|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
36-1501 |
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: 1376.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 36 CFLRAAGSWVPPMYLWVLGPIYLLYIHRHGCCYLRMSRLFKIKMVLGFALI------LLYTFnaavplWRIHRGMPQAPE 109
Cdd:TIGR00957 26 CFQNTVLAWVPCFYLWVCFPCYFLYLSRHDRGYIQMTHLNKTKTALGFLLWivcwadLFYSF------WERSHGRAPAPV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 110 LLIHPTVWLTTMSFATFLIHMERKKGVRASGLLFGYWLL---CCLVPAIDTVQQASAGSFRQEPLHHLATYLCLSLVVAE 186
Cdd:TIGR00957 100 FLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLValvCALAILRSKILLALKEDAIVDPFRDTTFYIYFALVLSQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 187 LVLSCLVDQPPFFSEDSKPLNPCPEAEASFPSKAMFWWASGLLWKGYRKLLGPKDLWSLERENSSEELVSQLEREWRRNF 266
Cdd:TIGR00957 180 LVLSCFSDKSPLFSETNHDPNPCPESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKEC 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 267 SELPGHKGHSGMGTP---------------ETEAFL--QPERSQRGPLLRAIWRVFRSTFLLGTLSLVISDAFRFAVPKL 329
Cdd:TIGR00957 260 KKTRKQPVSAVYGKKdpskpkgssqldaneEVEALIvkSPHKPRKPSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQI 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 330 LSLFLEFMGDLESSAWTGWLLAVLMFLSACLQTLFEQQYMYRVKVLQMRLRTAITGLVYRKVLVLSSGSRKSSAAGDVVN 409
Cdd:TIGR00957 340 LSLLIRFVNDPMAPDWQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKSSTVGEIVN 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 410 LVSVDVQRLVESILHLNGLWLLFLWIIVCFVYLWQLLGPSALTAVAVFLSLLPLNFFITKKRSFHQEEQMRQKASRARLT 489
Cdd:TIGR00957 420 LMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLM 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 490 SSMLRTVRTIKSHGWECAFLERLLHIRGQELGALKTSAFLFSVSLVSFQVSTFLVALVVFAVHTLVAEDNAMDAEKAFVT 569
Cdd:TIGR00957 500 NEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENNILDAEKAFVS 579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 570 LTVLSILNKAQAFLPFSVHCLVQARVSFDRLAAFLCLEEVDPNGMVLSPSRCSSKDRISIHNGTFAWSQESPPCLHGINL 649
Cdd:TIGR00957 580 LALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGEGNSITVHNATFTWARDLPPTLNGITF 659
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 650 TVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGSVAYVPQEAWVQNTSVVENVCFRQELDLPWLQEVLEACAL 729
Cdd:TIGR00957 660 SIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACAL 739
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 730 GSDVASFPAGVHTPVGEQGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKQVIGPSGLLQGTTRILVT 809
Cdd:TIGR00957 740 LPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGVLKNKTRILVT 819
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 810 HTLHVLPQADQILVLANGTIAEMGSYQDLLHRNGALVGLL--------DGARQ---PAGEGEGEAHAAATSDDLGGFSGG 878
Cdd:TIGR00957 820 HGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLrtyapdeqQGHLEdswTALVSGEGKEAKLIENGMLVTDVV 899
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 879 GTPTRRPERPRPSDAAPVK---GSTSEAQMEPSlddVEVTGLTAGEDSVQYGRVKSATYLSYLRAVGTPLCTYTLFLFLC 955
Cdd:TIGR00957 900 GKQLQRQLSASSSDSGDQSrhhGSSAELQKAEA---KEETWKLMEADKAQTGQVELSVYWDYMKAIGLFITFLSIFLFVC 976
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 956 QQVASFCQGYWLSLWADDPVVDGKQMHSALRGSIFGLLGCLQAIGLFASMAAVFLGGARASCLLFRSLLWDVARSPIGFF 1035
Cdd:TIGR00957 977 NHVSALASNYWLSLWTDDPMVNGTQNNTSLRLSVYGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFF 1056
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1036 ERTPVGNLLNRFSKETDIVDVDIPDKMRTLLTYAFGLLEVGLAVSMATPLAIVAILPLMLLYAGFQSLYVATCCQLRRLE 1115
Cdd:TIGR00957 1057 ERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLE 1136
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1116 SASYSSVCSHLAETFQGSQVVRAFQAQGPFTAQHDALMDENQRISFPRLVADRWLAANLELLGNGLVFVAATCAVLSKAH 1195
Cdd:TIGR00957 1137 SVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHS 1216
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1196 LSAGLAGFSVSAALQVTQTLQWVVRSWTDLENSMVAVERVQDYVHTPKEAPWRLPSSAAQPLWPCGGQIEFRDFGLRHRP 1275
Cdd:TIGR00957 1217 LSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSGWPPRGRVEFRNYCLRYRE 1296
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1276 ELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRITIIPQDPVLFPGSL 1355
Cdd:TIGR00957 1297 DLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSL 1376
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1356 RMNLDLLQENTDEGIWAALETVQLKAFVTSLPGQLQYECSGQGDDLSVGQKQLLCLARALLRKTQILILDEATASVDPGT 1435
Cdd:TIGR00957 1377 RMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET 1456
|
1450 1460 1470 1480 1490 1500
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 1436 EIQMQAALERWFAQCTVLLIAHRLRSVMNCARVLVMDEGQVAESGSPAQLLAQKGLFYRLAQESGL 1501
Cdd:TIGR00957 1457 DNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSMAKDAGL 1522
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
207-1502 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 705.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 207 NPCPEAEASFPSKAMFWWASGLLWKGYRKLLGPKDLWSLERENSSEELVSQLEREWrrnfselpghkghsgmgtpeteaf 286
Cdd:PLN03232 225 NICPERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCW------------------------ 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 287 lqPERSQRGP--LLRAIWRVFRSTFLLGTLSLVISDAFRFAVPKLLSLFLEFM--GDlesSAWTGWLLAVLMFLSACLQT 362
Cdd:PLN03232 281 --TEESRRPKpwLLRALNNSLGGRFWLGGIFKIGHDLSQFVGPVILSHLLQSMqeGD---PAWVGYVYAFLIFFGVTFGV 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 363 LFEQQYMYRVKVLQMRLRTAITGLVYRKVLVLSSGSRKSSAAGDVVNLVSVDVQRLVESILHLNGLWLLFLWIIVCFVYL 442
Cdd:PLN03232 356 LCESQYFQNVGRVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 443 WQLLGPSALTAVAVFLSLLPLNFFITKKRSFHQEEQMRQKASRARLTSSMLRTVRTIKSHGWECAFLERLLHIRGQELGA 522
Cdd:PLN03232 436 YQQLGVASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSW 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 523 LKTSAFLFSVSlvSFQVSTF--LVALVVFAVHTLVAEDnaMDAEKAFVTLTVLSILNKAQAFLPFSVHCLVQARVSFDRL 600
Cdd:PLN03232 516 FRKAQLLSAFN--SFILNSIpvVVTLVSFGVFVLLGGD--LTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRI 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 601 AAFLCLEE--VDPNgmvlsPSRCSSKDRISIHNGTFAW-SQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGE 677
Cdd:PLN03232 592 EELLLSEEriLAQN-----PPLQPGAPAISIKNGYFSWdSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGE 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 678 LLKVE-GSVSIEGSVAYVPQEAWVQNTSVVENVCFRQELDLPWLQEVLEACALGSDVASFPAGVHTPVGEQGMNLSGGQK 756
Cdd:PLN03232 667 LSHAEtSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQK 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 757 QRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKQVIGPSglLQGTTRILVTHTLHVLPQADQILVLANGTIAEMGSYQ 836
Cdd:PLN03232 747 QRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDE--LKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFA 824
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 837 DlLHRNGALVGLLdgaRQPAGEGEGEAHAAATSDDLGGFSgggtptrrperprpsdaAPVKGSTSEAQMEPSLDDVEVTG 916
Cdd:PLN03232 825 E-LSKSGSLFKKL---MENAGKMDATQEVNTNDENILKLG-----------------PTVTIDVSERNLGSTKQGKRGRS 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 917 LTAGEDSVQYGRVKSATYLSYLRAVGTPLCTYTLFL-FLCQQVASFCQGYWLSLWADDPVVdgKQMHSALRGSIFGLLGC 995
Cdd:PLN03232 884 VLVKQEERETGIISWNVLMRYNKAVGGLWVVMILLVcYLTTEVLRVSSSTWLSIWTDQSTP--KSYSPGFYIVVYALLGF 961
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 996 LQAIGLFASMAAVFLGGARASCLLFRSLLWDVARSPIGFFERTPVGNLLNRFSKETDIVDVDIPDKMRTLLTYAFGLLEV 1075
Cdd:PLN03232 962 GQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLST 1041
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1076 GLAVSMATPLAIVAILPLMLLYAGFQSLYVATCCQLRRLESASYSSVCSHLAETFQGSQVVRAFQAQGPFTAQHDALMDE 1155
Cdd:PLN03232 1042 FALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDN 1121
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1156 NQRISFPRLVADRWLAANLELLGNGLVFVAATCAVL--SKAHLSAGLA---GFSVSAALQVTQTLQWVVRSWTDLENSMV 1230
Cdd:PLN03232 1122 NIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLrnGNAENQAGFAstmGLLLSYTLNITTLLSGVLRQASKAENSLN 1201
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1231 AVERVQDYVHTPKEAPWRLPSSAAQPLWPCGGQIEFRDFGLRHRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWG 1310
Cdd:PLN03232 1202 SVERVGNYIDLPSEATAIIENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNA 1281
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1311 LLRLQEATEGGIWIDGVPITDMGLHTLRSRITIIPQDPVLFPGSLRMNLDLLQENTDEGIWAALETVQLKAFVTSLPGQL 1390
Cdd:PLN03232 1282 LFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGL 1361
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1391 QYECSGQGDDLSVGQKQLLCLARALLRKTQILILDEATASVDPGTEIQMQAALERWFAQCTVLLIAHRLRSVMNCARVLV 1470
Cdd:PLN03232 1362 DAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILV 1441
|
1290 1300 1310
....*....|....*....|....*....|...
