACS---LNKDLEVFPFRDQTVIGERGINLSGGQKQRIQIARALYQD 766
Cdd:cd03248 91 SLVGQEPVLFARSLQDNIAYG--LQSCSFECVKEAAQkahAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 30682486 767 ADIYLFDDPFSAVDAHTgSHLFKEVLLGLLRNKTVIYVTHQLEFLPEADLILVMKDGRI 825
Cdd:cd03248 169 PQVLILDEATSALDAES-EQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
744-829 |
4.46e-18 |
|
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: 83.64 E-value: 4.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 744 ERGIN-LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHlfkevLLGLLR------NKTVIYVTHQLEF-LPEAD 815
Cdd:cd03214 92 DRPFNeLSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIE-----LLELLRrlarerGKTVVMVLHDLNLaARYAD 166
|
90
....*....|....
gi 30682486 816 LILVMKDGRITQAG 829
Cdd:cd03214 167 RVILLKDGRIVAQG 180
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1245-1451 |
5.44e-18 |
|
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: 82.86 E-value: 5.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1245 NLQVRYGPHLpmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRsRLSIipqe 1324
Cdd:cd03216 5 GITKRFGGVK--ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDAR-RAGI---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1325 ptmfeGTVrsnldpleeYaddqiwealdkcQLgdeirkkelkldspvsengqnwSVGQRQLVCLGRVLLKRSKVLILDEA 1404
Cdd:cd03216 78 -----AMV---------Y------------QL----------------------SVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 30682486 1405 TASVDTA-TDTLIQ--ETLRQhfSGCTVITIAHRISSVID-SDMVLLLDQG 1451
Cdd:cd03216 110 TAALTPAeVERLFKviRRLRA--QGVAVIFISHRLDEVFEiADRVTVLRDG 158
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1272-1439 |
6.29e-18 |
|
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: 86.65 E-value: 6.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1272 GIVGRTGCGKSTLIQTLFRIVEP---AAGEIRIDGINILTIGLHDLR----SRLSIIPQE------PTMfegTVRsnldp 1338
Cdd:COG0444 35 GLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRkirgREIQMIFQDpmtslnPVM---TVG----- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1339 leeyadDQIWEALDKCQLGD--EIRKK--EL----KLDSPVSENGQ---NWSVGQRQLVCLGRVLLKRSKVLILDEATas 1407
Cdd:COG0444 107 ------DQIAEPLRIHGGLSkaEARERaiELlervGLPDPERRLDRyphELSGGMRQRVMIARALALEPKLLIADEPT-- 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 30682486 1408 vdTATDTLIQ-------ETLRQHFsGCTVITIAHRISSV 1439
Cdd:COG0444 179 --TALDVTIQaqilnllKDLQREL-GLAILFITHDLGVV 214
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
740-837 |
7.65e-18 |
|
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: 89.04 E-value: 7.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 740 TVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAhTGSHLFKEVLLGL-LRNKTVIYVTHQLEFLPEADLIL 818
Cdd:COG4618 459 TRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD-EGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLL 537
|
90
....*....|....*....
gi 30682486 819 VMKDGRITQAGKYNEILES 837
Cdd:COG4618 538 VLRDGRVQAFGPRDEVLAR 556
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
624-843 |
8.00e-18 |
|
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: 84.31 E-value: 8.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 624 VEVSNGAFSWDDSSPIptLKDIRFKIPHGMNIAICG-------TVGsgkssllssilgevpKI--------SGNLKVCGR 688
Cdd:COG1122 1 IELENLSFSYPGGTPA--LDDVSLSIEKGEFVAIIGpngsgksTLL---------------RLlngllkptSGEVLVDGK 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 689 K-------------AYIAQSPWIQ--SGKVEENILFGkPMQR-----EWYQRVLEACslnKDLEVFPFRDQTVIgergiN 748
Cdd:COG1122 64 DitkknlrelrrkvGLVFQNPDDQlfAPTVEEDVAFG-PENLglpreEIRERVEEAL---ELVGLEHLADRPPH-----E 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHtGSHLFKEVLLGL-LRNKTVIYVTHQLEFLPE-ADLILVMKDGRIT 826
Cdd:COG1122 135 LSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPR-GRRELLELLKRLnKEGKTVIIVTHDLDLVAElADRVIVLDDGRIV 213
|
250
....*....|....*..
gi 30682486 827 QAGKYNEILESGTDFME 843
Cdd:COG1122 214 ADGTPREVFSDYELLEE 230
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1241-1465 |
8.71e-18 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 84.76 E-value: 8.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRY----GPHLpmVLRGLTCTFRGGLKTGIVGRTGCGKStliqTLFRIV----EPAAGEIRIDGINIltiglH 1312
Cdd:COG1116 8 LELRGVSKRFptggGGVT--ALDDVSLTVAAGEFVALVGPSGCGKS----TLLRLIagleKPTSGEVLVDGKPV-----T 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1313 DLRSRLSIIPQEPTMFE-GTVRSNLD-PLE------EYADDQIWEALDKCQLGDEIRK--KELkldspvsengqnwSVGQ 1382
Cdd:COG1116 77 GPGPDRGVVFQEPALLPwLTVLDNVAlGLElrgvpkAERRERARELLELVGLAGFEDAypHQL-------------SGGM 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1383 RQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLRQHF--SGCTVITIAHRIS-SVIDSDMVLLLDQGlieehdsP 1459
Cdd:COG1116 144 RQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWqeTGKTVLFVTHDVDeAVFLADRVVVLSAR-------P 216
|
....*.
gi 30682486 1460 ARLLED 1465
Cdd:COG1116 217 GRIVEE 222
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
690-835 |
1.07e-17 |
|
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: 84.32 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 690 AYIAQSPWIQSG-KVEENILFG--------KPMQREWYQRVLEACSLnkdLEVFPFRDQTViGErginLSGGQKQRIQIA 760
Cdd:COG1120 78 AYVPQEPPAPFGlTVRELVALGryphlglfGRPSAEDREAVEEALER---TGLEHLADRPV-DE----LSGGERQRVLIA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 761 RALYQDADIYLFDDPFSAVDAHtgsHLFKevLLGLLR------NKTVIYVTHQLEF-LPEADLILVMKDGRITQAGKYNE 833
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDLA---HQLE--VLELLRrlarerGRTVVMVLHDLNLaARYADRLVLLKDGRIVAQGPPEE 224
|
..
gi 30682486 834 IL 835
Cdd:COG1120 225 VL 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1241-1455 |
1.29e-17 |
|
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: 83.78 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHLPMV--LRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTI---GLHDLR 1315
Cdd:cd03258 2 IELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLsgkELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1316 SRLSIIPQEPTMFEG-TVRSNLD-PLE------EYADDQIWEALDKCQLGDEIRKKELKLdspvsengqnwSVGQRQLVC 1387
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVAlPLEiagvpkAEIEERVLELLELVGLEDKADAYPAQL-----------SGGQKQRVG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30682486 1388 LGRVLLKRSKVLILDEATASVDTATDTLIQETLR---QHFsGCTVITIAHRISSVID-SDMVLLLDQGLIEE 1455
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRdinREL-GLTIVLITHEMEVVKRiCDRVAVMEKGEVVE 221
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
703-829 |
1.38e-17 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 86.31 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 703 VEENILFGKPMQR----EWYQRVLEACSLnKDLEVFpfrdqtviGERGIN-LSGGQKQRIQIARALYQDADIYLFDDPFS 777
Cdd:COG3842 94 VAENVAFGLRMRGvpkaEIRARVAELLEL-VGLEGL--------ADRYPHqLSGGQQQRVALARALAPEPRVLLLDEPLS 164
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 30682486 778 AVDAHTGSHLFKEvLLGLLR--NKTVIYVTH-QLEFLPEADLILVMKDGRITQAG 829
Cdd:COG3842 165 ALDAKLREEMREE-LRRLQRelGITFIYVTHdQEEALALADRIAVMNDGRIEQVG 218
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1256-1431 |
1.43e-17 |
|
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: 82.79 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1256 MVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSIIPQEPTMFEGTVRSN 1335
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1336 LD---PLEEYADDQIWEALDKCQLGDeirkkelKLDSPVSEngqnWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTAT 1412
Cdd:TIGR01189 94 LHfwaAIHGGAQRTIEDALAAVGLTG-------FEDLPAAQ----LSAGQQRRLALARLWLSRRPLWILDEPTTALDKAG 162
|
170 180
....*....|....*....|.
gi 30682486 1413 DTLIQETLRQHFS--GCTVIT 1431
Cdd:TIGR01189 163 VALLAGLLRAHLArgGIVLLT 183
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
703-825 |
1.86e-17 |
|
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: 82.92 E-value: 1.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 703 VEENILFG-------KPMQREWYQRVLEACSLNKDLEVFPFrdqtvigergiNLSGGQKQRIQIARALYQDADIYLFDDP 775
Cdd:cd03255 99 ALENVELPlllagvpKKERRERAEELLERVGLGDRLNHYPS-----------ELSGGQQQRVAIARALANDPKIILADEP 167
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 30682486 776 FSAVDAHTGS---HLFKEvlLGLLRNKTVIYVTHQLEFLPEADLILVMKDGRI 825
Cdd:cd03255 168 TGNLDSETGKevmELLRE--LNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
702-846 |
2.22e-17 |
|
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: 83.37 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 702 KVEENILF---GKPMQREWYQRVLEacSLNKDLEVFPFRDQTVIGerginLSGGQKQRIQIARALYQDADIYLFDDPFSA 778
Cdd:COG4555 90 TVRENIRYfaeLYGLFDEELKKRIE--ELIELLGLEEFLDRRVGE-----LSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30682486 779 VDAHTgSHLFKEVLLGLL-RNKTVIYVTHQLEFLPE-ADLILVMKDGRITQAGKYNEILESGTD------FMELVG 846
Cdd:COG4555 163 LDVMA-RRLLREILRALKkEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGEenledaFVALIG 237
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
949-1164 |
2.42e-17 |
|
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: 84.14 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 949 VSKDVKPLVSGSTLILVYVFLATASSFcilVRAMLSAMTGFKIATELFNQMHFRIFRASMSFFDATPIGRILNRASTDQS 1028
Cdd:cd07346 31 PAGDLSLLLWIALLLLLLALLRALLSY---LRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1029 AVDLRLPSQFSNLAIAAVNILGIIGVMGQVAWQ---VLIVFIPVIAACTWYrqyYISAARELARLSGISRSPLVQHFSET 1105
Cdd:cd07346 108 AVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKltlVALLLLPLYVLILRY---FRRRIRKASREVRESLAELSAFLQES 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 30682486 1106 LSGITTIRSFDQEPRFRTDIMRLNDCYSRLRFHAISAMEWLCFRLDLLSTVAFALSLVI 1164
Cdd:cd07346 185 LSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLY 243
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
703-837 |
2.42e-17 |
|
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: 83.15 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 703 VEENILFG----KPMQREWYQRVLE-ACSLNKD--LEVFPFRdqtvigerginLSGGQKQRIQIARALYQDADIYLFDDP 775
Cdd:cd03299 88 VYKNIAYGlkkrKVDKKEIERKVLEiAEMLGIDhlLNRKPET-----------LSGGEQQRVAIARALVVNPKILLLDEP 156
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30682486 776 FSAVDAHTgshlfKEVLLGLLR------NKTVIYVTHQL-EFLPEADLILVMKDGRITQAGKYNEILES 837
Cdd:cd03299 157 FSALDVRT-----KEKLREELKkirkefGVTVLHVTHDFeEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1258-1467 |
3.64e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 83.50 E-value: 3.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1258 LRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIG-LHDLRSRLSIIPQEP-TMFEG-TVRS 1334
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGIVFQNPeTQFVGrTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1335 NLDPLEEyaddqiwealDKCQLGDEIRKK------ELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVLILDEATASV 1408
Cdd:PRK13644 98 DLAFGPE----------NLCLPPIEIRKRvdralaEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSML 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1409 DTATDTLIQETLRQ-HFSGCTVITIAHRISSVIDSDMVLLLDQGLIEEHDSPARLLEDKS 1467
Cdd:PRK13644 168 DPDSGIAVLERIKKlHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
744-826 |
4.20e-17 |
|
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: 80.17 E-value: 4.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 744 ERGIN----LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKevLLGLLRN--KTVIYVTHQLEFLPE-ADL 816
Cdd:cd03216 74 RAGIAmvyqLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK--VIRRLRAqgVAVIFISHRLDEVFEiADR 151
|
90
....*....|
gi 30682486 817 ILVMKDGRIT 826
Cdd:cd03216 152 VTVLRDGRVV 161
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
747-825 |
5.12e-17 |
|
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: 80.13 E-value: 5.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 747 INLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgSHLFKEVLLGLL-RNKTVIYVTHQLEFLPE-ADLILVMKDGR 824
Cdd:cd03230 94 LKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPES-RREFWELLRELKkEGKTILLSSHILEEAERlCDRVAILNNGR 172
|
.
gi 30682486 825 I 825
Cdd:cd03230 173 I 173
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
309-578 |
5.82e-17 |
|
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: 82.69 E-value: 5.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 309 ILLSTLFAFVYTVSCYVAPYLMDTFVQYLNGQRQYSNQGVVLVTTFFVAKLVECQARrNWYFrlQKAGIGMRSVLVSMIY 388
Cdd:pfam00664 5 ILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQ-SYLL--NHTGERLSRRLRRKLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 389 EKGLTLPCYSKQGHTSGEIINLMTVDAERISAFSWYMHDPWILVLQISLALLILYRSLGLG-SIAAFAATFLVMLGNIPL 467
Cdd:pfam00664 82 KKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKlTLVLLAVLPLYILVSAVF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 468 AKLEEKFQGNLMESKDNRMKKTSEALLNMRILKLQGWEMKFLHKILD-LRGIEAGWLKKFVYNsAAISSVLWAAPSFVSA 546
Cdd:pfam00664 162 AKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKaLEEALKAGIKKAVAN-GLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....
gi 30682486 547 TA--FGACMLLKIPLESGKIIAALATFRILQTPI 578
Cdd:pfam00664 241 LAlwFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
574-837 |
7.54e-17 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 85.93 E-value: 7.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 574 LQTPIYKLPDTISMIVQTKVSLDRIatFLCLDDLQQD-GMERLPSGSSKMDVEvsNGAFSWDDSSPIptLKDIRFKIPHG 652
Cdd:PRK10790 294 LNEPLIELTTQQSMLQQAVVAGERV--FELMDGPRQQyGNDDRPLQSGRIDID--NVSFAYRDDNLV--LQNINLSVPSR 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 653 MNIAICGTVGSGKSSLLSSILGEVPKISGNLKVCGRK-------------AYIAQSPWIQSGKVEENILFGKPMQREWYQ 719
Cdd:PRK10790 368 GFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPlsslshsvlrqgvAMVQQDPVVLADTFLANVTLGRDISEEQVW 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 720 RVLEACSLNKDLEVFPFRDQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEvlLGLLRNK 799
Cdd:PRK10790 448 QALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQA--LAAVREH 525
|
250 260 270
....*....|....*....|....*....|....*....
gi 30682486 800 TVIYV-THQLEFLPEADLILVMKDGRITQAGKYNEILES 837
Cdd:PRK10790 526 TTLVViAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1240-1434 |
8.72e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 81.98 E-value: 8.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1240 EITICNLQVRYGPHlpMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLS 1319
Cdd:PRK11231 2 TLRTENLTVGYGTK--RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1320 IIPQEPTMFEG-TVRSnldpLEEY-------------ADDQ--IWEALDKCQLgDEIrkkelkLDSPVSEngqnWSVGQR 1383
Cdd:PRK11231 80 LLPQHHLTPEGiTVRE----LVAYgrspwlslwgrlsAEDNarVNQAMEQTRI-NHL------ADRRLTD----LSGGQR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 30682486 1384 QLVCLGRVLLKRSKVLILDEATASVDTATDT----LIQEtLRQhfSGCTVITIAH 1434
Cdd:PRK11231 145 QRAFLAMVLAQDTPVVLLDEPTTYLDINHQVelmrLMRE-LNT--QGKTVVTVLH 196
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1242-1434 |
1.23e-16 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 79.99 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1242 TICNLQVRYGpHLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINiltIGLHDLRSRLSII 1321
Cdd:cd03226 1 RIENISFSYK-KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKERRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1322 PQEPT--MFEGTVRSNLDP-LEEYADD--QIWEALdkcqlgdeirkKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRS 1396
Cdd:cd03226 77 MQDVDyqLFTDSVREELLLgLKELDAGneQAETVL-----------KDLDLYALKERHPLSLSGGQKQRLAIAAALLSGK 145
|
170 180 190
....*....|....*....|....*....|....*....
gi 30682486 1397 KVLILDEATASVDTATDTLIQETLRQHFS-GCTVITIAH 1434
Cdd:cd03226 146 DLLIFDEPTSGLDYKNMERVGELIRELAAqGKAVIVITH 184
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
703-829 |
1.25e-16 |
|
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: 80.38 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 703 VEENILFG----KPMQREWYQRVLEACSLnkdLEVfpfrdQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSA 778
Cdd:cd03301 89 VYDNIAFGlklrKVPKDEIDERVREVAEL---LQI-----EHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 30682486 779 VDAhtgsHLFKEVLLGLLR-----NKTVIYVTH-QLEFLPEADLILVMKDGRITQAG 829
Cdd:cd03301 161 LDA----KLRVQMRAELKRlqqrlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1241-1448 |
1.33e-16 |
|
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: 80.21 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHLP--MVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINIltiglHDLRSRL 1318
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV-----TGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1319 SIIPQEPTMFE-GTVRSN-LDPLE------EYADDQIWEALDKCQLGDEIRK--KELkldspvsengqnwSVGQRQLVCL 1388
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNvALGLElqgvpkAEARERAEELLELVGLSGFENAypHQL-------------SGGMRQRVAL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30682486 1389 GRVLLKRSKVLILDEATASVDTATDTLIQETL----RQHfsGCTVITIAHRIS-SVIDSDMVLLL 1448
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELldiwRET--GKTVLLVTHDIDeAVFLADRVVVL 205
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1273-1464 |
1.41e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 81.60 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1273 IVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSIIPQEP-TMFEG-TVRSNLD--------PLEEY 1342
Cdd:PRK13635 38 IVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQNPdNQFVGaTVQDDVAfglenigvPREEM 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1343 AdDQIWEALdkcqlgDEIRKKELKLDSPVSENGqnwsvGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLRQ 1422
Cdd:PRK13635 118 V-ERVDQAL------RQVGMEDFLNREPHRLSG-----GQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQ 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 30682486 1423 --HFSGCTVITIAHRISSVIDSDMVLLLDQGLIEEHDSPARLLE 1464
Cdd:PRK13635 186 lkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
692-835 |
1.61e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 84.88 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 692 IAQSPWIQSGKVEENILFGKP-MQREWYQRVLEACSLNKDLEVFPFRDqTVIGERGINLSGGQKQRIQIARALYQDADIY 770
Cdd:PRK11160 419 VSQRVHLFSATLRDNLLLAAPnASDEALIEVLQQVGLEKLLEDDKGLN-AWLGEGGRQLSGGEQRRLGIARALLHDAPLL 497
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30682486 771 LFDDPFSAVDAHTGSHLFkEVLLGLLRNKTVIYVTHQLEFLPEADLILVMKDGRITQAGKYNEIL 835
Cdd:PRK11160 498 LLDEPTEGLDAETERQIL-ELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELL 561
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
619-837 |
1.64e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 81.58 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 619 SSKMdVEVSNGAFSWDDSSPiPTLKDIRFKIPHGMNIAICG-------TVGSGKSSLLSSILGEVpKISG------NLKV 685
Cdd:PRK13632 4 KSVM-IKVENVSFSYPNSEN-NALKNVSFEINEGEYVAILGhngsgksTISKILTGLLKPQSGEI-KIDGitiskeNLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 686 CGRK-AYIAQSPWIQ--SGKVEENILFG---KPMQREWYQRVLEACSLNKDLEVFPFRDQTvigergiNLSGGQKQRIQI 759
Cdd:PRK13632 81 IRKKiGIIFQNPDNQfiGATVEDDIAFGlenKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQ-------NLSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 760 ARALYQDADIYLFDDPFSAVDAhTGSHLFKEVLLGL--LRNKTVIYVTHQLEFLPEADLILVMKDGRITQAGKYNEILES 837
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDP-KGKREIKKIMVDLrkTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
703-836 |
1.70e-16 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 83.07 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 703 VEENILFGKPMQR----EWYQRVLEACSLNKdLEVFPFRdqtvigeRGINLSGGQKQRIQIARALYQDADIYLFDDPFSA 778
Cdd:PRK09452 103 VFENVAFGLRMQKtpaaEITPRVMEALRMVQ-LEEFAQR-------KPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30682486 779 VDAhtgsHLFKEV---LLGLLR--NKTVIYVTH-QLEFLPEADLILVMKDGRITQAGKYNEILE 836
Cdd:PRK09452 175 LDY----KLRKQMqneLKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYE 234
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
703-836 |
1.79e-16 |
|
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: 80.36 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 703 VEENILFGKPMQR----EWYQRVLEACSLNKdLEVFPFRDqtvIGErginLSGGQKQRIQIARALYQDADIYLFDDPFSA 778
Cdd:cd03300 89 VFENIAFGLRLKKlpkaEIKERVAEALDLVQ-LEGYANRK---PSQ----LSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30682486 779 VDAHTGSHLFKEVL-----LGLlrnkTVIYVTH-QLEFLPEADLILVMKDGRITQAGKYNEILE 836
Cdd:cd03300 161 LDLKLRKDMQLELKrlqkeLGI----TFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
697-824 |
1.91e-16 |
|
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: 78.77 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 697 WIQSGKVEeniLFGKPMQREWYQRVLEACSLN---KDLEVFPFRdqTVIGERGINLSGGQKQRIQIARALYQDADIYLFD 773
Cdd:cd03229 51 EPDSGSIL---IDGEDLTDLEDELPPLRRRIGmvfQDFALFPHL--TVLENIALGLSGGQQQRVALARALAMDPDVLLLD 125
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 30682486 774 DPFSAVDAHTGSHLfKEVLLGLLRN--KTVIYVTHQLEFLPE-ADLILVMKDGR 824
Cdd:cd03229 126 EPTSALDPITRREV-RALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
703-829 |
2.05e-16 |
|
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: 79.65 E-value: 2.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 703 VEENILFGKPMQREWYQRVLEacslNKDLEVFpfrDQTVIGERGI-NLSGGQKQRIQIARALYQDADIYLFDDPFSAVDA 781
Cdd:cd03297 92 VRENLAFGLKRKRNREDRISV----DELLDLL---GLDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 30682486 782 HTgshlfKEVLLGLLR------NKTVIYVTHQLEFLPE-ADLILVMKDGRITQAG 829
Cdd:cd03297 165 AL-----RLQLLPELKqikknlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1241-1434 |
2.21e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 80.66 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHlpMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVE--PAA---GEIRIDGINILTIGLH--D 1313
Cdd:PRK14267 5 IETVNLRVYYGSN--HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElnEEArveGEVRLFGRNIYSPDVDpiE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1314 LRSRLSIIPQEP------TMFE----GTVRSNLDPLEEYADDQIWEALDKCQLGDEIrKKELKlDSPvsengQNWSVGQR 1383
Cdd:PRK14267 83 VRREVGMVFQYPnpfphlTIYDnvaiGVKLNGLVKSKKELDERVEWALKKAALWDEV-KDRLN-DYP-----SNLSGGQR 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 30682486 1384 QLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLRQHFSGCTVITIAH 1434
Cdd:PRK14267 156 QRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
960-1164 |
2.30e-16 |
|
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: 81.45 E-value: 2.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 960 STLILVYVFLATASSFCILVRAMLSAMTGFKIATELFNQMHFRIFRASMSFFDATPIGRILNRASTDQSAVDLRLPSQFS 1039
Cdd:cd18557 36 NELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1040 NLAIAAVNILGIIGVMGQVAWQ---VLIVFIPVIAACTWyrqYYISAARELARLSGISRSPLVQHFSETLSGITTIRSFD 1116
Cdd:cd18557 116 QLLRNILQVIGGLIILFILSWKltlVLLLVIPLLLIASK---IYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFS 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 30682486 1117 QEP----RFRT---DIMRLNdcYSRLRFHAI-SAMEWLCFRLDLLSTVAFALSLVI 1164
Cdd:cd18557 193 AEEkeirRYSEaldRSYRLA--RKKALANALfQGITSLLIYLSLLLVLWYGGYLVL 246
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1257-1451 |
3.78e-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: 78.36 E-value: 3.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1257 VLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTL--FRIVEPAAGEIRIDGINIltiGLHDLRSRLSIIPQE----PTMfeg 1330
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPL---DKRSFRKIIGYVPQDdilhPTL--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1331 TVRSNLDpleeyaddqiwealdkcqlgdeirkkelkldspVSENGQNWSVGQRQLVCLGRVLLKRSKVLILDEATASVDT 1410
Cdd:cd03213 98 TVRETLM---------------------------------FAAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 30682486 1411 ATDTLIQETLRQ-HFSGCTVITIAHRISSVIDS--DMVLLLDQG 1451
Cdd:cd03213 145 SSALQVMSLLRRlADTGRTIICSIHQPSSEIFElfDKLLLLSQG 188
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1249-1448 |
4.84e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 78.04 E-value: 4.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1249 RYGPHlpMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGiniltiglhdlRSRLSIIPQE---- 1324
Cdd:NF040873 1 GYGGR--PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRsevp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1325 ---PTMFEGTV-------RSNLDPLEEYADDQIWEALDKCQLGDEIRKkelkldsPVSEngqnWSVGQRQLVCLGRVLLK 1394
Cdd:NF040873 68 dslPLTVRDLVamgrwarRGLWRRLTRDDRAAVDDALERVGLADLAGR-------QLGE----LSGGQRQRALLAQGLAQ 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 30682486 1395 RSKVLILDEATASVDTATDTLIQETLRQ-HFSGCTVITIAHRISSVIDSDMVLLL 1448
Cdd:NF040873 137 EADLLLLDEPTTGLDAESRERIIALLAEeHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
939-1216 |
5.58e-16 |
|
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: 80.34 E-value: 5.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 939 SNYWMAwVTPVSKDVKPLVSGSTLILVYVFLATASSFCILVRAMLSAMTGFKIATELFNQMHFRIFRASMSFFDATPIGR 1018
Cdd:cd18559 18 SNLWLL-LWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSGE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1019 ILNRASTDQSAVDLRLPS---QFS---NLAIAAVNILGIIGVMGQVAWQVLIVFIPViaactwyRQYYISAARELARLSG 1092
Cdd:cd18559 97 LVNLFSKDLDRVDSMAPQvikMWMgplQNVIGLYLLILLAGPMAAVGIPLGLLYVPV-------NRVYAASSRQLKRLES 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1093 ISRSPLVQHFSETLSGITTIRSFDQEPRF--RTDIMRLNDcysRLRFHAISAMEWLCFRLDLLSTVAFAL-SLVILVSVP 1169
Cdd:cd18559 170 VSKDPRYKLFNETLLGISVIKAFEWEEAFirQVDAKRDNE---LAYLPSIVYLRALAVRLWCVGPCIVLFaSFFAYVSRH 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 30682486 1170 EgviNPSFAGLAVTYALNLNSLQATLIWTLCDLENKMISVERMLQYI 1216
Cdd:cd18559 247 S---LAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
690-825 |
5.97e-16 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 78.32 E-value: 5.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 690 AYIAQSPWIQSGKVEENILF-----GKPMQREWYQRVLEACSLNKDlevfpFRDQTVIgergiNLSGGQKQRIQIARALY 764
Cdd:COG4619 77 AYVPQEPALWGGTVRDNLPFpfqlrERKFDRERALELLERLGLPPD-----ILDKPVE-----RLSGGERQRLALIRALL 146
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30682486 765 QDADIYLFDDPFSAVDAHTgSHLFKEVLLGLLR--NKTVIYVTH---QLEFLpeADLILVMKDGRI 825
Cdd:COG4619 147 LQPDVLLLDEPTSALDPEN-TRRVEELLREYLAeeGRAVLWVSHdpeQIERV--ADRVLTLEAGRL 209
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1240-1466 |
1.19e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 79.29 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1240 EITICNLQVRYGPHLPMVLRGLT---CTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIdGINILTIG-----L 1311
Cdd:PRK13634 2 DITFQKVEHRYQYKTPFERRALYdvnVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGkknkkL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1312 HDLRSRLSIIPQ--EPTMFEGTVR-------SNLDPLEEYADDQIWEALDKCQLGDEIRKKelkldSPVSENGqnwsvGQ 1382
Cdd:PRK13634 81 KPLRKKVGIVFQfpEHQLFEETVEkdicfgpMNFGVSEEDAKQKAREMIELVGLPEELLAR-----SPFELSG-----GQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1383 RQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQE---TLRQHfSGCTVITIAHRISSVID-SDMVLLLDQGLIEEHDS 1458
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEmfyKLHKE-KGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGT 229
|
....*...
gi 30682486 1459 PARLLEDK 1466
Cdd:PRK13634 230 PREIFADP 237
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
703-826 |
1.65e-15 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 77.39 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 703 VEENILF-----GKPMQ--REWYQRVLEACSLNKDLEVFPfrDQtvigerginLSGGQKQRIQIARALYQDADIYLFDDP 775
Cdd:COG1136 103 ALENVALplllaGVSRKerRERARELLERVGLGDRLDHRP--SQ---------LSGGQQQRVAIARALVNRPKLILADEP 171
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 30682486 776 FSAVDAHTGSHLFkEVLLGLLR--NKTVIYVTHQLEFLPEADLILVMKDGRIT 826
Cdd:COG1136 172 TGNLDSKTGEEVL-ELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIV 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
749-825 |
3.00e-15 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 75.33 E-value: 3.00e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDaHTGSHLFKEVLLGL-LRNKTVIYVTHQLEFLPEADLILVMKDGRI 825
Cdd:cd03246 97 LSGGQRQRLGLARALYGNPRILVLDEPNSHLD-VEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1241-1409 |
3.54e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 79.50 E-value: 3.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHlpMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSI 1320
Cdd:PRK09536 4 IDVSDLSVEFGDT--TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1321 IPQEPTM-FEGTVR-----------SNLDPLEEYADDQIWEALDKCQLGDEIrkkelklDSPVSEngqnWSVGQRQLVCL 1388
Cdd:PRK09536 82 VPQDTSLsFEFDVRqvvemgrtphrSRFDTWTETDRAAVERAMERTGVAQFA-------DRPVTS----LSGGERQRVLL 150
|
170 180
....*....|....*....|.