gi 13591916 1471 MDEGQVAESGSPAQLLAQKG-LFYRLAQESGLA 1502
Cdd:PLN03232 1442 LSSGQVLEYDSPQELLSRDTsAFFRMVHSTGPA 1474
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
209-1502 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 704.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 209 CPEAEASFPSKAMFWWASGLLWKGYRKLLGPKDLWSLERENSSEELVSQLEREWRRnfselpghkghsgmgtpeteaflq 288
Cdd:PLN03130 227 CPERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDE------------------------ 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 289 pERSQRGP-LLRAIWRVFRSTFLLGTLSLVISDAFRFAVPKLLSLFLEFMGDLESsAWTGWLLAVLMFLSACLQTLFEQQ 367
Cdd:PLN03130 283 -ELKKPKPwLLRALNNSLGGRFWLGGFFKIGNDLSQFVGPLLLNLLLESMQNGEP-AWIGYIYAFSIFVGVVLGVLCEAQ 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 368 YMYRVKVLQMRLRTAITGLVYRKVLVLSSGSRKSSAAGDVVNLVSVDVQRLVESILHLNGLWLLFLWIIVCFVYLWQLLG 447
Cdd:PLN03130 361 YFQNVMRVGFRLRSTLVAAVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLG 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 448 PSALTAVAVFLSLLPLNFFITKKRSFHQEEQMRQKASRARLTSSMLRTVRTIKSHGWECAFLERLLHIRGQELGALKTSA 527
Cdd:PLN03130 441 VASLIGSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQ 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 528 FLFSVSLVSFQVSTFLVALVVFAVHTLVAEDnaMDAEKAFVTLTVLSILNKAQAFLPFSVHCLVQARVSFDRLAAFLCLE 607
Cdd:PLN03130 521 LLSAFNSFILNSIPVLVTVVSFGVFTLLGGD--LTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLLAE 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 608 EvdpngMVLSPSRCSSKDR--ISIHNGTFAW-SQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVE-G 683
Cdd:PLN03130 599 E-----RVLLPNPPLEPGLpaISIKNGYFSWdSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdA 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 684 SVSIEGSVAYVPQEAWVQNTSVVENVCFRQELDLPWLQEVLEACALGSDVASFPAGVHTPVGEQGMNLSGGQKQRLSLAR 763
Cdd:PLN03130 674 SVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMAR 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 764 AVYRRAAVYLMDDPLAALDAHVSQEVFKQVIgpSGLLQGTTRILVTHTLHVLPQADQILVLANGTIAEMGSYQDLLHrNG 843
Cdd:PLN03130 754 AVYSNSDVYIFDDPLSALDAHVGRQVFDKCI--KDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSN-NG 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 844 ALVGLL---DGARQPAGEGEGEAHAAATSDDlggfsgggtptrrperPRPSDAAPVKGSTSEAQMEPSlddvEVTGLTAG 920
Cdd:PLN03130 831 PLFQKLmenAGKMEEYVEENGEEEDDQTSSK----------------PVANGNANNLKKDSSSKKKSK----EGKSVLIK 890
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 921 EDSVQYGRVKSATYLSYLRAVGTPLCTYTLFLF-LCQQVASFCQGYWLSLWADDpvvDGKQMHSAL-RGSIFGLLGCLQA 998
Cdd:PLN03130 891 QEERETGVVSWKVLERYKNALGGAWVVMILFLCyVLTEVFRVSSSTWLSEWTDQ---GTPKTHGPLfYNLIYALLSFGQV 967
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 999 IGLFASMAAVFLGGARASCLLFRSLLWDVARSPIGFFERTPVGNLLNRFSKETDIVDVDIPDKMRTLLTYAFGLLEVGLA 1078
Cdd:PLN03130 968 LVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVL 1047
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1079 VSMATPLAIVAILPLMLLYAGFQSLYVATCCQLRRLESASYSSVCSHLAETFQGSQVVRAFQAQGPFTAQHDALMDENQR 1158
Cdd:PLN03130 1048 IGIVSTISLWAIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEINGRSMDNNIR 1127
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1159 ISFPRLVADRWLAANLELLGNGLVFVAATCAVLSKAHLS-----AGLAGFSVSAALQVTQTLQWVVRSWTDLENSMVAVE 1233
Cdd:PLN03130 1128 FTLVNMSSNRWLAIRLETLGGLMIWLTASFAVMQNGRAEnqaafASTMGLLLSYALNITSLLTAVLRLASLAENSLNAVE 1207
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1234 RVQDYVHTPKEAPWRLPSSAAQPLWPCGGQIEFRDFGLRHRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLR 1313
Cdd:PLN03130 1208 RVGTYIDLPSEAPLVIENNRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFR 1287
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1314 LQEATEGGIWIDGVPITDMGLHTLRSRITIIPQDPVLFPGSLRMNLDLLQENTDEGIWAALETVQLKAFVTSLPGQLQYE 1393
Cdd:PLN03130 1288 IVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAE 1367
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1394 CSGQGDDLSVGQKQLLCLARALLRKTQILILDEATASVDPGTEIQMQAALERWFAQCTVLLIAHRLRSVMNCARVLVMDE 1473
Cdd:PLN03130 1368 VSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDA 1447
|
1290 1300 1310
....*....|....*....|....*....|
gi 13591916 1474 GQVAESGSPAQLLAQKG-LFYRLAQESGLA 1502
Cdd:PLN03130 1448 GRVVEFDTPENLLSNEGsAFSKMVQSTGAA 1477
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
270-1485 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 594.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 270 PGHKGHSGMGTPETEAFL-----------QPERSQRGPLLRAIWRVFRSTFLLGTLSLVISDAFRFAVPKLLSLFLEFMg 338
Cdd:PTZ00243 196 PEQSNMSTLEEPTDVRLYlsstgsvvrpgPPPTPKRLSLLRTLFAALPYYVWWQIPFKLLSDVCTLTLPVLLKYFVKFL- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 339 DLESSAWT-GWLLAVLMFLSACLQTLFEQQYMYRVKVLQMRLRTAITGLVYRKVLVLSSGS--RKSSAAGDVVNLVSVDV 415
Cdd:PTZ00243 275 DADNATWGrGLGLVLTLFLTQLIQSVCLHRFYYISIRCGLQYRSALNALIFEKCFTISSKSlaQPDMNTGRIINMMSTDV 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 416 QRLVESILHLNGLWLLFLWIIVCFVYLWQLLGPSALTAVAVFLSLLPLNFFITKKRSFHQEEQMRQKASRARLTSSMLRT 495
Cdd:PTZ00243 355 ERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSG 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 496 VRTIKSHGWECAFLERLLHIRGQELGALK---TSAFLFSvsLVSFQVSTFLVAlVVFAVHTLVAedNAMDAEKAFVTLTV 572
Cdd:PTZ00243 435 IRIAKFMAWEPCFVANIEDKRARELRYLRdvqLARVATS--FVNNATPTLMIA-VVFTVYYLLG--HELTPEVVFPTIAL 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 573 LSILNKAQAFLPFSVHCLVQARVSFDRLAAFL------------------------------------------------ 604
Cdd:PTZ00243 510 LGVLRMPFFMIPWVFTTVLQFLVSIKRISTFLecdnatcstvqdmeeywreqrehstacqlaavlenvdvtafvpvklpr 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 605 ----------------CLEEVDPNGMVLSPS---------RCSSKDRISIHNGTFAWSQESPP----------------- 642
Cdd:PTZ00243 590 apkvktsllsralrmlCCEQCRPTKRHPSPSvvvedtdygSPSSASRHIVEGGTGGGHEATPTsersaktpkmktddffe 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 643 -----CLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGSVAYVPQEAWVQNTSVVENVCFRQELDL 717
Cdd:PTZ00243 670 lepkvLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDA 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 718 PWLQEVLEACALGSDVASFPAGVHTPVGEQGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKQVIgpS 797
Cdd:PTZ00243 750 ARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECF--L 827
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 798 GLLQGTTRILVTHTLHVLPQADQILVLANGTIAEMGSYQDLLHRN---GALVGLLDGARQPAGEGEGEAHAAATSDDLGG 874
Cdd:PTZ00243 828 GALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTSlyaTLAAELKENKDSKEGDADAEVAEVDAAPGGAV 907
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 875 FSGGGtptrrperprpsdaaPVKGSTSEAQMEPSLDDVEVTGLTAGEDSVQyGRVKSATYLSYLRAV-GTPLCTYTLFLF 953
Cdd:PTZ00243 908 DHEPP---------------VAKQEGNAEGGDGAALDAAAGRLMTREEKAS-GSVPWSTYVAYLRFCgGLHAAGFVLATF 971
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 954 LCQQVASFCQGYWLSLWADDPvvdgkqmhsalrgsifglLGCLQAIGLFASMAAVFLGGA--------------RASCLL 1019
Cdd:PTZ00243 972 AVTELVTVSSGVWLSMWSTRS------------------FKLSAATYLYVYLGIVLLGTFsvplrfflsyeamrRGSRNM 1033
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1020 FRSLLWDVARSPIGFFERTPVGNLLNRFSKETDIVDVDIPDKMRTLLTYAFGLLEVGLAVSMATPLAIVAILPLMLLYAG 1099
Cdd:PTZ00243 1034 HRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYR 1113
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1100 FQSLYVATCCQLRRLESASYSSVCSHLAETFQGSQVVRAFQAQGPFTAQHDALMDENQRISFPRLVADRWLAANLELLGN 1179
Cdd:PTZ00243 1114 LMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSN 1193
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1180 GLVFVAA----TCAVLSKAHLSAGLAGFSVSAALQVTQTLQWVVRSWTDLENSMVAVERVQDYVH-TPKEA--------- 1245
Cdd:PTZ00243 1194 IVVTVIAligvIGTMLRATSQEIGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTDeVPHEDmpeldeevd 1273
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1246 -------------------PWRLPSSAAQPLWPcgGQIEFRDFGLRHRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSS 1306
Cdd:PTZ00243 1274 alerrtgmaadvtgtvviePASPTSAAPHPVQA--GSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKST 1351
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1307 LTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRITIIPQDPVLFPGSLRMNLDLLQENTDEGIWAALETVQLKAFVTSL 1386
Cdd:PTZ00243 1352 LLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASE 1431
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1387 PGQLQYECSGQGDDLSVGQKQLLCLARALLRKTQILIL-DEATASVDPGTEIQMQAALERWFAQCTVLLIAHRLRSVMNC 1465
Cdd:PTZ00243 1432 SEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQY 1511
|
1370 1380
....*....|....*....|
gi 13591916 1466 ARVLVMDEGQVAESGSPAQL 1485
Cdd:PTZ00243 1512 DKIIVMDHGAVAEMGSPREL 1531
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
210-1492 |
2.25e-128 |
|
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: 435.49 E-value: 2.25e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 210 PEAEASFPSKAMFWWASGLLWKGYRKLLGPKDLWSLERENSSEELVSQLEREWRRNFSElpghkghsgmgtpeteaflqp 289
Cdd:TIGR01271 5 PVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELAS--------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 290 erSQRGP-LLRAIWRVFRSTFLLGTLSLVISDAFRFAVPKLLS-LFLEFMGDLESSAWTGWLLAVLMFLSACLQTLFEQQ 367
Cdd:TIGR01271 64 --AKKNPkLLNALRRCFFWRFVFYGILLYFGEATKAVQPLLLGrIIASYDPFNAPEREIAYYLALGLCLLFIVRTLLLHP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 368 YMYRVKVLQMRLRTAITGLVYRKVLVLSSGSRKSSAAGDVVNLVSVDVQRLVESILHLNGLWLLFLWIIVCFVYLWQLLG 447
Cdd:TIGR01271 142 AIFGLHHLGMQMRIALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 448 PSALTAVAVFLSLLPLNFFITKKRSFHQEEQMRQKASRARLTSSMLRTVRTIKSHGWECAFLERLLHIRGQELGALKTSA 527
Cdd:TIGR01271 222 VNGFCGLGFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 528 FLFSVSLVSFQVSTFLVALVVFAVHTLVaedNAMDAEKAFVTLTVLSILNKAQAF-LPFSVHCLVQARVSFDRLAAFLCL 606
Cdd:TIGR01271 302 YLRYFYSSAFFFSGFFVVFLSVVPYALI---KGIILRRIFTTISYCIVLRMTVTRqFPGAIQTWYDSLGAITKIQDFLCK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 607 EE---VDPN-------------------GMVLSPSRCSSKDRiSIHNGT----FA-WSQESPPCLHGINLTVPQGCLLAV 659
Cdd:TIGR01271 379 EEyktLEYNltttevemvnvtaswdegiGELFEKIKQNNKAR-KQPNGDdglfFSnFSLYVTPVLKNISFKLEKGQLLAV 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 660 VGPVGAGKSSLLSALLGELLKVEGSVSIEGSVAYVPQEAWVQNTSVVENVCFRQELDLPWLQEVLEACALGSDVASFPAG 739
Cdd:TIGR01271 458 AGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEK 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 740 VHTPVGEQGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKQVIgpSGLLQGTTRILVTHTLHVLPQAD 819
Cdd:TIGR01271 538 DKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCL--CKLMSNKTRILVTSKLEHLKKAD 615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 820 QILVLANGTIAEMGSYQDLL----------------------HRNGALVGLL-------DGA------------RQP--- 855
Cdd:TIGR01271 616 KILLLHEGVCYFYGTFSELQakrpdfsslllgleafdnfsaeRRNSILTETLrrvsidgDSTvfsgpetikqsfKQPppe 695
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 856 AGEGEGEAHAAATSDDLGGFSGGGTPTRRPERPRPSDAAPVKGS------TSEAQMEPSLDDVEV--TGLT--------- 918
Cdd:TIGR01271 696 FAEKRKQSIILNPIASARKFSFVQMGPQKAQATTIEDAVREPSErkfslvPEDEQGEESLPRGNQyhHGLQhqaqrrqsv 775
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 919 --------AGEDSVQ------------------------YGRVKS------------------------------ATYLS 936
Cdd:TIGR01271 776 lqlmthsnRGENRREqlqtsfrkkssitqqnelaseldiYSRRLSkdsvyeiseeineedlkecfaderenvfetTTWNT 855
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 937 YLRAVGTP-----LCTYTLFLFLCQQVASFCqGYWLslWADDPV----VDGKQMHSALRGSIF----------------- 990
Cdd:TIGR01271 856 YLRYITTNrnlvfVLIFCLVIFLAEVAASLL-GLWL--ITDNPSapnyVDQQHANASSPDVQKpviitptsayyifyiyv 932
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 991 GLLGCLQAIGLFASMAAVFLGgARASCLLFRSLLWDVARSPIGFFERTPVGNLLNRFSKETDIVDVDIPDKMRTLLTYAF 1070
Cdd:TIGR01271 933 GTADSVLALGFFRGLPLVHTL-LTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTL 1011
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1071 GLLEVGLAVSMATPLAIVAILPLMLLYAGFQSLYVATCCQLRRLESASYSSVCSHLAETFQGSQVVRAFQAQGPF-TAQH 1149
Cdd:TIGR01271 1012 IVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFeTLFH 1091
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1150 DALmDENQRISFPRLVADRWLAANLELLGNgLVFVAATCAVLSKAHLSAGLAGFSVSAALQVTQTLQWVVRSWTDLENSM 1229
Cdd:TIGR01271 1092 KAL-NLHTANWFLYLSTLRWFQMRIDIIFV-FFFIAVTFIAIGTNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLM 1169
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1230 VAVERVQDYVHTPKEAP--------------WRLPSSAAQPLWPCGGQIEFRDFGLRHRPELPMAVQGVSLKIHAGEKVG 1295
Cdd:TIGR01271 1170 RSVSRVFKFIDLPQEEPrpsggggkyqlstvLVIENPHAQKCWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVG 1249
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1296 IVGRTGAGKSSLTWGLLRLQeATEGGIWIDGVPITDMGLHTLRSRITIIPQDPVLFPGSLRMNLDLLQENTDEGIWAALE 1375
Cdd:TIGR01271 1250 LLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAE 1328
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1376 TVQLKAFVTSLPGQLQYECSGQGDDLSVGQKQLLCLARALLRKTQILILDEATASVDPGTEIQMQAALERWFAQCTVLLI 1455
Cdd:TIGR01271 1329 EVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILS 1408
|
1450 1460 1470
....*....|....*....|....*....|....*..
gi 13591916 1456 AHRLRSVMNCARVLVMDEGQVAESGSPAQLLAQKGLF 1492
Cdd:TIGR01271 1409 EHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLF 1445
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
946-1238 |
9.28e-116 |
|
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: 366.03 E-value: 9.28e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 946 CTYTLFLFLCQQVASFCQGYWLSLWADDPVVDGKQ--MHSALRGSIFGLLGCLQAIGLFASMAAVFLGGARASCLLFRSL 1023
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSDDPALNGTQdtEQRDYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHNKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1024 LWDVARSPIGFFERTPVGNLLNRFSKETDIVDVDIPDKMRTLLTYAFGLLEVGLAVSMATPLAIVAILPLMLLYAGFQSL 1103
Cdd:cd18603 81 LHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1104 YVATCCQLRRLESASYSSVCSHLAETFQGSQVVRAFQAQGPFTAQHDALMDENQRISFPRLVADRWLAANLELLGNGLVF 1183
Cdd:cd18603 161 YVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLIVL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 13591916 1184 VAATCAVLSKAHLSAGLAGFSVSAALQVTQTLQWVVRSWTDLENSMVAVERVQDY 1238
Cdd:cd18603 241 FAALFAVLSRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEY 295
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
311-600 |
6.76e-110 |
|
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: 349.46 E-value: 6.76e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 311 LGTLSLVISDAFRFAVPKLLSLFLEFMGDLESSAWTGWLLAVLMFLSACLQTLFEQQYMYRVKVLQMRLRTAITGLVYRK 390
Cdd:cd18595 1 LAALLKLLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 391 VLVLSSGSRKSSAAGDVVNLVSVDVQRLVESILHLNGLWLLFLWIIVCFVYLWQLLGPSALTAVAVFLSLLPLNFFITKK 470
Cdd:cd18595 81 ALRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 471 RSFHQEEQMRQKASRARLTSSMLRTVRTIKSHGWECAFLERLLHIRGQELGALKTSAFLFSVSLVSFQVSTFLVALVVFA 550
Cdd:cd18595 161 IKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 13591916 551 VHTLVAEDNAMDAEKAFVTLTVLSILNKAQAFLPFSVHCLVQARVSFDRL 600
Cdd:cd18595 241 TYVLSDPDNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1262-1482 |
2.78e-104 |
|
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: 331.00 E-value: 2.78e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1262 GQIEFRDFGLRHRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRI 1341
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1342 TIIPQDPVLFPGSLRMNLDLLQENTDEGIWAALETVQLKAFVTSLPGQLQYECSGQGDDLSVGQKQLLCLARALLRKTQI 1421
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13591916 1422 LILDEATASVDPGTEIQMQAALERWFAQCTVLLIAHRLRSVMNCARVLVMDEGQVAESGSP 1482
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
948-1497 |
8.31e-99 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 329.82 E-value: 8.31e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 948 YTLFLFLCQQVASFCQ--GYWLSLWADDPVVDGKQMHSALR-GSIFGLLGCLQAIGLFASMAAVFLGGARASCLLFRSLL 1024
Cdd:COG1132 22 LLILALLLLLLSALLEllLPLLLGRIIDALLAGGDLSALLLlLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1025 WDVARSPIGFFERTPVGNLLNRFSKETDIVDVDIPDKMRTLLTYAFGLleVGLAVSMAT---PLAIVAILPlMLLYAGFQ 1101
Cdd:COG1132 102 EHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTL--IGALVVLFVidwRLALIVLLV-LPLLLLVL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1102 SLYVATCCQLRRLESASYSSVCSHLAETFQGSQVVRAFQAQGPFTAQHDALMDENQRISFPRLVADRWLAANLELLGN-G 1180
Cdd:COG1132 179 RLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNlG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1181 LVFVAATCAVL-SKAHLSAGLAGFSVSAALQVTQTLQWVVRSWTDLENSMVAVERVQDYVHTPKEAPwrlPSSAAQPLWP 1259
Cdd:COG1132 259 LALVLLVGGLLvLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIP---DPPGAVPLPP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1260 CGGQIEFRDFGLRHRPELPmAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRS 1339
Cdd:COG1132 336 VRGEIEFENVSFSYPGDRP-VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRR 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1340 RITIIPQDPVLFPGSLRMNLDLLQEN-TDEGIWAALETVQLKAFVTSLPGQLQYECSGQGDDLSVGQKQllclarallrK 1418
Cdd:COG1132 415 QIGVVPQDTFLFSGTIRENIRYGRPDaTDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQriaiarallkD 494
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13591916 1419 TQILILDEATASVDPGTEIQMQAALERWFAQCTVLLIAHRLRSVMNCARVLVMDEGQVAESGSPAQLLAQKGLFYRLAQ 1497
Cdd:COG1132 495 PPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYR 573
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
627-828 |
1.52e-87 |
|
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: 283.59 E-value: 1.52e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 627 ISIHNGTFAW---SQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGSVAYVPQEAWVQNT 703
Cdd:cd03250 1 ISVEDASFTWdsgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 704 SVVENVCFRQELDLPWLQEVLEACALGSDVASFPAGVHTPVGEQGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDA 783
Cdd:cd03250 81 TIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 13591916 784 HVSQEVFKQVIGPsGLLQGTTRILVTHTLHVLPQADQILVLANGT 828
Cdd:cd03250 161 HVGRHIFENCILG-LLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
311-600 |
1.77e-85 |
|
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: 281.30 E-value: 1.77e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 311 LGTLSLVISDAFRFAVPKLLSLFLEFMGDLES-SAWTGWLLAVLMFLSACLQTLFEQQYMYRVKVLQMRLRTAITGLVYR 389
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPDePLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 390 KVLVLSSGSRKSSAAGDVVNLVSVDVQRLVESILHLNGLWLLFLWIIVCFVYLWQLLGPSALTAVAVFLSLLPLNFFITK 469
Cdd:cd18579 81 KALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 470 KRSFHQEEQMRQKASRARLTSSMLRTVRTIKSHGWECAFLERLLHIRGQELGALKTSAFLFSVSLVSFQVSTFLVALVVF 549
Cdd:cd18579 161 LISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 13591916 550 AVHTLVaeDNAMDAEKAFVTLTVLSILNKAQAFLPFSVHCLVQARVSFDRL 600
Cdd:cd18579 241 ATYVLL--GNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
950-1239 |
2.33e-81 |
|
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: 269.76 E-value: 2.33e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 950 LFLFLCQQVASFCQGYWLSLWADDPVVDGKQMHSALRGSIFGLLGCLQAIGLFASMAAVFLGGARASCLLFRSLLWDVAR 1029
Cdd:cd18580 5 LLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1030 SPIGFFERTPVGNLLNRFSKETDIVDVDIPDKMRTLLTYAFGLLEVGLAVSMATPLAIVAILPLMLLYAGFQSLYVATCC 1109
Cdd:cd18580 85 APMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYYLRTSR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1110 QLRRLESASYSSVCSHLAETFQGSQVVRAFQAQGPFTAQHDALMDENQRISFPRLVADRWLAANLELLGNGLVFVAATCA 1189
Cdd:cd18580 165 QLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALLALVVALLA 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 13591916 1190 VLSKAHLSAGLAGFSVSAALQVTQTLQWVVRSWTDLENSMVAVERVQDYV 1239
Cdd:cd18580 245 VLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1019-1498 |
3.74e-80 |
|
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: 280.18 E-value: 3.74e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1019 LFRSLLwdvaRSPIGFFERTPVGNLLNRFSketdivDVDipdKMRTLLTYA---------FGLLEVGLAVSMATPLAIVA 1089
Cdd:COG2274 235 FFRHLL----RLPLSFFESRSVGDLASRFR------DVE---SIREFLTGSlltalldllFVLIFLIVLFFYSPPLALVV 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1090 ILpLMLLYAGFqSLYVATccQLRRL---ESASYSSVCSHLAETFQGSQVVRAFQAQGPFTAQHDALMDENQRISFPRLVA 1166
Cdd:COG2274 302 LL-LIPLYVLL-GLLFQP--RLRRLsreESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1167 DRWL---AANLELLGNGLVFVAATCAVLSKaHLSAG-LAGFSvSAALQVTQTLQWVVRSWTDLENSMVAVERVQDYVHTP 1242
Cdd:COG2274 378 SNLLstlSGLLQQLATVALLWLGAYLVIDG-QLTLGqLIAFN-ILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLP 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1243 KEapwRLPSSAAQPLWPCGGQIEFRDFGLRHRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGI 1322
Cdd:COG2274 456 PE---REEGRSKLSLPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRI 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1323 WIDGVPITDMGLHTLRSRITIIPQDPVLFPGSLRMNLDLLQEN-TDEGIWAALETVQLKAFVTSLPGQLQYECSGQGDDL 1401
Cdd:COG2274 533 LIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDaTDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1402 SVGQKQLLCLARALLRKTQILILDEATASVDPGTEIQMQAALERWFAQCTVLLIAHRLRSVMNCARVLVMDEGQVAESGS 1481
Cdd:COG2274 613 SGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGT 692
|
490
....*....|....*..
gi 13591916 1482 PAQLLAQKGLFYRLAQE 1498
Cdd:COG2274 693 HEELLARKGLYAELVQQ 709
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1258-1482 |
7.52e-71 |
|
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: 236.15 E-value: 7.52e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1258 WPCGGQIEFRDFGLRHRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTL 1337
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1338 RSRITIIPQDPVLFPGSLRMNLDLLQENTDEGIWAALETvqlkafvtslpgqlqyecSGQGDDLSVGQKQLLCLARALLR 1417
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALRV------------------SEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13591916 1418 KTQILILDEATASVDPGTEIQMQAALERWFAQCTVLLIAHRLRSVMNCARVLVMDEGQVAESGSP 1482
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
950-1238 |
4.37e-70 |
|
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: 236.99 E-value: 4.37e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 950 LFLFLCQQVASFCQGYWLSLWADD--PVVDGKQMhsalrgSIFGLLGCLQAIGLFASMAAVFLGGARASCLLFRSLLWDV 1027
Cdd:cd18606 5 LLLLILSQFAQVFTNLWLSFWTEDffGLSQGFYI------GIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1028 ARSPIGFFERTPVGNLLNRFSKETDIVDVDIPDKMRTLLTYAFGLLEVGLAVSMATPLAIVAILPLMLLYAGFQSLYVAT 1107
Cdd:cd18606 79 LRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYRAS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1108 CCQLRRLESASYSSVCSHLAETFQGSQVVRAFQAQGPFTAQHDALMDENQRISFPRLVADRWLAANLELLGNGLVFVAAT 1187
Cdd:cd18606 159 SRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLLVLIVAL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 13591916 1188 CAVLSKAHLSAGLAGFSVSAALQVTQTLQWVVRSWTDLENSMVAVERVQDY 1238
Cdd:cd18606 239 LCVTRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHY 289
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
297-843 |
1.91e-66 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 236.60 E-value: 1.91e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 297 LLRAIWRVF---RSTFLLGTLSLVISDAFRFAVPKLLSLFLEFM---GDLESSAWTGWLLAVLMFLSACLqTLFEQQYMY 370
Cdd:COG1132 8 LLRRLLRYLrpyRGLLILALLLLLLSALLELLLPLLLGRIIDALlagGDLSALLLLLLLLLGLALLRALL-SYLQRYLLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 371 RVKV-LQMRLRTAItglvYRKVLVLSSGSRKSSAAGDVVNLVSVDVQRLVESILH-LNGLWLLFLWIIVCFVYL----WQ 444
Cdd:COG1132 87 RLAQrVVADLRRDL----FEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHgLPQLVRSVVTLIGALVVLfvidWR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 445 LlgpsALTAVAVFLSLLPLNFFITKKRSFHQEEQMRQKASRARLTSSMLRTVRTIKSHGWECAFLERLLHI----RGQEL 520
Cdd:COG1132 163 L----ALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREAneelRRANL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 521 GALKTSAFLFSVSLVSFQVSTFLVALV--VFAVH------TLVAednamdaekaFVTLtVLSILNKAQAFLpFSVHCLVQ 592
Cdd:COG1132 239 RAARLSALFFPLMELLGNLGLALVLLVggLLVLSgsltvgDLVA----------FILY-LLRLFGPLRQLA-NVLNQLQR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 593 ARVSFDRLAAFLCLEE--VDPNGMVLSPSrcsSKDRISIHNGTFAWsQESPPCLHGINLTVPQGCLLAVVGPVGAGKssl 670
Cdd:COG1132 307 ALASAERIFELLDEPPeiPDPPGAVPLPP---VRGEIEFENVSFSY-PGDRPVLKDISLTIPPGETVALVGPSGSGKstl 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 671 lsallgellkvEGSVSIEG-------------SVAYVPQEAWVQNTSVVENVCF-RQELDLPWLQEVLEACALGSDVASF 736
Cdd:COG1132 383 vnlllrfydptSGRILIDGvdirdltleslrrQIGVVPQDTFLFSGTIRENIRYgRPDATDEEVEEAAKAAQAHEFIEAL 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 737 PAGVHTPVGEQGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKQVigpSGLLQGTTRILVTHTLHVLP 816
Cdd:COG1132 463 PDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEAL---ERLMKGRTTIVIAHRLSTIR 539
|
570 580
....*....|....*....|....*..