gi 30682486 1389 GRVLLKRSKVLILDEATASVD 1409
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLD 171
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1245-1451 |
6.77e-15 |
|
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: 75.01 E-value: 6.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1245 NLQVRYGPHlpMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGiNILTIglhDLRSRLSIIPQE 1324
Cdd:cd03269 5 NVTKRFGRV--TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG-KPLDI---AARNRIGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1325 ----PTMfegTVRSNLDPL-------EEYADDQIWEALDKCQLGD--EIRKKELkldspvsengqnwSVGQRQLVCLGRV 1391
Cdd:cd03269 79 rglyPKM---KVIDQLVYLaqlkglkKEEARRRIDEWLERLELSEyaNKRVEEL-------------SKGNQQKVQFIAA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30682486 1392 LLKRSKVLILDEATASVD-TATDTLIQETLRQHFSGCTVITIAHRISSVID-SDMVLLLDQG 1451
Cdd:cd03269 143 VIHDPELLILDEPFSGLDpVNVELLKDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKG 204
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1245-1457 |
8.39e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 79.34 E-value: 8.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1245 NLQVRYGPHLpmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIdGINIltiglhdlrsRLSIIPQE 1324
Cdd:COG0488 320 GLSKSYGDKT--LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGYFDQH 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1325 ptmfegtvRSNLDPleeyaDDQIWEALdkCQLGDEIRKKEL------------KLDSPVSengqNWSVGQRQLVCLGRVL 1392
Cdd:COG0488 387 --------QEELDP-----DKTVLDEL--RDGAPGGTEQEVrgylgrflfsgdDAFKPVG----VLSGGEKARLALAKLL 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30682486 1393 LKRSKVLILDEATASVDTATDTLIQETLrQHFSGcTVITIAH-R--ISSVIDSdmVLLLDQGLIEEHD 1457
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDIETLEALEEAL-DDFPG-TVLLVSHdRyfLDRVATR--ILEFEDGGVREYP 511
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
624-875 |
8.59e-15 |
|
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: 79.18 E-value: 8.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 624 VEVSNGAFSWDDSsPIPTLKDIRFKIPHGMNIAICG------TVGSGKSSLLSSILGEvpkISGNLKVCG---------- 687
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGesgsgkSTLALALMGLLPHGGR---ISGEVLLDGrdllelseal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 688 ---RKAYIAQSPWIQ--SGKVEENILFG-------KPMQREWYQRVLEACSLNKDLEVFPFRdqtvigerginLSGGQKQ 755
Cdd:COG1123 81 rgrRIGMVFQDPMTQlnPVTVGDQIAEAlenlglsRAEARARVLELLEAVGLERRLDRYPHQ-----------LSGGQRQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 756 RIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEVL-LGLLRNKTVIYVTHQLEFLPE-ADLILVMKDGRITQAGKYNE 833
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLReLQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEE 229
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 30682486 834 ILesgtdfmelvgAHTDALAAVDSYEKGSASAQSTTSKESKV 875
Cdd:COG1123 230 IL-----------AAPQALAAVPRLGAARGRAAPAAAAAEPL 260
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1241-1439 |
9.08e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 76.23 E-value: 9.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHlpMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEpAAGEIRIDG--------INILTIGLH 1312
Cdd:PRK14258 8 IKVNNLSFYYDTQ--KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGrveffnqnIYERRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1313 DLRSRLSIIPQEPTMFEGTVRSNL---------DPLEEYaDDQIWEALDKCQLGDEIRKKelkldspVSENGQNWSVGQR 1383
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVaygvkivgwRPKLEI-DDIVESALKDADLWDEIKHK-------IHKSALDLSGGQQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 30682486 1384 QLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLRQHF--SGCTVITIAHRISSV 1439
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQV 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1249-1453 |
9.78e-15 |
|
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: 74.84 E-value: 9.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1249 RYGpHLPMvlrGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTigLHDLRSRLSIIPQEPTMF 1328
Cdd:cd03298 9 SYG-EQPM---HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTA--APPADRPVSMLFQENNLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1329 EG-TVRSNLD----P-LEEYADDQiwEALDKC--QLGdeIRKKELKLDSPVSEngqnwsvGQRQLVCLGRVLLKRSKVLI 1400
Cdd:cd03298 83 AHlTVEQNVGlglsPgLKLTAEDR--QAIEVAlaRVG--LAGLEKRLPGELSG-------GERQRVALARVLVRDKPVLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 30682486 1401 LDEATASVDTA----TDTLIQETLRQhfSGCTVITIAHRISSVID-SDMVLLLDQGLI 1453
Cdd:cd03298 152 LDEPFAALDPAlraeMLDLVLDLHAE--TKMTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1250-1451 |
1.25e-14 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 74.67 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1250 YGPHLPmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSR----LSIIPQEP 1325
Cdd:cd03290 10 WGSGLA-TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1326 TMFEGTVRSNLDPLEEYADDQIWEALDKCQLGDEIRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVLILDEAT 1405
Cdd:cd03290 89 WLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 30682486 1406 ASVDT-ATDTLIQETLRQHFSG--CTVITIAHRISSVIDSDMVLLLDQG 1451
Cdd:cd03290 169 SALDIhLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
748-825 |
1.45e-14 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 75.09 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 748 NLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGshlfkEVLLGLLR------NKTVIYVTHQLEFLPE-ADLILVM 820
Cdd:COG3638 146 QLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTA-----RQVMDLLRriaredGITVVVNLHQVDLARRyADRIIGL 220
|
....*
gi 30682486 821 KDGRI 825
Cdd:COG3638 221 RDGRV 225
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1241-1422 |
1.47e-14 |
|
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: 74.89 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHLpmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDlRSRLSI 1320
Cdd:cd03218 1 LRAENLSKRYGKRK--VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1321 I--PQEPTMFEG-TVRSNLDPLEEYADDQIWEALDKC-QLGDEirkkeLKLDSPVSENGQNWSVGQRQLVCLGRVLLKRS 1396
Cdd:cd03218 78 GylPQEASIFRKlTVEENILAVLEIRGLSKKEREEKLeELLEE-----FHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180
....*....|....*....|....*.
gi 30682486 1397 KVLILDEATASVDTATDTLIQETLRQ 1422
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQKIIKI 178
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1240-1468 |
2.13e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 75.01 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1240 EITICNLQVRYGPHlpMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTI---------- 1309
Cdd:PRK10619 5 KLNVIDLHKRYGEH--EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkva 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1310 ---GLHDLRSRLSIIPQE------PTMFEGTVRSNLDPL---EEYADDQIWEALDKCQLGDEIRKKelkldSPVSENGqn 1377
Cdd:PRK10619 83 dknQLRLLRTRLTMVFQHfnlwshMTVLENVMEAPIQVLglsKQEARERAVKYLAKVGIDERAQGK-----YPVHLSG-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1378 wsvGQRQLVCLGRVLLKRSKVLILDEATASVDTatdTLIQETLR--QHFS--GCTVITIAHRISSVID-SDMVLLLDQGL 1452
Cdd:PRK10619 156 ---GQQQRVSIARALAMEPEVLLFDEPTSALDP---ELVGEVLRimQQLAeeGKTMVVVTHEMGFARHvSSHVIFLHQGK 229
|
250
....*....|....*.
gi 30682486 1453 IEEHDSPARLLEDKSS 1468
Cdd:PRK10619 230 IEEEGAPEQLFGNPQS 245
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
692-860 |
2.85e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 78.53 E-value: 2.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 692 IAQSPWIQSGKVEENILFGKP-MQREWYQRVLEACSLNKDLEVFPFRDQTVIGERGINLSGGQKQRIQIARALYQDADIY 770
Cdd:PTZ00265 1301 VSQEPMLFNMSIYENIKFGKEdATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKIL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 771 LFDDPFSAVDAHTGSHLFKEVL-LGLLRNKTVIYVTHQLEFLPEADLILVmkdgritqagkYNEILESGTdFMELVGAHT 849
Cdd:PTZ00265 1381 LLDEATSSLDSNSEKLIEKTIVdIKDKADKTIITIAHRIASIKRSDKIVV-----------FNNPDRTGS-FVQAHGTHE 1448
|
170
....*....|..
gi 30682486 850 DALAAVDS-YEK 860
Cdd:PTZ00265 1449 ELLSVQDGvYKK 1460
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
748-825 |
3.01e-14 |
|
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: 74.14 E-value: 3.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 748 NLSGGQKQRIQIARALYQDADIYLFDDPFSAVD---AHTGSHLFKEvlLGLLRNKTVIYVTHQLEFLPE-ADLILVMKDG 823
Cdd:cd03256 144 QLSGGQQQRVAIARALMQQPKLILADEPVASLDpasSRQVMDLLKR--INREEGITVIVSLHQVDLAREyADRIVGLKDG 221
|
..
gi 30682486 824 RI 825
Cdd:cd03256 222 RI 223
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1252-1434 |
3.05e-14 |
|
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: 73.21 E-value: 3.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1252 PHLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINIltIGLHD-----LRSRLSIIPQE-- 1324
Cdd:cd03292 11 PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDV--SDLRGraipyLRRKIGVVFQDfr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1325 --PTMfegTVRSNLD-PLE-EYADDQIW-----EALDKCQLGDEIRKKELKLdspvsengqnwSVGQRQLVCLGRVLLKR 1395
Cdd:cd03292 89 llPDR---NVYENVAfALEvTGVPPREIrkrvpAALELVGLSHKHRALPAEL-----------SGGEQQRVAIARAIVNS 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 30682486 1396 SKVLILDEATASVDTATDTLIQETLRQ-HFSGCTVITIAH 1434
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIMNLLKKiNKAGTTVVVATH 194
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
702-837 |
3.12e-14 |
|
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: 77.25 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 702 KVEENI-----LFGKPMQREWYQRV---LEACSLNKD-LEVFPFRdqtvigerginLSGGQKQRIQIARALYQDADIYLF 772
Cdd:COG1123 360 TVGDIIaeplrLHGLLSRAERRERVaelLERVGLPPDlADRYPHE-----------LSGGQRQRVAIARALALEPKLLIL 428
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30682486 773 DDPFSAVDAHTGSHlfkevLLGLLR------NKTVIYVTHQLEFLPE-ADLILVMKDGRITQAGKYNEILES 837
Cdd:COG1123 429 DEPTSALDVSVQAQ-----ILNLLRdlqrelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1272-1445 |
3.17e-14 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 75.54 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1272 GIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIG---LHDLRSRLSIIPQEPT------MfegTVRSNL-DPLEE 1341
Cdd:COG4608 48 GLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDPYaslnprM---TVGDIIaEPLRI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1342 Y-------ADDQIWEALDKCQLGDEIRKK---ELkldspvsengqnwSVGQRQLVCLGRVLLKRSKVLILDEATAsvdtA 1411
Cdd:COG4608 125 HglaskaeRRERVAELLELVGLRPEHADRyphEF-------------SGGQRQRIGIARALALNPKLIVCDEPVS----A 187
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 30682486 1412 TDTLIQ-------ETLRQHFsGCTVITIAHRISSV--IdSDMV 1445
Cdd:COG4608 188 LDVSIQaqvlnllEDLQDEL-GLTYLFISHDLSVVrhI-SDRV 228
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1273-1449 |
3.52e-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: 3.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1273 IVGRTGCGKSTLIQTLFRIVEPAAGeiridginilTIGLHDlRSRLSIIPQEPTMFEGTVRsnldpleeyadDQI---WE 1349
Cdd:cd03223 32 ITGPSGTGKSSLFRALAGLWPWGSG----------RIGMPE-GEDLLFLPQRPYLPLGTLR-----------EQLiypWD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1350 aldkcqlgdeirkKELkldspvsengqnwSVGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLRQHfsGCTV 1429
Cdd:cd03223 90 -------------DVL-------------SGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL--GITV 141
|
170 180
....*....|....*....|
gi 30682486 1430 ITIAHRISSVIDSDMVLLLD 1449
Cdd:cd03223 142 ISVGHRPSLWKFHDRVLDLD 161
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1241-1466 |
4.31e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 74.04 E-value: 4.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHlpMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRI--VEP---AAGEIRIDGINIL--TIGLHD 1313
Cdd:PRK14239 6 LQVSDLSVYYNKK--KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIYspRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1314 LRSRLSIIPQEPTMFEGTVRSN------LDPLEEYA--DDQIWEALDKCQLGDEIrkKELKLDSPVSENGqnwsvGQRQL 1385
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPMSIYENvvyglrLKGIKDKQvlDEAVEKSLKGASIWDEV--KDRLHDSALGLSG-----GQQQR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1386 VCLGRVLLKRSKVLILDEATASVDTATDTLIQETLRQHFSGCTVITIAHRI--SSVIDSDMVLLLDQGLIEEHDSPARLL 1463
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMqqASRISDRTGFFLDGDLIEYNDTKQMFM 236
|
...
gi 30682486 1464 EDK 1466
Cdd:PRK14239 237 NPK 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
749-825 |
6.97e-14 |
|
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: 72.18 E-value: 6.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDahtgSHLFKEVlLGLLRN-----KTVIYVTHQLEFLPE-ADLILVMKD 822
Cdd:cd03262 136 LSGGQQQRVAIARALAMNPKVMLFDEPTSALD----PELVGEV-LDVMKDlaeegMTMVVVTHEMGFAREvADRVIFMDD 210
|
...
gi 30682486 823 GRI 825
Cdd:cd03262 211 GRI 213
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1256-1452 |
7.10e-14 |
|
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: 72.14 E-value: 7.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1256 MVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGI-----------NILTIGLHD-LRSRLSiipq 1323
Cdd:cd03231 14 ALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpldfqrdsiarGLLYLGHAPgIKTTLS---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1324 eptmfegtVRSNLDPL-EEYADDQIWEALDKCQL-GDEirkkelklDSPVSEngqnWSVGQRQLVCLGRVLLKRSKVLIL 1401
Cdd:cd03231 90 --------VLENLRFWhADHSDEQVEEALARVGLnGFE--------DRPVAQ----LSAGQQRRVALARLLLSGRPLWIL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 30682486 1402 DEATASVDTATDTLIQETLRQHFSGCTVITIAHRISSVIDSDMVLLLDQGL 1452
Cdd:cd03231 150 DEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDLGF 200
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
749-847 |
7.21e-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: 7.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgshlfKEVLLGLLR------NKTVIYVTH-QLEFLPEADLILVMK 821
Cdd:cd03296 137 LSGGQRQRVALARALAVEPKVLLLDEPFGALDAKV-----RKELRRWLRrlhdelHVTTVFVTHdQEEALEVADRVVVMN 211
|
90 100
....*....|....*....|....*...
gi 30682486 822 DGRITQAGKYNEILES-GTDF-MELVGA 847
Cdd:cd03296 212 KGRIEQVGTPDEVYDHpASPFvYSFLGE 239
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1257-1463 |
7.57e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.50 E-value: 7.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1257 VLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDG--INILTIGLHDLRSRLSIIPQEP--TMFEGTV 1332
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQDPeqQIFYTDI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1333 RS-------NLDPLEEYADDQIWEALdkcQLGDEIRKKElkldSPVsengQNWSVGQRQLVCLGRVLLKRSKVLILDEAT 1405
Cdd:PRK13638 96 DSdiafslrNLGVPEAEITRRVDEAL---TLVDAQHFRH----QPI----QCLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1406 ASVDTATDTLIQETLRQHFS-GCTVITIAHRISSVID-SDMVLLLDQGLIEEHDSPARLL 1463
Cdd:PRK13638 165 AGLDPAGRTQMIAIIRRIVAqGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVF 224
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
624-835 |
8.07e-14 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 73.23 E-value: 8.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 624 VEVSNGAFSWDDSSPiPTLKDIRFKIPHGMNIAICG-------TVGsgkssllssilgevpKI--------SGNLKVCGR 688
Cdd:TIGR04520 1 IEVENVSFSYPESEK-PALKNVSLSIEKGEFVAIIGhngsgksTLA---------------KLlnglllptSGKVTVDGL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 689 KAYIAQSPW----------------IQSGKVEENILFGK-----PmQREWYQRVLEACslnKDLEVFPFRDQTVIgergi 747
Cdd:TIGR04520 65 DTLDEENLWeirkkvgmvfqnpdnqFVGATVEDDVAFGLenlgvP-REEMRKRVDEAL---KLVGMEDFRDREPH----- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 748 NLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAhTGShlfKEVLLGLLR-----NKTVIYVTHQLEFLPEADLILVMKD 822
Cdd:TIGR04520 136 LLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDP-KGR---KEVLETIRKlnkeeGITVISITHDMEEAVLADRVIVMNK 211
|
250
....*....|...
gi 30682486 823 GRITQAGKYNEIL 835
Cdd:TIGR04520 212 GKIVAEGTPREIF 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1271-1437 |
8.76e-14 |
|
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: 71.94 E-value: 8.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1271 TGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINIL----TIGLHDLRSRLSIIPQEPTMFEG-TVRSNLD---PLEEY 1342
Cdd:cd03297 26 TGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFdsrkKINLPPQQRKIGLVFQQYALFPHlNVRENLAfglKRKRN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1343 ADDQIW--EALDKCQLGDEIRKKELKLdspvsengqnwSVGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETL 1420
Cdd:cd03297 106 REDRISvdELLDLLGLDHLLNRYPAQL-----------SGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170 180
....*....|....*....|
gi 30682486 1421 RQ---HFSGcTVITIAHRIS 1437
Cdd:cd03297 175 KQikkNLNI-PVIFVTHDLS 193
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
748-835 |
8.79e-14 |
|
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: 72.61 E-value: 8.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 748 NLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgshlfKEVLLGLLR--NK----TVIYVTHQLEFLPE-ADLILVM 820
Cdd:cd03258 140 QLSGGQKQRVGIARALANNPKVLLCDEATSALDPET-----TQSILALLRdiNRelglTIVLITHEMEVVKRiCDRVAVM 214
|
90
....*....|....*
gi 30682486 821 KDGRITQAGKYNEIL 835
Cdd:cd03258 215 EKGEVVEEGTVEEVF 229
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
705-829 |
1.29e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 73.99 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 705 ENILFGKPMQ----REWYQRVLEACSLnKDLEVFPFR--DQtvigerginLSGGQKQRIQIARALYQDADIYLFDDPFSA 778
Cdd:PRK11432 97 ENVGYGLKMLgvpkEERKQRVKEALEL-VDLAGFEDRyvDQ---------ISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 30682486 779 VDAHTGSHLfKEVLLGLLR--NKTVIYVTH-QLEFLPEADLILVMKDGRITQAG 829
Cdd:PRK11432 167 LDANLRRSM-REKIRELQQqfNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIG 219
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1258-1466 |
1.68e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 72.57 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1258 LRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDG--INILTIGLHDLRSRLSIIPQEP--TMFEGTVR 1333
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESVGMVFQDPdnQLFSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1334 snldpleeyaDDQIWEALDKCQLGDEIRKK-----ELKLDSPVSENGQNW-SVGQRQLVCLGRVLLKRSKVLILDEATAS 1407
Cdd:PRK13636 102 ----------QDVSFGAVNLKLPEDEVRKRvdnalKRTGIEHLKDKPTHClSFGQKKRVAIAGVLVMEPKVLVLDEPTAG 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30682486 1408 VDTATDTLIQETLR--QHFSGCTVITIAHRISSV-IDSDMVLLLDQGLIEEHDSPARLLEDK 1466
Cdd:PRK13636 172 LDPMGVSEIMKLLVemQKELGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
962-1164 |
1.70e-13 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the 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 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. 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. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. 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: 349986 [Multi-domain] Cd Length: 292 Bit Score: 72.85 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 962 LILVYVFLATASSFCILVRAMLSAMTGFKIATELFNQMHFRIFRASMSFFDATPIGRILNRASTDQSAVDLRLPSQFSNL 1041
Cdd:cd18542 41 LALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1042 AIAAVNILGIIGVMGQVAWQ---VLIVFIPVIAACTWY-----RQYYISAARELARLSGIsrsplVQhfsETLSGITTIR 1113
Cdd:cd18542 121 VRAVLLFIGALIIMFSINWKltlISLAIIPFIALFSYVffkkvRPAFEEIREQEGELNTV-----LQ---ENLTGVRVVK 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 30682486 1114 SFDQEP----RFRtdimRLNDCYSRLRFHAISAMEWLCFRLDLLSTVAFALSLVI 1164
Cdd:cd18542 193 AFAREDyeieKFD----KENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWV 243
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1273-1448 |
2.46e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 70.90 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1273 IVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSIIPQEPTMFEGTVRSNL-----------DPlEE 1341
Cdd:PRK10247 38 ITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDNLifpwqirnqqpDP-AI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1342 YADDqiweaLDKCQLGDEIrkkelkLDSPVSEngqnWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLR 1421
Cdd:PRK10247 117 FLDD-----LERFALPDTI------LTKNIAE----LSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIH 181
|
170 180
....*....|....*....|....*....
gi 30682486 1422 QHFS--GCTVITIAHRISSVIDSDMVLLL 1448
Cdd:PRK10247 182 RYVReqNIAVLWVTHDKDEINHADKVITL 210
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1273-1462 |
3.03e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 71.69 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1273 IVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGiNILTI-GLHDLRSRLSIIPQEP-TMFEG-TVRSNLD--------PLEE 1341
Cdd:PRK13650 38 IIGHNGSGKSTTVRLIDGLLEAESGQIIIDG-DLLTEeNVWDIRHKIGMVFQNPdNQFVGaTVEDDVAfglenkgiPHEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1342 YAdDQIWEALDKCQLGDEIRKKELKLdspvsengqnwSVGQRQLVCLGRVLLKRSKVLILDEATASVD-TATDTLIQ--E 1418
Cdd:PRK13650 117 MK-ERVNEALELVGMQDFKEREPARL-----------SGGQKQRVAIAGAVAMRPKIIILDEATSMLDpEGRLELIKtiK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 30682486 1419 TLRQHFsGCTVITIAHRISSVIDSDMVLLLDQGLIEEHDSPARL 1462
Cdd:PRK13650 185 GIRDDY-QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1257-1475 |
3.42e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 71.67 E-value: 3.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1257 VLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAG-----EIRIDGINILTI-GLHDLRSRLSIIPQEPTMFEG 1330
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1331 TVRSN---------LDPLEEYADdqIWEA-LDKCQLGDEIrkKELKLDSPVSENGqnwsvGQRQLVCLGRVLLKRSKVLI 1400
Cdd:PRK14271 116 SIMDNvlagvrahkLVPRKEFRG--VAQArLTEVGLWDAV--KDRLSDSPFRLSG-----GQQQLLCLARTLAVNPEVLL 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30682486 1401 LDEATASVDTATDTLIQETLRQHFSGCTVITIAHRISSV--IDSDMVLLLDQGLIEEHDSPARLLEDKSSSFSKLVA 1475
Cdd:PRK14271 187 LDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAarISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVA 263
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
748-855 |
3.93e-13 |
|
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: 72.83 E-value: 3.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 748 NLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgshlfK-EVL--LGLLRNKT---VIYVTHQLEflpE----ADLI 817
Cdd:COG4148 133 TLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR-----KaEILpyLERLRDELdipILYVSHSLD---EvarlADHV 204
|
90 100 110
....*....|....*....|....*....|....*...
gi 30682486 818 LVMKDGRITQAGKYNEILeSGTDFMELvgAHTDALAAV 855
Cdd:COG4148 205 VLLEQGRVVASGPLAEVL-SRPDLLPL--AGGEEAGSV 239
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
749-825 |
4.54e-13 |
|
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: 70.23 E-value: 4.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgshlfKEVLLGLLR------NKTVIYVTHQLEFLPE-ADLILVMK 821
Cdd:cd03257 146 LSGGQRQRVAIARALALNPKLLIADEPTSALDVSV-----QAQILDLLKklqeelGLTLLFITHDLGVVAKiADRVAVMY 220
|
....
gi 30682486 822 DGRI 825
Cdd:cd03257 221 AGKI 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1239-1462 |
5.65e-13 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 72.03 E-value: 5.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1239 GEITICNLQVRYGPHLpmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIqtlfRIV----EPAAGEIRIDGINILtiGLHDL 1314
Cdd:COG3839 2 ASLELENVSKSYGGVE--ALKDIDLDIEDGEFLVLLGPSGCGKSTLL----RMIagleDPTSGEILIGGRDVT--DLPPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1315 RSRLSIIPQE----PTMfegTVRSNLD-PLE------EYADDQIWEALDKCQLGDEI-RK-KELkldspvsengqnwSVG 1381
Cdd:COG3839 74 DRNIAMVFQSyalyPHM---TVYENIAfPLKlrkvpkAEIDRRVREAAELLGLEDLLdRKpKQL-------------SGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1382 QRQLVCLGRVLLKRSKVLILDEATASVD----TATDTLIQETLRQhfSGCTVI----------TIAHRIssvidsdmvLL 1447
Cdd:COG3839 138 QRQRVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRR--LGTTTIyvthdqveamTLADRI---------AV 206
|
250
....*....|....*
gi 30682486 1448 LDQGLIEEHDSPARL 1462
Cdd:COG3839 207 MNDGRIQQVGTPEEL 221
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1257-1465 |
7.96e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 70.60 E-value: 7.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1257 VLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEP---AAGEIRIDGINILTIGLHDLRSRLSIIPQEP-TMFEG-T 1331
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIREKVGIVFQNPdNQFVGaT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1332 VrsnldpleeyaDDQIWEALDKCQLGdeiRKKELK-----------LDSPVSENgQNWSVGQRQLVCLGRVLLKRSKVLI 1400
Cdd:PRK13640 102 V-----------GDDVAFGLENRAVP---RPEMIKivrdvladvgmLDYIDSEP-ANLSGGQKQRVAIAGILAVEPKIII 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30682486 1401 LDEATASVDTATDTLIQETLR--QHFSGCTVITIAHRISSVIDSDMVLLLDQGLIEEHDSPARLLED 1465
Cdd:PRK13640 167 LDESTSMLDPAGKEQILKLIRklKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1241-1453 |
8.21e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 70.09 E-value: 8.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHlpMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDginilTIGLHDLR--SRL 1318
Cdd:PRK11247 13 LLLNAVSKRYGER--TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-----TAPLAEARedTRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1319 siipqeptMFEgtvRSNLDPLEEYAD-----------DQIWEALDKCQLGDeiRKKELkldsPVSENGqnwsvGQRQLVC 1387
Cdd:PRK11247 86 --------MFQ---DARLLPWKKVIDnvglglkgqwrDAALQALAAVGLAD--RANEW----PAALSG-----GQKQRVA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30682486 1388 LGRVLLKRSKVLILDEATASVDTAT----DTLIQETLRQHfsGCTVITIAHRIS-SVIDSDMVLLLDQGLI 1453
Cdd:PRK11247 144 LARALIHRPGLLLLDEPLGALDALTriemQDLIESLWQQH--GFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
915-1164 |
9.09e-13 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the 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 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. 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 by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. 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: 349996 [Multi-domain] Cd Length: 292 Bit Score: 70.53 E-value: 9.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 915 LAYGGALVPIILVVQILFQVLNIGSNYWMAWVTPVskdvkplvsgsTLILVYVFlataSSFCILVRAMLSAMTGFKIATE 994
Cdd:cd18552 9 ILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPL-----------AIIGLFLL----RGLASYLQTYLMAYVGQRVVRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 995 LFNQMHFRIFRASMSFFDATPIGRILNRASTDQSAVDLRLPSQFSNLAIAAVNILGIIGVMGQVAWQ---VLIVFIPVIA 1071
Cdd:cd18552 74 LRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKltlIALVVLPLAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1072 ACTWY-----RQYyisAARELARLSGISrsplvQHFSETLSGITTIRSFDQEPRFRTDIMRLNDCYSRLRFHAISAMEWL 1146
Cdd:cd18552 154 LPIRRigkrlRKI---SRRSQESMGDLT-----SVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALS 225
|
250
....*....|....*...
gi 30682486 1147 CFRLDLLSTVAFALSLVI 1164
Cdd:cd18552 226 SPLMELLGAIAIALVLWY 243
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
749-835 |
1.02e-12 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 69.73 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHtGSHLFKEVL--LGLLRNKTVIYVTHQLEFLPEA-DLILVMKDGRI 825
Cdd:COG1119 143 LSQGEQRRVLIARALVKDPELLILDEPTAGLDLG-ARELLLALLdkLAAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRV 221
|
90
....*....|
gi 30682486 826 TQAGKYNEIL 835
Cdd:COG1119 222 VAAGPKEEVL 231
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
921-1143 |
1.06e-12 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes 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. 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 the chemical 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. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. 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: 350007 [Multi-domain] Cd Length: 296 Bit Score: 70.62 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 921 LVPIILVVQILFQVLNI---GSNYWMAWVtpvskdvkplvsgstLILVYVFLATASSFCILVRAMLSAMTGFKIATELFN 997
Cdd:cd18563 16 LVPPYLTKILIDDVLIQlgpGGNTSLLLL---------------LVLGLAGAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 998 QMHFRIFRASMSFFDATPIGRILNRASTDQSAVDLRLPSQFSNLAIAAVNILGIIGVMGQVAWQV-LIVFIPV--IAACT 1074
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLaLLVLIPVplVVWGS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30682486 1075 WY-----RQYYISAARELARLSGisrsplvqHFSETLSGITTIRSFDQEP----RFRTDIMRLndCYSRLRFHAISAM 1143
Cdd:cd18563 161 YFfwkkiRRLFHRQWRRWSRLNS--------VLNDTLPGIRVVKAFGQEKreikRFDEANQEL--LDANIRAEKLWAT 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1256-1446 |
1.07e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.39 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1256 MVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINI--LTIGL-HDLrsRLSIIPQEPTMFEG-T 1331
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCarLTPAKaHQL--GIYLVPQEPLLFPNlS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1332 VRSN-LDPLEEYADD-QIWEALDKcQLGdeirkKELKLDSPVSengqNWSVGQRQLVCLGRVLLKRSKVLILDEATASVD 1409
Cdd:PRK15439 103 VKENiLFGLPKRQASmQKMKQLLA-ALG-----CQLDLDSSAG----SLEVADRQIVEILRGLMRDSRILILDEPTASLT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 30682486 1410 TA-TDTLIQE--TLRQHFSGCTVIT--------IAHRISSVIDSDMVL 1446
Cdd:PRK15439 173 PAeTERLFSRirELLAQGVGIVFIShklpeirqLADRISVMRDGTIAL 220
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1241-1477 |
1.11e-12 |
|
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: 69.19 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHLpmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHdlRSRLSI 1320
Cdd:cd03300 1 IELENVSKFYGGFV--ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1321 IPQEPTMFEG-TVRSNLD-PL------EEYADDQIWEALDKCQLGDEIRKKELKLdspvsengqnwSVGQRQLVCLGRVL 1392
Cdd:cd03300 77 VFQNYALFPHlTVFENIAfGLrlkklpKAEIKERVAEALDLVQLEGYANRKPSQL-----------SGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1393 LKRSKVLILDEATASVDTATDTLIQETLR--QHFSGCTVITIAHRISSVID-SDMVLLLDQGLIEEHDSPARLLEDKSSS 1469
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQLELKrlQKELGITFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEIYEEPANR 225
|
....*...
gi 30682486 1470 FsklVAEY 1477
Cdd:cd03300 226 F---VADF 230
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
690-777 |
1.13e-12 |
|
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: 66.90 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 690 AYIAQSPWIQSGK-VEENILFGKPMQ---REWYQRVLEAcSLNKdLEVFPFRDqTVIGERGINLSGGQKQRIQIARALYQ 765
Cdd:pfam00005 62 GYVFQDPQLFPRLtVRENLRLGLLLKglsKREKDARAEE-ALEK-LGLGDLAD-RPVGERPGTLSGGQRQRVAIARALLT 138
|
90
....*....|..
gi 30682486 766 DADIYLFDDPFS 777
Cdd:pfam00005 139 KPKLLLLDEPTA 150
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1257-1466 |
1.16e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.54 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1257 VLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDlRSRLSI--IPQEPTMFEG-TVR 1333
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA-RARRGIgyLPQEASIFRRlSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1334 SNLDPLEEYADDqiweaLDKCQLGDeiRKKELKLDSPVSE----NGQNWSVGQRQLVCLGRVLLKRSKVLILDEATASVD 1409
Cdd:PRK10895 97 DNLMAVLQIRDD-----LSAEQRED--RANELMEEFHIEHlrdsMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1410 TATDTLIQETLrQHF--SGCTVITIAHRISSVID-SDMVLLLDQGLIEEHDSPARLLEDK 1466
Cdd:PRK10895 170 PISVIDIKRII-EHLrdSGLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1258-1456 |
1.21e-12 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 70.88 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1258 LRGLTCTFRGGLKT-----------------GIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTI---GLHDLRSR 1317
Cdd:COG1135 4 LENLSKTFPTKGGPvtalddvsltiekgeifGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALserELRAARRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1318 LSIIPQEPTMFEG-TVRSNLD-PLEeyaddqIWEaLDKcqlgDEIRKK--EL--------KLDSPVSEngqnWSVGQRQL 1385
Cdd:COG1135 84 IGMIFQHFNLLSSrTVAENVAlPLE------IAG-VPK----AEIRKRvaELlelvglsdKADAYPSQ----LSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30682486 1386 VCLGRVLLKRSKVLILDEATASVDTATdT-----LIQEtLRQHFsGCTVITIAHRIsSVIDS--DMVLLLDQGLIEEH 1456
Cdd:COG1135 149 VGIARALANNPKVLLCDEATSALDPET-TrsildLLKD-INREL-GLTIVLITHEM-DVVRRicDRVAVLENGRIVEQ 222
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
922-1160 |
1.31e-12 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the 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 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. 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. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. 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: 349989 [Multi-domain] Cd Length: 293 Bit Score: 70.19 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 922 VPIILVVQILFQVLNIGSNYWMAWVT---PVSKDVKPLVsgsTLILVYVFLATASSFCILVRAMLSAMTG----FKIATE 994
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPYLIKIAIdeyIPNGDLSGLL---IIALLFLALNLVNWVASRLRIYLMAKVGqrilYDLRQD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 995 LFNQMHfrifRASMSFFDATPIGRILNRASTDQSAV-DLrLPSQFSNLAIAAVNILGIIGVMGQVAWQ---VLIVFIPVI 1070
Cdd:cd18545 79 LFSHLQ----KLSFSFFDSRPVGKILSRVINDVNSLsDL-LSNGLINLIPDLLTLVGIVIIMFSLNVRlalVTLAVLPLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1071 AACTWYRQYYisaARELARLSGISRSPLVQHFSETLSGITTIRSFDQEPRFRTDIMRLNDCYSRLRFHAISAMEWLCFRL 1150
Cdd:cd18545 154 VLVVFLLRRR---ARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLV 230
|
250
....*....|
gi 30682486 1151 DLLSTVAFAL 1160
Cdd:cd18545 231 ELISALGTAL 240
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
749-837 |
1.37e-12 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 69.25 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAhtgsHLFKEVlLGLLRN-----KTVIYVTHQLEFLPE-ADLILVMKD 822
Cdd:COG1126 137 LSGGQQQRVAIARALAMEPKVMLFDEPTSALDP----ELVGEV-LDVMRDlakegMTMVVVTHEMGFAREvADRVVFMDG 211
|
90
....*....|....*
gi 30682486 823 GRITQAGKYNEILES 837
Cdd:COG1126 212 GRIVEEGPPEEFFEN 226
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1253-1492 |
1.39e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 73.02 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1253 HLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGiniltiglhdlrsRLSIIPQEPTMFEGTV 1332
Cdd:TIGR01271 437 YVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1333 RSNLDPLEEYADDQIWEALDKCQLGDEIRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTAT 1412
Cdd:TIGR01271 504 KDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1413 DTLIQET-LRQHFSGCTVITIAHRISSVIDSDMVLLLDQGLIEEHDSPARLLEDKSSSFSKLVAEYTASSDSRFKRSSMK 1491
Cdd:TIGR01271 584 EKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLLGLEAFDNFSAERRNSIL 663
|
.
gi 30682486 1492 T 1492
Cdd:TIGR01271 664 T 664
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1241-1434 |
1.42e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 70.22 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHLpmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHdLRSRLSI 1320
Cdd:PRK13537 8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH-ARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1321 IPQ----EPTMfegTVRSNLDPLEEYADDQIWEALDKCQLGDEIRKKELKLDSPVSEngqnWSVGQRQLVCLGRVLLKRS 1396
Cdd:PRK13537 85 VPQfdnlDPDF---TVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALVNDP 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 30682486 1397 KVLILDEATASVDTATDTLIQETLRQHF-SGCTVITIAH 1434
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTH 196
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1258-1467 |
1.78e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 69.81 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1258 LRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIG----LHDLRSRLSIIPQ--EPTMFEGT 1331
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRPVRKRIGMVFQfpESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1332 VRS-----------NLDPLEEYADDQIwealdkCQLGDEirkKELKLDSPVSENGqnwsvGQRQLVCLGRVLLKRSKVLI 1400
Cdd:PRK13646 103 VEReiifgpknfkmNLDEVKNYAHRLL------MDLGFS---RDVMSQSPFQMSG-----GQMRKIAIVSILAMNPDIIV 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1401 LDEATASVDTATDTLIQETLR--QHFSGCTVITIAHRISSVID-SDMVLLLDQGLIEEHDSPARLLEDKS 1467
Cdd:PRK13646 169 LDEPTAGLDPQSKRQVMRLLKslQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKDKK 238
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1241-1466 |
1.82e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 69.03 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHLpmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSI 1320
Cdd:PRK13548 3 LEARNLSVRLGGRT--LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1321 IPQEPTM-FEGTVRS----NLDPL-EEYADDQ--IWEALDKCQLGDEIRKKELKLdspvsengqnwSVGQRQLVCLGRVL 1392
Cdd:PRK13548 81 LPQHSSLsFPFTVEEvvamGRAPHgLSRAEDDalVAAALAQVDLAHLAGRDYPQL-----------SGGEQQRVQLARVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1393 LKRS------KVLILDEATASVDTATDTLIQETLRQ--HFSGCTVITIAHrissviD-------SDMVLLLDQGLIEEHD 1457
Cdd:PRK13548 150 AQLWepdgppRWLLLDEPTSALDLAHQHHVLRLARQlaHERGLAVIVVLH------DlnlaaryADRIVLLHQGRLVADG 223
|
....*....
gi 30682486 1458 SPARLLEDK 1466
Cdd:PRK13548 224 TPAEVLTPE 232
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
703-834 |
1.89e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 70.26 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 703 VEENILFG-------KPMQREWYQRVLEACSLNKD-LEVFPFrdqtvigergiNLSGGQKQRIQIARALYQDADIYLFDD 774
Cdd:PRK13631 134 IEKDIMFGpvalgvkKSEAKKLAKFYLNKMGLDDSyLERSPF-----------GLSGGQKRRVAIAGILAIQPEILIFDE 202
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30682486 775 PFSAVDAHTGSHLFKEVLLGLLRNKTVIYVTHQLEFLPE-ADLILVMKDGRITQAGKYNEI 834
Cdd:PRK13631 203 PTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEI 263
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1271-1468 |
2.27e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 69.01 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1271 TGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSIIPQEP-TMFEGTV---------RSNLDPLE 1340
Cdd:PRK13648 38 TSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPdNQFVGSIvkydvafglENHAVPYD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1341 EYADdQIWEALDKCQLgdeirkkelkLDSPVSENgQNWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTATD----TLI 1416
Cdd:PRK13648 118 EMHR-RVSEALKQVDM----------LERADYEP-NALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARqnllDLV 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 30682486 1417 QETLRQHfsGCTVITIAHRISSVIDSDMVLLLDQGLIEEHDSPARLLEDKSS 1468
Cdd:PRK13648 186 RKVKSEH--NITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEE 235
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
749-859 |
2.34e-12 |
|
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: 68.68 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHlfkevLLGLL------RNKTVIYVTHQL---EFLpeADLILV 819
Cdd:COG1124 139 LSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAE-----ILNLLkdlreeRGLTYLFVSHDLavvAHL--CDRVAV 211
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 30682486 820 MKDGRITqagkynEILESGTDFMELVGAHTDAL-AAVDSYE 859
Cdd:COG1124 212 MQNGRIV------EELTVADLLAGPKHPYTRELlAASLAFE 246
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1253-1451 |
2.74e-12 |
|
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: 69.12 E-value: 2.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1253 HLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGiniltiglhdlrsRLSIIPQEPTMFEGTV 1332
Cdd:cd03291 48 VGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1333 RSNLDPLEEYADDQIWEALDKCQLGDEIRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTAT 1412
Cdd:cd03291 115 KENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 30682486 1413 DTLIQET-LRQHFSGCTVITIAHRISSVIDSDMVLLLDQG 1451
Cdd:cd03291 195 EKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1261-1463 |
2.85e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 68.66 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1261 LTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGiNILTIGLHDLRS-RLSIIPQEPT-----------MF 1328
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD-HPLHFGDYSYRSqRIRMIFQDPStslnprqrisqIL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1329 EGTVRSNLDPLEEYADDQIWEALDKCQLgdeirkkelkLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVLILDEATASV 1408
Cdd:PRK15112 111 DFPLRLNTDLEPEQREKQIIETLRQVGL----------LPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 30682486 1409 DTATDT-LIQETLR-QHFSGCTVITIAHRISSVID-SDMVLLLDQGLIEEHDSPARLL 1463
Cdd:PRK15112 181 DMSMRSqLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
749-830 |
2.85e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 70.06 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTG-------SHLFKEVllgllrNKTVIYVTH-QLEFLPEADLILVM 820
Cdd:PRK11000 134 LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRvqmrieiSRLHKRL------GRTMIYVTHdQVEAMTLADKIVVL 207
|
90
....*....|
gi 30682486 821 KDGRITQAGK 830
Cdd:PRK11000 208 DAGRVAQVGK 217
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
749-830 |
4.23e-12 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 67.19 E-value: 4.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAhtgshLFKEVLLGLL------RNKTVIYVTHQLEFLPE-ADLILVMK 821
Cdd:TIGR01277 129 LSGGQRQRVALARCLVRPNPILLLDEPFSALDP-----LLREEMLALVkqlcseRQRTLLMVTHHLSDARAiASQIAVVS 203
|
....*....
gi 30682486 822 DGRITQAGK 830
Cdd:TIGR01277 204 QGKIKVVSD 212
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1257-1484 |
4.24e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 71.35 E-value: 4.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1257 VLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDginiltiglhdlRSrLSIIPQEPTMFEGTVRSNL 1336
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE------------RS-IAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1337 DPLEEYADDQIWEALDKCQLGDEIRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLI 1416
Cdd:PTZ00243 742 LFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERV 821
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30682486 1417 -QETLRQHFSGCTVITIAHRISSVIDSDMVLLLDQGLIEEHDSPARLLEdkSSSFSKLVAEYTASSDSR 1484
Cdd:PTZ00243 822 vEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR--TSLYATLAAELKENKDSK 888
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
749-846 |
4.55e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 69.34 E-value: 4.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAhtgsHLFKEvLLGLLRNK------TVIYVTH-QLEFLPEADLILVMK 821
Cdd:PRK10851 137 LSGGQKQRVALARALAVEPQILLLDEPFGALDA----QVRKE-LRRWLRQLheelkfTSVFVTHdQEEAMEVADRVVVMS 211
|
90 100
....*....|....*....|....*..
gi 30682486 822 DGRITQAGKYNEIL-ESGTDF-MELVG 846
Cdd:PRK10851 212 QGNIEQAGTPDQVWrEPATRFvLEFMG 238
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1241-1466 |
4.93e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 68.22 E-value: 4.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRY--GPHlpmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRL 1318
Cdd:PRK13647 5 IEVEDLHFRYkdGTK---ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1319 SIIPQEP-------TMFE----GTVRSNLDPLEeyADDQIWEALDKcqlgdeIRKKELKLDSPvsengQNWSVGQRQLVC 1387
Cdd:PRK13647 82 GLVFQDPddqvfssTVWDdvafGPVNMGLDKDE--VERRVEEALKA------VRMWDFRDKPP-----YHLSYGQKKRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1388 LGRVLLKRSKVLILDEATASVDTATDTLIQETL-RQHFSGCTVITIAHRISSVID-SDMVLLLDQGLIEEHDSPARLLED 1465
Cdd:PRK13647 149 IAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILdRLHNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDE 228
|
.
gi 30682486 1466 K 1466
Cdd:PRK13647 229 D 229
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1241-1476 |
5.28e-12 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 68.97 E-value: 5.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHLpmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTL--FriVEPAAGEIRIDGINILTIGLHDlRsRL 1318
Cdd:COG3842 6 LELENVSKRYGDVT--ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIagF--ETPDSGRILLDGRDVTGLPPEK-R-NV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1319 SIIPQE----PTMfegTVRSNLD-PLE------EYADDQIWEALDKCQLGD-EIRK-KELkldspvsengqnwSVGQRQL 1385
Cdd:COG3842 80 GMVFQDyalfPHL---TVAENVAfGLRmrgvpkAEIRARVAELLELVGLEGlADRYpHQL-------------SGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1386 VCLGRVLLKRSKVLILDEATASVDTAT-DTLIQETLR-QHFSGCTVITIAHrissviD-------SDMVLLLDQGLIEEH 1456
Cdd:COG3842 144 VALARALAPEPRVLLLDEPLSALDAKLrEEMREELRRlQRELGITFIYVTH------DqeealalADRIAVMNDGRIEQV 217
|
250 260
....*....|....*....|
gi 30682486 1457 DSPARLLEDKSSSFsklVAE 1476
Cdd:COG3842 218 GTPEEIYERPATRF---VAD 234
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
623-829 |
5.69e-12 |
|
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: 66.67 E-value: 5.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 623 DVEVSNGAFSWDDSSPiPTLKDIRFKIPHGMNIAICGTVGSGKSSLLSSILGEVPKISGNLKVCG-------------RK 689
Cdd:cd03369 6 EIEVENLSVRYAPDLP-PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 690 AYIAQSPWIQSGKVEENI-LFGKPMQREWYQrVLEacslnkdlevfpfrdqtvIGERGINLSGGQKQRIQIARALYQDAD 768
Cdd:cd03369 85 TIIPQDPTLFSGTIRSNLdPFDEYSDEEIYG-ALR------------------VSEGGLNLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30682486 769 IYLFDDPFSAVDAHTgSHLFKEVLLGLLRNKTVIYVTHQLEFLPEADLILVMKDGRITQAG 829
Cdd:cd03369 146 VLVLDEATASIDYAT-DALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
749-835 |
6.26e-12 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 67.09 E-value: 6.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVD-AhtgshLFKEvLLGLL------RNKTVIYVTHQLE-FLPEADLILVM 820
Cdd:COG3840 130 LSGGQRQRVALARCLVRKRPILLLDEPFSALDpA-----LRQE-MLDLVdelcreRGLTVLMVTHDPEdAARIADRVLLV 203
|
90
....*....|....*
gi 30682486 821 KDGRITQAGKYNEIL 835
Cdd:COG3840 204 ADGRIAADGPTAALL 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1272-1409 |
6.60e-12 |
|
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: 70.10 E-value: 6.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1272 GIVGRTGCGKSTLIQTLFRIVePAAGEIRIDGINILTIG---LHDLRSRLSIIPQEPtmF--------------EG--TV 1332
Cdd:COG4172 316 GLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--FgslsprmtvgqiiaEGlrVH 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1333 RSNLDPLEEyaDDQIWEALDKCQLGDEIRKK---ELkldspvsengqnwSVGQRQLVCLGRVLLKRSKVLILDEATASVD 1409
Cdd:COG4172 393 GPGLSAAER--RARVAEALEEVGLDPAARHRyphEF-------------SGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
961-1164 |
6.89e-12 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the 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 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. 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. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. 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: 349987 [Multi-domain] Cd Length: 291 Bit Score: 67.89 E-value: 6.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 961 TLILVYVFLATASSFCILVRAMLSAMTGFKIATELFNQMHFRIFRASMSFFDATPIGRILNRASTDQSAVDlRLPSQFSN 1040
Cdd:cd18543 40 PLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQ-RFLAFGPF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1041 LAIAAVNILGIIGVMGQVAWQ----VLIVFIPVIAACTWYRQYYISAARELARLSGIsrspLVQHFSETLSGITTIRSFD 1116
Cdd:cd18543 119 LLGNLLTLVVGLVVMLVLSPPlalvALASLPPLVLVARRFRRRYFPASRRAQDQAGD----LATVVEESVTGIRVVKAFG 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 30682486 1117 QEP----RFRTDIMRLNDcySRLRfhAISAMEWLCFRLDLLSTVAFALSLVI 1164
Cdd:cd18543 195 RERreldRFEAAARRLRA--TRLR--AARLRARFWPLLEALPELGLAAVLAL 242
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
961-1142 |
7.01e-12 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the 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 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. 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 by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. 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: 349991 [Multi-domain] Cd Length: 298 Bit Score: 68.20 E-value: 7.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 961 TLILVYVFLATASSFCILVRAMLSAMTGFKIATELFNQMHfrifRASMSFFDATPIGRILNRASTDQSAVDLRLPSQFSN 1040
Cdd:cd18547 50 LLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQ----RLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1041 LAIAAVNILGIIGVMGQVAWQ---VLIVFIPVIAACTWY-----RQYYISAARELARLSGisrsplvqHFSETLSGITTI 1112
Cdd:cd18547 126 LISSILTIVGTLIMMLYISPLltlIVLVTVPLSLLVTKFiakrsQKYFRKQQKALGELNG--------YIEEMISGQKVV 197
|
170 180 190
....*....|....*....|....*....|
gi 30682486 1113 RSFDQEPRFRTDIMRLNDcysRLRFHAISA 1142
Cdd:cd18547 198 KAFNREEEAIEEFDEINE---ELYKASFKA 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
748-829 |
8.03e-12 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 68.57 E-value: 8.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 748 NLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGshlfKEVlLGLLR--NK----TVIYVTHQLEFLPE-ADLILVM 820
Cdd:COG1135 140 QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETT----RSI-LDLLKdiNRelglTIVLITHEMDVVRRiCDRVAVL 214
|
....*....
gi 30682486 821 KDGRITQAG 829
Cdd:COG1135 215 ENGRIVEQG 223
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1241-1451 |
8.04e-12 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 67.03 E-value: 8.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHLpmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAG-EIRIDGINILTIGLHDLRSRLS 1319
Cdd:COG1119 4 LELRNVTVRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1320 I--------IPQEPTMFEgTVRS----NLDPLEEYADDQI---WEALDkcQLG-DEIRKKELkldspvsengQNWSVGQR 1383
Cdd:COG1119 82 LvspalqlrFPRDETVLD-VVLSgffdSIGLYREPTDEQReraRELLE--LLGlAHLADRPF----------GTLSQGEQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30682486 1384 QLVCLGRVLLKRSKVLILDEATASVD-TATDTLIQ--ETLRQHfSGCTVITIAHRISSVIDS-DMVLLLDQG 1451
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDlGARELLLAllDKLAAE-GAPTLVLVTHHVEEIPPGiTHVLLLKDG 219
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1257-1455 |
8.47e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 66.99 E-value: 8.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1257 VLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRID------GINILTIGLHDLRSRLSIIPQEPTMFEG 1330
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDgkvlyfGKDIFQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1331 -TVRSNLD-PLEEYADDQ-------IWEALDKCQLGDEIRKkelKLDSPVSEngqnWSVGQRQLVCLGRVLLKRSKVLIL 1401
Cdd:PRK14246 105 lSIYDNIAyPLKSHGIKEkreikkiVEECLRKVGLWKEVYD---RLNSPASQ----LSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 30682486 1402 DEATASVDTATDTLIQETLRQHFSGCTVITIAHRISSVID-SDMVLLLDQGLIEE 1455
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVE 232
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
309-598 |
9.61e-12 |
|
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: 67.58 E-value: 9.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 309 ILLSTLFAFVYTVSCYVAPYLMDTFVQYLNGQRQYS--NQGVVLVTTFFVAKLVeCQARRNWYFRlqKAGIGMRSVLVSM 386
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSllLWIALLLLLLALLRAL-LSYLRRYLAA--RLGQRVVFDLRRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 387 IYEKGLTLPCYSKQGHTSGEIINLMTVDAERISAF-SWYMHDPWILVLQISLALLIL-YRSLGLgSIAAFAATFLVMLGN 464
Cdd:cd07346 78 LFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLvSSGLLQLLSDVLTLIGALVILfYLNWKL-TLVALLLLPLYVLIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 465 IPLAKLEEKFQGNLMESKDNRMKKTSEALLNMRILKLQGWEMKFLHKILDLrgieAGWLKKFVYNSAAISSVLWAAPSFV 544
Cdd:cd07346 157 RYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREA----NRDLRDANLRAARLSALFSPLIGLL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 545 SATA------FGACMLLKIPLESGKIIAALATFRILQTPIYKLPDTISMIVQTKVSLDRI 598
Cdd:cd07346 233 TALGtalvllYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
963-1192 |
1.26e-11 |
|
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: 67.18 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 963 ILVYVFLATASSFCILVRAMLSAMTGFKIATELFNQMHFRIFRASMSFFDATPIGRILNRASTDQSAVDLRLPSQFSNLA 1042
Cdd:cd18572 39 VLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1043 IAAVNILGIIGVMGQVAWQ----VLIVFIPVIAACTWYRQYYISAARE----LARLSGISRsplvqhfsETLSGITTIRS 1114
Cdd:cd18572 119 RNLVQLVGGLAFMFSLSWRltllAFITVPVIALITKVYGRYYRKLSKEiqdaLAEANQVAE--------EALSNIRTVRS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1115 FDQEP----RFRTdimRLNDCYSRLRFHAI--SAMEWLCFRLDLLSTVafALSLVILVSVPEGVINpsfAGLAVTYALNL 1188
Cdd:cd18572 191 FATEErearRYER---ALDKALKLSVRQALayAGYVAVNTLLQNGTQV--LVLFYGGHLVLSGRMS---AGQLVTFMLYQ 262
|
....
gi 30682486 1189 NSLQ 1192
Cdd:cd18572 263 QQLG 266
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
749-827 |
1.98e-11 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 66.04 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLfKEVLLGLLR--NKTVIYVTHQLE---FLpeADLILVMKD- 822
Cdd:COG4525 135 LSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQM-QELLLDVWQrtGKGVFLITHSVEealFL--ATRLVVMSPg 211
|
....*.
gi 30682486 823 -GRITQ 827
Cdd:COG4525 212 pGRIVE 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1245-1434 |
2.19e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.17 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1245 NLQVRYGPHLpmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGiniltiGLhdlrsRLSIIPQE 1324
Cdd:COG0488 3 NLSKSFGGRP--LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK------GL-----RIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1325 PTMFEG-TVRSNL-------------------------DPLEEYADDQ-IWEALDKCQLGDEIRK-------KELKLDSP 1370
Cdd:COG0488 70 PPLDDDlTVLDTVldgdaelraleaeleeleaklaepdEDLERLAELQeEFEALGGWEAEARAEEilsglgfPEEDLDRP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30682486 1371 VSEngqnWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLRQhFSGcTVITIAH 1434
Cdd:COG0488 150 VSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKN-YPG-TVLVVSH 207
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
749-844 |
2.35e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 66.19 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgshlfKEVLLGLLR------NKTVIYVTHQLEFLPEADLILVMKD 822
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRG-----RREVLETVRqlkeqkGITVLSITHDLDEAAQADRVIVMNK 215
|
90 100
....*....|....*....|..
gi 30682486 823 GRITQAGKYNEILESGTDFMEL 844
Cdd:PRK13635 216 GEILEEGTPEEIFKSGHMLQEI 237
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
749-852 |
2.84e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 66.37 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHtGSHLFKEVLLGLL-RNKTVIYVTHqleFLPEA----DLILVMKDG 823
Cdd:PRK13537 139 LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ-ARHLMWERLRSLLaRGKTILLTTH---FMEEAerlcDRLCVIEEG 214
|
90 100 110
....*....|....*....|....*....|.
gi 30682486 824 RITQAGKYNEILES--GTDFMELVGAHTDAL 852
Cdd:PRK13537 215 RKIAEGAPHALIESeiGCDVIEIYGPDPVAL 245
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1245-1464 |
3.09e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 65.57 E-value: 3.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1245 NLQVRYGPHLpmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVE-----PAAGEIRIDGINILTIGLH--DLRSR 1317
Cdd:PRK14243 15 NLNVYYGSFL--AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYAPDVDpvEVRRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1318 LSIIPQEPTMFEGTVRSNL------DPLEEYADDQIWEALDKCQLGDEIRKKelkldspVSENGQNWSVGQRQLVCLGRV 1391
Cdd:PRK14243 93 IGMVFQKPNPFPKSIYDNIaygariNGYKGDMDELVERSLRQAALWDEVKDK-------LKQSGLSLSGGQQQRLCIARA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30682486 1392 LLKRSKVLILDEATASVDTATDTLIQETLRQHFSGCTVITIAHRISSVID-SDMVLLLDQGLIEEHDSPARLLE 1464
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARvSDMTAFFNVELTEGGGRYGYLVE 239
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
680-826 |
3.12e-11 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 64.20 E-value: 3.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 680 SGNLKVCGRKA----------YIAQSPWIQ--SGKVEENILFGKPMQREWYQR---VLEACSLNKDLEVFPFrdqtvige 744
Cdd:cd03226 54 SGSILLNGKPIkakerrksigYVMQDVDYQlfTDSVREELLLGLKELDAGNEQaetVLKDLDLYALKERHPL-------- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 745 rgiNLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTG---SHLFKEVllgLLRNKTVIYVTHQLEFLPE-ADLILVM 820
Cdd:cd03226 126 ---SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMervGELIREL---AAQGKAVIVITHDYEFLAKvCDRVLLL 199
|
....*.
gi 30682486 821 KDGRIT 826
Cdd:cd03226 200 ANGAIV 205
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
702-838 |
3.57e-11 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 66.67 E-value: 3.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 702 KVEENILFGK-----PMQREWYQRVLEACSLNKDLEVFPFRdqtvigerginLSGGQKQRIQIARALYQDADIYLFDDPF 776
Cdd:TIGR02142 91 SVRGNLRYGMkrarpSERRISFERVIELLGIGHLLGRLPGR-----------LSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30682486 777 SAVDahtgSHLFKEVLLGLLR-----NKTVIYVTHQL-EFLPEADLILVMKDGRITQAGKYNEILESG 838
Cdd:TIGR02142 160 AALD----DPRKYEILPYLERlhaefGIPILYVSHSLqEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
635-848 |
4.09e-11 |
|
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: 65.32 E-value: 4.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 635 DSSPIPTLKDIRFKIPHGMNIAICGTVGSGKSSLLSSILGEVPKISGNLKVCG-------------RKAYIAQSPWIQSG 701
Cdd:cd03288 30 ENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtlrsRLSIILQDPILFSG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 702 KVEENILFGKPMQREWYQRVLEACSLNKDLEVFPFRDQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDA 781
Cdd:cd03288 110 SIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDM 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30682486 782 HTgSHLFKEVLLGLLRNKTVIYVTHQLEFLPEADLILVMKDGRITQAGKYNEIL-ESGTDFMELVGAH 848
Cdd:cd03288 190 AT-ENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLVRTD 256
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1240-1470 |
4.54e-11 |
|
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: 64.67 E-value: 4.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1240 EITICNLQVRYGPHlpMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGiniLTIGLHDLRSR-L 1318
Cdd:cd03296 2 SIEVRNVSKRFGDF--VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG---EDATDVPVQERnV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1319 SIIPQEPTMFEG-TVRSNLD-PLEEyadDQIWEALDKcqlgDEIRKK--EL----KLDSPVSENGQNWSVGQRQLVCLGR 1390
Cdd:cd03296 77 GFVFQHYALFRHmTVFDNVAfGLRV---KPRSERPPE----AEIRAKvhELlklvQLDWLADRYPAQLSGGQRQRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1391 VLLKRSKVLILDEATASVDTATDTLIQETLRQ--HFSGCTVITIAHRISSVID-SDMVLLLDQGLIEEHDSPARLLEDKS 1467
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLRRlhDELHVTTVFVTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYDHPA 229
|
...
gi 30682486 1468 SSF 1470
Cdd:cd03296 230 SPF 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
703-825 |
4.73e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 66.97 E-value: 4.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 703 VEENILFGKPM----------QREWYQRVLEACSLNKDLEvfpfrdqTVIGErginLSGGQKQRIQIARALYQDADIYLF 772
Cdd:COG1129 96 VAENIFLGREPrrgglidwraMRRRARELLARLGLDIDPD-------TPVGD----LSVAQQQLVEIARALSRDARVLIL 164
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 30682486 773 DDPFSAVDAHTGSHLFKevLLGLLRNK--TVIYVTHqleFLPE----ADLILVMKDGRI 825
Cdd:COG1129 165 DEPTASLTEREVERLFR--IIRRLKAQgvAIIYISH---RLDEvfeiADRVTVLRDGRL 218
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
749-829 |
5.75e-11 |
|
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: 63.84 E-value: 5.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAhTGSHLFKEVLLGLLRN-KTVIYVTHQLEFLPE-ADLILVMKDGRIT 826
Cdd:cd03269 129 LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VNVELLKDVIRELARAgKTVILSTHQMELVEElCDRVLLLNKGRAV 207
|
...
gi 30682486 827 QAG 829
Cdd:cd03269 208 LYG 210
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
719-836 |
5.97e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 66.02 E-value: 5.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 719 QRVLEACslnKDLEVFPFRDQtvigeRGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEvLLGLLR- 797
Cdd:PRK11650 113 ERVAEAA---RILELEPLLDR-----KPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLE-IQRLHRr 183
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 30682486 798 -NKTVIYVTH-QLEFLPEADLILVMKDGRITQAGKYNEILE 836
Cdd:PRK11650 184 lKTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVEVYE 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
749-829 |
6.17e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 64.39 E-value: 6.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDahtgSHLFKEVlLGLLR-----NKTVIYVTHQLEFLPE-ADLILVMKD 822
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALD----PELVGEV-LNTIRqlaqeKRTMVIVTHEMSFARDvADRAIFMDQ 219
|
....*..
gi 30682486 823 GRITQAG 829
Cdd:PRK11264 220 GRIVEQG 226
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1248-1455 |
7.01e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 64.71 E-value: 7.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1248 VRYGPHLpMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILT------------------- 1308
Cdd:PRK10419 19 SGKHQHQ-TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnraqrkafrrdiqmvfqd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1309 -IGLHDLRSRLSIIPQEPtmfegtVR--SNLDPLEEYAddQIWEALDKCQLGDEIRKKElkldsPvsengQNWSVGQRQL 1385
Cdd:PRK10419 98 sISAVNPRKTVREIIREP------LRhlLSLDKAERLA--RASEMLRAVDLDDSVLDKR-----P-----PQLSGGQLQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1386 VCLGRVLLKRSKVLILDEATASVDTATDT-LIQ--ETLRQHF-SGCTVIT--------IAHRissvidsdmVLLLDQGLI 1453
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLVLQAgVIRllKKLQQQFgTACLFIThdlrlverFCQR---------VMVMDNGQI 230
|
..