gi 13591916 817 QADQILVLANGTIAEMGSYQDLLHRNG 843
Cdd:COG1132 540 NADRILVLDDGRIVEQGTHEELLARGG 566
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
299-844 |
3.41e-65 |
|
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: 236.27 E-value: 3.41e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 299 RAIWRVFRSTFLLGTLSLVISDAFRFAVPKLLSlflefMGDLEssawTGWLLAVLMFLSACLQTLFE--QQYMyrVKVLQ 376
Cdd:COG2274 156 RLLLQVLLASLLINLLALATPLFTQVVIDRVLP-----NQDLS----TLWVLAIGLLLALLFEGLLRllRSYL--LLRLG 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 377 MRLRTAITGLVYRKVLVLSSGSRKSSAAGDVVNLVSvDVQRLVESI------LHLNGLWLLFLwIIVCFVYLWQLLGPSA 450
Cdd:COG2274 225 QRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLtgslltALLDLLFVLIF-LIVLFFYSPPLALVVL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 451 LTAVAVFLsllpLNFFITKKRSFHQEEQMRQKASRARLTSSMLRTVRTIKSHGWECAFLERLLHIRGQ----ELGALKTS 526
Cdd:COG2274 303 LLIPLYVL----LGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKylnaRFKLRRLS 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 527 AFLFSVSLVSFQVSTflVALVVFAVHTLVAEDNAMDAEKAFVTLT------VLSILNKAQAFLpfsvhclvQARVSFDRL 600
Cdd:COG2274 379 NLLSTLSGLLQQLAT--VALLWLGAYLVIDGQLTLGQLIAFNILSgrflapVAQLIGLLQRFQ--------DAKIALERL 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 601 AAFLCLE-EVDPNGMVLSPSRcsSKDRISIHNGTFAWSQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLsallgell 679
Cdd:COG2274 449 DDILDLPpEREEGRSKLSLPR--LKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLL-------- 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 680 KV--------EGSVSIEG-------------SVAYVPQEAWVQNTSVVENVCF-RQELDLPWLQEVLEACALGSDVASFP 737
Cdd:COG2274 519 KLllglyeptSGRILIDGidlrqidpaslrrQIGVVLQDVFLFSGTIRENITLgDPDATDEEIIEAARLAGLHDFIEALP 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 738 AGVHTPVGEQGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHvSQEVFKQVIgpSGLLQGTTRILVTHTLHVLPQ 817
Cdd:COG2274 599 MGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAE-TEAIILENL--RRLLKGRTVIIIAHRLSTIRL 675
|
570 580
....*....|....*....|....*..
gi 13591916 818 ADQILVLANGTIAEMGSYQDLLHRNGA 844
Cdd:COG2274 676 ADRIIVLDKGRIVEDGTHEELLARKGL 702
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
950-1238 |
7.40e-64 |
|
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: 219.65 E-value: 7.40e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 950 LFLFLCQQVASFCQGYWLSLWA----DDPVVDGKQMHSALRGSIFGLLGCLQAIGLFASMAAVFLGGARASCLLFRSLLW 1025
Cdd:cd18604 5 LLLFVLSQLLSVGQSWWLGIWAsayeTSSALPPSEVSVLYYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHERLLH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1026 DVARSPIGFFERTPVGNLLNRFSKETDIVDVDIPDKMRTLLTYAFGLLEVGLAVSMATPLAIVAILPLMLLYAGFQSLYV 1105
Cdd:cd18604 85 SVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGRLYL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1106 ATCCQLRRLESASYSSVCSHLAETFQGSQVVRAFQAQGPFTAQHDALMDENQRISFPRLVADRWLAANLELLGnGLVFVA 1185
Cdd:cd18604 165 RASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLG-ALFSFA 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 13591916 1186 ATCAVLSKAHLSAGLAGFSVSAALQVTQTLQWVVRSWTDLENSMVAVERVQDY 1238
Cdd:cd18604 244 TAALLVYGPGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEY 296
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1262-1490 |
3.04e-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: 212.09 E-value: 3.04e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1262 GQIEFRDFGLRHRPELPmAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRI 1341
Cdd:cd03254 1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1342 TIIPQDPVLFPGSLRMNLDL-LQENTDEGIWAALETVQLKAFVTSLPGQLQYECSGQGDDLSVGQKQLLCLARALLRKTQ 1420
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLgRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1421 ILILDEATASVDPGTEIQMQAALERWFAQCTVLLIAHRLRSVMNCARVLVMDEGQVAESGSPAQLLAQKG 1490
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1007-1497 |
9.49e-62 |
|
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: 222.33 E-value: 9.49e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1007 AVFLGGARASCLLFRSLlwdvARSPIGFFERTPVGNLLNRFSKETDIVDvDIPdkMRTLL------------TYAFGLLE 1074
Cdd:COG4987 82 ATLRLLADLRVRLYRRL----EPLAPAGLARLRSGDLLNRLVADVDALD-NLY--LRVLLpllvallvilaaVAFLAFFS 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1075 VGLAVSMATPLAIVAIL-PLMLLYAGfqslyVATCCQLRRLESASYSsvcsHLAETFQGSQVVRAFQAQGPFTAQHDALM 1153
Cdd:COG4987 155 PALALVLALGLLLAGLLlPLLAARLG-----RRAGRRLAAARAALRA----RLTDLLQGAAELAAYGALDRALARLDAAE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1154 DenqrisfpRLVADRWLAANLELLGNGLVFVA---ATCAVL-------SKAHLSAGLAGFSVSAALQVTQTLQWVVRSWT 1223
Cdd:COG4987 226 A--------RLAAAQRRLARLSALAQALLQLAaglAVVAVLwlaaplvAAGALSGPLLALLVLAALALFEALAPLPAAAQ 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1224 DLENSMVAVERVQDYVHTPKEAPwrlpSSAAQPLWPCGGQIEFRDFGLRHRPELPMAVQGVSLKIHAGEKVGIVGRTGAG 1303
Cdd:COG4987 298 HLGRVRAAARRLNELLDAPPAVT----EPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1304 KSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRITIIPQDPVLFPGSLRMNLDLLQEN-TDEGIWAALETVQLKAF 1382
Cdd:COG4987 374 KSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDaTDEELWAALERVGLGDW 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1383 VTSLPGQLQYECSGQGDDLSVGQKQLLCLARALLRKTQILILDEATASVDPGTEIQMQAALERWFAQCTVLLIAHRLRSV 1462
Cdd:COG4987 454 LAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGL 533
|
490 500 510
....*....|....*....|....*....|....*
gi 13591916 1463 MNCARVLVMDEGQVAESGSPAQLLAQKGLFYRLAQ 1497
Cdd:COG4987 534 ERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1019-1495 |
1.12e-60 |
|
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: 219.20 E-value: 1.12e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1019 LFRSLLwdvaRSPIGFFERTPVGNLLNRFSKETDIVDVDIPDKMRTLLTYAF---GLLEVGLAVSMATPLAIVAILPLMl 1095
Cdd:TIGR02203 93 MFEKLL----GLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLtviGLFIVLLYYSWQLTLIVVVMLPVL- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1096 lyaGFQSLYVATccQLRRLESASYSS---VCSHLAETFQGSQVVRAFQAQGPFTAQHDALMDENQRISFPRLVADRWLAA 1172
Cdd:TIGR02203 168 ---SILMRRVSK--RLRRISKEIQNSmgqVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSP 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1173 NLELLGN-GLVFVAATCAVLSKA-HLSAG-LAGFsVSAALQVTQTLqwvvRSWTDLENSM----VAVERVQDYVHTPKEa 1245
Cdd:TIGR02203 243 ITQLIASlALAVVLFIALFQAQAgSLTAGdFTAF-ITAMIALIRPL----KSLTNVNAPMqrglAAAESLFTLLDSPPE- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1246 pwrlPSSAAQPLWPCGGQIEFRDFGLRHRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWID 1325
Cdd:TIGR02203 317 ----KDTGTRAIERARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLD 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1326 GVPITDMGLHTLRSRITIIPQDPVLFPGSLRMNLDL--LQENTDEGIWAALETVQLKAFVTSLPGQLQYECSGQGDDLSV 1403
Cdd:TIGR02203 393 GHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYgrTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSG 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1404 GQKQLLCLARALLRKTQILILDEATASVDPGTEIQMQAALERWFAQCTVLLIAHRLRSVMNCARVLVMDEGQVAESGSPA 1483
Cdd:TIGR02203 473 GQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHN 552
|
490
....*....|..