gi 30682486 1454 EE 1455
Cdd:PRK10419 231 VE 232
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1257-1423 |
7.06e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 63.35 E-value: 7.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1257 VLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINiltIGLHDLRSRLSII----PQEPTMfegTV 1332
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD---IDDPDVAEACHYLghrnAMKPAL---TV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1333 RSNLDPLEEY---ADDQIWEALDKCQLGD--EIRKKELkldspvsengqnwSVGQRQLVCLGRVLLKRSKVLILDEATAS 1407
Cdd:PRK13539 91 AENLEFWAAFlggEELDIAAALEAVGLAPlaHLPFGYL-------------SAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170
....*....|....*.
gi 30682486 1408 VDTATDTLIQETLRQH 1423
Cdd:PRK13539 158 LDAAAVALFAELIRAH 173
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
749-829 |
7.24e-11 |
|
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: 63.28 E-value: 7.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgSHLFKEVLLGLLRNK--TVIYVTHQLE-FLPEADLILVMKDGRI 825
Cdd:cd03298 129 LSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL-RAEMLDLVLDLHAETkmTVLMVTHQPEdAKRLAQRVVFLDNGRI 207
|
....
gi 30682486 826 TQAG 829
Cdd:cd03298 208 AAQG 211
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
703-843 |
7.46e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 65.11 E-value: 7.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 703 VEENILFGkPM-----QREWYQR---VLEACSLNKD-LEVFPFrdqtvigergiNLSGGQKQRIQIARALYQDADIYLFD 773
Cdd:PRK13651 123 IEKDIIFG-PVsmgvsKEEAKKRaakYIELVGLDESyLQRSPF-----------ELSGGQKRRVALAGILAMEPDFLVFD 190
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30682486 774 DPFSAVDAHtGShlfKEVLLGL----LRNKTVIYVTHQLE-FLPEADLILVMKDGRITQAGKYNEILeSGTDFME 843
Cdd:PRK13651 191 EPTAGLDPQ-GV---KEILEIFdnlnKQGKTIILVTHDLDnVLEWTKRTIFFKDGKIIKDGDTYDIL-SDNKFLI 260
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1258-1451 |
9.86e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.11 E-value: 9.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1258 LRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRiVEPAA---GEIRIDGINILTIGLHDL-RSRLSIIPQEPTMFEG-TV 1332
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHGtyeGEIIFEGEELQASNIRDTeRAGIAIIHQELALVKElSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1333 RSNLdpleeyaddqiwealdkcQLGDEIRK-----------------KELKLDSPVSENGQNWSVGQRQLVCLGRVLLKR 1395
Cdd:PRK13549 100 LENI------------------FLGNEITPggimdydamylraqkllAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1396 SKVLILDEATASV-DTATDTL--IQETLRQHfsGCTVITIAHRISSVID-SDMVLLLDQG 1451
Cdd:PRK13549 162 ARLLILDEPTASLtESETAVLldIIRDLKAH--GIACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
749-825 |
1.05e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 66.29 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGshlfKEVL--LGLLRNK--TVIYVTHQLEFLPEADLILVMKDGR 824
Cdd:PRK10535 145 LSGGQQQRVSIARALMNGGQVILADEPTGALDSHSG----EEVMaiLHQLRDRghTVIIVTHDPQVAAQAERVIEIRDGE 220
|
.
gi 30682486 825 I 825
Cdd:PRK10535 221 I 221
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1272-1464 |
1.19e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.82 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1272 GIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINIltiglhDLRS-----RLSI--IPQEPTMFEG-TVRSNL----DPL 1339
Cdd:COG3845 35 ALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV------RIRSprdaiALGIgmVHQHFMLVPNlTVAENIvlglEPT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1340 EeyaddqiWEALDKCQLGDEIRKK------ELKLDSPVSEngqnWSVGQRQLVCLGRVLLKRSKVLILDEATAsVDT--A 1411
Cdd:COG3845 109 K-------GGRLDRKAARARIRELseryglDVDPDAKVED----LSVGEQQRVEILKALYRGARILILDEPTA-VLTpqE 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30682486 1412 TDTLIqETLRQhF--SGCTVITIAHRISSVID-SDMVLLLDQG-LIEEHD----SPARLLE 1464
Cdd:COG3845 177 ADELF-EILRR-LaaEGKSIIFITHKLREVMAiADRVTVLRRGkVVGTVDtaetSEEELAE 235
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
749-844 |
1.22e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 64.00 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgshlfKEVLLGLLR------NKTVIYVTHQLEFLPEADLILVMKD 822
Cdd:PRK13648 143 LSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA-----RQNLLDLVRkvksehNITIISITHDLSEAMEADHVIVMNK 217
|
90 100
....*....|....*....|..
gi 30682486 823 GRITQAGKYNEILESGTDFMEL 844
Cdd:PRK13648 218 GTVYKEGTPTEIFDHAEELTRI 239
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
696-827 |
1.29e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 63.57 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 696 PWIQsgkVEENILFG------KPMQREwyQRVLEAcsLNK-DLEVFpfrdqtviGERGI-NLSGGQKQRIQIARALYQDA 767
Cdd:PRK11248 83 PWRN---VQDNVAFGlqlagvEKMQRL--EIAHQM--LKKvGLEGA--------EKRYIwQLSGGQRQRVGIARALAANP 147
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30682486 768 DIYLFDDPFSAVDAHTGSHLfKEVLLGLLRN--KTVIYVTHQLE---FLPeADLILVMKD-GRITQ 827
Cdd:PRK11248 148 QLLLLDEPFGALDAFTREQM-QTLLLKLWQEtgKQVLLITHDIEeavFMA-TELVLLSPGpGRVVE 211
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1257-1457 |
1.35e-10 |
|
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: 62.94 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1257 VLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGiNI-----LTIGLH-DLRSRlsiipqEPTMFEG 1330
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVssllgLGGGFNpELTGR------ENIYLNG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1331 TVrSNLDPleEYADDQIWEALDKCQLGDEIrkkelklDSPVSengqNWSVGQRQLVCLGRVLLKRSKVLILDEATASVDT 1410
Cdd:cd03220 110 RL-LGLSR--KEIDEKIDEIIEFSELGDFI-------DLPVK----TYSSGMKARLAFAIATALEPDILLIDEVLAVGDA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 30682486 1411 ATDTLIQETLRQHFSGC-TVITIAHRISSVID-SDMVLLLDQGLIEEHD 1457
Cdd:cd03220 176 AFQEKCQRRLRELLKQGkTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
624-844 |
1.40e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 63.98 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 624 VEVSNGAFSWDDSSPIPTLKDIRFKIPHGMNIAICGTVGSGKSSLLSSILGEVPKISGNLKVCGRK-------------A 690
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLlteenvwdirhkiG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 691 YIAQSPWIQ--SGKVEENILFGKPMQ----REWYQRVLEACSLnKDLEVFPFRDQTvigergiNLSGGQKQRIQIARALY 764
Cdd:PRK13650 85 MVFQNPDNQfvGATVEDDVAFGLENKgiphEEMKERVNEALEL-VGMQDFKEREPA-------RLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 765 QDADIYLFDDPFSAVDAHTGSHLFKEVllGLLRNK---TVIYVTHQLEFLPEADLILVMKDGRITQAGKYNEILESGTDF 841
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTI--KGIRDDyqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGNDL 234
|
...
gi 30682486 842 MEL 844
Cdd:PRK13650 235 LQL 237
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1257-1453 |
1.51e-10 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 62.67 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1257 VLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAA---GEIRIDG--INIltiglHDLRSRLSIIPQEPTMFEG- 1330
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGqpRKP-----DQFQKCVAYVRQDDILLPGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1331 TVRSNL---------DPLEEYADDQIWEALDKCQLGDE-IRKKELKldspvsengqNWSVGQRQLVCLGRVLLKRSKVLI 1400
Cdd:cd03234 97 TVRETLtytailrlpRKSSDAIRKKRVEDVLLRDLALTrIGGNLVK----------GISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 30682486 1401 LDEATASVDTATDTLIQETLRQHF-SGCTVITIAHRISSVIDS--DMVLLLDQGLI 1453
Cdd:cd03234 167 LDEPTSGLDSFTALNLVSTLSQLArRNRIVILTIHQPRSDLFRlfDRILLLSSGEI 222
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
748-825 |
1.92e-10 |
|
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: 62.52 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 748 NLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFkEVLLGLLRNKTVIYVTHQLEflpEADL----ILVMKDG 823
Cdd:cd03263 133 TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIW-DLILEVRKGRSIILTTHSMD---EAEAlcdrIAIMSDG 208
|
..
gi 30682486 824 RI 825
Cdd:cd03263 209 KL 210
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1238-1434 |
1.98e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 63.08 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1238 RGEiticNLQVRYGPHlpMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSR 1317
Cdd:PRK10253 9 RGE----QLTLGYGKY--TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1318 LSIIPQEPTMFEGTVRSNLDPLEEYADDQI---WEALDKCQLGDEIRKKelKLDSPVSENGQNWSVGQRQLVCLGRVLLK 1394
Cdd:PRK10253 83 IGLLAQNATTPGDITVQELVARGRYPHQPLftrWRKEDEEAVTKAMQAT--GITHLADQSVDTLSGGQRQRAWIAMVLAQ 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 30682486 1395 RSKVLILDEATASVDTATDTLIQETLRQ--HFSGCTVITIAH 1434
Cdd:PRK10253 161 ETAIMLLDEPTTWLDISHQIDLLELLSElnREKGYTLAAVLH 202
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
642-829 |
2.84e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 62.98 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 642 LKDIRFKIPHGMNIAICGTVGSGKSSLLSSILGEVPKISGNLKVCGRK----------AYIAQSP---WIQSGKVEENIL 708
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPtrqalqknlvAYVPQSEevdWSFPVLVEDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 709 FGKPMQREWYQR-------VLEACSLNKDLEVFPFRDqtvIGErginLSGGQKQRIQIARALYQDADIYLFDDPFSAVDA 781
Cdd:PRK15056 103 MGRYGHMGWLRRakkrdrqIVTAALARVDMVEFRHRQ---IGE----LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 30682486 782 HTGSHLFKevLLGLLRN--KTVIYVTHQLEFLPEADLILVMKDGRITQAG 829
Cdd:PRK15056 176 KTEARIIS--LLRELRDegKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1258-1463 |
2.85e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 62.80 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1258 LRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSIIPQEP-TMFEG-TVRSN 1335
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPdNQFVGaTVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1336 LD--------PLEEYAdDQIWEALDKCQLGDeirkkeLKLDSPVSENGqnwsvGQRQLVCLGRVLLKRSKVLILDEATAS 1407
Cdd:PRK13642 103 VAfgmenqgiPREEMI-KRVDEALLAVNMLD------FKTREPARLSG-----GQKQRVAVAGIIALRPEIIILDESTSM 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30682486 1408 VDTATDTLIQETLRQ-----HFsgcTVITIAHRISSVIDSDMVLLLDQGLIEEHDSPARLL 1463
Cdd:PRK13642 171 LDPTGRQEIMRVIHEikekyQL---TVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1270-1465 |
2.85e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 63.45 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1270 KT-GIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINIL---TIGLHDLRSRLSIIPQEPTmfegtvrSNLDP------- 1338
Cdd:PRK11308 42 KTlAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadPEAQKLLRQKIQIVFQNPY-------GSLNPrkkvgqi 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1339 LEEYAddQIWEALDKcqlgDEIRKKELKLDSPV---SENGQNW----SVGQRQLVCLGRVLLKRSKVLILDEATasvdTA 1411
Cdd:PRK11308 115 LEEPL--LINTSLSA----AERREKALAMMAKVglrPEHYDRYphmfSGGQRQRIAIARALMLDPDVVVADEPV----SA 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30682486 1412 TDTLIQET-------LRQHFsGCTVITIAHRISSV---IDSDMVLLLdqGLIEEHDSPARLLED 1465
Cdd:PRK11308 185 LDVSVQAQvlnlmmdLQQEL-GLSYVFISHDLSVVehiADEVMVMYL--GRCVEKGTKEQIFNN 245
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
738-835 |
3.18e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 62.29 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 738 DQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDahtgSHLFKEVLLGLLR----NKTVIYVTHQLEFLPE 813
Cdd:PRK10619 142 DERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALD----PELVGEVLRIMQQlaeeGKTMVVVTHEMGFARH 217
|
90 100
....*....|....*....|...
gi 30682486 814 -ADLILVMKDGRITQAGKYNEIL 835
Cdd:PRK10619 218 vSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1255-1459 |
3.30e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 62.80 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1255 PMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIG-LHDLRSRLSIIPQEP------TM 1327
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIRNKAGMVFQNPdnqivaTI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1328 FEGTVR---SNLDPLEEYADDQIWEALDKCQLGdEIRKKELKLdspvsengqnWSVGQRQLVCLGRVLLKRSKVLILDEA 1404
Cdd:PRK13633 103 VEEDVAfgpENLGIPPEEIRERVDESLKKVGMY-EYRRHAPHL----------LSGGQKQRVAIAGILAMRPECIIFDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 30682486 1405 TASVDTATDTLIQETLRQ--HFSGCTVITIAHRISSVIDSDMVLLLDQGLIEEHDSP 1459
Cdd:PRK13633 172 TAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTP 228
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
749-825 |
3.38e-10 |
|
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: 60.91 E-value: 3.38e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEVLLGLLRNKTVIYVTHQLEFLPE-ADLILVMKDGRI 825
Cdd:cd03215 105 LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1256-1431 |
3.40e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 61.36 E-value: 3.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1256 MVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGlHDLRSRLSIIPQEPtmfeGtVRSN 1335
Cdd:PRK13538 15 ILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR-DEYHQDLLYLGHQP----G-IKTE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1336 LDPLE----------EYADDQIWEALDKCQL-GDEirkkelklDSPVSengqNWSVGQRQLVCLGRVLLKRSKVLILDEA 1404
Cdd:PRK13538 89 LTALEnlrfyqrlhgPGDDEALWEALAQVGLaGFE--------DVPVR----QLSAGQQRRVALARLWLTRAPLWILDEP 156
|
170 180
....*....|....*....|....*....
gi 30682486 1405 TASVDTATDTLIQETLRQHFS--GCTVIT 1431
Cdd:PRK13538 157 FTAIDKQGVARLEALLAQHAEqgGMVILT 185
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
749-837 |
3.45e-10 |
|
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: 61.75 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgSHLFKEVLLGLLR--NKTVIYVTHQLEFLPE-ADLILVMKDGRI 825
Cdd:cd03261 137 LSGGMKKRVALARALALDPELLLYDEPTAGLDPIA-SGVIDDLIRSLKKelGLTSIMVTHDLDTAFAiADRIAVLYDGKI 215
|
90
....*....|..
gi 30682486 826 TQAGKYNEILES 837
Cdd:cd03261 216 VAEGTPEELRAS 227
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1257-1434 |
3.49e-10 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 61.68 E-value: 3.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1257 VLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRID----GINILTIG---LHDLRSR--------LSII 1321
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASpreILALRRRtigyvsqfLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1322 PQEPTmfegtvrsnLD----PL------EEYADDQIWEALDKCQLgdeirKKELkldspvsengqnWSV-------GQRQ 1384
Cdd:COG4778 106 PRVSA---------LDvvaePLlergvdREEARARARELLARLNL-----PERL------------WDLppatfsgGEQQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 30682486 1385 LVCLGRVLLKRSKVLILDEATASVDTATDT----LIQETLRQhfsGCTVITIAH 1434
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAvvveLIEEAKAR---GTAIIGIFH 210
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1241-1455 |
3.54e-10 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 63.28 E-value: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHLPMV--LRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRS-R 1317
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1318 LSI--IPQEptmF----EGTVRSNLD-PLEeyaddqiWEALDKcqlgDEIRKK--EL--------KLDSPVSengqNWSV 1380
Cdd:PRK11153 82 RQIgmIFQH---FnllsSRTVFDNVAlPLE-------LAGTPK----AEIKARvtELlelvglsdKADRYPA----QLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1381 GQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLRQHFS--GCTVITIAHRIsSVIDS--DMVLLLDQG-LIEE 1455
Cdd:PRK11153 144 GQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEM-DVVKRicDRVAVIDAGrLVEQ 222
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1257-1466 |
3.87e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 62.95 E-value: 3.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1257 VLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINI-------LTIGLHD---------LRSRLSI 1320
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIgdkknnhELITNPYskkiknfkeLRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1321 IPQEP--TMFEGTVRS-------NLDPLEEYADDQIWEALDKCQLGDEIRKKelkldSPVSENGqnwsvGQRQLVCLGRV 1391
Cdd:PRK13631 121 VFQFPeyQLFKDTIEKdimfgpvALGVKKSEAKKLAKFYLNKMGLDDSYLER-----SPFGLSG-----GQKRRVAIAGI 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30682486 1392 LLKRSKVLILDEATASVDTATDT-LIQETLRQHFSGCTVITIAHRISSVID-SDMVLLLDQGLIEEHDSPARLLEDK 1466
Cdd:PRK13631 191 LAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
694-834 |
4.33e-10 |
|
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: 61.43 E-value: 4.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 694 QSPWIQSGKVEENILFGKPMQREWYQRVLEAC---SLNK-DL--EVfpfRDQTvigeRGINLSGGQKQRIQIARALYQDA 767
Cdd:cd03260 88 QKPNPFPGSIYDNVAYGLRLHGIKLKEELDERveeALRKaALwdEV---KDRL----HALGLSGGQQQRLCLARALANEP 160
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30682486 768 DIYLFDDPFSAVDAHTgSHLFKEVLLGLLRNKTVIYVTHQLE-FLPEADLILVMKDGRITQAGKYNEI 834
Cdd:cd03260 161 EVLLLDEPTSALDPIS-TAKIEELIAELKKEYTIVIVTHNMQqAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
950-1120 |
4.57e-10 |
|
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: 62.53 E-value: 4.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 950 SKDVKPLVSGSTLILVYVFLA---TASSFCILVRAMLSAMTGFKIATELFNQMHFRIFRASMSFFDATPIGRILNRASTD 1026
Cdd:cd18573 28 KESGDIEIFGLSLKTFALALLgvfVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1027 QSAVDLRLPSQFSNLAIAAVNILGIIGVMGQVAWQ---VLIVFIPVIAACTWyrqYYISAARELARLSGISRSPLVQHFS 1103
Cdd:cd18573 108 TSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKltlVMLLVVPPIAVGAV---FYGRYVRKLSKQVQDALADATKVAE 184
|
170
....*....|....*..
gi 30682486 1104 ETLSGITTIRSFDQEPR 1120
Cdd:cd18573 185 ERLSNIRTVRAFAAERK 201
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1273-1482 |
5.21e-10 |
|
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: 61.89 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1273 IVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIG---LHDLRS-RLSIIPQE----PTMfegTVRSN--------- 1335
Cdd:cd03294 55 IMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRkKISMVFQSfallPHR---TVLENvafglevqg 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1336 LDPLEEYADDQiwEALDKCQLGDEIRKKELKLdspvsengqnwSVGQRQLVCLGRVLLKRSKVLILDEATasvdTATDTL 1415
Cdd:cd03294 132 VPRAEREERAA--EALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILLMDEAF----SALDPL 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30682486 1416 IQETLRQHF------SGCTVITIAHRISSVID-SDMVLLLDQGLIEEHDSPARLLEDKSSSFsklVAEYTASSD 1482
Cdd:cd03294 195 IRREMQDELlrlqaeLQKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILTNPANDY---VREFFRGVD 265
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1273-1439 |
6.85e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 63.72 E-value: 6.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1273 IVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIG---LHDLRSRLSIIPQEPTmfegtvrSNLDPlEEYADDQIWE 1349
Cdd:PRK10261 355 LVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPY-------ASLDP-RQTVGDSIME 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1350 ALDKCQL--GDEIRKKELKLDSPVS---ENG----QNWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETL 1420
Cdd:PRK10261 427 PLRVHGLlpGKAAAARVAWLLERVGllpEHAwrypHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLL 506
|
170 180
....*....|....*....|.
gi 30682486 1421 --RQHFSGCTVITIAHRISSV 1439
Cdd:PRK10261 507 ldLQRDFGIAYLFISHDMAVV 527
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1261-1451 |
7.72e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.10 E-value: 7.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1261 LTCTFRGGLKTGIVGRTGCGKSTLiqtLFRI--VEPAAGEIRIDGINILTIGLHDL-RSRLSIIPQEPTMFEGTV----- 1332
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTL---LARMagLLPGSGSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPFAMPVfqylt 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1333 RSNLDPLEEYAD-DQIWEALDKCQLGDeirkkelKLDSPVsengQNWSVGQRQLVCLGRVLLK-------RSKVLILDEA 1404
Cdd:PRK03695 92 LHQPDKTRTEAVaSALNEVAEALGLDD-------KLGRSV----NQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 30682486 1405 TASVD----TATDTLIQETLRQhfsGCTVITIAHRISSVID-SDMVLLLDQG 1451
Cdd:PRK03695 161 MNSLDvaqqAALDRLLSELCQQ---GIAVVMSSHDLNHTLRhADRVWLLKQG 209
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
749-836 |
8.49e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 60.88 E-value: 8.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDahtgSHLFKEVlLGLLRN-----KTVIYVTHQLEFLPE-ADLILVMKD 822
Cdd:PRK09493 137 LSGGQQQRVAIARALAVKPKLMLFDEPTSALD----PELRHEV-LKVMQDlaeegMTMVIVTHEIGFAEKvASRLIFIDK 211
|
90
....*....|....
gi 30682486 823 GRITQAGKYNEILE 836
Cdd:PRK09493 212 GRIAEDGDPQVLIK 225
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1241-1450 |
8.77e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.90 E-value: 8.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHlpMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRidginiltiglHDLRSRLSI 1320
Cdd:PRK09544 5 VSLENVSVSFGQR--RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-----------RNGKLRIGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1321 IPQ----EPTMFEGTVR-SNLDPLEEYADdqIWEALDKCQLGDeirkkelKLDSPVsengQNWSVGQRQLVCLGRVLLKR 1395
Cdd:PRK09544 72 VPQklylDTTLPLTVNRfLRLRPGTKKED--ILPALKRVQAGH-------LIDAPM----QKLSGGETQRVLLARALLNR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1396 SKVLILDEATASVDT----ATDTLIQEtLRQHFsGCTVITIAHRISSVI-DSDMVLLLDQ 1450
Cdd:PRK09544 139 PQLLVLDEPTQGVDVngqvALYDLIDQ-LRREL-DCAVLMVSHDLHLVMaKTDEVLCLNH 196
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
749-855 |
8.94e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 62.16 E-value: 8.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHtGSHLFKEVLLGLL-RNKTVIYVTHqleFLPEA----DLILVMKDG 823
Cdd:PRK13536 173 LSGGMKRRLTLARALINDPQLLILDEPTTGLDPH-ARHLIWERLRSLLaRGKTILLTTH---FMEEAerlcDRLCVLEAG 248
|
90 100 110
....*....|....*....|....*....|....
gi 30682486 824 RITQAGKYNEILES--GTDFMELVGAHTDALAAV 855
Cdd:PRK13536 249 RKIAEGRPHALIDEhiGCQVIEIYGGDPHELSSL 282
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
678-835 |
8.99e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 61.54 E-value: 8.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 678 KISGNLKVCGrkaYIAQSPWIQ--SGKVEENILFGK------PMQ-REWYQRVLEACSLNKdlevfpFRDQTvigerGIN 748
Cdd:PRK13644 71 KLQGIRKLVG---IVFQNPETQfvGRTVEEDLAFGPenlclpPIEiRKRVDRALAEIGLEK------YRHRS-----PKT 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEVLLGLLRNKTVIYVTHQLEFLPEADLILVMKDGRITQA 828
Cdd:PRK13644 137 LSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLE 216
|
....*..
gi 30682486 829 GKYNEIL 835
Cdd:PRK13644 217 GEPENVL 223
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1246-1451 |
9.09e-10 |
|
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: 59.37 E-value: 9.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1246 LQVRyGPHLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHD-LRSRLSIIPQE 1324
Cdd:cd03215 5 LEVR-GLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVPED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1325 ptmfegtvrsnldpleeyaddqiwealdkcqlgdeiRKKE-LKLDSPVSEN---GQNWSVGQRQLVCLGRVLLKRSKVLI 1400
Cdd:cd03215 84 ------------------------------------RKREgLVLDLSVAENialSSLLSGGNQQKVVLARWLARDPRVLI 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 30682486 1401 LDEATASVDTATDTLIQETLRQHFS-GCTVITiahrISSVID-----SDMVLLLDQG 1451
Cdd:cd03215 128 LDEPTRGVDVGAKAEIYRLIRELADaGKAVLL----ISSELDellglCDRILVMYEG 180
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
749-851 |
9.44e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 61.66 E-value: 9.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFS-----AVDahtgshLFKEVLLGLLRN-KTVIYVTHQLEFLPE-ADLILVMK 821
Cdd:COG4152 130 LSKGNQQKVQLIAALLHDPELLILDEPFSgldpvNVE------LLKDVIRELAAKgTTVIFSSHQMELVEElCDRIVIIN 203
|
90 100 110
....*....|....*....|....*....|
gi 30682486 822 DGRITQAGKYNEILESGTDFMELVGAHTDA 851
Cdd:COG4152 204 KGRKVLSGSVDEIRRQFGRNTLRLEADGDA 233
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1258-1439 |
9.72e-10 |
|
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: 62.92 E-value: 9.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1258 LRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAA--GEIRIDGINILTIGLHDL-RSRLSIIPQEPTMF-EGTVR 1333
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVpELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1334 SNLDPLEEYADDQIWEALDKCQLGDEIRKKELKLD-SPVSENGQNWSVGQRQLVCLGRVLLKRSKVLILDEATASVdTAT 1412
Cdd:TIGR02633 97 ENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDaDNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL-TEK 175
|
170 180 190
....*....|....*....|....*....|..
gi 30682486 1413 DT-----LIQEtLRQHFSGCtvITIAHRISSV 1439
Cdd:TIGR02633 176 ETeilldIIRD-LKAHGVAC--VYISHKLNEV 204
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
702-837 |
1.44e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 61.43 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 702 KVEENILFG-KPMQREWYQRVLEACSLNKDLEVFPfrdqtvigergINLSGGQKQRIQIARALYQDADIYLFDDPFSAVD 780
Cdd:PRK11144 92 KVRGNLRYGmAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30682486 781 AHTGshlfKEVLLGLLR-----NKTVIYVTHQL-EFLPEADLILVMKDGRITQAGKYNEILES 837
Cdd:PRK11144 161 LPRK----RELLPYLERlareiNIPILYVSHSLdEILRLADRVVVLEQGKVKAFGPLEEVWAS 219
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
749-837 |
1.48e-09 |
|
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: 59.99 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgSHLFKEVLLGL--LRNKTVIYVTHQLEFLPE-ADLILVMKDGRI 825
Cdd:COG1127 142 LSGGMRKRVALARALALDPEILLYDEPTAGLDPIT-SAVIDELIRELrdELGLTSVVVTHDLDSAFAiADRVAVLADGKI 220
|
90
....*....|..
gi 30682486 826 TQAGKYNEILES 837
Cdd:COG1127 221 IAEGTPEELLAS 232
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
624-844 |
1.73e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 60.49 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 624 VEVSNGAFSWDDSSPIPTLKDIRFKIPHGMNIAICGTVGSGKSSLLSSILGEVPKISGNLKVCGRK-------------A 690
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELltaenvwnlrrkiG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 691 YIAQSPWIQ--SGKVEENILFGKPMQ----REWYQRVLEACsLNKDLEVFPFRDQTvigergiNLSGGQKQRIQIARALY 764
Cdd:PRK13642 85 MVFQNPDNQfvGATVEDDVAFGMENQgiprEEMIKRVDEAL-LAVNMLDFKTREPA-------RLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 765 QDADIYLFDDPFSAVDAHTGSHLFKevLLGLLRNK---TVIYVTHQLEFLPEADLILVMKDGRITQAGKYNEILESGTDF 841
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMR--VIHEIKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDM 234
|
...
gi 30682486 842 MEL 844
Cdd:PRK13642 235 VEI 237
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
749-837 |
1.95e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 60.24 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEVL-----LGLlrnkTVIYVTHQLEFLPE-ADLILVMKD 822
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLelqekLGI----SYIYVSQHLGIVKHiSDKVLVMHQ 225
|
90
....*....|....*
gi 30682486 823 GRITQAGKYNEILES 837
Cdd:COG4167 226 GEVVEYGKTAEVFAN 240
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
925-1123 |
1.99e-09 |
|
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: 60.73 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 925 ILVVQILF-QVLNIGSNYwmawVTPVSKDVKPLVSGSTLILVYVFLAtaSSFCILVRAMLSAMTGFKIATELFNQMHFRI 1003
Cdd:cd18780 12 NLALPYFFgQVIDAVTNH----SGSGGEEALRALNQAVLILLGVVLI--GSIATFLRSWLFTLAGERVVARLRKRLFSAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1004 FRASMSFFDATPIGRILNRASTD----QSAVDlrlpsqfSNLAIAAVNILGIIG---VMGQVAWQ---VLIVFIPVIAAC 1073
Cdd:cd18780 86 IAQEIAFFDVTRTGELLNRLSSDtqvlQNAVT-------VNLSMLLRYLVQIIGglvFMFTTSWKltlVMLSVVPPLSIG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 30682486 1074 T-WYRQYYISAAR----ELARLSGISRsplvqhfsETLSGITTIRSFDQEPRFRT 1123
Cdd:cd18780 159 AvIYGKYVRKLSKkfqdALAAASTVAE--------ESISNIRTVRSFAKETKEVS 205
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1273-1472 |
2.02e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 61.59 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1273 IVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRS----RLSIIPQE-PTMFEGTVRSNLDPLEEYADDQI 1347
Cdd:PRK10070 59 IMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSfALMPHMTVLDNTAFGMELAGINA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1348 WEALDKCQlgDEIRkkELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETL--RQHFS 1425
Cdd:PRK10070 139 EERREKAL--DALR--QVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELvkLQAKH 214
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 30682486 1426 GCTVITIAHRISSVID-SDMVLLLDQGLIEEHDSPARLLEDKSSSFSK 1472
Cdd:PRK10070 215 QRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1257-1434 |
2.03e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 61.00 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1257 VLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGlHDLRSRLSIIPQEPTM-FEGTVRSN 1335
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA-RLARARIGVVPQFDNLdLEFTVREN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1336 LDPLEEY---ADDQIwEALDKCQLgdEIRKKELKLDSPVSEngqnWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTAT 1412
Cdd:PRK13536 135 LLVFGRYfgmSTREI-EAVIPSLL--EFARLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHA 207
|
170 180
....*....|....*....|...