gi 13591916 1484 QLLAQKGLFYRL 1495
Cdd:TIGR02203 553 ELLARNGLYAQL 564
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1261-1492 |
3.51e-60 |
|
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: 207.45 E-value: 3.51e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1261 GGQIEFRDFGLRHRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSR 1340
Cdd:cd03288 17 GGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1341 ITIIPQDPVLFPGSLRMNLDLLQENTDEGIWAALETVQLKAFVTSLPGQLQYECSGQGDDLSVGQKQLLCLARALLRKTQ 1420
Cdd:cd03288 97 LSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13591916 1421 ILILDEATASVDPGTEIQMQAALERWFAQCTVLLIAHRLRSVMNCARVLVMDEGQVAESGSPAQLLAQK-GLF 1492
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVF 249
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1227-1490 |
4.42e-60 |
|
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: 217.32 E-value: 4.42e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1227 NSMVAVERVQDYVHTPKEAPwrlPSSAAQPLWPCGGQIEFRDFGLRHRPELPmAVQGVSLKIHAGEKVGIVGRTGAGKSS 1306
Cdd:COG4988 303 NGIAAAEKIFALLDAPEPAA---PAGTAPLPAAGPPSIELEDVSFSYPGGRP-ALDGLSLTIPPGERVALVGPSGAGKST 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1307 LTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRITIIPQDPVLFPGSLRMNLDLLQEN-TDEGIWAALETVQLKAFVTS 1385
Cdd:COG4988 379 LLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDaSDEELEAALEAAGLDEFVAA 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1386 LPGQLQYECSGQGDDLSVGQKQLLCLARALLRKTQILILDEATASVDPGTEIQMQAALERWFAQCTVLLIAHRLRSVMNC 1465
Cdd:COG4988 459 LPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQA 538
|
250 260
....*....|....*....|....*
gi 13591916 1466 ARVLVMDEGQVAESGSPAQLLAQKG 1490
Cdd:COG4988 539 DRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
310-600 |
1.70e-59 |
|
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: 207.35 E-value: 1.70e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 310 LLGTLSLVISdAFRFAVPKLLSLFLEFMGDLESSA-WTGWLLAVLMFLSACLQTLFEQQYMYRVKVLQMRLRTAITGLVY 388
Cdd:cd18596 1 LQALLAVLSS-VLSFAPPFFLNRLLRYLEDPGEDAtVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 389 RKVLVL-------------------SSGSRKSSAAGDVVNLVSVDVQRLVESILHLNGLWLLFLWIIVCFVYLWQLLGPS 449
Cdd:cd18596 80 EKALRRrdksgssksseskkkdkeeDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 450 ALTAVAVFLSLLPLNFFITKKRSFHQEEQMRQKASRARLTSSMLRTVRTIKSHGWECAFLERLLHIRGQELGALKTSAFL 529
Cdd:cd18596 160 ALVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13591916 530 FSVSLVSFQVSTFLVALVVFAVHTLVAeDNAMDAEKAFVTLTVLSILNKAQAFLPFSVHCLVQARVSFDRL 600
Cdd:cd18596 240 DLLLSLLWFLIPILVTVVTFATYTLVM-GQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
310-600 |
4.14e-55 |
|
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: 193.92 E-value: 4.14e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 310 LLGTLSLvISDAFRFAVPKLLSLFLEFMGDLESSAWTGWLLAVLMFLSACLQTLFEQQYMYRVKVLQMRLRTAITGLVYR 389
Cdd:cd18598 1 PLGLLKL-LADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTAVYR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 390 KVLVLSSGSRKSSAAGDVVNLVSVDVQRLVESILHLNGLWLLFLWIIVCFVYLWQLLGPSALTAVAVFLSLLPLNFFITK 469
Cdd:cd18598 80 KALRVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 470 KRSFHQEEQMRQKASRARLTSSMLRTVRTIKSHGWECAFLERLLHIRGQELGALKTSAFLFSVsLVSFQVST-FLVALVV 548
Cdd:cd18598 160 RIGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDAL-CVYFWATTpVLISILT 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 549 FAvhTLVAEDNAMDAEKAFVTLTVLSIL----NkaqAFlPFSVHCLVQARVSFDRL 600
Cdd:cd18598 239 FA--TYVLMGNTLTAAKVFTSLALFNMLigplN---AF-PWVLNGLVEAWVSLKRL 288
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1264-1495 |
1.36e-54 |
|
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: 190.52 E-value: 1.36e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1264 IEFRDFGLRHRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRITI 1343
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1344 IPQDPVLFPGSLRMNLDLLQEN-TDEGIWAALETVQLKAFVTSLPGQLQYECSGQGDDLSVGQKQLLCLARALLRKTQIL 1422
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGaTREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13591916 1423 ILDEATASVDPGTEIQMQAALERWFAQCTVLLIAHRLRSVMNCARVLVMDEGQVAESGSPAQLLAQKGLFYRL 1495
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1264-1498 |
1.69e-53 |
|
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: 187.44 E-value: 1.69e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1264 IEFRDFGLRHRPELPmAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRITI 1343
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1344 IPQDPVLFPGSLRMNLDLLQEN-TDEGIWAALETVQLKAFVTSLPGQLQYECSGQGDDLSVGQKQLLCLARALLRKTQIL 1422
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRPDaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 1423 ILDEATASVDPGTEIQMQAALERWFAQCTVLLIAHRLRSVMNCARVLVMDEGQVAESGSPAQLLAQKGLFYRLAQE 1498
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKA 235
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1264-1475 |
3.60e-52 |
|
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: 181.04 E-value: 3.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1264 IEFRDFGLRHRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRITI 1343
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1344 IPQDPVLFPGSLRMNLdllqentdegiwaaletvqlkafvtslpgqlqyecsgqgddLSVGQKQLLCLARALLRKTQILI 1423
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 13591916 1424 LDEATASVDPGTEIQMQAALERWFAQCTVLLIAHRLRSVMNCARVLVMDEGQ 1475
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1264-1497 |
8.00e-52 |
|
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: 182.74 E-value: 8.00e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1264 IEFRDFGLRH--RPELPmAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRI 1341
Cdd:cd03249 1 IEFKNVSFRYpsRPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1342 TIIPQDPVLFPGSLRMNLDL-LQENTDEGIWAALETVQLKAFVTSLPGQLQYECSGQGDDLSVGQKQLLCLARALLRKTQ 1420
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIRYgKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13591916 1421 ILILDEATASVDPGTEIQMQAALERWFAQCTVLLIAHRLRSVMNCARVLVMDEGQVAESGSPAQLLAQKGLFYRLAQ 1497
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVK 236
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
950-1238 |
9.64e-52 |
|
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: 185.11 E-value: 9.64e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 950 LFLFLCQQVASFCQGYWLSLWAD---DPVVDGKQM-HSALRGS-------IFGLLGCLQAIGLFASMAAVFLGGARASCL 1018
Cdd:cd18602 5 LALALLKQGLRVATDFWLADWTEanhDVASVVFNItSSSLEDDevsyyisVYAGLSLGAVILSLVTNLAGELAGLRAARR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1019 LFRSLLWDVARSPIGFFERTPVGNLLNRFSKETDIVDVDIPDKMRTLLTYAFGLLEVGLAVSMATPLAIVAILPLMLLYA 1098
Cdd:cd18602 85 LHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIIIVYY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1099 GFQSLYVATCCQLRRLESASYSSVCSHLAETFQGSQVVRAFQAQGPFTAQHDALMDENQrISFPRL-VADRWLAANLELL 1177
Cdd:cd18602 165 FLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNN-TAFLFLnTANRWLGIRLDYL 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13591916 1178 GNGLVFVAATCAVLSKAH--LSAGLAGFSVSAALQVTQTLQWVVRSWTDLENSMVAVERVQDY 1238
Cdd:cd18602 244 GAVIVFLAALSSLTAALAgyISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEY 306
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
297-843 |
1.86e-51 |
|
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: 191.90 E-value: 1.86e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 297 LLRAIWRVFRSTFLLGTLSLVISDAFRFAVPKLLSLFLEFMGDLESSAWTGWLLAVLMFLSACLqTLFEQQYMYRvkvLQ 376
Cdd:COG4988 11 LARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPLSALLPLLGLLLAVLLLRALL-AWLRERAAFR---AA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 377 MRLRTAITGLVYRKVLVLSSGSRKSSAAGDVVNLvsvdvqrLVESILHLNG---LWL--LFLWIIVC---FVYLWQLLGP 448
Cdd:COG4988 87 ARVKRRLRRRLLEKLLALGPAWLRGKSTGELATL-------LTEGVEALDGyfaRYLpqLFLAALVPlliLVAVFPLDWL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 449 SALTaVAVFLSLLPLnFFI-----TKKRSfhqEEQMRQkasRARLTSSMLRTVR---TIKSHG---WECAFLERL-LHIR 516
Cdd:COG4988 160 SGLI-LLVTAPLIPL-FMIlvgkgAAKAS---RRQWRA---LARLSGHFLDRLRgltTLKLFGrakAEAERIAEAsEDFR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 517 GQELGALKTsAFLFSVSLVSF-QVSTFLVAlvVFAVHTLVAEDnaMDAEKAFVTLtVLSilnkAQAFLPF-----SVHCL 590
Cdd:COG4988 232 KRTMKVLRV-AFLSSAVLEFFaSLSIALVA--VYIGFRLLGGS--LTLFAALFVL-LLA----PEFFLPLrdlgsFYHAR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 591 VQARVSFDRLAAFLCL-EEVDPNGMVLSPSrcSSKDRISIHNGTFAWSQEsPPCLHGINLTVPQGCLLAVVGPVGAGKSS 669
Cdd:COG4988 302 ANGIAAAEKIFALLDApEPAAPAGTAPLPA--AGPPSIELEDVSFSYPGG-RPALDGLSLTIPPGERVALVGPSGAGKST 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 670 LLSALLGELLKVEGSVSIEG-------------SVAYVPQEAWVQNTSVVENVCF-RQELDLPWLQEVLEACALGSDVAS 735
Cdd:COG4988 379 LLNLLLGFLPPYSGSILINGvdlsdldpaswrrQIAWVPQNPYLFAGTIRENLRLgRPDASDEELEAALEAAGLDEFVAA 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 736 FPAGVHTPVGEQGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHvSQEVFKQVIgpSGLLQGTTRILVTHTLHVL 815
Cdd:COG4988 459 LPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAE-TEAEILQAL--RRLAKGRTVILITHRLALL 535
|
570 580
....*....|....*....|....*...
gi 13591916 816 PQADQILVLANGTIAEMGSYQDLLHRNG 843
Cdd:COG4988 536 AQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
378-850 |
8.17e-51 |
|
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: 189.98 E-value: 8.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 378 RLRTAitglVYRKVLVLSSGSRKSSAAGDVVNLVSVDVQRLVESILHLNG--LWLLFLWIIVCFVyLWQLLGPSALTAVA 455
Cdd:COG4987 89 DLRVR----LYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLplLVALLVILAAVAF-LAFFSPALALVLAL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 456 VFLS---LLPLNFFITKKRSFHQEEQMRQkASRARLTSsMLRTVRTIKSHGWECAFLERLLHIRGQELGALKTSAFL--F 530
Cdd:COG4987 164 GLLLaglLLPLLAARLGRRAGRRLAAARA-ALRARLTD-LLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLsaL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 531 SVSLVSFQVSTFLVALVVFAVHtLVAEDNAMDAEKAFVTLTVLSIlnkAQAFLPFS--VHCLVQARVSFDRLAAFLclEE 608
Cdd:COG4987 242 AQALLQLAAGLAVVAVLWLAAP-LVAAGALSGPLLALLVLAALAL---FEALAPLPaaAQHLGRVRAAARRLNELL--DA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 609 VDPNGMVLSPSRCSSKDRISIHNGTFAWSQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIE 688
Cdd:COG4987 316 PPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLG 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 689 G-------------SVAYVPQEAWVQNTSVVENVCF-RQELDLPWLQEVLEACALGSDVASFPAGVHTPVGEQGMNLSGG 754
Cdd:COG4987 396 GvdlrdldeddlrrRIAVVPQRPHLFDTTLRENLRLaRPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGG 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 755 QKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKQVIgpsGLLQGTTRILVTHTLHVLPQADQILVLANGTIAEMGS 834
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLL---EALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGT 552
|
490
....*....|....*.