gi 30682486 1413 DTLIQETLRQHFS-GCTVITIAH 1434
Cdd:PRK13536 208 RHLIWERLRSLLArGKTILLTTH 230
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
749-837 |
2.20e-09 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 59.81 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDahtgSHLFKEVlLGLLRN-----KTVIYVTHQLEFLPE-ADLILVMKD 822
Cdd:COG4598 155 LSGGQQQRAAIARALAMEPEVMLFDEPTSALD----PELVGEV-LKVMRDlaeegRTMLVVTHEMGFARDvSSHVVFLHQ 229
|
90
....*....|....*
gi 30682486 823 GRITQAGKYNEILES 837
Cdd:COG4598 230 GRIEEQGPPAEVFGN 244
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
749-837 |
2.37e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 61.20 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEVL-LGLLRNKTVIYVTHQL-EFLPEADLILVMKDGRIT 826
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVkLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVV 244
|
90
....*....|.
gi 30682486 827 QAGKYNEILES 837
Cdd:PRK10070 245 QVGTPDEILNN 255
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
749-836 |
2.59e-09 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 59.40 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLfKEVLLGLLRNK--TVIYVTHQL-EFLPEADLILVMKDGRI 825
Cdd:TIGR01184 115 LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL-QEELMQIWEEHrvTVLMVTHDVdEALLLSDRVVMLTNGPA 193
|
90
....*....|.
gi 30682486 826 TQAGkynEILE 836
Cdd:TIGR01184 194 ANIG---QILE 201
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
624-835 |
2.70e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 59.75 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 624 VEVSNGAFSWDDSSPipTLKDIRFKIPHGMNIAICGTVGSGKSSLLSSILGEVPKISGNLKVCGRKAYIAQSPWIQ---- 699
Cdd:PRK13647 5 IEVEDLHFRYKDGTK--ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRskvg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 700 -----------SGKVEENILFGkPM-----QREWYQRVLEACslnKDLEVFPFRDQTvigerGINLSGGQKQRIQIARAL 763
Cdd:PRK13647 83 lvfqdpddqvfSSTVWDDVAFG-PVnmgldKDEVERRVEEAL---KAVRMWDFRDKP-----PYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30682486 764 YQDADIYLFDDPFSAVDAhTGSHLFKEVLLGLLRN-KTVIYVTHQLEFLPE-ADLILVMKDGRITQAGKyNEIL 835
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDP-RGQETLMEILDRLHNQgKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGD-KSLL 225
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
703-836 |
3.06e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 60.62 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 703 VEENILFGKPMQR----EWYQRVLEACSLnkdlevfpFRDQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSA 778
Cdd:PRK11607 108 VEQNIAFGLKQDKlpkaEIASRVNEMLGL--------VHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 779 VDAHTGSHLFKEVLLGLLR-NKTVIYVTH-QLEFLPEADLILVMKDGRITQAGKYNEILE 836
Cdd:PRK11607 180 LDKKLRDRMQLEVVDILERvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1272-1465 |
3.23e-09 |
|
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: 61.36 E-value: 3.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1272 GIVGRTGCGKSTLIQTLFRIVEPAAGEIRI----DGINILTIGLhDLRSR----LSIIPQEPTMFegTVRSNLDPLEEYA 1343
Cdd:TIGR03269 314 GIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGP-DGRGRakryIGILHQEYDLY--PHRTVLDNLTEAI 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1344 DDQIWEALDKCQ-------LGDEIRKKELKLDSPVSEngqnWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLI 1416
Cdd:TIGR03269 391 GLELPDELARMKavitlkmVGFDEEKAEEILDKYPDE----LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDV 466
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 30682486 1417 QETL---RQHFsGCTVITIAHRISSVID-SDMVLLLDQGLIEEHDSPARLLED 1465
Cdd:TIGR03269 467 THSIlkaREEM-EQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1255-1451 |
3.64e-09 |
|
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: 61.95 E-value: 3.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1255 PMVLRgLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTiGLHDLRSRLSIIPQEPTMFEGTVRS 1334
Cdd:TIGR01257 944 PAVDR-LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHLTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1335 NLDPLEEYADDQIWEaldKCQLGDEIRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTATDT 1414
Cdd:TIGR01257 1022 EHILFYAQLKGRSWE---EAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
170 180 190
....*....|....*....|....*....|....*...
gi 30682486 1415 LIQETLRQHFSGCTVITIAHRISSV-IDSDMVLLLDQG 1451
Cdd:TIGR01257 1099 SIWDLLLKYRSGRTIIMSTHHMDEAdLLGDRIAIISQG 1136
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
964-1121 |
3.67e-09 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 60.16 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 964 LVYVFLATASSFCILVRAMLSAMTGFKIATELFNQMHFRIFRASMSFFDA---TPiGRILNRASTD----QSAVDLRLPS 1036
Cdd:cd18578 56 LMFLVLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDDpenST-GALTSRLSTDasdvRGLVGDRLGL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1037 QFSNLA--IAAVnILGIIgvmgqVAWQ---VLIVFIPVIAACTWYRQYYIS-----AARELARLSGIsrsplvqhFSETL 1106
Cdd:cd18578 135 ILQAIVtlVAGL-IIAFV-----YGWKlalVGLATVPLLLLAGYLRMRLLSgfeekNKKAYEESSKI--------ASEAV 200
|
170
....*....|....*
gi 30682486 1107 SGITTIRSFDQEPRF 1121
Cdd:cd18578 201 SNIRTVASLTLEDYF 215
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
703-835 |
4.18e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 58.83 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 703 VEENILFG-------KPMQREWYQRVLEACSLNKDLEVFPfrdqtviGErginLSGGQKQRIQIARALYQDADIYLFDDP 775
Cdd:PRK10771 88 VAQNIGLGlnpglklNAAQREKLHAIARQMGIEDLLARLP-------GQ----LSGGQRQRVALARCLVREQPILLLDEP 156
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 776 FSAVDahtgSHLFKEvLLGLL------RNKTVIYVTHQLEflpEADLI----LVMKDGRITQAGKYNEIL 835
Cdd:PRK10771 157 FSALD----PALRQE-MLTLVsqvcqeRQLTLLMVSHSLE---DAARIaprsLVVADGRIAWDGPTDELL 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
748-834 |
4.32e-09 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 60.20 E-value: 4.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 748 NLSGGQKQRIQIARALYQDADIYLFDDPFSAVD-AHTGS--HLFKEV--LLGLlrnkTVIYVTHQLEFLPE-ADLILVMK 821
Cdd:PRK11153 140 QLSGGQKQRVAIARALASNPKVLLCDEATSALDpATTRSilELLKDInrELGL----TIVLITHEMDVVKRiCDRVAVID 215
|
90
....*....|...
gi 30682486 822 DGRITQAGKYNEI 834
Cdd:PRK11153 216 AGRLVEQGTVSEV 228
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1240-1470 |
4.66e-09 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 59.78 E-value: 4.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1240 EITICNLQVRYGPHlpMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGiniltiglHDLRSRLS 1319
Cdd:COG1118 2 SIEVRNISKRFGSF--TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG--------RDLFTNLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1320 iiPQE-------------PTMfegTVRSN-------LDPLEEYADDQIWEALDKCQLGD-EIRK-KELkldspvsengqn 1377
Cdd:COG1118 72 --PRErrvgfvfqhyalfPHM---TVAENiafglrvRPPSKAEIRARVEELLELVQLEGlADRYpSQL------------ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1378 wSVGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLRQHFS--GCTVITIAH------RIssvidSDMVLLLD 1449
Cdd:COG1118 135 -SGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDelGGTTVFVTHdqeealEL-----ADRVVVMN 208
|
250 260
....*....|....*....|.
gi 30682486 1450 QGLIEEHDSPARLLEDKSSSF 1470
Cdd:COG1118 209 QGRIEQVGTPDEVYDRPATPF 229
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1241-1420 |
4.94e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 58.44 E-value: 4.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYgPHLPMvlrGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINiltiglHDL----RS 1316
Cdd:PRK10771 2 LKLTDITWLY-HHLPM---RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD------HTTtppsRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1317 RLSIIPQEPTMFEG-TVRSN----LDPLEEYADDQiwealdKCQLGDEIRKkeLKLDSPVSENGQNWSVGQRQLVCLGRV 1391
Cdd:PRK10771 72 PVSMLFQENNLFSHlTVAQNiglgLNPGLKLNAAQ------REKLHAIARQ--MGIEDLLARLPGQLSGGQRQRVALARC 143
|
170 180
....*....|....*....|....*....
gi 30682486 1392 LLKRSKVLILDEATASVDTAtdtLIQETL 1420
Cdd:PRK10771 144 LVREQPILLLDEPFSALDPA---LRQEML 169
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1241-1453 |
5.16e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 58.94 E-value: 5.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHLP---MVLRGLTCTfrggLKTG----IVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHD 1313
Cdd:COG1101 2 LELKNLSKTFNPGTVnekRALDGLNLT----IEEGdfvtVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1314 lRSRL-SIIPQEPTMfeGT-----VRSNL------------------DPLEEYAddqiwEALDKCQLGDEIRkkelkLDS 1369
Cdd:COG1101 78 -RAKYiGRVFQDPMM--GTapsmtIEENLalayrrgkrrglrrgltkKRRELFR-----ELLATLGLGLENR-----LDT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1370 PVSengqNWSVGQRQLVCLGRVLLKRSKVLILDEATASVD--TA------TDTLIQEtlrqhfSGCTVITIAHRISSVID 1441
Cdd:COG1101 145 KVG----LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDpkTAalvlelTEKIVEE------NNLTTLMVTHNMEQALD 214
|
250
....*....|...
gi 30682486 1442 -SDMVLLLDQGLI 1453
Cdd:COG1101 215 yGNRLIMMHEGRI 227
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
732-839 |
5.40e-09 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 60.24 E-value: 5.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 732 EVFPFRDQTVIgergiNLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHtgsHLFKEvlLGLLRN-----KTVIYVTH 806
Cdd:PRK09536 128 GVAQFADRPVT-----SLSGGERQRVLLARALAQATPVLLLDEPTASLDIN---HQVRT--LELVRRlvddgKTAVAAIH 197
|
90 100 110
....*....|....*....|....*....|....
gi 30682486 807 QLEFLPE-ADLILVMKDGRITQAGKYNEILESGT 839
Cdd:PRK09536 198 DLDLAARyCDELVLLADGRVRAAGPPADVLTADT 231
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
749-829 |
5.53e-09 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 58.49 E-value: 5.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFkEVLLGLLRNK-TVIYVTHQLEFLPE-ADLILVMKDGRIT 826
Cdd:COG4161 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVV-EIIRELSQTGiTQVIVTHEVEFARKvASQVVYMEKGRII 220
|
...
gi 30682486 827 QAG 829
Cdd:COG4161 221 EQG 223
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1273-1437 |
5.80e-09 |
|
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: 60.53 E-value: 5.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1273 IVGRTGCGKSTLiqtlFRIVepaaGEIRIDGINILTIglhDLRSRLSIIPQEPTMFEGTVRSNL---DPLEE-----YAD 1344
Cdd:TIGR00954 483 ICGPNGCGKSSL----FRIL----GELWPVYGGRLTK---PAKGKLFYVPQRPYMTLGTLRDQIiypDSSEDmkrrgLSD 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1345 DQIWEALDKCQLGDeIRKKELKLDSPvsengQNW----SVGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETL 1420
Cdd:TIGR00954 552 KDLEQILDNVQLTH-ILEREGGWSAV-----QDWmdvlSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLC 625
|
170
....*....|....*..
gi 30682486 1421 RQHfsGCTVITIAHRIS 1437
Cdd:TIGR00954 626 REF--GITLFSVSHRKS 640
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
961-1168 |
6.54e-09 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-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. 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. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. 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: 349985 [Multi-domain] Cd Length: 293 Bit Score: 58.96 E-value: 6.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 961 TLILVYVFLATASSFCILVRAMLSAMTGFKIATELFNQMHFRIFRASMSFFDATPIGRILNRASTDQSAVDLRLPSQFSN 1040
Cdd:cd18541 41 RYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILY 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1041 LAIAAVNILGIIGVMGQVAWQV-LIVFIP--VIAACTWY-----RQYYISAARELARLSGIsrsplVQhfsETLSGITTI 1112
Cdd:cd18541 121 LVDALFLGVLVLVMMFTISPKLtLIALLPlpLLALLVYRlgkkiHKRFRKVQEAFSDLSDR-----VQ---ESFSGIRVI 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 30682486 1113 RSFDQEPRFRTDIMRLNDCYSR--LRFHAISAMewlcfrLDLLSTVAFALSLVILVSV 1168
Cdd:cd18541 193 KAFVQEEAEIERFDKLNEEYVEknLRLARVDAL------FFPLIGLLIGLSFLIVLWY 244
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
749-835 |
7.74e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 58.10 E-value: 7.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKevLLGLLRN--KTVIYVTHQLEflpEA----DLILVMKD 822
Cdd:PRK11231 139 LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMR--LMRELNTqgKTVVTVLHDLN---QAsrycDHLVVLAN 213
|
90
....*....|...
gi 30682486 823 GRITQAGKYNEIL 835
Cdd:PRK11231 214 GHVMAQGTPEEVM 226
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
748-836 |
1.04e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 58.27 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 748 NLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgshlfKEVLLGLLR------NKTVIYVTHQLEFLPEADLILVMK 821
Cdd:PRK13640 143 NLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG-----KEQILKLIRklkkknNLTVISITHDIDEANMADQVLVLD 217
|
90
....*....|....*
gi 30682486 822 DGRITQAGKYNEILE 836
Cdd:PRK13640 218 DGKLLAQGSPVEIFS 232
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1257-1453 |
1.19e-08 |
|
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: 57.34 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1257 VLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGiNILTIGLHDLRSRLSIIPQEPTmfegTVRSNL 1336
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-LVPWKRRKKFLRRIGVVFGQKT----QLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1337 DPLEEYA---------DDQIWEALDKC----QLGDEirkkelkLDSPVsengQNWSVGQRQLVCLGRVLLKRSKVLILDE 1403
Cdd:cd03267 111 PVIDSFYllaaiydlpPARFKKRLDELsellDLEEL-------LDTPV----RQLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 30682486 1404 ATASVDTATDTLIQETLRQHFS--GCTVITIAHRISSVID-SDMVLLLDQGLI 1453
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYNRerGTTVLLTSHYMKDIEAlARRVLVIDKGRL 232
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1241-1451 |
1.23e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 58.20 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHLpmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDG--INiltiglHDLRSRL 1318
Cdd:COG4152 2 LELKGLTKRFGDKT--AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGepLD------PEDRRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1319 SIIPQE----PTMfegTVRS---------NLDPLEeyADDQIWEALDKCQLGDEIRKK--ELkldspvsengqnwSVGQR 1383
Cdd:COG4152 74 GYLPEErglyPKM---KVGEqlvylarlkGLSKAE--AKRRADEWLERLGLGDRANKKveEL-------------SKGNQ 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1384 QLVCLGRVLLKRSKVLILDEATASVD-TATDTLIQETLRQHFSGCTVITIAHRISSVID-SDMVLLLDQG 1451
Cdd:COG4152 136 QKVQLIAALLHDPELLILDEPFSGLDpVNVELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKG 205
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1272-1448 |
1.23e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 58.56 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1272 GIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIG---LHDLRSRLSIIPQE------PTMFEGTVRSnlDPLEEY 1342
Cdd:PRK15079 51 GVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKddeWRAVRSDIQMIFQDplaslnPRMTIGEIIA--EPLRTY 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1343 ADDqiweaLDKCQLGDEIRKKELK---LDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTATD----TL 1415
Cdd:PRK15079 129 HPK-----LSRQEVKDRVKAMMLKvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQaqvvNL 203
|
170 180 190
....*....|....*....|....*....|....*
gi 30682486 1416 IQETLRQhfSGCTVITIAHRISSV--IdSDMVLLL 1448
Cdd:PRK15079 204 LQQLQRE--MGLSLIFIAHDLAVVkhI-SDRVLVM 235
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
688-886 |
1.49e-08 |
|
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: 57.56 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 688 RKAY--IAQSPWIQSGKVEENI-LFGKPMQREWYqRVLEACSLNKDLEVFPFRDQTVIGERGINLSGGQKQRIQIARALY 764
Cdd:cd03289 76 RKAFgvIPQKVFIFSGTFRKNLdPYGKWSDEEIW-KVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 765 QDADIYLFDDPFSAVDAHTgSHLFKEVLLGLLRNKTVIYVTHQLEFLPEADLILVMKDGRITQAGKYNEILESGTDFMEL 844
Cdd:cd03289 155 SKAKILLLDEPSAHLDPIT-YQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQA 233
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 30682486 845 VgAHTDALAAVdsyeKGSASAQSTTSKESKVSNDEEKQEEDL 886
Cdd:cd03289 234 I-SPSDRLKLF----PRRNSSKSKRKPRPQIQALQEETEEEV 270
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1239-1459 |
1.55e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 57.71 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1239 GEITICNLQVRYGPHLPMVLRGL---TCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIrIDGINILTIGL---- 1311
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFEFKALnntSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQT-IVGDYAIPANLkkik 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1312 --HDLRSRLSIIPQEP--TMFEGTVRS-------NLDPLEEYADDQIWEALDKCQLGDEIRKKelkldSPVSENGqnwsv 1380
Cdd:PRK13645 84 evKRLRKEIGLVFQFPeyQLFQETIEKdiafgpvNLGENKQEAYKKVPELLKLVQLPEDYVKR-----SPFELSG----- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1381 GQRQLVCLGRVLLKRSKVLILDEATASVD-TATDTLIQETLRQHFS-GCTVITIAHRISSVID-SDMVLLLDQGLIEEHD 1457
Cdd:PRK13645 154 GQKRRVALAGIIAMDGNTLVLDEPTGGLDpKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIG 233
|
..
gi 30682486 1458 SP 1459
Cdd:PRK13645 234 SP 235
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
749-824 |
1.61e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.15 E-value: 1.61e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKevLLGLLR--NKTVIYVTHQLEFLPE-ADLILVMKDGR 824
Cdd:PRK11288 141 LSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFR--VIRELRaeGRVILYVSHRMEEIFAlCDAITVFKDGR 217
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1240-1465 |
1.75e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 57.79 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1240 EITICNLQVRYGPHLPM---VLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEI-----------RIDGIN 1305
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPTelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1306 ILTIGL-------------HDLRSRLSIIPQ--EPTMFEGTVRSNL--DPLEEYADDQiwEALdkcqlgdEIRKKELKL- 1367
Cdd:PRK13651 82 KVLEKLviqktrfkkikkiKEIRRRVGVVFQfaEYQLFEQTIEKDIifGPVSMGVSKE--EAK-------KRAAKYIELv 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1368 ---DSPVSENGQNWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLRQ-HFSGCTVITIAHRISSVID-S 1442
Cdd:PRK13651 153 gldESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNVLEwT 232
|
250 260
....*....|....*....|...
gi 30682486 1443 DMVLLLDQGLIEEHDSPARLLED 1465
Cdd:PRK13651 233 KRTIFFKDGKIIKDGDTYDILSD 255
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
696-825 |
1.77e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 57.38 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 696 PWiqsGKVEENILFGkpMQREWYQRVLEAcslnkdLEVFPFRDQTviGERGINLSGGQKQRIQIARALYQDADIYLFDDP 775
Cdd:PRK11247 94 PW---KKVIDNVGLG--LKGQWRDAALQA------LAAVGLADRA--NEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 30682486 776 FSAVDAHTGSHLfKEVLLGLLRNK--TVIYVTHQL-EFLPEADLILVMKDGRI 825
Cdd:PRK11247 161 LGALDALTRIEM-QDLIESLWQQHgfTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
919-1121 |
1.88e-08 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 57.48 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 919 GALVPIILvvqILF-QVLNIGSNYWMAWVTPvsKDVKPLVSGSTLILVYVFLATAssFCILVRAMLSAMTGFKIA----T 993
Cdd:cd18577 12 GAALPLMT---IVFgDLFDAFTDFGSGESSP--DEFLDDVNKYALYFVYLGIGSF--VLSYIQTACWTITGERQArrirK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 994 ELFNqmhfRIFRASMSFFDATPIGRILNRASTD----QSAVDLRLPSQFSNLA--IAAVnILGIIgvmgqVAWQ---VLI 1064
Cdd:cd18577 85 RYLK----ALLRQDIAWFDKNGAGELTSRLTSDtnliQDGIGEKLGLLIQSLStfIAGF-IIAFI-----YSWKltlVLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30682486 1065 VFIPVIAACTWYRQYYISAA-----RELARLSGISrsplvqhfSETLSGITTIRSFDQEPRF 1121
Cdd:cd18577 155 ATLPLIAIVGGIMGKLLSKYtkkeqEAYAKAGSIA--------EEALSSIRTVKAFGGEEKE 208
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
958-1462 |
2.08e-08 |
|
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: 58.66 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 958 SGSTLILVYVFLATASSFCILVRAMLSAMT--GFKIATELFNQMHFRIFRASMSFFDATPIGRILNRASTDQSAVdlrlp 1035
Cdd:COG4615 44 GAALARLLLLFAGLLVLLLLSRLASQLLLTrlGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTI----- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1036 SQ-FSNLAIAAVNILGIIGVMGQVAW---QVLIVFIPVIAACTWYRQYYISAARELARLSGISRSPLVQHFSETLSGITT 1111
Cdd:COG4615 119 SQaFVRLPELLQSVALVLGCLAYLAWlspPLFLLTLVLLGLGVAGYRLLVRRARRHLRRAREAEDRLFKHFRALLEGFKE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1112 IRsFDQEPR--FRTDimRLNDCYSRLRFHAISAMEWLCFRLDLLSTVAFALSLVILVSVPegVINPSFAGLAVTYAL--- 1186
Cdd:COG4615 199 LK-LNRRRRraFFDE--DLQPTAERYRDLRIRADTIFALANNWGNLLFFALIGLILFLLP--ALGWADPAVLSGFVLvll 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1187 --------------NLNSLQATLiwtlcdleNKMISVERMLqyiDIPSEPSLVIESTRPEKSWpcrGEITICNLQVRY-- 1250
Cdd:COG4615 274 flrgplsqlvgalpTLSRANVAL--------RKIEELELAL---AAAEPAAADAAAPPAPADF---QTLELRGVTYRYpg 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1251 ---------GPhlpmvlrgLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSII 1321
Cdd:COG4615 340 edgdegftlGP--------IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAV 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1322 PQEPTMFEgtvrSNLDPLEEYADDQIWEALDKcqlgdeirkkeLKLDSPVS-ENGQ----NWSVGQRQLVCLGRVLLKRS 1396
Cdd:COG4615 412 FSDFHLFD----RLLGLDGEADPARARELLER-----------LELDHKVSvEDGRfsttDLSQGQRKRLALLVALLEDR 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30682486 1397 KVLILDEATASVDTA-----TDTLIQEtLRQhfSGCTVITIAHrissviD------SDMVLLLDQGLIEEHDSPARL 1462
Cdd:COG4615 477 PILVFDEWAADQDPEfrrvfYTELLPE-LKA--RGKTVIAISH------DdryfdlADRVLKMDYGKLVELTGPAAL 544
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
964-1166 |
2.24e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes 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. 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 the chemical 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. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. 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: 350008 [Multi-domain] Cd Length: 307 Bit Score: 57.52 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 964 LVYVFLATASSFCILVRAMLSAMTG----FKIATELFNQMHfrifRASMSFFDATPIGRILNRASTDQSAVDLRLPSQFS 1039
Cdd:cd18564 58 AALVGIALLRGLASYAGTYLTALVGqrvvLDLRRDLFAHLQ----RLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1040 NLAIAAVNILGIIGVMGQVAWQ----VLIVFIPVIAACTWYRQYYISAARELARLSGiSRSPLVQhfsETLSGITTIRSF 1115
Cdd:cd18564 134 PLLTNLLTLVGMLGVMFWLDWQlaliALAVAPLLLLAARRFSRRIKEASREQRRREG-ALASVAQ---ESLSAIRVVQAF 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 30682486 1116 DQEPRFRTDIMRLNDCYSRLRFHAI---SAMEWLcfrLDLLstVAFALSLVILV 1166
Cdd:cd18564 210 GREEHEERRFARENRKSLRAGLRAArlqALLSPV---VDVL--VAVGTALVLWF 258
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
748-826 |
2.50e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 58.50 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 748 NLSGGQKQRIQIARALYQDADIYLFDDPfSAV--DAHTgshlfkEVLLGLLRN-----KTVIYVTHQLEflpE----ADL 816
Cdd:COG3845 141 DLSVGEQQRVEILKALYRGARILILDEP-TAVltPQEA------DELFEILRRlaaegKSIIFITHKLR---EvmaiADR 210
|
90
....*....|
gi 30682486 817 ILVMKDGRIT 826
Cdd:COG3845 211 VTVLRRGKVV 220
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
749-834 |
2.86e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 57.02 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAhTGShlfKEVL-----LGLLRNKTVIYVTHQLEFLPEADLILVMKDG 823
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDP-SGR---REVVntikeLNKKYGITIILITHYMEEAVEADRIIVMDSG 220
|
90
....*....|.
gi 30682486 824 RITQAGKYNEI 834
Cdd:PRK13633 221 KVVMEGTPKEI 231
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
749-838 |
4.32e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 54.64 E-value: 4.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDAD--IYLFDDPFSAVDAHTGSHLFkEVLLGLLRNK-TVIYVTHQLEFLPEADLILVMKDGri 825
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLL-EVIKGLIDLGnTVILIEHNLDVLSSADWIIDFGPG-- 164
|
90
....*....|....
gi 30682486 826 tqAGKY-NEILESG 838
Cdd:cd03238 165 --SGKSgGKVVFSG 176
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1257-1434 |
4.56e-08 |
|
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: 57.64 E-value: 4.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1257 VLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRI-DGInilTIGlhdlrsrlsIIPQEPTMFEG-TVRS 1334
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGI---KVG---------YLPQEPQLDPTkTVRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1335 N-----------LDPLEE----YAD-DQIWEALDKCQ--LGDEI---------RKKE-----LKL---DSPVSengqNWS 1379
Cdd:TIGR03719 88 NveegvaeikdaLDRFNEisakYAEpDADFDKLAAEQaeLQEIIdaadawdldSQLEiamdaLRCppwDADVT----KLS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 30682486 1380 VGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLRQhFSGcTVITIAH 1434
Cdd:TIGR03719 164 GGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQE-YPG-TVVAVTH 216
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
748-837 |
4.76e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 56.00 E-value: 4.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 748 NLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAhTGSHLFKEVLLGLLRNKTVIYVTHQ-LEFLPEADLILVMKDGRIT 826
Cdd:PRK14267 149 NLSGGQRQRLVIARALAMKPKILLMDEPTANIDP-VGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLI 227
|
90
....*....|.
gi 30682486 827 QAGKYNEILES 837
Cdd:PRK14267 228 EVGPTRKVFEN 238
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1264-1451 |
4.87e-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: 57.53 E-value: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1264 TFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPA-AGEIRIDG--INILTIgLHDLRSRLSIIPQE-------PTMFEGTvR 1333
Cdd:TIGR02633 282 SLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDIRNP-AQAIRAGIAMVPEDrkrhgivPILGVGK-N 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1334 SNLDPLEEYAD-DQIWEALDKCQLGDEIRKKELKLDSPVSENGQnWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTAT 1412
Cdd:TIGR02633 360 ITLSVLKSFCFkMRIDAAAELQIIGSAIQRLKVKTASPFLPIGR-LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 30682486 1413 DTLIQETLRQHFS-GCTVITIAHRISSVID-SDMVLLLDQG 1451
Cdd:TIGR02633 439 KYEIYKLINQLAQeGVAIIVVSSELAEVLGlSDRVLVIGEG 479
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
703-830 |
5.77e-08 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 55.06 E-value: 5.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 703 VEENILF-----GKPmQREWYQRVLEACSL----NKdLEVFPfrdqtvigergINLSGGQKQRIQIARALYQDADIYLFD 773
Cdd:COG2884 96 VYENVALplrvtGKS-RKEIRRRVREVLDLvglsDK-AKALP-----------HELSGGEQQRVAIARALVNRPELLLAD 162
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30682486 774 DPFSAVDAHTGS---HLFKEVllgllrNK---TVIYVTHQLEFLPEADL-ILVMKDGRITQAGK 830
Cdd:COG2884 163 EPTGNLDPETSWeimELLEEI------NRrgtTVLIATHDLELVDRMPKrVLELEDGRLVRDEA 220
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
691-837 |
8.07e-08 |
|
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: 54.86 E-value: 8.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 691 YIAQSPWIQSG-KVEENIL----FGKPMQREWYQRvLEAcsLNKDLEVFPFRDQtvigeRGINLSGGQKQRIQIARALYQ 765
Cdd:cd03218 79 YLPQEASIFRKlTVEENILavleIRGLSKKEREEK-LEE--LLEEFHITHLRKS-----KASSLSGGERRRVEIARALAT 150
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30682486 766 DADIYLFDDPFSAVDAHTGSHLFKevLLGLLRNKTV-IYVT-HQL-EFLPEADLILVMKDGRITQAGKYNEILES 837
Cdd:cd03218 151 NPKFLLLDEPFAGVDPIAVQDIQK--IIKILKDRGIgVLITdHNVrETLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1258-1451 |
8.25e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 54.50 E-value: 8.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1258 LRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHD---LRSRLSIIPQE-PTMFEGTVR 1333
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDhHLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1334 SNLD-PL------EEYADDQIWEALDKCQLGDEIRKKELKLdspvsengqnwSVGQRQLVCLGRVLLKRSKVLILDEATA 1406
Cdd:PRK10908 98 DNVAiPLiiagasGDDIRRRVSAALDKVGLLDKAKNFPIQL-----------SGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 30682486 1407 SVDtatDTLIQETLR--QHFS--GCTVITIAHRISSVIDSDM-VLLLDQG 1451
Cdd:PRK10908 167 NLD---DALSEGILRlfEEFNrvGVTVLMATHDIGLISRRSYrMLTLSDG 213
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1272-1455 |
8.73e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.55 E-value: 8.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1272 GIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLR-SRLSIIPQEPTMF-EGTVRSNLDPLEEYADdqIWE 1349
Cdd:PRK10762 34 ALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQeAGIGIIHQELNLIpQLTIAENIFLGREFVN--RFG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1350 ALDKCQLGDEIRK--KELKL----DSPVSEngqnWSVGQRQLVCLGRVLLKRSKVLILDEAT-ASVDTATDTL---IQEt 1419
Cdd:PRK10762 112 RIDWKKMYAEADKllARLNLrfssDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTdALTDTETESLfrvIRE- 186
|
170 180 190
....*....|....*....|....*....|....*...
gi 30682486 1420 LRQHfsGCTVITIAHRISSV--IDSDMVLLLDQGLIEE 1455
Cdd:PRK10762 187 LKSQ--GRGIVYISHRLKEIfeICDDVTVFRDGQFIAE 222
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
744-809 |
9.80e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 54.78 E-value: 9.80e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30682486 744 ERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLfKEVLLGLLRNKTVIYVTHQLE 809
Cdd:PRK14239 144 DSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKI-EETLLGLKDDYTMLLVTRSMQ 208
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
962-1120 |
1.07e-07 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the 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 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. 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 by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. 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: 349995 [Multi-domain] Cd Length: 289 Bit Score: 55.13 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 962 LILVYVFLATASSFCILvramLSAMTGFKIATELFNQMHFRIFRASMSFFDATPIGRILNRASTDQSAVDLRLPSQFSNL 1041
Cdd:cd18551 42 LVALFLLQAVLSALSSY----LLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1042 AIAAVNILGIIGVMGQVAWQ---VLIVFIPVIAACTWY-----RQYYISAARELARLSGisrsplvqHFSETLSGITTIR 1113
Cdd:cd18551 118 VTGVLTVVGAVVLMFLLDWVltlVTLAVVPLAFLIILPlgrriRKASKRAQDALGELSA--------ALERALSAIRTVK 189
|
....*..