gi 13591916 835 YQDLLHRNGALVGLLD 850
Cdd:COG4987 553 HEELLAQNGRYRQLYQ 568
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
950-1238 |
4.18e-50 |
|
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: 180.03 E-value: 4.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 950 LFLFLCQ--QVASFcqgYWLSLWADDPVVDGKQMHSALRGS---IFGLLGCLQAIGLFASMAAVFLGGARASCLLFRSLL 1024
Cdd:cd18605 6 LSLILMQasRNLID---FWLSYWVSHSNNSFFNFINDSFNFfltVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1025 WDVARSPIGFFERTPVGNLLNRFSKETDIVDVDIPDKMRTLLTYAFGLLEVGLAVSMATPLAIVAILPLMLLYAGFQSLY 1104
Cdd:cd18605 83 SSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQRYY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1105 VATCCQLRRLESASYSSVCSHLAETFQGSQVVRAFQAQGPFTAQHDALMDENQRISFPRLVADRWLAANLELLGNGLV-F 1183
Cdd:cd18605 163 RATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGVLIVtF 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 13591916 1184 VAATCAV--LSKAHLSAGLAGFSVSAALQVTQTLQWVVRSWTDLENSMVAVERVQDY 1238
Cdd:cd18605 243 VALTAVVqhFFGLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQY 299
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
984-1495 |
6.39e-49 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 187.24 E-value: 6.39e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 984 ALRGSIFgLLGCLqaiglfaSMAAVFLGGARASCL--------------LFRSLLwdvaRSPIGFFERTPVGNLLNRFSK 1049
Cdd:TIGR00958 199 ALASAIF-FMCLL-------SIASSVSAGLRGGSFnytmarinlriredLFRSLL----RQDLGFFDENKTGELTSRLSS 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1050 ETDIVDVDIPDKMRTLLTY---AFGLLevGLAVSMATPLAIVAILPLMLLYAG---FQSLYVATccqLRRLESASYSSvc 1123
Cdd:TIGR00958 267 DTQTMSRSLSLNVNVLLRNlvmLLGLL--GFMLWLSPRLTMVTLINLPLVFLAekvFGKRYQLL---SEELQEAVAKA-- 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1124 SHLA-ETFQGSQVVRAFQAQGPFTAQHDALMDENQRISFPRLVADRWLAANLELLGNGLVFVAATCA---VLSKAHLSAG 1199
Cdd:TIGR00958 340 NQVAeEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGgqlVLTGKVSSGN 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1200 LAGFsVSAALQVTQTLQWVVRSWTDLENSMVAVERVQDYV-HTPkeapwRLPSSAAQPLWPCGGQIEFRD--FGLRHRPE 1276
Cdd:TIGR00958 420 LVSF-LLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLdRKP-----NIPLTGTLAPLNLEGLIEFQDvsFSYPNRPD 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1277 LPMaVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRITIIPQDPVLFPGSLR 1356
Cdd:TIGR00958 494 VPV-LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVR 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1357 MNLDL-LQENTDEGIWAALETVQLKAFVTSLPGQLQYECSGQGDDLSVGQKQLLCLARALLRKTQILILDEATASVDpgt 1435
Cdd:TIGR00958 573 ENIAYgLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD--- 649
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13591916 1436 eIQMQAALERW--FAQCTVLLIAHRLRSVMNCARVLVMDEGQVAESGSPAQLLAQKGLFYRL 1495
Cdd:TIGR00958 650 -AECEQLLQESrsRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
311-600 |
8.76e-49 |
|
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: 175.72 E-value: 8.76e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 311 LGTLSLVISDAFRFAVPKLLSLFLEF-----MGDLESSAWTGWLLAVLMFLSACLQTLFEQQYMYRVKVLQMRLRTAITG 385
Cdd:cd18597 1 LAGLLKLLADVLQVLSPLLLKYLINFvedayLGGPPPSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 386 LVYRKVLVLSSGSRKSSAAGDVVNLVSVDVQRLVESILHLNGLWLLFLWIIVCFVYLWQLLGPSALTAVAVFLSLLPLNF 465
Cdd:cd18597 81 AIYRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 466 FITKKRSFHQEEQMRQKASRARLTSSMLRTVRTIKSHGWECAFLERLLHIRGQELGALKTSAFLFSVSLVSFQVSTFLVA 545
Cdd:cd18597 161 FLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLAS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 13591916 546 LVVFAvhTLVAEDNAMDAEKAFVTLTVLSILNKAQAFLPFSVHCLVQARVSFDRL 600
Cdd:cd18597 241 MLSFI--TYYATGHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1254-1495 |
2.38e-48 |
|
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: 183.48 E-value: 2.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1254 AQPLWPCGGQIEFRDFGLRHRPELPMaVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMG 1333
Cdd:COG5265 348 APPLVVGGGEVRFENVSFGYDPERPI-LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVT 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1334 LHTLRSRITIIPQDPVLFPGSLRMNLDLLQEN-TDEGIWAALETVQLKAFVTSLPGQLQYECSGQGDDLSVGQKQLLCLA 1412
Cdd:COG5265 427 QASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIA 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1413 RALLRKTQILILDEATASVDPGTEIQMQAALERWFAQCTVLLIAHRLRSVMNCARVLVMDEGQVAESGSPAQLLAQKGLF 1492
Cdd:COG5265 507 RTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLY 586
|
...
gi 13591916 1493 YRL 1495
Cdd:COG5265 587 AQM 589
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1029-1497 |
4.41e-48 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 182.23 E-value: 4.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1029 RSPIGFFERTPVGNLLNRFSKETDIVDVDIPDKMRTLLTYAfgLLEVGLAVSMAT---PLAIVAI------LPLMLLYAG 1099
Cdd:PRK10790 110 RQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSA--ALIGAMLVAMFSldwRMALVAImifpavLVVMVIYQR 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1100 FQSLYVatccqlRRlesasyssVCSHLA-------ETFQGSQVVRAFQAQGPFTAQhdalMDENQRISF-PRLVA---DR 1168
Cdd:PRK10790 188 YSTPIV------RR--------VRAYLAdindgfnEVINGMSVIQQFRQQARFGER----MGEASRSHYmARMQTlrlDG 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1169 WLAANLELLGNGLVFvaatCAVLSkahlsagLAGFSVSAALQV-------------TQTLQWVVRSWTDLENSMVAVERV 1235
Cdd:PRK10790 250 FLLRPLLSLFSALIL----CGLLM-------LFGFSASGTIEVgvlyafisylgrlNEPLIELTTQQSMLQQAVVAGERV 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1236 QDYVHTPKEAPwrlpSSAAQPLwpCGGQIEFRDFGLRHRPELPMaVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQ 1315
Cdd:PRK10790 319 FELMDGPRQQY----GNDDRPL--QSGRIDIDNVSFAYRDDNLV-LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYY 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1316 EATEGGIWIDGVPITDMGLHTLRSRITIIPQDPVLFPGSLRMNLDLLQENTDEGIWAALETVQLKAFVTSLPGQLQYECS 1395
Cdd:PRK10790 392 PLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLG 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1396 GQGDDLSVGQKQLLCLARALLRKTQILILDEATASVDPGTEIQMQAALERWFAQCTVLLIAHRLRSVMNCARVLVMDEGQ 1475
Cdd:PRK10790 472 EQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQ 551
|
490 500
....*....|....*....|..
gi 13591916 1476 VAESGSPAQLLAQKGLFYRLAQ 1497
Cdd:PRK10790 552 AVEQGTHQQLLAAQGRYWQMYQ 573
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
324-600 |
1.50e-47 |
|
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: 172.40 E-value: 1.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 324 FAVPKLLSLFLEFMGDLESSAWTGWLLAVLMFLSACLQTLFEQQYMYRVKVLQMRLRTAITGLVYRKVLVLSSGSRKSSA 403
Cdd:cd18559 14 FSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 404 AGDVVNLVSVDVQRLVESILHLNGLWLLFLWIIVCFVYLWQLLGPSALTAVAVFLSLLPLNFFITKKRSFHQEEQMRQKA 483
Cdd:cd18559 94 SGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQLKRLESVSKD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 484 SRARLTSSMLRTVRTIKSHGWECAFLERLLHIRGQELGALKTSAFLFSVSLVSFQVSTFLVALVVFAVHTLVAEDNAMDA 563
Cdd:cd18559 174 PRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSRHSLAGLVA 253
|
250 260 270
....*....|....*....|....*....|....*..
gi 13591916 564 EKAFVTLTVLSILNKAQAFLPFSVHCLVQARVSFDRL 600
Cdd:cd18559 254 LKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
316-600 |
2.73e-47 |
|
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: 171.66 E-value: 2.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 316 LVISDAFRFAVPKLLSLFLE-FMGDLESSAWTGWLLAVLMFLSACLQTLFEQQYMYRVKVLQMRLRTAITGLVYRKVLVL 394
Cdd:cd18594 6 LFLEESLKIVQPLLLGRLVAyFVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKKTLKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 395 SSGSRKSSAAGDVVNLVSVDVQRLVESILHLNGLWLLFLWIIVCFVYLWQLLGPSALTAVAVFLSLLPLNFFITKKRSfh 474
Cdd:cd18594 86 SSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFA-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 475 qeeQMRQKAS-----RARLTSSMLRTVRTIKSHGWECAFLERLLHIRGQELGALKTSAFLFSVSLVSFQVSTFLVALVVF 549
Cdd:cd18594 164 ---KYRRKTAgltdeRVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 13591916 550 AVHTLVaeDNAMDAEKAFVTLTVLSILNKAQA-FLPFSVHCLVQARVSFDRL 600
Cdd:cd18594 241 VPYVLT--GNTLTARKVFTVISLLNALRMTITrFFPESIQTLSESRVSLKRI 290
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1262-1476 |
5.29e-47 |
|
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: 168.15 E-value: 5.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1262 GQIEFRDFGLRHRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRI 1341
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1342 TIIPQDPVLFPGSLRMNLDL-LQENTDEGIWAALETVQLKAFVTSLPGQLQYECSGQGDDLSVGQKQLLCLARALLRKTQ 1420
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLgAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 1421 ILILDEATASVDPGTEIQMQAALERWFAQCTVLLIAHRLRSVMNCARVLVMDEGQV 1476
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
950-1239 |
6.71e-47 |
|
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: 170.47 E-value: 6.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 950 LFLFLCQQVASFCQGYWLSLWADDPVvDGKQMHSALRGSIFGLLGCLQAIGLFASMAAVFLGGARASCLLFRSLLWDVAR 1029
Cdd:cd18559 5 IKLVLCNHVFSGPSNLWLLLWFDDPV-NGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1030 SPIGFFERTPVGNLLNRFSKETDIVDVDIPDKMRTLLTYAFGLLEVGLAVSMATPlAIVAILPLMLLYAGFQSLYVATCC 1109
Cdd:cd18559 84 SPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGP-MAAVGIPLGLLYVPVNRVYAASSR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1110 QLRRLESASYSSVCSHLAETFQGSQVVRAFQAQGPFTAQHDALMDeNQRISFPRLVADRWLAANLELLGNGLVFVAATCA 1189
Cdd:cd18559 163 QLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRD-NELAYLPSIVYLRALAVRLWCVGPCIVLFASFFA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 13591916 1190 VLSKAHLsAGLAGFSVSAALQVTQTLQWVVRSWTDLENSMVAVERVQDYV 1239
Cdd:cd18559 242 YVSRHSL-AGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
311-600 |
1.37e-46 |
|
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: 170.11 E-value: 1.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 311 LGTLSLVISDAFRFAVPKLLSLFLEFMGDLESSAWT------------------GWLLAVLMFLSACLQTLFEQQYMYRV 372
Cdd:cd18591 1 LGGILKLLGDLLGFVGPLCISGIVDYVEENTYSSSNstdklsvsyvtveeffsnGYVLAVILFLALLLQATFSQASYHIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 373 KVLQMRLRTAITGLVYRKVLVLSSGSRKSSA--AGDVVNLVSVDVQRLVESILHLNGLWLLFLWIIVCFVYLWQLLGPSA 450
Cdd:cd18591 81 IREGIRLKTALQAMIYEKALRLSSWNLSSGSmtIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 451 LTAVAVFLSLLPLNFFITKKRSFHQEEQMRQKASRARLTSSMLRTVRTIKSHGWECAFLERLLHIRGQELGALKTSAFLF 530
Cdd:cd18591 161 LIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYW 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 531 SVSLVSFQVSTFLVALVVFAVHTLVaEDNAMDAEKAFVTLTVLSILNKAQAFLPFSVHCLVQARVSFDRL 600
Cdd:cd18591 241 SLMTFLTQASPILVTLVTFGLYPYL-EGEPLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
942-1239 |
3.04e-46 |
|
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: 169.28 E-value: 3.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 942 GTPLCTYTLFLFLCQQVASFCQGYWLSLWADDPvvDGKQM-----HSALRGSI----------FGLLGCLQAIGLFASMA 1006
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQG--SGNTTnnvdnSTVDSGNIsdnpdlnfyqLVYGGSILVILLLSLIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1007 AVFLGGA--RASCLLFRSLLWDVARSPIGFFERTPVGNLLNRFSKETDIVDVDIPDKMRTLLTYAFGLLEVGLAVSMATP 1084
Cdd:cd18599 79 GFVFVKVtlRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1085 LAIVAILPLMLLYAGFQSLYVATCCQLRRLESASYSSVCSHLAETFQGSQVVRAFQAQGPFTAQHDALMDENQRISFPRL 1164
Cdd:cd18599 159 WFLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFN 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13591916 1165 VADRWLAANLELLGNGLVFVAATCAVLSKAHLSAGLAGFSVSAALQVTQTLQWVVRSWTDLENSMVAVERVQDYV 1239
Cdd:cd18599 239 CAMRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
950-1238 |
3.46e-46 |
|
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: 169.04 E-value: 3.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 950 LFLFLCQQVASFCQGYWLSLWADDPVVDGKQMHSALRG----------------SIFGLLGCLQAIGLFASMAAVFLGGA 1013
Cdd:cd18601 9 VLLNIAAQVLYVLSDWWLSYWANLEEKLNDTTDRVQGEnstnvdiedldrdfnlGIYAGLTAATFVFGFLRSLLFFHVAV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1014 RASCLL----FRSLLwdvaRSPIGFFERTPVGNLLNRFSKETDIVDVDIP----DKMRTLLTyAFGLLEVGLAVSmatPL 1085
Cdd:cd18601 89 SASKNLhnkmFASVL----RAPIRFFDTNPIGRILNRFSKDIGHLDDLLPltflDFLQLLLQ-VVGVVLLAVVVN---PW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1086 AIVAILPLMLLYAGFQSLYVATCCQLRRLESASYSSVCSHLAETFQGSQVVRAFQAQGPFTAQHDALMDENQRISFPRLV 1165
Cdd:cd18601 161 VLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFLA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13591916 1166 ADRWLAANLELLGNGLVFVAATCAVLSKAHLSAGLAGFSVSAALQVTQTLQWVVRSWTDLENSMVAVERVQDY 1238
Cdd:cd18601 241 TSRWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEY 313
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1264-1497 |
4.42e-44 |
|
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: 160.34 E-value: 4.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1264 IEFRDFGLRHRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRITI 1343
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1344 IPQDPVLFPGSLRMNLDLLQENTD-EGIWAALETVQLKAFVTSLPGQLQYECSGQGDDLSVGQKQLLCLARALLRKTQIL 1422
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSmERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13591916 1423 ILDEATASVDPGTEIQMQAALERWFAQCTVLLIAHRLRSVMNCARVLVMDEGQVAESGSPAQLLAQKGLFYRLAQ 1497
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQ 235
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1262-1492 |
6.62e-44 |
|
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: 161.18 E-value: 6.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1262 GQIEFRDFGLRHRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEaTEGGIWIDGVPITDMGLHTLRSRI 1341
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1342 TIIPQDPVLFPGSLRMNLDLLQENTDEGIWAALETVQLKAFVTSLPGQLQYECSGQGDDLSVGQKQLLCLARALLRKTQI 1421
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13591916 1422 LILDEATASVDPGTEIQMQAALERWFAQCTVLLIAHRLRSVMNCARVLVMDEGQVAESGSPAQLLAQKGLF 1492
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
314-600 |
7.76e-44 |
|
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: 161.57 E-value: 7.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 314 LSLVISDAFRFAVPK-LLSLFLEFMGDLESSAWTGWLLAVLMFLSACLQTLFEQQY---MYRVKVlqmRLRTAITGLVYR 389
Cdd:cd18592 4 LLLLISLIFGFIGPTiLIRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTwaiSYRTGI---RLRGAVLGLLYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 390 KVLVLSSGSRKSSaaGDVVNLVSVDVQRLVESILHLNGLWLLFLWIIVCFVYLWQLLGPSALTAVAVFLSLLPLNFFITK 469
Cdd:cd18592 81 KILRLRSLGDKSV--GELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 470 KRSFHQEEQMRQKASRARLTSSMLRTVRTIKSHGWECAFLERLLHIRGQELGALKTSAFLFSVSLVSFQVSTFLVALVVF 549
Cdd:cd18592 159 LTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTF 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 13591916 550 AVHTLVAEDnaMDAEKAFVTLTVLSILNKAQAFLPFSVHCLVQARVSFDRL 600
Cdd:cd18592 239 LAHVALGND--LTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
311-600 |
6.56e-41 |
|
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: 153.15 E-value: 6.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 311 LGTLSLVISDAFRFAVPKLLSLFLEF--MGDLESSAWTGWLLAVLMFLSACLQTLFEQQYMYRVKVLQMRLRTAITGLVY 388
Cdd:cd18593 1 LLGIFLFLEEAIRVVQPIFLGKLIRYfeGNGSSISLTEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 389 RKVLVLSSGSRKSSAAGDVVNLVSVDVQRLVESILHLNGLWLLFLWIIVCFVYLWQLLGPSALTAVAVFLSLLPLNFFIT 468
Cdd:cd18593 81 RKALRLSQAALGKTTVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 469 KKrsFHqeeQMRQKA-----SRARLTSSMLRTVRTIKSHGWECAFLERLLHIRGQELGALKTSAFLFSVSLVSFQVSTFL 543
Cdd:cd18593 161 KL--FS---KLRRKTaartdKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 13591916 544 VALVVFAVHTLVaeDNAMDAEKAFVTLTVLSILNKAQA-FLPFSVHCLVQARVSFDRL 600
Cdd:cd18593 236 ILFLTFLAYILL--GNILTAERVFVTMALYNAVRLTMTlFFPFAIQFGSELSVSIRRI 291
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1262-1502 |
1.48e-40 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 159.74 E-value: 1.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1262 GQIEFRDFGLRHrPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRI 1341
Cdd:PRK13657 333 GAVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1342 TIIPQDPVLFPGSLRMNLDLLQEN-TDEGIWAALETVQLKAFVTSLPGQLQYECSGQGDDLSVGQKQLLCLARALLRKTQ 1420
Cdd:PRK13657 412 AVVFQDAGLFNRSIEDNIRVGRPDaTDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPP 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1421 ILILDEATASVDPGTEIQMQAALERWFAQCTVLLIAHRLRSVMNCARVLVMDEGQVAESGSPAQLLAQKGLFYRLAQESG 1500
Cdd:PRK13657 492 ILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQG 571
|
..
gi 13591916 1501 LA 1502
Cdd:PRK13657 572 ML 573
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
627-828 |
6.07e-40 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 147.86 E-value: 6.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 627 ISIHNGTFAWSQESPpCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSV-----------------SIEG 689
Cdd:cd03290 1 VQVTNGYFSWGSGLA-TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 690 SVAYVPQEAWVQNTSVVENVCFRQELDLPWLQEVLEACALGSDVASFPAGVHTPVGEQGMNLSGGQKQRLSLARAVYRRA 769
Cdd:cd03290 80 SVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13591916 770 AVYLMDDPLAALDAHVSQEVFKQviGPSGLLQGTTR--ILVTHTLHVLPQADQILVLANGT 828
Cdd:cd03290 160 NIVFLDDPFSALDIHLSDHLMQE--GILKFLQDDKRtlVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
642-838 |
1.50e-38 |
|
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: 146.15 E-value: 1.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 642 PCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGSVAYVPQEAWVQNTSVVENVCFRQELDLPWLQ 721
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 722 EVLEACALGSDVASFPAGVHTPVGEQGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKQVIgpSGLLQ 801
Cdd:cd03291 131 SVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCV--CKLMA 208
|
170 180 190
....*....|....*....|....*....|....*..
gi 13591916 802 GTTRILVTHTLHVLPQADQILVLANGTIAEMGSYQDL 838
Cdd:cd03291 209 NKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1262-1476 |
8.65e-38 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 141.84 E-value: 8.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1262 GQIEFRD--FGLRHRPELPMaVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRS 1339
Cdd:cd03248 10 GIVKFQNvtFAYPTRPDTLV-LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1340 RITIIPQDPVLFPGSLRMNLDL-LQENTDEGIWAALETVQLKAFVTSLPGQLQYECSGQGDDLSVGQKQLLCLARALLRK 1418
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAYgLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 13591916 1419 TQILILDEATASVDPGTEIQMQAALERWFAQCTVLLIAHRLRSVMNCARVLVMDEGQV 1476
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1284-1495 |
2.53e-37 |
|
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: 151.43 E-value: 2.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1284 VSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRITIIPQDPVLFPGSLRMNLdLLQ 1363
Cdd:TIGR01193 493 ISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENL-LLG 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1364 EN---TDEGIWAALETVQLKAFVTSLPGQLQYECSGQGDDLSVGQKQLLCLARALLRKTQILILDEATASVDPGTEIQMQ 1440
Cdd:TIGR01193 572 AKenvSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIV 651
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 13591916 1441 AALERwFAQCTVLLIAHRLRSVMNCARVLVMDEGQVAESGSPAQLLAQKGLFYRL 1495
Cdd:TIGR01193 652 NNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
303-824 |
2.67e-37 |
|
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: 148.59 E-value: 2.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 303 RVFRSTFLLGTLSLVISDAFRFAVPKLLSLFLEFMGDLESSAWTGWLLAVLMFLSACLqTLFEQQYMYRvkvLQMRLRTA 382
Cdd:TIGR02857 3 RALALLALLGVLGALLIIAQAWLLARVVDGLISAGEPLAELLPALGALALVLLLRALL-GWLQERAAAR---AAAAVKSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 383 ITGLVYRKVLVLSSGSRKSSAAGDVVNLVSVDVQRLVESIlhlnGLWL--LFLWIIVCFVYLWQLLGPSALTAVAVFLSL 460
Cdd:TIGR02857 79 LRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYF----ARYLpqLVLAVIVPLAILAAVFPQDWISGLILLLTA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 461 LPLNFFITKKRSFHQEEQMRQKASRARLTSSMLRTVR---TIKSHGWECAFLERLLHI----RGQELGALKTsAFLFSVS 533
Cdd:TIGR02857 155 PLIPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRglpTLKLFGRAKAQAAAIRRSseeyRERTMRVLRI-AFLSSAV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 534 LVSFqvSTFLVALV-VFAVHTLVAEDnaMDAEKAFVTLtvlsILnKAQAFLPF-----SVHCLVQARVSFDRLAAFLclE 607
Cdd:TIGR02857 234 LELF--ATLSVALVaVYIGFRLLAGD--LDLATGLFVL----LL-APEFYLPLrqlgaQYHARADGVAAAEALFAVL--D 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 608 EVDPNGMVLSPSRCSSKDRISIHNGTFAWsQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSI 687
Cdd:TIGR02857 303 AAPRPLAGKAPVTAAPASSLEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 688 EG-------------SVAYVPQEAWVQNTSVVENVCFRQ-ELDLPWLQEVLEACALGSDVASFPAGVHTPVGEQGMNLSG 753
Cdd:TIGR02857 382 NGvpladadadswrdQIAWVPQHPFLFAGTIAENIRLARpDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSG 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13591916 754 GQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKQVigpSGLLQGTTRILVTHTLHVLPQADQILVL 824
Cdd:TIGR02857 462 GQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEAL---RALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
627-848 |
9.59e-37 |
|
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: 139.29 E-value: 9.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 627 ISIHNGTFAWSQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-------------SVAY 693
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlaslrrQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 694 VPQEAWVQNTSVVENVCF-RQELDLPWLQEVLEACALGSDVASFPAGVHTPVGEQGMNLSGGQKQRLSLARAVYRRAAVY 772
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYgRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 773 LMDDPLAALDAhVSQEVFKQVIgpSGLLQGTTRILVTHTLHVLPQADQILVLANGTIAEMGSYQDLLHRNGALVGL 848
Cdd:cd03251 161 ILDEATSALDT-ESERLVQAAL--ERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1284-1498 |
1.73e-36 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 147.30 E-value: 1.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1284 VSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQeATEGGIWIDGVPITDMGLHTLRSRITIIPQDPVLFPGSLRMNLDLLQ 1363
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1364 EN-TDEGIWAALETVQLKAFVTSLPGQLQYECSGQGDDLSVGQKQLLCLARALLRKTQILILDEATASVDPGTEIQMQAA 1442
Cdd:PRK11174 448 PDaSDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQA 527
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 1443 LERWFAQCTVLLIAHRLRSVMNCARVLVMDEGQVAESGSPAQLLAQKGLFYRLAQE 1498
Cdd:PRK11174 528 LNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAH 583
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
627-844 |
1.84e-36 |
|
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: 138.52 E-value: 1.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 627 ISIHNGTFAWSQESPpCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-------------SVAY 693
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 694 VPQEAWVQNTSVVENVCFRQELDLPwlQEVLEAC---ALGSDVASFPAGVHTPVGEQGMNLSGGQKQRLSLARAVYRRAA 770
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRPDATD--EEVIEAAkaaQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13591916 771 VYLMDDPLAALDAHVSQEVFKQVigpSGLLQGTTRILVTHTLHVLPQADQILVLANGTIAEMGSYQDLLHRNGA 844
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAAL---RDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGL 228
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1264-1489 |
6.18e-36 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 136.69 E-value: 6.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1264 IEFRDFGLRHRPELPmAVQGVSLKIHAGEKVGIVGRTGAGKSSLTW---GLLRlqeATEGGIWIDGVPITDMGLHTLRSR 1340
Cdd:COG1122 1 IELENLSFSYPGGTP-ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRllnGLLK---PTSGEVLVDGKDITKKNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1341 ITIIPQDP------------VLFpgSLRmNLDLLQENTDEGIWAALETVQLKAFVTSLPgqlqyecsgqgDDLSVGQKQL 1408
Cdd:COG1122 77 VGLVFQNPddqlfaptveedVAF--GPE-NLGLPREEIRERVEEALELVGLEHLADRPP-----------HELSGGQKQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1409 LCLARALLRKTQILILDEATASVDPGTEIQMQAALERWFAQ-CTVLLIAHRLRSVMNCA-RVLVMDEGQVAESGSPAQLL 1486
Cdd:COG1122 143 VAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEgKTVIIVTHDLDLVAELAdRVIVLDDGRIVADGTPREVF 222
|
...