gi 30682486 1114 SFDQEPR 1120
Cdd:cd18551 190 ASNAEER 196
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
749-829 |
1.07e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 54.64 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKeVLLGLLRNK-TVIYVTHQLEFLPE-ADLILVMKDGRIT 826
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVS-IIRELAETGiTQVIVTHEVEVARKtASRVVYMENGHIV 220
|
...
gi 30682486 827 QAG 829
Cdd:PRK11124 221 EQG 223
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
688-886 |
1.09e-07 |
|
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: 56.84 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 688 RKAY--IAQSPWIQSGKVEENIlfgKPMQR---EWYQRVLEACSLNKDLEVFPFRDQTVIGERGINLSGGQKQRIQIARA 762
Cdd:TIGR01271 1291 RKAFgvIPQKVFIFSGTFRKNL---DPYEQwsdEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARS 1367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 763 LYQDADIYLFDDPFSAVDAHTgSHLFKEVLLGLLRNKTVIYVTHQLEFLPEADLILVMKDGRITQAGKYNEILESGTDFM 842
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLDPVT-LQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFK 1446
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 30682486 843 ELVGaHTDALAAVDSYEKGSASAQSttskESKVSNDEEKQEEDL 886
Cdd:TIGR01271 1447 QAMS-AADRLKLFPLHRRNSSKRKP----QPKITALREEAEEEV 1485
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
749-829 |
1.15e-07 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 54.78 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADI-----YLF-DDPFSAVD-AHtgshlfKEVLLGLLRNKT------VIYVTHQLE----Fl 811
Cdd:PRK13548 135 LSGGEQQRVQLARVLAQLWEPdgpprWLLlDEPTSALDlAH------QHHVLRLARQLAherglaVIVVLHDLNlaarY- 207
|
90
....*....|....*...
gi 30682486 812 peADLILVMKDGRITQAG 829
Cdd:PRK13548 208 --ADRIVLLHQGRLVADG 223
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
749-829 |
1.17e-07 |
|
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: 54.12 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgSHLFKEVLLGLLRNKTVIYVTHQLEFLPE-ADLILVMKDGRITQ 827
Cdd:cd03264 131 LSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEE-RIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVF 209
|
..
gi 30682486 828 AG 829
Cdd:cd03264 210 EG 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1245-1466 |
1.23e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 54.70 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1245 NLQVRYgPHLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDG--INILTIGLHDLRSRLSIIP 1322
Cdd:PRK13639 6 DLKYSY-PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTVGIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1323 QEP--TMFEGTVRS-------NLDPLEEYADDQIWEALDKCQLGDEIRKKELKLdspvsengqnwSVGQRQLVCLGRVLL 1393
Cdd:PRK13639 85 QNPddQLFAPTVEEdvafgplNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHL-----------SGGQKKRVAIAGILA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30682486 1394 KRSKVLILDEATASVDTATDTLIQETLRQ-HFSGCTVITIAHRISSV-IDSDMVLLLDQGLIEEHDSPARLLEDK 1466
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDlNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
708-834 |
1.25e-07 |
|
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: 53.91 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 708 LFGKPmQREWYQRVLEACSLnkdLEVFPFRDQTVIgergiNLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHL 787
Cdd:cd03265 100 LYGVP-GAERRERIDELLDF---VGLLEAADRLVK-----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHV 170
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 30682486 788 FkEVLLGLLR--NKTVIYVTHQLEflpEADL----ILVMKDGRITQAGKYNEI 834
Cdd:cd03265 171 W-EYIEKLKEefGMTILLTTHYME---EAEQlcdrVAIIDHGRIIAEGTPEEL 219
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1258-1439 |
1.39e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.95 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1258 LRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGI--NILTiglHDLRSRL--SIIPQEPTMF-EGTV 1332
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInyNKLD---HKLAAQLgiGIIYQELSVIdELTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1333 RSNL------------DPLEEYADDQIWEALDKCQLGdeirkkeLKLDspVSENGQNWSVGQRQLVCLGRVLLKRSKVLI 1400
Cdd:PRK09700 98 LENLyigrhltkkvcgVNIIDWREMRVRAAMMLLRVG-------LKVD--LDEKVANLSISHKQMLEIAKTLMLDAKVII 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 30682486 1401 LDEATASV-DTATDTL--IQETLRQhfSGCTVITIAHRISSV 1439
Cdd:PRK09700 169 MDEPTSSLtNKEVDYLflIMNQLRK--EGTAIVYISHKLAEI 208
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
636-834 |
1.46e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 54.81 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 636 SSPIPTLKDIRFKIPHGMNIAICGTVGSGKSSLLSSILGEVPKISGNLKVCG-----------RK--AYIAQSP--WIQS 700
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGepitkenirevRKfvGLVFQNPddQIFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 701 GKVEENILFGkpmqrewyqrvleACSLNKDLEVFPFRDQTVIGERGI---------NLSGGQKQRIQIARALYQDADIYL 771
Cdd:PRK13652 94 PTVEQDIAFG-------------PINLGLDEETVAHRVSSALHMLGLeelrdrvphHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30682486 772 FDDPFSAVDAHTGSHLFKEV-LLGLLRNKTVIYVTHQLEFLPE-ADLILVMKDGRITQAGKYNEI 834
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLnDLPETYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEI 225
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
749-834 |
1.58e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 54.70 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKevLLGLLRNK--TVIYVTHQLEFLPE-ADLILVMKDGRI 825
Cdd:PRK13639 138 LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMK--LLYDLNKEgiTIIISTHDVDLVPVyADKVYVMSDGKI 215
|
....*....
gi 30682486 826 TQAGKYNEI 834
Cdd:PRK13639 216 IKEGTPKEV 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1257-1422 |
1.58e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 55.87 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1257 VLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVePAAGEIRIDGINILTIG---LHDLRSRLSIIPQEPTmfegtvr 1333
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDPN------- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1334 SNLDPLEEYAddQIWE--------ALDKCQLGDEIRK--KELKLDsPVSEN--GQNWSVGQRQLVCLGRVLLKRSKVLIL 1401
Cdd:PRK15134 373 SSLNPRLNVL--QIIEeglrvhqpTLSAAQREQQVIAvmEEVGLD-PETRHryPAEFSGGQRQRIAIARALILKPSLIIL 449
|
170 180
....*....|....*....|.
gi 30682486 1402 DEATASVDTATDTLIQETLRQ 1422
Cdd:PRK15134 450 DEPTSSLDKTVQAQILALLKS 470
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1241-1455 |
1.92e-07 |
|
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: 53.41 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHLpmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINIltiglHDLRSR--- 1317
Cdd:cd03301 1 VELENVTKRFGNVT--ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-----TDLPPKdrd 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1318 LSIIPQE----PTMfegTVRSNLD-PLEEYADDQiwealdkcqlgDEIRK------KELKLDSPVSENGQNWSVGQRQLV 1386
Cdd:cd03301 74 IAMVFQNyalyPHM---TVYDNIAfGLKLRKVPK-----------DEIDErvrevaELLQIEHLLDRKPKQLSGGQRQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30682486 1387 CLGRVLLKRSKVLILDEATASVdtatDTLIQETLRQHFS------GCTVITIAH-RISSVIDSDMVLLLDQGLIEE 1455
Cdd:cd03301 140 ALGRAIVREPKVFLMDEPLSNL----DAKLRVQMRAELKrlqqrlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQ 211
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1241-1434 |
1.96e-07 |
|
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: 51.68 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHLpmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGinILTIGLhdlrsrlsi 1320
Cdd:cd03221 1 IELENLSKTYGGKL--LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS--TVKIGY--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1321 ipqeptmFEgtvrsnldpleeyaddqiwealdkcQLgdeirkkelkldspvsengqnwSVGQRQLVCLGRVLLKRSKVLI 1400
Cdd:cd03221 68 -------FE-------------------------QL----------------------SGGEKMRLALAKLLLENPNLLL 93
|
170 180 190
....*....|....*....|....*....|....
gi 30682486 1401 LDEATASVDTATDTLIQETLRQhFSGcTVITIAH 1434
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKE-YPG-TVILVSH 125
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
745-827 |
2.57e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 53.28 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 745 RGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKevLLGLL--RNKTV-IYVTHQLEFLPEADLILVMK 821
Cdd:PRK11629 142 RPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQ--LLGELnrLQGTAfLVVTHDLQLAKRMSRQLEMR 219
|
....*.
gi 30682486 822 DGRITQ 827
Cdd:PRK11629 220 DGRLTA 225
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
745-829 |
2.65e-07 |
|
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: 52.53 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 745 RGIN--LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAhTGSHLFKEVLLGLLR-NKTVIYVTHQLEFL--PEADLILV 819
Cdd:cd03217 99 RYVNegFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI-DALRLVAEVINKLREeGKSVLIITHYQRLLdyIKPDRVHV 177
|
90
....*....|
gi 30682486 820 MKDGRITQAG 829
Cdd:cd03217 178 LYDGRIVKSG 187
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
961-1128 |
2.99e-07 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to 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. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 53.64 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 961 TLILVYVFLATA-SSFcilVRAMLSAMTGFKIATELFNQMHFRIFRASMSFFDATPIGRILNRASTD----QSAVDlrlp 1035
Cdd:cd18576 39 ALLLLGLFLLQAvFSF---FRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDvtqiQDTLT---- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1036 sqfSNLAIAAVNILGIIG---VMGQVAWQ----VLIVFIPVIAACTWY----RQYYISAARELARLSGIsrsplVQhfsE 1104
Cdd:cd18576 112 ---TTLAEFLRQILTLIGgvvLLFFISWKltllMLATVPVVVLVAVLFgrriRKLSKKVQDELAEANTI-----VE---E 180
|
170 180
....*....|....*....|....*...
gi 30682486 1105 TLSGITTIRSFDQEP----RFRTDIMRL 1128
Cdd:cd18576 181 TLQGIRVVKAFTREDyeieRYRKALERV 208
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1241-1477 |
3.02e-07 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 54.57 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHlpMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINIltiglhdlrsrlSI 1320
Cdd:PRK09452 15 VELRGISKSFDGK--EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI------------TH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1321 IPQEP----TMFEG-------TVRSNLD--------PLEEYADdQIWEALDKCQLGDEIRKKELKLdspvsengqnwSVG 1381
Cdd:PRK09452 81 VPAENrhvnTVFQSyalfphmTVFENVAfglrmqktPAAEITP-RVMEALRMVQLEEFAQRKPHQL-----------SGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1382 QRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLR--QHFSGCTVITIAH-RISSVIDSDMVLLLDQGLIEEHDS 1458
Cdd:PRK09452 149 QQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKalQRKLGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
250
....*....|....*....
gi 30682486 1459 PARLLEDKSSSFsklVAEY 1477
Cdd:PRK09452 229 PREIYEEPKNLF---VARF 244
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
727-829 |
3.59e-07 |
|
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: 52.76 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 727 LNKDLEVFPFRDQtvigeRGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAhTGSHLFKEVLLGLLR-NKTVIYVT 805
Cdd:cd03266 120 LADRLGMEELLDR-----RVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV-MATRALREFIRQLRAlGKCILFST 193
|
90 100
....*....|....*....|....*
gi 30682486 806 HQLEFLPE-ADLILVMKDGRITQAG 829
Cdd:cd03266 194 HIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
703-837 |
3.90e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 53.47 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 703 VEENILFGkPM-----QREWYQRVLEACSLNKDLEVFPFRDQtvigergINLSGGQKQRIQIARALYQDADIYLFDDPFS 777
Cdd:PRK13645 108 IEKDIAFG-PVnlgenKQEAYKKVPELLKLVQLPEDYVKRSP-------FELSGGQKRRVALAGIIAMDGNTLVLDEPTG 179
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30682486 778 AVDAhTGSHLFKEVLLGLLRN--KTVIYVTHQL-EFLPEADLILVMKDGRITQAGKYNEILES 837
Cdd:PRK13645 180 GLDP-KGEEDFINLFERLNKEykKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
960-1160 |
3.95e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes 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. 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 the chemical 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. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. 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: 349994 [Multi-domain] Cd Length: 294 Bit Score: 53.64 E-value: 3.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 960 STLILVYVFLATASSFCILVRAMLSAMTGFKIATELFNQMHFRIFRASMSFFDATPIGRILNRASTD----QSAVDLRLP 1035
Cdd:cd18550 39 VLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDvggaQSVVTGTLT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1036 SQFSNLAIAAVnilgIIGVMGQVAWQVLIVFIPVIAACTWYRQYYISAARELARLSGISRSPLVQHFSETLS--GITTIR 1113
Cdd:cd18550 119 SVVSNVVTLVA----TLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLSvsGALLVK 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 30682486 1114 SF----DQEPRFRTDIMRLndcySRLRFHAISAMEWLCFRLDLLSTVAFAL 1160
Cdd:cd18550 195 LFgredDEAARFARRSREL----RDLGVRQALAGRWFFAALGLFTAIGPAL 241
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1273-1463 |
4.18e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 54.59 E-value: 4.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1273 IVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSIIPQEPTMFEGTvrsnLDPLEEYADDQIWEA-L 1351
Cdd:PRK10522 354 LIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQL----LGPEGKPANPALVEKwL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1352 DKCQLGDEIRKKELKLDSPvsengqNWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTatdtliqeTLRQHF------- 1424
Cdd:PRK10522 430 ERLKMAHKLELEDGRISNL------KLSKGQKKRLALLLALAEERDILLLDEWAADQDP--------HFRREFyqvllpl 495
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 30682486 1425 ---SGCTVITIAHRISSVIDSDMVLLLDQGLIEEHDSPARLL 1463
Cdd:PRK10522 496 lqeMGKTIFAISHDDHYFIHADRLLEMRNGQLSELTGEERDA 537
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1264-1409 |
4.43e-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: 52.80 E-value: 4.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1264 TFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINIltiglhdlrsrlSIIPQEPTM-FEGTVRsnlDPLEEY 1342
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV------------SYKPQYIKAdYEGTVR---DLLSSI 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30682486 1343 ADDqiweALDKCQLGDEIrKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVLILDEATASVD 1409
Cdd:cd03237 86 TKD----FYTHPYFKTEI-AKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
749-837 |
4.52e-07 |
|
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: 54.31 E-value: 4.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGshlfKEVlLGLLR------NKTVIYVTHQL---EFLpeADLILV 819
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQ----AQI-LDLLRdlqrehGLAYLFISHDLavvRAL--AHRVMV 498
|
90
....*....|....*...
gi 30682486 820 MKDGRITQAGKYNEILES 837
Cdd:COG4172 499 MKDGKVVEQGPTEQVFDA 516
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1257-1303 |
5.06e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 52.78 E-value: 5.06e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 30682486 1257 VLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDG 1303
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG 87
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
705-835 |
5.66e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 52.61 E-value: 5.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 705 ENILFGKPMQR------EWYQRVLEAcslnkdLEVFPFRDQTV--IGERGINLSGGQKQRIQIARALYQDADIYLFDDPF 776
Cdd:PRK14247 101 ENVALGLKLNRlvkskkELQERVRWA------LEKAQLWDEVKdrLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPT 174
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30682486 777 SAVDAHTGSHLfKEVLLGLLRNKTVIYVTHqleFLPEA----DLILVMKDGRITQAGKYNEIL 835
Cdd:PRK14247 175 ANLDPENTAKI-ESLFLELKKDMTIVLVTH---FPQQAarisDYVAFLYKGQIVEWGPTREVF 233
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1270-1462 |
5.98e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 52.88 E-value: 5.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1270 KTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDLRSRLSIIPQEP--TMFEGTVRS-------NLDPLE 1340
Cdd:PRK13652 32 RIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQdiafgpiNLGLDE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1341 EYADDQIWEALDkcQLGDEirkkELKLDSPvsengQNWSVGQRQLVCLGRVLLKRSKVLILDEATASVD-TATDTLIQ-- 1417
Cdd:PRK13652 112 ETVAHRVSSALH--MLGLE----ELRDRVP-----HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDpQGVKELIDfl 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 30682486 1418 ETLRQHFsGCTVITIAHRISSVID-SDMVLLLDQGLIEEHDSPARL 1462
Cdd:PRK13652 181 NDLPETY-GMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEI 225
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
744-809 |
7.67e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 52.48 E-value: 7.67e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30682486 744 ERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAhTGSHLFKEVLLGLLRNKTVIYVTHQLE 809
Cdd:PRK14243 147 QSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDP-ISTLRIEELMHELKEQYTIIIVTHNMQ 211
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
744-806 |
8.58e-07 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 51.96 E-value: 8.58e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30682486 744 ERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLfkEVLLGLLRNK-TVIYVTH 806
Cdd:COG1117 150 KSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKI--EELILELKKDyTIVIVTH 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
748-826 |
9.63e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 53.10 E-value: 9.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 748 NLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAhtGShlfKEVLLGLLRN-----KTVIYVTHQlefLPE----ADLIL 818
Cdd:COG1129 394 NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDV--GA---KAEIYRLIRElaaegKAVIVISSE---LPEllglSDRIL 465
|
....*...
gi 30682486 819 VMKDGRIT 826
Cdd:COG1129 466 VMREGRIV 473
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
962-1118 |
9.97e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes 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. 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 the chemical 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. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. 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: 349984 [Multi-domain] Cd Length: 295 Bit Score: 52.10 E-value: 9.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 962 LILVYVFLATASSFCILVRAMLSAMTGFKIATELFNQMHFRIFRASMSFFDATPIGRILNRASTDQSAVDLRLPSQFSNL 1041
Cdd:cd18540 44 FILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1042 AIAAVNILGIIGVMGQVAWQV-LIVF--IPVIAACTWYRQYYI-SAARELARLSgisrSPLVQHFSETLSGITTIRSFDQ 1117
Cdd:cd18540 124 VWGITYMIGILIVMLILNWKLaLIVLavVPVLAVVSIYFQKKIlKAYRKVRKIN----SRITGAFNEGITGAKTTKTLVR 199
|
.
gi 30682486 1118 E 1118
Cdd:cd18540 200 E 200
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
703-780 |
1.01e-06 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 51.57 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 703 VEENIL----FGKPMQREWYQRvLEacSLNKDLEVFPFRDQtvigeRGINLSGGQKQRIQIARALYQDADIYLFDDPFSA 778
Cdd:COG1137 95 VEDNILavleLRKLSKKEREER-LE--ELLEEFGITHLRKS-----KAYSLSGGERRRVEIARALATNPKFILLDEPFAG 166
|
..
gi 30682486 779 VD 780
Cdd:COG1137 167 VD 168
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
680-820 |
1.05e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.27 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 680 SGNLKVCGRKAYIAQSPWIQSGKVEEniLFGKPMQREWYQRVLEACSLNKDLEvfpfrdqtvigeRGI-NLSGGQKQRIQ 758
Cdd:PRK13409 157 NGEIKVVHKPQYVDLIPKVFKGKVRE--LLKKVDERGKLDEVVERLGLENILD------------RDIsELSGGELQRVA 222
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30682486 759 IARALYQDADIYLFDDPFSAVDAH---TGSHLFKEvllgLLRNKTVIYVTHQ---LEFLpeADLILVM 820
Cdd:PRK13409 223 IAAALLRDADFYFFDEPTSYLDIRqrlNVARLIRE----LAEGKYVLVVEHDlavLDYL--ADNVHIA 284
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
749-824 |
1.05e-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: 49.75 E-value: 1.05e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgshlfKEVLLGLLRN--KTVIYVTHQLEFLPE-ADLILVMKDGR 824
Cdd:cd03221 71 LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLES-----IEALEEALKEypGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1273-1451 |
1.08e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.19 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1273 IVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINI-LTIGLHDLRSRLSIIPQEPTMF-EGTVRSNLdPLEEYADDQIWea 1350
Cdd:PRK10982 29 LMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdFKSSKEALENGISMVHQELNLVlQRSVMDNM-WLGRYPTKGMF-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1351 LDKCQLGDEIRK--KELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVLILDEATASV-DTATDTL--IQETLRQhfS 1425
Cdd:PRK10982 106 VDQDKMYRDTKAifDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLtEKEVNHLftIIRKLKE--R 183
|
170 180
....*....|....*....|....*..
gi 30682486 1426 GCTVITIAHRISSVID-SDMVLLLDQG 1451
Cdd:PRK10982 184 GCGIVYISHKMEEIFQlCDEITILRDG 210
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
744-825 |
1.11e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 51.94 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 744 ERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgSHLFKEVLLGLLRNK--TVIYVTHQLEF-LPEADLILVM 820
Cdd:PRK09984 148 QRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPES-ARIVMDTLRDINQNDgiTVVVTLHQVDYaLRYCERIVAL 226
|
....*
gi 30682486 821 KDGRI 825
Cdd:PRK09984 227 RQGHV 231
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1257-1434 |
1.17e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 53.19 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1257 VLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHDL----RSRLSIIPQE-------- 1324
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRyhllshlt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1325 -------PTMFEGTVRSNldpLEEYADdqiwEALDKCQLGDEIRKKELKLdspvsengqnwSVGQRQLVCLGRVLLKRSK 1397
Cdd:PRK10535 103 aaqnvevPAVYAGLERKQ---RLLRAQ----ELLQRLGLEDRVEYQPSQL-----------SGGQQQRVSIARALMNGGQ 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 30682486 1398 VLILDEATASVDTATDTLIQETLRQ-HFSGCTVITIAH 1434
Cdd:PRK10535 165 VILADEPTGALDSHSGEEVMAILHQlRDRGHTVIIVTH 202
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
749-837 |
1.26e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 51.59 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAhTGSHLFKEVLLGLLRNKTVIYVTHQLEFLPE-ADLILVMKDGRITQ 827
Cdd:PRK14246 154 LSGGQQQRLTIARALALKPKVLLMDEPTSMIDI-VNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVE 232
|
90
....*....|
gi 30682486 828 AGKYNEILES 837
Cdd:PRK14246 233 WGSSNEIFTS 242
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
750-835 |
1.42e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 51.47 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 750 SGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHlfkevLLGLLRNKT------VIYVTHQL---EFLpeADLILVM 820
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQAR-----LLDLLRGLVrelglaVVIVTHDLavaRLL--AHRLLVM 225
|
90
....*....|....*
gi 30682486 821 KDGRITQAGKYNEIL 835
Cdd:PRK11701 226 KQGRVVESGLTDQVL 240
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1241-1463 |
1.59e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.79 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQV--RYGPHLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRI-----VEPAAGEIRIDGINILTIGLHD 1313
Cdd:PRK15134 6 LAIENLSVafRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1314 LR----SRLSIIPQEPTMfegtvrsNLDPL------------------EEYADDQIWEALDKcqLGdeIRKKELKL-DSP 1370
Cdd:PRK15134 86 LRgvrgNKIAMIFQEPMV-------SLNPLhtlekqlyevlslhrgmrREAARGEILNCLDR--VG--IRQAAKRLtDYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1371 vsengQNWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLR--QHFSGCTVITIAHRISSVID-SDMVLL 1447
Cdd:PRK15134 155 -----HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVRKlADRVAV 229
|
250
....*....|....*.
gi 30682486 1448 LDQGLIEEHDSPARLL 1463
Cdd:PRK15134 230 MQNGRCVEQNRAATLF 245
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
960-1118 |
1.60e-06 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. 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. 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.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 51.54 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 960 STLILVYVFLATASSFCILVRAMLsamtgFKIATELFN----QMHFR-IFRASMSFFDATPIGRILNRASTDQSAVDLRL 1034
Cdd:cd18784 36 SRAIIIMGLLAIASSVAAGIRGGL-----FTLAMARLNirirNLLFRsIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1035 pSQFSNLAIAA-VNILGIIGVMGQVAWQV-LIVFI--PVIAACT-WYRQYYISAARE----LARLSGISrsplvqhfSET 1105
Cdd:cd18784 111 -SLNLNIFLRSlVKAIGVIVFMFKLSWQLsLVTLIglPLIAIVSkVYGDYYKKLSKAvqdsLAKANEVA--------EET 181
|
170
....*....|...
gi 30682486 1106 LSGITTIRSFDQE 1118
Cdd:cd18784 182 ISSIRTVRSFANE 194
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
703-829 |
1.63e-06 |
|
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: 53.09 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 703 VEENILFGKPMQ-REWYQRVLEACSLNKDLEVFPFRDqtvigERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDA 781
Cdd:TIGR01257 1020 VAEHILFYAQLKgRSWEEAQLEMEAMLEDTGLHHKRN-----EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP 1094
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 30682486 782 HTGSHLFkEVLLGLLRNKTVIYVTHQLEflpEADL----ILVMKDGRITQAG 829
Cdd:TIGR01257 1095 YSRRSIW-DLLLKYRSGRTIIMSTHHMD---EADLlgdrIAIISQGRLYCSG 1142
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1245-1465 |
1.77e-06 |
|
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: 52.38 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1245 NLQVRYGPHLPM--VLRGLTCTFRGGLKTGIVGRTGCGKS----TLIQTLFRIVEPAAGEIRIDGINILTIGLHDLR--- 1315
Cdd:COG4172 11 DLSVAFGQGGGTveAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRrir 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1316 -SRLSIIPQEPtMfegtvrSNLDPL---EeyadDQIWEALdkcQL-----GDEIRKKELKL------DSPvsENGQNW-- 1378
Cdd:COG4172 91 gNRIAMIFQEP-M------TSLNPLhtiG----KQIAEVL---RLhrglsGAAARARALELlervgiPDP--ERRLDAyp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1379 ---SVGQRQLVCLGRVLLKRSKVLILDEATasvdTATDTLIQ----ETLR--QHFSGCTVITIAH------RIssvidSD 1443
Cdd:COG4172 155 hqlSGGQRQRVMIAMALANEPDLLIADEPT----TALDVTVQaqilDLLKdlQRELGMALLLITHdlgvvrRF-----AD 225
|
250 260
....*....|....*....|..
gi 30682486 1444 MVLLLDQGLIEEHDSPARLLED 1465
Cdd:COG4172 226 RVAVMRQGEIVEQGPTAELFAA 247
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
749-839 |
1.77e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 51.32 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSH---LFKEvlLGLLRNKTVIYVTHQL-EFLPEADLILVMKDGR 824
Cdd:PRK13646 146 MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQvmrLLKS--LQTDENKTIILVSHDMnEVARYADEVIVMKEGS 223
|
90
....*....|....*
gi 30682486 825 ITQAGKYNEILESGT 839
Cdd:PRK13646 224 IVSQTSPKELFKDKK 238
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
749-828 |
1.87e-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: 50.90 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGshlfkEVLLGLL------RNKTVIYVTHQLEFLPEADLILVMKD 822
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPTGNLDAATG-----EQIIDLLfelnreRGTTLVLVTHDPALAARCDRVLRLRA 221
|
....*.
gi 30682486 823 GRITQA 828
Cdd:COG4181 222 GRLVED 227
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
731-837 |
2.01e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 51.67 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 731 LEVFPFRdqtvigerginLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFkEVLLGLLR--NKTVIYVTHQL 808
Cdd:PRK11022 147 LDVYPHQ-----------LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQII-ELLLELQQkeNMALVLITHDL 214
|
90 100 110
....*....|....*....|....*....|
gi 30682486 809 EFLPE-ADLILVMKDGRITQAGKYNEILES 837
Cdd:PRK11022 215 ALVAEaAHKIIVMYAGQVVETGKAHDIFRA 244
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1245-1470 |
2.23e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 51.64 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1245 NLQVRYGPHlpMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINIL--TIGLHDLrsrlSIIP 1322
Cdd:PRK11432 11 NITKRFGSN--TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVThrSIQQRDI----CMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1323 QE----PTMFEG-TVRSNLD----PLEEYADdQIWEALDKCQLG-------DEIrkkelkldspvsengqnwSVGQRQLV 1386
Cdd:PRK11432 85 QSyalfPHMSLGeNVGYGLKmlgvPKEERKQ-RVKEALELVDLAgfedryvDQI------------------SGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1387 CLGRVLLKRSKVLILDEATASVDTATDTLIQETLR---QHFsGCTVITIAHRISSVID-SDMVLLLDQGLIEEHDSPARL 1462
Cdd:PRK11432 146 ALARALILKPKVLLFDEPLSNLDANLRRSMREKIRelqQQF-NITSLYVTHDQSEAFAvSDTVIVMNKGKIMQIGSPQEL 224
|
....*...
gi 30682486 1463 LEDKSSSF 1470
Cdd:PRK11432 225 YRQPASRF 232
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1257-1434 |
2.36e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.04 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1257 VLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRI-DGInilTIGlhdlrsrlsIIPQEPTMFEG-TVRS 1334
Cdd:PRK11819 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGI---KVG---------YLPQEPQLDPEkTVRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1335 N-----------LDPLEE----YADD------------QIWEALDKCQLGDEIRKKE-----LKL---DSPVSengqNWS 1379
Cdd:PRK11819 90 NveegvaevkaaLDRFNEiyaaYAEPdadfdalaaeqgELQEIIDAADAWDLDSQLEiamdaLRCppwDAKVT----KLS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 30682486 1380 VGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLRQhFSGcTVITIAH 1434
Cdd:PRK11819 166 GGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHD-YPG-TVVAVTH 218
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
690-829 |
2.37e-06 |
|
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: 50.35 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 690 AYIAQSP-WIQSGKVEENILFGKPM-----QREWYQRVLEACSLNKDLEVFPFRDQTVIGerginLSGGQKQRIQIARAL 763
Cdd:cd03234 84 AYVRQDDiLLPGLTVRETLTYTAILrlprkSSDAIRKKRVEDVLLRDLALTRIGGNLVKG-----ISGGERRRVSIAVQL 158
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 764 YQDADIYLFDDPFSAVDAHTGSHLFKevLLGLL--RNKTVIYVTHQ--LEFLPEADLILVMKDGRITQAG 829
Cdd:cd03234 159 LWDPKVLILDEPTSGLDSFTALNLVS--TLSQLarRNRIVILTIHQprSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
748-824 |
2.76e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.85 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 748 NLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKevLLGLLRNKTV--IYVTHQLEFLPE-ADLILVMKDGR 824
Cdd:PRK13549 143 NLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLD--IIRDLKAHGIacIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1241-1485 |
2.90e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 50.47 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYG--PhlpmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINIltiglhdlrsrl 1318
Cdd:PRK11248 2 LQISHLYADYGgkP----ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1319 siipQEPTMFEGTVRSN------LDPLEEYADDQIWEALDKCQLGDEIRKKELKLDSPVSENGQNW--SVGQRQLVCLGR 1390
Cdd:PRK11248 66 ----EGPGAERGVVFQNegllpwRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWqlSGGQRQRVGIAR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1391 VLLKRSKVLILDEATASVDTATDTLIQETLRQ--HFSGCTVITIAHRISSVI--DSDMVLLldqglieeHDSPARLLEDK 1466
Cdd:PRK11248 142 ALAANPQLLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITHDIEEAVfmATELVLL--------SPGPGRVVERL 213
|
250 260
....*....|....*....|...
gi 30682486 1467 SSSFSKLVAEYTAS----SDSRF 1485
Cdd:PRK11248 214 PLNFARRFVAGESSrsikSDPQF 236
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
637-834 |
3.00e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.59 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 637 SPIPTLKDIRFKIPHGMNIAICGTVGSGKSSLLSSILGEVPKISGNLKVCGR--------KAY------IAQSPWI---Q 699
Cdd:PRK15439 22 SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpaKAHqlgiylVPQEPLLfpnL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 700 SgkVEENILFGKPMQREWYQRVLE-----ACSLNKD-----LEVfpfRDQtvigerginlsggqkQRIQIARALYQDADI 769
Cdd:PRK15439 102 S--VKENILFGLPKRQASMQKMKQllaalGCQLDLDssagsLEV---ADR---------------QIVEILRGLMRDSRI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30682486 770 YLFDDPFSAVDAHTGSHLFKEvlLGLLRNKTV--IYVTHQlefLPE----ADLILVMKDGRITQAGKYNEI 834
Cdd:PRK15439 162 LILDEPTASLTPAETERLFSR--IRELLAQGVgiVFISHK---LPEirqlADRISVMRDGTIALSGKTADL 227
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
748-823 |
3.07e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 51.71 E-value: 3.07e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30682486 748 NLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFkeVLLGLLRN--KTVIYVTHQL-EFLPEADLILVMKDG 823
Cdd:PRK09700 145 NLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLF--LIMNQLRKegTAIVYISHKLaEIRRICDRYTVMKDG 221
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
924-1121 |
3.92e-06 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 50.52 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 924 IILVVQILFQVLNIGSNYWMAWVTP---VSKDVKPLVSGSTLILVYVFLATASSFcilVRAMLSAMTGFKIATELFNQMH 1000
Cdd:cd18570 6 LILLLSLLITLLGIAGSFFFQILIDdiiPSGDINLLNIISIGLILLYLFQSLLSY---IRSYLLLKLSQKLDIRLILGYF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1001 FRIFRASMSFFDATPIGRILNR---ASTDQSAVdlrlpsqfSNLAI-AAVNILGIIGVMGQVAWQ------VLIVFIPVI 1070
Cdd:cd18570 83 KHLLKLPLSFFETRKTGEIISRfndANKIREAI--------SSTTIsLFLDLLMVIISGIILFFYnwklflITLLIIPLY 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 30682486 1071 AACTW-YRQYYISAARELARLSGISRSPLVqhfsETLSGITTIRSFDQEPRF 1121
Cdd:cd18570 155 ILIILlFNKPFKKKNREVMESNAELNSYLI----ESLKGIETIKSLNAEEQF 202
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
681-780 |
5.43e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 49.67 E-value: 5.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 681 GNLKVCGRKAYIAQSPWIQSGKVEEniLFGKPMQREWYQRVLEACSLNKDLEvfpfrdqtvigeRGI-NLSGGQKQRIQI 759
Cdd:cd03236 85 GDVKVIVKPQYVDLIPKAVKGKVGE--LLKKKDERGKLDELVDQLELRHVLD------------RNIdQLSGGELQRVAI 150
|
90 100
....*....|....*....|.
gi 30682486 760 ARALYQDADIYLFDDPFSAVD 780
Cdd:cd03236 151 AAALARDADFYFFDEPSSYLD 171
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
690-815 |
5.62e-06 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 49.33 E-value: 5.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 690 AYIAQSPWIQSGKVEENILFgkPMQREwyQRVLEACSLNKDLEVFPFRDQTVigERGIN-LSGGQKQRIQIARALYQDAD 768
Cdd:PRK10247 84 SYCAQTPTLFGDTVYDNLIF--PWQIR--NQQPDPAIFLDDLERFALPDTIL--TKNIAeLSGGEKQRISLIRNLQFMPK 157
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 30682486 769 IYLFDDPFSAVDAHTgSHLFKEVLLGLLRNK--TVIYVTHQLEFLPEAD 815
Cdd:PRK10247 158 VLLLDEITSALDESN-KHNVNEIIHRYVREQniAVLWVTHDKDEINHAD 205
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
703-829 |
6.63e-06 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 49.06 E-value: 6.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 703 VEENILFGKPMQREWYQRVLEACslnkdLEVFPFRDQtVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPF-----S 777
Cdd:TIGR03410 92 VEENLLTGLAALPRRSRKIPDEI-----YELFPVLKE-MLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTegiqpS 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 30682486 778 AVD--AHTGSHLFKEvllgllRNKTVIYVTHQLEFLPE-ADLILVMKDGRITQAG 829
Cdd:TIGR03410 166 IIKdiGRVIRRLRAE------GGMAILLVEQYLDFARElADRYYVMERGRVVASG 214
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
739-830 |
6.71e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 50.82 E-value: 6.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 739 QTVIGERGI--NLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKeVLLGL-LRNKTVIYVTHQleflPEAD 815
Cdd:TIGR00955 155 NTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQ-VLKGLaQKGKTIICTIHQ----PSSE 229
|
90 100
....*....|....*....|.
gi 30682486 816 L------ILVMKDGRITQAGK 830
Cdd:TIGR00955 230 LfelfdkIILMAEGRVAYLGS 250
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
749-837 |
6.97e-06 |
|
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: 49.67 E-value: 6.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDahtgshlfkeVL-----LGLLR------NKTVIYVTHQLEFLPE-ADL 816
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALD----------VTiqaqiLNLLKdlqrelGLAILFITHDLGVVAEiADR 220
|
90 100
....*....|....*....|.
gi 30682486 817 ILVMKDGRITQAGKYNEILES 837
Cdd:COG0444 221 VAVMYAGRIVEEGPVEELFEN 241
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1268-1449 |
7.16e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 47.37 E-value: 7.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1268 GLKTGIVGRTGCGKSTLIQTLfrivepaAGEIRIDGINILTIGlhdlrsrlsiipqeptmfegtvrsnldpleeyaddqi 1347
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARAL-------ARELGPPGGGVIYID------------------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1348 wealdkcqlGDEIRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRS--KVLILDEATASVDTATDTLIQETLR---- 1421
Cdd:smart00382 38 ---------GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLkpDVLILDEITSLLDAEQEALLLLLEElrll 108
|
170 180 190
....*....|....*....|....*....|.
gi 30682486 1422 ---QHFSGCTVITIAHRISSVIDSDMVLLLD 1449
Cdd:smart00382 109 lllKSEKNLTVILTTNDEKDLGPALLRRRFD 139
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
749-825 |
8.23e-06 |
|
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: 48.32 E-value: 8.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHlfkevLLGLLR-----NKTVIYVTHQL--EFLPEADLILVMK 821
Cdd:cd03213 112 LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ-----VMSLLRrladtGRTIICSIHQPssEIFELFDKLLLLS 186
|
....
gi 30682486 822 DGRI 825
Cdd:cd03213 187 QGRV 190
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
747-846 |
8.24e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 47.95 E-value: 8.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 747 INLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEVL-LGLLRNKTVIYVTHQLEFLPE-ADLILVM--KD 822
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRrLSEEGKKTALVVEHDLAVLDYlSDRIHVFegEP 149
|
90 100
....*....|....*....|....
gi 30682486 823 GRITQAGKYNEILESGTDFMELVG 846
Cdd:cd03222 150 GVYGIASQPKGTREGINRFLRGYL 173
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1247-1462 |
1.01e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 48.93 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1247 QVRYGPHLPMVlRGLTCTFRGGLKTGIVGRTGCGKS----TLIQTLFRIVEPAAGEIRIDGINILtigLHDLRSRL-SII 1321
Cdd:PRK10418 9 NIALQAAQPLV-HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVA---PCALRGRKiATI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1322 PQEPtmfegtvRSNLDPLEEYA---------------DDQIWEALDKCQLGDeiRKKELKLdSPVSENGqnwSVGQRQLV 1386
Cdd:PRK10418 85 MQNP-------RSAFNPLHTMHtharetclalgkpadDATLTAALEAVGLEN--AARVLKL-YPFEMSG---GMLQRMMI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1387 CLGrvLLKRSKVLILDEATASVDTATDT----LIQETLRQHFSGCTVITiaHRISSVID-SDMVLLLDQGLIEEHDSPAR 1461
Cdd:PRK10418 152 ALA--LLCEAPFIIADEPTTDLDVVAQArildLLESIVQKRALGMLLVT--HDMGVVARlADDVAVMSHGRIVEQGDVET 227
|
.
gi 30682486 1462 L 1462
Cdd:PRK10418 228 L 228
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
748-825 |
1.02e-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: 48.59 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 748 NLSGGQKQRIQIARALYQDADIYLFDDPFSAVdahtgSHLFKEVLLGLLRN-----KTVIYVTHQLEFLPE-ADLILVMK 821
Cdd:cd03219 143 ELSYGQQRRLEIARALATDPKLLLLDEPAAGL-----NPEETEELAELIRElrergITVLLVEHDMDVVMSlADRVTVLD 217
|
....
gi 30682486 822 DGRI 825
Cdd:cd03219 218 QGRV 221
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1257-1453 |
1.03e-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: 47.91 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1257 VLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTL--FRIVEPAAGEIRIDGINILTIGLHDlRSRLSII--PQEPTMFEGTv 1332
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEE-RARLGIFlaFQYPPEIPGV- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1333 rSNLDPLEEyaddqiweaLDKCQLGDEIRKKELkldspvsengqnwsvgqRQLVCLgrvllkRSKVLILDEATASVDTAT 1412
Cdd:cd03217 93 -KNADFLRY---------VNEGFSGGEKKRNEI-----------------LQLLLL------EPDLAILDEPDSGLDIDA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 30682486 1413 DTLIQETLRQ-HFSGCTVITIAH--RISSVIDSDMVLLLDQGLI 1453
Cdd:cd03217 140 LRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRI 183
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1257-1449 |
1.08e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.94 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1257 VLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINI-------LTIGLHDLRSRLsiipqeptmfE 1329
Cdd:PRK13541 15 NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNInniakpyCTYIGHNLGLKL----------E 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1330 GTVRSNLDPLEEYAD--DQIWEALDKCQLGDEIRKKELKLDSpvsengqnwsvGQRQLVCLGRVLLKRSKVLILDEATAS 1407
Cdd:PRK13541 85 MTVFENLKFWSEIYNsaETLYAAIHYFKLHDLLDEKCYSLSS-----------GMQKIVAIARLIACQSDLWLLDEVETN 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 30682486 1408 VDTATDTLIQETLRQHFSGCTVITIAHRISSVIDSDMVLLLD 1449
Cdd:PRK13541 154 LSKENRDLLNNLIVMKANSGGIVLLSSHLESSIKSAQILQLD 195
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
748-845 |
1.21e-05 |
|
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: 49.80 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 748 NLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgSHLFKEVLLGLLRNK--TVIYVTHQLEFLPE-ADLILVMKDGR 824
Cdd:TIGR03269 168 DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQT-AKLVHNALEEAVKASgiSMVLTSHWPEVIEDlSDKAIWLENGE 246
|
90 100
....*....|....*....|.
gi 30682486 825 ITQAGKYNEILESgtdFMELV 845
Cdd:TIGR03269 247 IKEEGTPDEVVAV---FMEGV 264
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
749-837 |
1.30e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 48.55 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLfKEVLLGLLRNKTVIYVTHQLEFLPE-ADLILVMKDGRITQ 827
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKI-EEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVE 242
|
90
....*....|
gi 30682486 828 AGKYNEILES 837
Cdd:PRK14271 243 EGPTEQLFSS 252
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
749-821 |
1.47e-05 |
|
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: 46.97 E-value: 1.47e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30682486 749 LSGGQKQRIQIARAL----YQDADIYLFDDPFSAVDAHTGSHLFKEVLLGLLRNKTVIYVTHQLEFLPEADLILVMK 821
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIK 154
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1257-1451 |
1.61e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 47.65 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1257 VLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVE--PAAGEIRIDGINIltiglhdlrsrlsiiPQEPTMFEgtvrs 1334
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQF---------------GREASLID----- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1335 NLDPLEEYadDQIWEALDKCQLGDEI----RKKELkldspvsengqnwSVGQRQLVCLGRVLLKRSKVLILDEATASVDT 1410
Cdd:COG2401 105 AIGRKGDF--KDAVELLNAVGLSDAVlwlrRFKEL-------------STGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 30682486 1411 ATDTL----IQETLRQHfsGCTVITIAHR--ISSVIDSDMVLLLDQG 1451
Cdd:COG2401 170 QTAKRvarnLQKLARRA--GITLVVATHHydVIDDLQPDLLIFVGYG 214
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
622-846 |
1.71e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 48.51 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 622 MDVEVSNGAFSWDDSSPIPT--LKDIRFKIPHGMNIAICGTVGSGKSSLLSSILGEVPKISGNLKVCG------------ 687
Cdd:PRK13637 1 MSIKIENLTHIYMEGTPFEKkaLDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 688 -RK--AYIAQSPWIQ--SGKVEENILFGkPM-----QREWYQRVLEACSLNKdLEVFPFRDQTvigerGINLSGGQKQRI 757
Cdd:PRK13637 81 iRKkvGLVFQYPEYQlfEETIEKDIAFG-PInlglsEEEIENRVKRAMNIVG-LDYEDYKDKS-----PFELSGGQKRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 758 QIARALYQDADIYLFDDPFSAVDAHTGSHLFKEV-LLGLLRNKTVIYVTHQLEFLPE-ADLILVMKDGRITQAGKYNEIL 835
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIkELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREVF 233
|
250
....*....|.
gi 30682486 836 ESgTDFMELVG 846
Cdd:PRK13637 234 KE-VETLESIG 243
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
750-824 |
1.97e-05 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 47.43 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 750 SGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgshlfKEVLLGLLRNK-----TVIYVTHQLEFLPE-ADLILVMKDG 823
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAAN-----RAVVVELIEEAkargtAIIGIFHDEEVREAvADRVVDVTPF 228
|
.
gi 30682486 824 R 824
Cdd:COG4778 229 S 229
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
747-826 |
2.07e-05 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 49.03 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 747 INLSGGQKQRIQIARALYQDADIYLFD------DP-FSavdahtgsHLFKEVLLGLLR--NKTVIYVTHQLEFLPEADLI 817
Cdd:COG4615 456 TDLSQGQRKRLALLVALLEDRPILVFDewaadqDPeFR--------RVFYTELLPELKarGKTVIAISHDDRYFDLADRV 527
|
....*....
gi 30682486 818 LVMKDGRIT 826
Cdd:COG4615 528 LKMDYGKLV 536
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
750-834 |
2.33e-05 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 48.16 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 750 SGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGS---HLFKEVL--LGLlrnkTVIYVTHQLEFLPE-ADLILVMKDG 823
Cdd:PRK15079 163 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAqvvNLLQQLQreMGL----SLIFIAHDLAVVKHiSDRVLVMYLG 238
|
90
....*....|.
gi 30682486 824 RITQAGKYNEI 834
Cdd:PRK15079 239 HAVELGTYDEV 249
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
710-834 |
2.41e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 47.77 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 710 GKPMQREWYQRVLEACSLNKD---LEVFPFRdqtvigerginLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSH 786
Cdd:PRK10418 110 GKPADDATLTAALEAVGLENAarvLKLYPFE-----------MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQAR 178
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 30682486 787 LFkEVLLGLLRNKT--VIYVTHQLEFLPE-ADLILVMKDGRITQAGKYNEI 834
Cdd:PRK10418 179 IL-DLLESIVQKRAlgMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETL 228
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
680-780 |
2.56e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 48.63 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 680 SGNLKVCGRKAYIAQSPWIQSGKVEEniLFGKPMQREWYQRVLEACSLNKDLEvfpfRDqtvIGErginLSGGQKQRIQI 759
Cdd:COG1245 157 NGEIKVAHKPQYVDLIPKVFKGTVRE--LLEKVDERGKLDELAEKLGLENILD----RD---ISE----LSGGELQRVAI 223
|
90 100
....*....|....*....|.
gi 30682486 760 ARALYQDADIYLFDDPFSAVD 780
Cdd:COG1245 224 AAALLRDADFYFFDEPSSYLD 244
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
739-837 |
3.22e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 48.31 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 739 QTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKevLLGLLRNKT---VIYVTHQLEFLPE-A 814
Cdd:PRK10261 159 QTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQ--LIKVLQKEMsmgVIFITHDMGVVAEiA 236
|
90 100
....*....|....*....|...
gi 30682486 815 DLILVMKDGRITQAGKYNEILES 837
Cdd:PRK10261 237 DRVLVMYQGEAVETGSVEQIFHA 259
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
735-826 |
3.43e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.37 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 735 PFRDQTVIgergiNLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFkEVLLGLL-RNKTVIYVTHQL-EFLP 812
Cdd:PRK11288 388 PSREQLIM-----NLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIY-NVIYELAaQGVAVLFVSSDLpEVLG 461
|
90
....*....|....
gi 30682486 813 EADLILVMKDGRIT 826
Cdd:PRK11288 462 VADRIVVMREGRIA 475
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1005-1164 |
3.58e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes 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. 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 the chemical 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. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. 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: 350009 [Multi-domain] Cd Length: 313 Bit Score: 47.56 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1005 RASMSFFDATPIGRILNRASTDQSAVDlRLPSQFSNLAI-AAVNILGIIGVMGQVAWQ---VLIVFIPVIAACTWYRQ-- 1078
Cdd:cd18565 99 RLDMAFFEDRQTGDLMSVLNNDVNQLE-RFLDDGANSIIrVVVTVLGIGAILFYLNWQlalVALLPVPLIIAGTYWFQrr 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1079 ---YYISAARELARLSGisrsplvqHFSETLSGITTIRSFDQEPRFRTDIMRLNDCYSRLRFHAIsaMEWLCFR--LDLL 1153
Cdd:cd18565 178 iepRYRAVREAVGDLNA--------RLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAI--RLRAAFFpvIRLV 247
|
170
....*....|.
gi 30682486 1154 STVAFALSLVI 1164
Cdd:cd18565 248 AGAGFVATFVV 258
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
744-824 |
3.59e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.19 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 744 ERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKevLLGLLRNK--TVIYVTHQLEFLPE-ADLILVM 820
Cdd:PRK10982 130 AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFT--IIRKLKERgcGIVYISHKMEEIFQlCDEITIL 207
|
....
gi 30682486 821 KDGR 824
Cdd:PRK10982 208 RDGQ 211
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1273-1434 |
4.10e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.02 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1273 IVGRTGCGKSTLIQTLfrivepaAGEIRIDG--INILTiglhDLR-SRLSIIPqePTMFEGTVRSNL--------DPLEE 1341
Cdd:PRK11147 34 LVGRNGAGKSTLMKIL-------NGEVLLDDgrIIYEQ----DLIvARLQQDP--PRNVEGTVYDFVaegieeqaEYLKR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1342 Y-------ADD----------QIWEALDKC---QLGDEIRK--KELKL--DSPVSENGQNWsvgQRQlVCLGRVLLKRSK 1397
Cdd:PRK11147 101 YhdishlvETDpseknlnelaKLQEQLDHHnlwQLENRINEvlAQLGLdpDAALSSLSGGW---LRK-AALGRALVSNPD 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 30682486 1398 VLILDEATASVDTATdtlIQ--ETLRQHFSGcTVITIAH 1434
Cdd:PRK11147 177 VLLLDEPTNHLDIET---IEwlEGFLKTFQG-SIIFISH 211
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
749-843 |
4.15e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 47.05 E-value: 4.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHL---FKEV-LLGLlrnkTVIYVTHQLEFLPE-ADLILVMKDG 823
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELmtlFKKLhQSGM----TIVLVTHLMDDVANyADFVYVLEKG 221
|
90 100
....*....|....*....|
gi 30682486 824 RITQAGKYNEILESgTDFME 843
Cdd:PRK13649 222 KLVLSGKPKDIFQD-VDFLE 240
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
750-780 |
5.39e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 47.27 E-value: 5.39e-05
10 20 30
....*....|....*....|....*....|.
gi 30682486 750 SGGQKQRIQIARALYQDADIYLFDDPFSAVD 780
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
748-898 |
5.56e-05 |
|
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: 47.62 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 748 NLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEvllgLLRNK-TVIYVTHQLEFLPE-ADLILVMKDGR- 824
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERH----LQEYPgTVVAVTHDRYFLDNvAGWILELDRGRg 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 825 ITQAGKYNEILESGTDFMELVG----AHTDALAAVDSYEKGSASAQSTTSK------ESKVSNDEEKQEEDL-----PSP 889
Cdd:TIGR03719 237 IPWEGNYSSWLEQKQKRLEQEEkeesARQKTLKRELEWVRQSPKGRQAKSKarlaryEELLSQEFQKRNETAeiyipPGP 316
|
170
....*....|
gi 30682486 890 K-GQLVQEEE 898
Cdd:TIGR03719 317 RlGDKVIEAE 326
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1272-1453 |
6.00e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.62 E-value: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1272 GIVGRTGCGKSTLIQTLFRiVEPAA--GEIRIDG--INILT--------IGL--HDlRSRLSIIPQEPtmfegtVRSN-- 1335
Cdd:PRK13549 292 GIAGLVGAGRTELVQCLFG-AYPGRweGEIFIDGkpVKIRNpqqaiaqgIAMvpED-RKRDGIVPVMG------VGKNit 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1336 LDPLEEYAD-DQIWEALDKCQLGDEIRKKELKLDSPVSENGqNWSVGQRQLVCLGRVLLKRSKVLILDEATASVDTATD- 1413
Cdd:PRK13549 364 LAALDRFTGgSRIDDAAELKTILESIQRLKVKTASPELAIA-RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKy 442
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 30682486 1414 ---TLIQETLRQhfsGCTVITIAHRISSVID-SDMVLLLDQGLI 1453
Cdd:PRK13549 443 eiyKLINQLVQQ---GVAIIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1257-1463 |
7.30e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 46.36 E-value: 7.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1257 VLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLF-RIVEPAA-------GEIRIDGINILTIGLHDLRSRLSIIPQ--EPT 1326
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQaaQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1327 mFEGTVRSNL-----------DPLEEYADDQIWEALdkcQLGDEirkkelklDSPVSENGQNWSVGQRQLVCLGRVLLK- 1394
Cdd:PRK13547 96 -FAFSAREIVllgrypharraGALTHRDGEIAWQAL---ALAGA--------TALVGRDVTTLSGGELARVQFARVLAQl 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1395 --------RSKVLILDEATASVDTATDTLIQETLRQ-----HFSgctVITIAHRIS-SVIDSDMVLLLDQGLIEEHDSPA 1460
Cdd:PRK13547 164 wpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRlardwNLG---VLAIVHDPNlAARHADRIAMLADGAIVAHGAPA 240
|
...
gi 30682486 1461 RLL 1463
Cdd:PRK13547 241 DVL 243
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
703-824 |
7.53e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 47.13 E-value: 7.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 703 VEENILFGK----PMQREWY-QRVLEACSLNKDLEVFPFRDQTVIGERGinlsGGQKQRIQIARALYQDADIYLFDDPFS 777
Cdd:TIGR02633 95 VAENIFLGNeitlPGGRMAYnAMYLRAKNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEPSS 170
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 30682486 778 AVDAHTgshlfKEVLLGLLR-----NKTVIYVTHQL-EFLPEADLILVMKDGR 824
Cdd:TIGR02633 171 SLTEKE-----TEILLDIIRdlkahGVACVYISHKLnEVKAVCDTICVIRDGQ 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
749-825 |
7.72e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 45.93 E-value: 7.72e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLfKEVLLGLLRN--KTVIYVTHQLEFLPEADLILVMKDGRI 825
Cdd:PRK10584 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI-ADLLFSLNREhgTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
703-838 |
7.87e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.52 E-value: 7.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 703 VEENILFGKPMQrewyqrvleaCSLNKDLEVFPFRD------QTVI---------GERGINLSGGQKQRIQIARALY--- 764
Cdd:PRK00635 1649 VYEGKHFGQLLQ----------TPIEEVAETFPFLKkiqkplQALIdnglgylplGQNLSSLSLSEKIAIKIAKFLYlpp 1718
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30682486 765 QDADIYLFDDPFSAVDAHTGSHLFKEVLLGLLRNKTVIYVTHQLEFLPEADLILVMKDGritqAGKY-NEILESG 838
Cdd:PRK00635 1719 KHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQADYLIEMGPG----SGKTgGKILFSG 1789
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
748-778 |
7.97e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.09 E-value: 7.97e-05
10 20 30
....*....|....*....|....*....|.
gi 30682486 748 NLSGGQKQRIQIARALYQDADIYLFDDPfSA 778
Cdd:COG1245 455 DLSGGELQRVAIAACLSRDADLYLLDEP-SA 484
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
748-778 |
8.45e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.11 E-value: 8.45e-05
10 20 30
....*....|....*....|....*....|.
gi 30682486 748 NLSGGQKQRIQIARALYQDADIYLFDDPfSA 778
Cdd:PRK13409 453 DLSGGELQRVAIAACLSRDADLYLLDEP-SA 482
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
749-827 |
9.14e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.70 E-value: 9.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKevllgLLRN-----KTVIYVTHQL-EFLPEADLILVMKD 822
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYK-----VMRQladdgKVILMVSSELpEIITVCDRIAVFCE 484
|
....*
gi 30682486 823 GRITQ 827
Cdd:PRK09700 485 GRLTQ 489
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1249-1451 |
9.97e-05 |
|
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: 44.95 E-value: 9.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1249 RYGPHLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAA---GEIRIDGINILTIGLHdLRSRLSIIPQE- 1324
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEK-YPGEIIYVSEEd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1325 ---PTMfegTVRSNLDpleeyaddqiwEALdKCQLGDEIRKkelkldspvsengqnWSVGQRQLVCLGRVLLKRSKVLIL 1401
Cdd:cd03233 93 vhfPTL---TVRETLD-----------FAL-RCKGNEFVRG---------------ISGGERKRVSIAEALVSRASVLCW 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 30682486 1402 DEATASVDTATDTLIQETLRQ--HFSGCTVITIAHRISSVIDS--DMVLLLDQG 1451
Cdd:cd03233 143 DNSTRGLDSSTALEILKCIRTmaDVLKTTTFVSLYQASDEIYDlfDKVLVLYEG 196
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1379-1451 |
1.02e-04 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 45.77 E-value: 1.02e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30682486 1379 SVGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLR--QHFSGCTVITIAHRISSVID-SDMVLLLDQG 1451
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDYALRyCERIVALRQG 229
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
668-817 |
1.02e-04 |
|
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: 45.16 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 668 LLSSILGEVPKISGNLKVCGRK------------AYIAQSPWIQSG-KVEENILF-----GKPMQREWYQRVLEACSLNK 729
Cdd:COG4133 44 LLRILAGLLPPSAGEVLWNGEPirdaredyrrrlAYLGHADGLKPElTVRENLRFwaalyGLRADREAIDEALEAVGLAG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 730 DLEVfPFRdqtvigergiNLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHtGSHLFKEVLLGLLRN-KTVIYVTHQL 808
Cdd:COG4133 124 LADL-PVR----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA-GVALLAELIAAHLARgGAVLLTTHQP 191
|
....*....
gi 30682486 809 EFLPEADLI 817
Cdd:COG4133 192 LELAAARVL 200
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
748-806 |
1.05e-04 |
|
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: 45.48 E-value: 1.05e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 748 NLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEV-LLGLLRNKTVIYVTH 806
Cdd:cd03237 115 ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIrRFAENNEKTAFVVEH 174
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
742-840 |
1.26e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 45.41 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 742 IGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEVLLGLLRNK-TVIYVTH---QLEFLPEADLI 817
Cdd:PRK14258 144 IHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHnlhQVSRLSDFTAF 223
|
90 100
....*....|....*....|....*.
gi 30682486 818 LVMKDGRITQA---GKYNEILESGTD 840
Cdd:PRK14258 224 FKGNENRIGQLvefGLTKKIFNSPHD 249
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
750-811 |
1.34e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 1.34e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30682486 750 SGGQKQRIQIARALYQDADIYLFDDPFSAVDAHtgSHLFKEVLLgLLRNKTVIYVTHQLEFL 811
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLH--AVLWLETYL-LKWPKTFIVVSHAREFL 404
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
749-839 |
1.46e-04 |
|
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: 46.33 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEVLLGLLR-NKTVIYVTHQLEFLPE-ADLILVMKDGRIT 826
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDvCDRAALMRDGKIV 507
|
90
....*....|...
gi 30682486 827 QAGKYNEILESGT 839
Cdd:TIGR03269 508 KIGDPEEIVEELT 520
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
749-824 |
1.47e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 46.24 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHlfkevLLGLLR------NKTVIYVTHQLEFLPE-ADLILVMK 821
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQ-----ILQLLRelqqelNMGLLFITHNLSIVRKlADRVAVMQ 231
|
...
gi 30682486 822 DGR 824
Cdd:PRK15134 232 NGR 234
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
714-846 |
1.52e-04 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 45.38 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 714 QREWYQRVLEACSLnkdLEVFPFRDQTVIGerginLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEVLL 793
Cdd:PRK13638 110 EAEITRRVDEALTL---VDAQHFRHQPIQC-----LSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRR 181
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 30682486 794 GLLRNKTVIYVTHQLEFLPE-ADLILVMKDGRITQAGKYNEILeSGTDFMELVG 846
Cdd:PRK13638 182 IVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVF-ACTEAMEQAG 234
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
749-823 |
1.61e-04 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 46.34 E-value: 1.61e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKeVLLGLLRNKTVIYVTHQLEFLPEADLILVMKDG 823
Cdd:COG4178 486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQ-LLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
719-839 |
1.65e-04 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 45.16 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 719 QRVLEACSLnkdLEVFPFRDQTVIgergiNLSGGQKQRIQIARALYQDADIYLFDDPFSAVD-AHTgshlfKEVL----- 792
Cdd:PRK10575 126 EKVEEAISL---VGLKPLAHRLVD-----SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiAHQ-----VDVLalvhr 192
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 30682486 793 LGLLRNKTVIYVTHQLEFLPE-ADLILVMKDGRITQAGKYNEILESGT 839
Cdd:PRK10575 193 LSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMRGET 240
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
749-835 |
1.66e-04 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 45.36 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFkEVLLGLLRNK--TVIYVTHQL-EFLPEADLILVMKDGRI 825
Cdd:PRK10253 144 LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLL-ELLSELNREKgyTLAAVLHDLnQACRYASHLIALREGKI 222
|
90
....*....|
gi 30682486 826 TQAGKYNEIL 835
Cdd:PRK10253 223 VAQGAPKEIV 232
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
749-837 |
1.71e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 45.17 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKevLLGLLRNK---TVIYVTHQLEFLPE-ADLILVMKDGR 824
Cdd:PRK15112 150 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLIN--LMLELQEKqgiSYIYVTQHLGMMKHiSDQVLVMHQGE 227
|
90
....*....|...
gi 30682486 825 ITQAGKYNEILES 837
Cdd:PRK15112 228 VVERGSTADVLAS 240
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
963-1163 |
1.93e-04 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); 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: 350033 [Multi-domain] Cd Length: 289 Bit Score: 45.15 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 963 ILVYVFLATASSFCILVRAMLSAMTGFKIATELFNQMHFRIFRASMSFFDATPIGRILNRASTDQSAVDLRLPSQFSNLA 1042
Cdd:cd18589 39 ITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1043 IAAVNILGIIGVMGQVAWQVLIVFI---PVI-----AACTWYRQYYISAARELARLSGISrsplvqhfSETLSGITTIRS 1114
Cdd:cd18589 119 WYLARGLFLFIFMLWLSPKLALLTAlglPLLllvpkFVGKFQQSLAVQVQKSLARANQVA--------VETFSAMKTVRS 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 30682486 1115 FDQE----PRFRTdimRLNDCYsrlrfhaisamewlcfRLDLLSTVAFALSLV 1163
Cdd:cd18589 191 FANEegeaQRYRQ---RLQKTY----------------RLNKKEAAAYAVSMW 224
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
994-1166 |
2.27e-04 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the 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 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. 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 by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. 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: 349993 [Multi-domain] Cd Length: 295 Bit Score: 44.75 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 994 ELFNQMHfrifRASMSFFDATPIGRILNRASTDqsavdLRLPSQFS-----NLAIAAVNILGIIGVMGQVAWQ---VLIV 1065
Cdd:cd18549 80 DLFEHLQ----KLSFSFFDNNKTGQLMSRITND-----LFDISELAhhgpeDLFISIITIIGSFIILLTINVPltlIVFA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1066 FIPVIAACTWYRQYYISAARELAR--LSGISrsplvQHFSETLSGITTIRSFDQEPRFRTDIMRLNDCYSRLRFHAISAM 1143
Cdd:cd18549 151 LLPLMIIFTIYFNKKMKKAFRRVRekIGEIN-----AQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAM 225
|
170 180
....*....|....*....|...
gi 30682486 1144 EWLCFRLDLLSTVafaLSLVILV 1166
Cdd:cd18549 226 AYFFSGMNFFTNL---LNLVVLV 245
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
747-827 |
2.49e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 45.35 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 747 INLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgSHLFKEVLLGLLR--NKTVIYVTHQLEFLPEADLILVMKDGR 824
Cdd:PRK10522 448 LKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHF-RREFYQVLLPLLQemGKTIFAISHDDHYFIHADRLLEMRNGQ 526
|
...
gi 30682486 825 ITQ 827
Cdd:PRK10522 527 LSE 529
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
961-1125 |
2.52e-04 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to 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. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 44.78 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 961 TLILVYVFLATASSFcilvRAMLSAMTGFKIATELFNQMHFRIFRASMSFFDATPIGRILNRASTD----QSAVDlrlps 1036
Cdd:cd18575 41 LLLAVALVLALASAL----RFYLVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDttliQTVVG----- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1037 qfSNLAIAAVNILGIIG--VM---------GQVAWQVLIVFIPVIAActwyrqyyisaARELARLSGISRSPL---VQHF 1102
Cdd:cd18575 112 --SSLSIALRNLLLLIGglVMlfitspkltLLVLLVIPLVVLPIILF-----------GRRVRRLSRASQDRLadlSAFA 178
|
170 180
....*....|....*....|....*..
gi 30682486 1103 SETLSGITTIRSFDQEP----RFRTDI 1125
Cdd:cd18575 179 EETLSAIKTVQAFTREDaerqRFATAV 205
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
739-836 |
2.69e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.49 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 739 QTVIGergiNLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEVLLGLLRNKTVIYVTHQL-EFLPEADLI 817
Cdd:PRK10982 386 RTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMpELLGITDRI 461
|
90 100
....*....|....*....|....
gi 30682486 818 LVMKDGRI-----TQAGKYNEILE 836
Cdd:PRK10982 462 LVMSNGLVagivdTKTTTQNEILR 485
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
749-837 |
2.71e-04 |
|
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: 45.45 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGshlfKEVlLGLLR------NKTVIYVTHQL----EFlpeADLIL 818
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQ----AQI-LDLLKdlqrelGMALLLITHDLgvvrRF---ADRVA 228
|
90
....*....|....*....
gi 30682486 819 VMKDGRITQAGKYNEILES 837
Cdd:COG4172 229 VMRQGEIVEQGPTAELFAA 247
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
719-780 |
3.20e-04 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 44.11 E-value: 3.20e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30682486 719 QRVLEACSLNKDLEVFPFRDQTvigerGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVD 780
Cdd:PRK10895 113 QREDRANELMEEFHIEHLRDSM-----GQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
964-1166 |
3.43e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 44.47 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 964 LVYVFLATASSFcilVRAMLSAMTGFKIATELFNQMHFRIFRASMSFFDATPIGRILNRASTDQsavdlRLPSQFSNLAI 1043
Cdd:cd18568 49 LIVGIFQILLSA---VRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRFQENQ-----KIRRFLTRSAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1044 -AAVNILGII---GVMGQVAWQ---VLIVFIPVIAACT-----WYRQYYISAARELARLSGisrsplvqHFSETLSGITT 1111
Cdd:cd18568 121 tTILDLLMVFiylGLMFYYNLQltlIVLAFIPLYVLLTllsspKLKRNSREIFQANAEQQS--------FLVEALTGIAT 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 30682486 1112 IRSFDQEPRFRtdiMRLNDCYSR---LRFHAisamEWLCFRLDLLSTVAFALSLVILV 1166
Cdd:cd18568 193 IKALAAERPIR---WRWENKFAKalnTRFRG----QKLSIVLQLISSLINHLGTIAVL 243
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
622-844 |
3.46e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 44.24 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 622 MDVEVSNGAFSWDDSSPIPT--LKDIRFKIPHGMNIAICGTVGSGKSSLLSSILGEVPKISG----------------NL 683
Cdd:PRK13634 1 MDITFQKVEHRYQYKTPFERraLYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGtvtigervitagkknkKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 684 KVCGRKAYIA-QSPWIQ--SGKVEENILFGkPM-----QREWYQR---VLEACSLNKD-LEVFPFrdqtvigergiNLSG 751
Cdd:PRK13634 81 KPLRKKVGIVfQFPEHQlfEETVEKDICFG-PMnfgvsEEDAKQKareMIELVGLPEElLARSPF-----------ELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 752 GQKQRIQIARALYQDADIYLFDDPFSAVDAHtGSHLFKEVLLGLLRNK--TVIYVTHQLEFLPE-ADLILVMKDGRITQA 828
Cdd:PRK13634 149 GQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK-GRKEMMEMFYKLHKEKglTTVLVTHSMEDAARyADQIVVMHKGTVFLQ 227
|
250
....*....|....*.
gi 30682486 829 GKYNEILESGTDFMEL 844
Cdd:PRK13634 228 GTPREIFADPDELEAI 243
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
735-826 |
3.52e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 44.99 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 735 PFRDQTvIGergiNLSGGQKQRIQIARALYQDADIYLFDDPFSAVDahTGSHlfKEVLlgLLRNK------TVIYVTHQL 808
Cdd:PRK10762 387 PSMEQA-IG----LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD--VGAK--KEIY--QLINQfkaeglSIILVSSEM 455
|
90
....*....|....*....
gi 30682486 809 -EFLPEADLILVMKDGRIT 826
Cdd:PRK10762 456 pEVLGMSDRILVMHEGRIS 474
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
703-806 |
4.13e-04 |
|
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: 43.55 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 703 VEENILF-----GKPmQREWYQRVLEAcslnkdLEVFPFRDQtvigERGI--NLSGGQKQRIQIARALYQDADIYLFDDP 775
Cdd:cd03292 95 VYENVAFalevtGVP-PREIRKRVPAA------LELVGLSHK----HRALpaELSGGEQQRVAIARAIVNSPTILIADEP 163
|
90 100 110
....*....|....*....|....*....|....
gi 30682486 776 FSAVDAHTGS---HLFKEVllgLLRNKTVIYVTH 806
Cdd:cd03292 164 TGNLDPDTTWeimNLLKKI---NKAGTTVVVATH 194
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
722-843 |
4.32e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 43.95 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 722 LEACSLNKDL-EVFPFRdqtvigerginLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEVLLGLLRNKT 800
Cdd:PRK13643 128 LEMVGLADEFwEKSPFE-----------LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQT 196
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 30682486 801 VIYVTHQLEFLPE-ADLILVMKDGRITQAGKYNEILESgTDFME 843
Cdd:PRK13643 197 VVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQE-VDFLK 239
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
749-836 |
5.70e-04 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 44.29 E-value: 5.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgshlfKEVLLGLLRN--KTVIYVTHQLEFLPE-ADLILVMKDGRI 825
Cdd:COG0488 433 LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET-----LEALEEALDDfpGTVLLVSHDRYFLDRvATRILEFEDGGV 507
|
90
....*....|..
gi 30682486 826 TQ-AGKYNEILE 836
Cdd:COG0488 508 REyPGGYDDYLE 519
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
748-836 |
5.75e-04 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 43.15 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 748 NLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHtgshlFKEVLLGLLRN-----KTVIYVTHQLEFLPE-ADLILVMK 821
Cdd:COG1134 146 TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAA-----FQKKCLARIRElresgRTVIFVSHSMGAVRRlCDRAIWLE 220
|
90
....*....|....*
gi 30682486 822 DGRITQAGKYNEILE 836
Cdd:COG1134 221 KGRLVMDGDPEEVIA 235
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
622-836 |
6.45e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 43.66 E-value: 6.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 622 MDVEVSNGAFSWDDSSPIPT--LKDIRFKIPHGMNIAICGTVGSGKSSLLSSILGEVPKISGNLKVCG------------ 687
Cdd:PRK13641 1 MSIKFENVDYIYSPGTPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 688 ---RK--AYIAQSPWIQ--SGKVEENILFG-----------KPMQREWYQRVleacSLNKDL-EVFPFrdqtvigergiN 748
Cdd:PRK13641 81 kklRKkvSLVFQFPEAQlfENTVLKDVEFGpknfgfsedeaKEKALKWLKKV----GLSEDLiSKSPF-----------E 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEVLLGLLRNKTVIYVTHQLEFLPE-ADLILVMKDGRITQ 827
Cdd:PRK13641 146 LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIK 225
|
....*....
gi 30682486 828 AGKYNEILE 836
Cdd:PRK13641 226 HASPKEIFS 234
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
749-840 |
7.00e-04 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 43.26 E-value: 7.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHtgshlFKEVLLGLLR------NKTVIYVTHQLEFLPE-ADLILVMK 821
Cdd:TIGR02769 151 LSGGQLQRINIARALAVKPKLIVLDEAVSNLDMV-----LQAVILELLRklqqafGTAYLFITHDLRLVQSfCQRVAVMD 225
|
90
....*....|....*....
gi 30682486 822 DGRITQAGKYNEILESGTD 840
Cdd:TIGR02769 226 KGQIVEECDVAQLLSFKHP 244
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1380-1446 |
8.37e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.62 E-value: 8.37e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30682486 1380 VGQRQLVCLGRVLLKRSKVLILDEATASVDTAtDT-----LIQEtLRQHfsGCTVITIAHR---ISSVIDSDMVL 1446
Cdd:NF040905 142 VGKQQLVEIAKALSKDVKLLILDEPTAALNEE-DSaalldLLLE-LKAQ--GITSIIISHKlneIRRVADSITVL 212
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
925-1122 |
8.98e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 43.22 E-value: 8.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 925 ILVVQILFQVLNIGSNYWMAWVT---PVSKDVKPLVsgsTLILVYVFLATASSFCILVRAM----LSAMTGFKIATELFN 997
Cdd:cd18567 7 ILLLSLALELFALASPLYLQLVIdevIVSGDRDLLT---VLAIGFGLLLLLQALLSALRSWlvlyLSTSLNLQWTSNLFR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 998 QMhfriFRASMSFFDATPIGRILNR-ASTD--QSAvdlrLPSQFSNLAIAAVNILGIIGVM----GQVAWQVLI-VFIPV 1069
Cdd:cd18567 84 HL----LRLPLSYFEKRHLGDIVSRfGSLDeiQQT----LTTGFVEALLDGLMAILTLVMMflysPKLALIVLAaVALYA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 30682486 1070 IAACTWYRqYYISAARELARLSGISRSplvqHFSETLSGITTIRSFDQEPRFR 1122
Cdd:cd18567 156 LLRLALYP-PLRRATEEQIVASAKEQS----HFLETIRGIQTIKLFGREAERE 203
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
726-840 |
9.20e-04 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 42.83 E-value: 9.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 726 SLNKDLEVF-----PFRDQT----------------VIGERGI------NLSGGQKQRIQIARALYQDADIYLFDDPFSA 778
Cdd:PRK11831 94 ALFTDMNVFdnvayPLREHTqlpapllhstvmmkleAVGLRGAaklmpsELSGGMARRAALARAIALEPDLIMFDEPFVG 173
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30682486 779 VDAHTGSHLFKEV-----LLGLlrnkTVIYVTHQL-EFLPEADLILVMKDGRITQAGKYNEiLESGTD 840
Cdd:PRK11831 174 QDPITMGVLVKLIselnsALGV----TCVVVSHDVpEVLSIADHAYIVADKKIVAHGSAQA-LQANPD 236
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1272-1409 |
1.04e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.64 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1272 GIVGRTGCGKSTLIQTLFRIVEPAAGEIridginiltiglhDLRSRLSIIPQE-PTMFEGTVRSNLDPLEEYADDQIW-- 1348
Cdd:PRK13409 369 GIVGPNGIGKTTFAKLLAGVLKPDEGEV-------------DPELKISYKPQYiKPDYDGTVEDLLRSITDDLGSSYYks 435
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30682486 1349 EALDKCQLgDEIrkkelkLDSPVSEngqnWSVGQRQLVCLGRVLLKRSKVLILDEATASVD 1409
Cdd:PRK13409 436 EIIKPLQL-ERL------LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1274-1462 |
1.10e-03 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 43.09 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1274 VGRTGCGKSTLIQTLFRIVEPAAGEIRIDG--INIL-----TIGL----HDLRSRLSIipqEPTMFEGTVRSNLDPLEey 1342
Cdd:PRK11000 35 VGPSGCGKSTLLRMIAGLEDITSGDLFIGEkrMNDVppaerGVGMvfqsYALYPHLSV---AENMSFGLKLAGAKKEE-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1343 ADDQIWEALDKCQLGD--EIRKKELkldspvsengqnwSVGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQ-ET 1419
Cdd:PRK11000 110 INQRVNQVAEVLQLAHllDRKPKAL-------------SGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRiEI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 30682486 1420 LRQHFS-GCTVITIAH-RISSVIDSDMVLLLDQGLIEEHDSPARL 1462
Cdd:PRK11000 177 SRLHKRlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
750-834 |
1.19e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 42.79 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 750 SGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFkeVLLGLLR---NKTVIYVTHQLEFLPE-ADLILVMKDGRI 825
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIM--TLLNELKrefNTAIIMITHDLGVVAGiCDKVLVMYAGRT 240
|
....*....
gi 30682486 826 TQAGKYNEI 834
Cdd:PRK09473 241 MEYGNARDV 249
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
748-843 |
1.19e-03 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 43.13 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 748 NLSGGQKQRIQIARALYQDADIYLFDDPfsavdahTgSHL-------FKEVLLGllRNKTVIYVTHQLEFLPE-ADLILV 819
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEP-------T-NHLdlesiewLEEFLKN--YPGTVLVVSHDRYFLDRvATRILE 221
|
90 100
....*....|....*....|....*
gi 30682486 820 MKDGRITQ-AGKYneilesgTDFME 843
Cdd:COG0488 222 LDRGKLTLyPGNY-------SAYLE 239
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1241-1342 |
1.23e-03 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 42.44 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGPHLpmVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTI---GLHDLRSR 1317
Cdd:PRK11831 8 VDMRGVSFTRGNRC--IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMsrsRLYTVRKR 85
|
90 100
....*....|....*....|....*..
gi 30682486 1318 LSIIPQEPTMF-EGTVRSNLD-PLEEY 1342
Cdd:PRK11831 86 MSMLFQSGALFtDMNVFDNVAyPLREH 112
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1257-1467 |
1.30e-03 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 42.17 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1257 VLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILTIGLHD-LRSRLSIIPQEPTMFEG-TVRS 1334
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAIVPEGRRVFSRmTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1335 NLDPLEEYADDQIWEALDKcqlgdeiRKKEL--KLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKVLILDEatASVDTAT 1412
Cdd:PRK11614 100 NLAMGGFFAERDQFQERIK-------WVYELfpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDE--PSLGLAP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30682486 1413 DTLIQ-----ETLRQHfsGCTVITIAHRISSVID-SDMVLLLDQGLIEEHDSPARLLEDKS 1467
Cdd:PRK11614 171 IIIQQifdtiEQLREQ--GMTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDALLANEA 229
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
639-826 |
1.36e-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: 41.93 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 639 IPTLKDIRFKIPHGMNIAICGTVGSGKSSLLSSILGEVPKISGNLKVCGRKayiaqsPWIQSGKVEENI--LFGKPMQRE 716
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV------PWKRRKKFLRRIgvVFGQKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 717 WYQRVLEACSLNKD-------------------LEVFPFRDQTVigeRgiNLSGGQKQRIQIARALYQDADIYLFDDPFS 777
Cdd:cd03267 108 WDLPVIDSFYLLAAiydlpparfkkrldelselLDLEELLDTPV---R--QLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 30682486 778 AVDAHTgshlfKEVLLGLLR--NK----TVIYVTHQL---EFLpeADLILVMKDGRIT 826
Cdd:cd03267 183 GLDVVA-----QENIRNFLKeyNRergtTVLLTSHYMkdiEAL--ARRVLVIDKGRLL 233
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1272-1445 |
1.49e-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: 43.23 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1272 GIVGRTGCGKSTLIQTLFRIVEPAAGEIridginiltiglhDLRSRLSIIPQEPTM-FEGTVRSNL-DPLEEYADDQIWE 1349
Cdd:COG1245 370 GIVGPNGIGKTTFAKILAGVLKPDEGEV-------------DEDLKISYKPQYISPdYDGTVEEFLrSANTDDFGSSYYK 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1350 AldkcqlgdEI-RKKELK--LDSPVSEngqnWSVGQRQLVCLGRVLLKRSKVLILDEATASVD----TATDTLIQETLRQ 1422
Cdd:COG1245 437 T--------EIiKPLGLEklLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrLAVAKAIRRFAEN 504
|
170 180
....*....|....*....|....*..
gi 30682486 1423 HfsGCTVITIAHRIsSVID--SD--MV 1445
Cdd:COG1245 505 R--GKTAMVVDHDI-YLIDyiSDrlMV 528
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
703-823 |
1.85e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 42.68 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 703 VEENILFGK----PMQR-EWYQRVLEACSLNKDLEVfPFRDQTVIGErginLSGGQKQRIQIARALYQDADIYLFDDPFS 777
Cdd:PRK10762 96 IAENIFLGRefvnRFGRiDWKKMYAEADKLLARLNL-RFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTD 170
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 30682486 778 AV-DAHTGShLFKevLLGLLRNKT--VIYVTHQL-EFLPEADLILVMKDG 823
Cdd:PRK10762 171 ALtDTETES-LFR--VIRELKSQGrgIVYISHRLkEIFEICDDVTVFRDG 217
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
749-825 |
1.90e-03 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 41.98 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKevLLGLLRNKT---VIYVTHQLEFLPE-ADLILVMKDGR 824
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIR--LLKKLQQQFgtaCLFITHDLRLVERfCQRVMVMDNGQ 229
|
.
gi 30682486 825 I 825
Cdd:PRK10419 230 I 230
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
749-807 |
1.94e-03 |
|
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: 41.32 E-value: 1.94e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAhTGSHLFKEVLLG-LLRNKTVIYVTHQ 807
Cdd:cd03231 126 LSAGQQRRVALARLLLSGRPLWILDEPTTALDK-AGVARFAEAMAGhCARGGMVVLTTHQ 184
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
749-780 |
1.94e-03 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 42.03 E-value: 1.94e-03
10 20 30
....*....|....*....|....*....|..
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVD 780
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
743-908 |
2.38e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.03 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 743 GERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEVLLGLLRNKTVIYVTHQLEFLPE-ADLILVMK 821
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQlAHELTVID 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 822 DGRITQAGKYNEI-LESGTDFMELVGAHT---DALAAVDSYEKGSASAQSTTSKESKVSNDEEKQEEDLPSPKGQLvqee 897
Cdd:NF000106 219 RGRVIADGKVDELkTKVGGRTLQIRPAHAaelDRMVGAIAQAGLDGIAGATADHEDGVVNVPIVSDEQLSAVVGML---- 294
|
170
....*....|.
gi 30682486 898 erekGKVGFTV 908
Cdd:NF000106 295 ----GERGFTI 301
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
642-835 |
2.89e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 41.37 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 642 LKDIRFKIPHGMNIAICGTVGSGKSSLLSSILGEVPKISGNLKVCG-------------RKA--YIAQSPWIQ--SGKVE 704
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpidysrkglmklRESvgMVFQDPDNQlfSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 705 ENILFGkPM-----QREWYQRVLEACslnKDLEVFPFRDQTVIGerginLSGGQKQRIQIARALYQDADIYLFDDPFSAV 779
Cdd:PRK13636 102 QDVSFG-AVnlklpEDEVRKRVDNAL---KRTGIEHLKDKPTHC-----LSFGQKKRVAIAGVLVMEPKVLVLDEPTAGL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30682486 780 DAHTGSHLFKEVL-----LGLlrnkTVIYVTHQLEFLP-EADLILVMKDGRITQAGKYNEIL 835
Cdd:PRK13636 173 DPMGVSEIMKLLVemqkeLGL----TIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1241-1434 |
3.14e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.08 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1241 ITICNLQVRYGphLPMVLRGLTCTFRGGLKTGIVGRTGCGKSTLIQTLfrivepaAGEIRIDGINILTIGlhdlRSRLSI 1320
Cdd:PRK10636 2 IVFSSLQIRRG--VRVLLDNATATINPGQKVGLVGKNGCGKSTLLALL-------KNEISADGGSYTFPG----NWQLAW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1321 IPQE-PTMFEGTVRSNLDPLEEY---------ADDQ--------IWEALDKCQLGdEIRKK-----------ELKLDSPV 1371
Cdd:PRK10636 69 VNQEtPALPQPALEYVIDGDREYrqleaqlhdANERndghaiatIHGKLDAIDAW-TIRSRaasllhglgfsNEQLERPV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30682486 1372 SEngqnWSVGQRQLVCLGRVLLKRSKVLILDEATASVDtaTDTLIQ-ETLRQHFSGcTVITIAH 1434
Cdd:PRK10636 148 SD----FSGGWRMRLNLAQALICRSDLLLLDEPTNHLD--LDAVIWlEKWLKSYQG-TLILISH 204
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
978-1164 |
3.54e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 41.03 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 978 LVRAMLSAMTGFKIATELFNQMHFRIFRASMSFFDATPIGRILNR-ASTDQSAVDLRLPSQFSNLAIAAVNI-LGIIGVM 1055
Cdd:cd18566 60 LLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERlNSLEQIREFLTGQALLALLDLPFVLIfLGLIWYL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1056 GQVAWQVLIVFIPVIAACTWYRQYYISAA-RELARLSGISRSPLVqhfsETLSGITTIRSFDQEPRFRTDIMRLNDCYSR 1134
Cdd:cd18566 140 GGKLVLVPLVLLGLFVLVAILLGPILRRAlKERSRADERRQNFLI----ETLTGIHTIKAMAMEPQMLRRYERLQANAAY 215
|
170 180 190
....*....|....*....|....*....|....*.
gi 30682486 1135 LRF------HAISAMEWLCFRLDLLSTVAFALSLVI 1164
Cdd:cd18566 216 AGFkvakinAVAQTLGQLFSQVSMVAVVAFGALLVI 251
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1267-1464 |
3.65e-03 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 41.96 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1267 GGLKTG----IVGRTGCGKSTLIQTL-FRIvepaAGEIRIDG---INILTIGLHDLRSRLSIIpQEPTMFEG--TVRSNL 1336
Cdd:TIGR00955 46 GVAKPGellaVMGSSGAGKTTLMNALaFRS----PKGVKGSGsvlLNGMPIDAKEMRAISAYV-QQDDLFIPtlTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1337 D-------PLEEYAD------DQIWEA--LDKCQ---LGDEIRKKELkldspvsengqnwSVGQRQLVCLGRVLLKRSKV 1398
Cdd:TIGR00955 121 MfqahlrmPRRVTKKekrervDEVLQAlgLRKCAntrIGVPGRVKGL-------------SGGERKRLAFASELLTDPPL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30682486 1399 LILDEATASVDTAT-DTLIQETLRQHFSGCTVITIAHRISSVIDS--DMVLLLDQGLIEEHDSPARLLE 1464
Cdd:TIGR00955 188 LFCDEPTSGLDSFMaYSVVQVLKGLAQKGKTIICTIHQPSSELFElfDKIILMAEGRVAYLGSPDQAVP 256
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
749-814 |
3.66e-03 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 40.56 E-value: 3.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHtGSHLFKEVLLGLLRNK-TVIYVTHQ-LEFLPEA 814
Cdd:PRK13538 130 LSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ-GVARLEALLAQHAEQGgMVILTTHQdLPVASDK 196
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
927-1160 |
3.69e-03 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 41.24 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 927 VVQILFQVLNIGSNYWMAW-VTPVSKDVKPLVSGSTLILVYVFLATASSFCILVRAMLSAMTGFKIATELFNQMHFRIFR 1005
Cdd:cd18584 3 LLGLLAALLIIAQAWLLARiIAGVFLEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARLLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1006 ASMSFFDATPIGRILNRASTDQSAVDLRLpSQF-SNLAIAAVNILGIIGVMGQVAWQ---VLIVFIPVI----------- 1070
Cdd:cd18584 83 LGPALLRRQSSGELATLLTEGVDALDGYF-ARYlPQLVLAAIVPLLILVAVFPLDWVsalILLVTAPLIplfmiligkaa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1071 ---AActwyRQYyisaaRELARLSGisrsplvqHFSETLSGITTIRSFDQEPRFRTDIMRLNDCYSR-----LR--FhaI 1140
Cdd:cd18584 162 qaaSR----RQW-----AALSRLSG--------HFLDRLRGLPTLKLFGRARAQAARIARASEDYRRrtmkvLRvaF--L 222
|
250 260
....*....|....*....|
gi 30682486 1141 SAmewlcFRLDLLSTVAFAL 1160
Cdd:cd18584 223 SS-----AVLEFFATLSIAL 237
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
960-1134 |
4.38e-03 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 41.04 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 960 STLILVYVFLATASSFCILV---RAMLSAMTGFKIATELFNQMHFRIFRASMSFFDATPIGRILNRAStdqsavDLRLPS 1036
Cdd:cd18782 39 ATLYVIGVVMLVAALLEAVLtalRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRIS------ELDTIR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1037 QF-----SNLAIAAVNILGIIGVMGQVAWQ---VLIVFIPVIAACTWY------RQYyisaaRELARLSGISRSPLVqhf 1102
Cdd:cd18782 113 GFltgtaLTTLLDVLFSVIYIAVLFSYSPLltlVVLATVPLQLLLTFLfgpilrRQI-----RRRAEASAKTQSYLV--- 184
|
170 180 190
....*....|....*....|....*....|..
gi 30682486 1103 sETLSGITTIRSFDQEPRFRTdimRLNDCYSR 1134
Cdd:cd18782 185 -ESLTGIQTVKAQNAELKARW---RWQNRYAR 212
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1379-1470 |
5.43e-03 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 40.84 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 1379 SVGQRQLVCLGRVLLKRSKVLILDEATASVDTATDTLIQETLRQ-H----FsgcTVITIAHRISSVID-SDMVLLLDQGL 1452
Cdd:PRK10851 138 SGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQlHeelkF---TSVFVTHDQEEAMEvADRVVVMSQGN 214
|
90
....*....|....*...
gi 30682486 1453 IEEHDSPARLLEDKSSSF 1470
Cdd:PRK10851 215 IEQAGTPDQVWREPATRF 232
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
749-825 |
6.04e-03 |
|
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: 40.96 E-value: 6.04e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30682486 749 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEVLLGLLRNKTVIYVTHQL-EFLPEADLILVMKDGRI 825
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELaEVLGLSDRVLVIGEGKL 481
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
921-1123 |
6.47e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 40.19 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 921 LVPIILVVQILFQVLNIGSNYWMAWVT---PVSKDVKPLvsgSTLILVYVFLATASSFCILVRAMLSAMTGFKIATELFN 997
Cdd:cd18555 3 LLISILLLSLLLQLLTLLIPILTQYVIdnvIVPGNLNLL---NVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 998 QMHFRIFRASMSFFDATPIGRILNRAstdQSAVDLR--LPSQFSNLAIAAVNILGIIGVM----GQVAWQVLIVFIPVIA 1071
Cdd:cd18555 80 DFFEHLLKLPYSFFENRSSGDLLFRA---NSNVYIRqiLSNQVISLIIDLLLLVIYLIYMlyysPLLTLIVLLLGLLIVL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 30682486 1072 ACTWYRQYYisaaRELARLSGISRSPLVQHFSETLSGITTIRSFDQEPRFRT 1123
Cdd:cd18555 157 LLLLTRKKI----KKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYK 204
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
738-830 |
7.19e-03 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 41.02 E-value: 7.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 738 DQTVIGE---RGInlSGGQKQRIQIARALYQDADIYLFDDPFSAVDAhTGSHLFKEVLLGLL-RNKTVIYVTHQleflPE 813
Cdd:PLN03211 195 ENTIIGNsfiRGI--SGGERKRVSIAHEMLINPSLLILDEPTSGLDA-TAAYRLVLTLGSLAqKGKTIVTSMHQ----PS 267
|
90 100
....*....|....*....|...
gi 30682486 814 A------DLILVMKDGRITQAGK 830
Cdd:PLN03211 268 SrvyqmfDSVLVLSEGRCLFFGK 290
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
1241-1286 |
7.70e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 39.40 E-value: 7.70e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 30682486 1241 ITICNLqvrygphlpMVLRGLTCTFRGGLkTGIVGRTGCGKSTLIQ 1286
Cdd:pfam13476 1 LTIENF---------RSFRDQTIDFSKGL-TLITGPNGSGKTTILD 36
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
742-818 |
7.94e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 39.91 E-value: 7.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 742 IGERGINLSGGQKQRIQIARALYQDAD---IYLFDDPFSAVDAHTGSHLFkEVLLGLL-RNKTVIYVTHQLEFLPEADLI 817
Cdd:cd03271 163 LGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLL-EVLQRLVdKGNTVVVIEHNLDVIKCADWI 241
|
.
gi 30682486 818 L 818
Cdd:cd03271 242 I 242
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
644-807 |
9.34e-03 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 40.50 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 644 DIRFKIPHGMNIAICGTVGSGKSSLLSSILGEVPKISGNLKVC--GRKAYIAQSPWIQSGKVEENILFgkPMQREWYQR- 720
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPakGKLFYVPQRPYMTLGTLRDQIIY--PDSSEDMKRr 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682486 721 -----VLEACSLNKDLevfpfrdqTVIGERGIN----------LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGS 785
Cdd:TIGR00954 548 glsdkDLEQILDNVQL--------THILEREGGwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEG 619
|
170 180
....*....|....*....|....
gi 30682486 786 HLFKevllgLLRNK--TVIYVTHQ 807
Cdd:TIGR00954 620 YMYR-----LCREFgiTLFSVSHR 638
|
|
| |