gi 13591916 1487 AQK 1489
Cdd:COG1122 223 SDY 225
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
303-848 |
1.70e-35 |
|
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: 144.09 E-value: 1.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 303 RVFRSTFLLGTLSLVISDAFRFAVPKLLSLFLE--FMGDLESSAWTGWLLAVLMFLSACLQTLFEQQYMYRVKVlqMRLR 380
Cdd:TIGR02203 10 RPYKAGLVLAGVAMILVAATESTLAALLKPLLDdgFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSWVSN--KVVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 381 TaITGLVYRKVLVLSSGSRKSSAAGDVVNLVSVDVQRLVES------ILHLNGLWLLFLwIIVCFVYLWQLLgpsalTAV 454
Cdd:TIGR02203 88 D-IRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAatdafiVLVRETLTVIGL-FIVLLYYSWQLT-----LIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 455 AVFLSLLPLNFFITKKRSFHQEEQMRQK-ASRARLTSSMLRTVRTIKSHGWECAFLERLLHI----RGQELGALKTSAFL 529
Cdd:TIGR02203 161 VVMLPVLSILMRRVSKRLRRISKEIQNSmGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVsnrnRRLAMKMTSAGSIS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 530 fsvslvsfQVSTFLVALVVFAVHTLVAEDNAMDAEKAFVTLTVLsILNKAQAFLPFSVHCLVQAR-----VSFDRLAAFL 604
Cdd:TIGR02203 241 --------SPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAF-ITAMIALIRPLKSLTNVNAPmqrglAAAESLFTLL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 605 CLE-EVDPNGMVLSPSRcsskDRISIHNGTFAWSQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEG 683
Cdd:TIGR02203 312 DSPpEKDTGTRAIERAR----GDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 684 SVSIEG-------------SVAYVPQEAWVQNTSVVENVCF--RQELDLPWLQEVLEACALGSDVASFPAGVHTPVGEQG 748
Cdd:TIGR02203 388 QILLDGhdladytlaslrrQVALVSQDVVLFNDTIANNIAYgrTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENG 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 749 MNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHvSQEVFKQVIgpSGLLQGTTRILVTHTLHVLPQADQILVLANGT 828
Cdd:TIGR02203 468 VLLSGGQRQRLAIARALLKDAPILILDEATSALDNE-SERLVQAAL--ERLMQGRTTLVIAHRLSTIEKADRIVVMDDGR 544
|
570 580
....*....|....*....|
gi 13591916 829 IAEMGSYQDLLHRNGALVGL 848
Cdd:TIGR02203 545 IVERGTHNELLARNGLYAQL 564
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
627-827 |
9.41e-35 |
|
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: 130.97 E-value: 9.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 627 ISIHNGTFAWSQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-------------SVAY 693
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 694 VPQEAWVQNTSVVENVcfrqeldlpwlqevleacalgsdvasfpagvhtpvgeqgmnLSGGQKQRLSLARAVYRRAAVYL 773
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 13591916 774 MDDPLAALDAHvSQEVFKQVIgpSGLLQGTTRILVTHTLHVLPQADQILVLANG 827
Cdd:cd03228 120 LDEATSALDPE-TEALILEAL--RALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
626-843 |
1.32e-34 |
|
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: 132.73 E-value: 1.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 626 RISIHNGTFAWsQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-------------SVA 692
Cdd:cd03254 2 EIEFENVNFSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 693 YVPQEAWVQNTSVVENVCF-RQELDLpwlQEVLEAC-ALGSD--VASFPAGVHTPVGEQGMNLSGGQKQRLSLARAVYRR 768
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLgRPNATD---EEVIEAAkEAGAHdfIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13591916 769 AAVYLMDDPLAALDAHvSQEVFKQVIGPsgLLQGTTRILVTHTLHVLPQADQILVLANGTIAEMGSYQDLLHRNG 843
Cdd:cd03254 158 PKILILDEATSNIDTE-TEKLIQEALEK--LMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1010-1459 |
3.28e-34 |
|
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: 139.42 E-value: 3.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1010 LGGARASclLFRSLlwdvARSPIGFFERTPVGNLLNRFSKETDIVDVDIPdkmRTLLTYAFGLLEVGLAVSMATPLAIVA 1089
Cdd:TIGR02868 85 LGALRVR--VYERL----ARQALAGRRRLRRGDLLGRLGADVDALQDLYV---RVIVPAGVALVVGAAAVAAIAVLSVPA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1090 --ILPLMLLYAGFqslyVATCCQLR------RLESASYSSVCSHLAETFQGSQVVRAFQAQGPFTAQHDALMDENQRISF 1161
Cdd:TIGR02868 156 alILAAGLLLAGF----VAPLVSLRaaraaeQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAER 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1162 PRLVADRWLAAnLELLGNGLV----FVAATCAVLSKAHLSAGLAGFSVS--AALQVTQTLQWVVRSWTDLENSMVAVERV 1235
Cdd:TIGR02868 232 RAAAATALGAA-LTLLAAGLAvlgaLWAGGPAVADGRLAPVTLAVLVLLplAAFEAFAALPAAAQQLTRVRAAAERIVEV 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1236 qdyvhTPKEAPWRLPSS-AAQPLWPCGGQIEFRDFGLRHrPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRL 1314
Cdd:TIGR02868 311 -----LDAAGPVAEGSApAAGAVGLGKPTLELRDLSAGY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGL 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1315 QEATEGGIWIDGVPITDMGLHTLRSRITIIPQDPVLFPGSLRMNLDLLQEN-TDEGIWAALETVQLKAFVTSLPGQLQYE 1393
Cdd:TIGR02868 385 LDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDaTDEELWAALERVGLADWLRALPDGLDTV 464
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 1394 CSGQGDDLSVGQKQLLCLARALLRKTQILILDEATASVDPGTEIQMQAALERWFAQCTVLLIAHRL 1459
Cdd:TIGR02868 465 LGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1262-1497 |
5.09e-34 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 139.57 E-value: 5.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1262 GQIEFRDFGLRHRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRI 1341
Cdd:PRK11160 337 VSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1342 TIIPQDPVLFPGSLRMNLDLLQEN-TDEGIWAALETVQLKAFVTSLPGQLQYECSGqGDDLSVGQKQLLCLARALLRKTQ 1420
Cdd:PRK11160 417 SVVSQRVHLFSATLRDNLLLAAPNaSDEALIEVLQQVGLEKLLEDDKGLNAWLGEG-GRQLSGGEQRRLGIARALLHDAP 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13591916 1421 ILILDEATASVDPGTEIQMQAALERWFAQCTVLLIAHRLRSVMNCARVLVMDEGQVAESGSPAQLLAQKGLFYRLAQ 1497
Cdd:PRK11160 496 LLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQ 572
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1244-1471 |
2.51e-33 |
|
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: 136.65 E-value: 2.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1244 EAPWRLPSSAAQPL-------WPCGGQIEFRdfGLRHR-PELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQ 1315
Cdd:TIGR02857 295 EALFAVLDAAPRPLagkapvtAAPASSLEFS--GVSVAyPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFV 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1316 EATEGGIWIDGVPITDMGLHTLRSRITIIPQDPVLFPGSLRMNLDLLQ-ENTDEGIWAALETVQLKAFVTSLPGQLQYEC 1394
Cdd:TIGR02857 373 DPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARpDASDAEIREALERAGLDEFVAALPQGLDTPI 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13591916 1395 SGQGDDLSVGQKQLLCLARALLRKTQILILDEATASVDPGTEIQMQAALERWFAQCTVLLIAHRLRSVMNCARVLVM 1471
Cdd:TIGR02857 453 GEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
642-844 |
2.48e-32 |
|
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: 126.50 E-value: 2.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 642 PCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGS-------------VAYVPQEAWVQNTSVVEN 708
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrsqIGLVSQEPVLFDGTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 709 VCF-RQELDLPWLQEVLEACALGSDVASFPAGVHTPVGEQGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQ 787
Cdd:cd03249 97 IRYgKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 13591916 788 EVFKQVigpSGLLQGTTRILVTHTLHVLPQADQILVLANGTIAEMGSYQDLLHRNGA 844
Cdd:cd03249 177 LVQEAL---DRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGV 230
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1265-1475 |
1.59e-31 |
|
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: 123.35 E-value: 1.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1265 EFRDFGLRHRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRITII 1344
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1345 PQDP------------VLFpgSLRmNLDLLQENTDEGIWAALETVQLKAFVTSLPgqlqyecsgqgDDLSVGQKQLLCLA 1412
Cdd:cd03225 81 FQNPddqffgptveeeVAF--GLE-NLGLPEEEIEERVEEALELVGLEGLRDRSP-----------FTLSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13591916 1413 RALLRKTQILILDEATASVDPGTEIQMQAALERWFAQC-TVLLIAHRLRSVMNCA-RVLVMDEGQ 1475
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGkTIIIVTHDLDLLLELAdRVIVLEDGK 211
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
276-849 |
2.25e-31 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 132.92 E-value: 2.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 276 SGMGTPETEAflQPERSQRGPLLRAI-------WRVFRSTFLLgtlsLVISDAFRFAVPKLLSLFLEFMG---DLESSAW 345
Cdd:TIGR00958 129 SSAGASEKEA--EQGQSETADLLFRLlglsgrdWPWLISAFVF----LTLSSLGEMFIPFYTGRVIDTLGgdkGPPALAS 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 346 TGWLLAVLMFLSACLQTLFEQQYMYRVKVLQMRLRtaitGLVYRKVLVLSSGSRKSSAAGDVVNLVSVDVQRLVESI-LH 424
Cdd:TIGR00958 203 AIFFMCLLSIASSVSAGLRGGSFNYTMARINLRIR----EDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLsLN 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 425 LNglwlLFLWIIVCFV--YLWQLLGPSALTAVAVFLslLPLNFFITKK-RSFHQEEQMRQKASRARLTS------SMLRT 495
Cdd:TIGR00958 279 VN----VLLRNLVMLLglLGFMLWLSPRLTMVTLIN--LPLVFLAEKVfGKRYQLLSEELQEAVAKANQvaeealSGMRT 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 496 VRTIKSHGWE-CAFLERLLHIRgqELGalKTSAFLFSVSLVSFQVSTFLVALVVFAVHTLVAEDNAMDAEK--AFV--TL 570
Cdd:TIGR00958 353 VRSFAAEEGEaSRFKEALEETL--QLN--KRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNlvSFLlyQE 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 571 TVLSILNKAQAFLPFSVHCLVQARVSFDRLAAFLCLEevdPNGMvLSPSRCssKDRISIHNGTFAW-SQESPPCLHGINL 649
Cdd:TIGR00958 429 QLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIP---LTGT-LAPLNL--EGLIEFQDVSFSYpNRPDVPVLKGLTF 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 650 TVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-------------SVAYVPQEAWVQNTSVVENVCFR-QEL 715
Cdd:TIGR00958 503 TLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqydhhylhrQVALVGQEPVLFSGSVRENIAYGlTDT 582
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 716 DLPWLQEVLEACALGSDVASFPAGVHTPVGEQGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVfkqviG 795
Cdd:TIGR00958 583 PDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLL-----Q 657
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 13591916 796 PSGLLQGTTRILVTHTLHVLPQADQILVLANGTIAEMGSYQDLLHRNGALVGLL 849
Cdd:TIGR00958 658 ESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1241-1488 |
3.18e-31 |
|
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: 130.02 E-value: 3.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1241 TPKEAPWRLPSSAAQPLwpcggqIEFRD----FGLRHRPELPmAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQE 1316
Cdd:COG1123 244 GAARGRAAPAAAAAEPL------LEVRNlskrYPVRGKGGVR-AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1317 ATEGGIWIDGVPITDMG---LHTLRSRITIIPQDPV--LFPgslRMN--------LDLLQENTDEGIWA----ALETVQL 1379
Cdd:COG1123 317 PTSGSILFDGKDLTKLSrrsLRELRRRVQMVFQDPYssLNP---RMTvgdiiaepLRLHGLLSRAERRErvaeLLERVGL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1380 KA-FVTSLPGQLqyecSGqgddlsvGQKQLLCLARALLRKTQILILDEATASVDPGTEIQMQAALERWFAQ--CTVLLIA 1456
Cdd:COG1123 394 PPdLADRYPHEL----SG-------GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElgLTYLFIS 462
|
250 260 270
....*....|....*....|....*....|...
gi 13591916 1457 HRLRSVMN-CARVLVMDEGQVAESGSPAQLLAQ 1488
Cdd:COG1123 463 HDLAVVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1264-1488 |
3.58e-31 |
|
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: 130.02 E-value: 3.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1264 IEFRDFGLRHRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEAT---EGGIWIDGVPITDMGLHTLRSR 1340
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1341 ITIIPQDP--VLFPGSLR-------MNLDLLQENTDEGIWAALETVQLKAFVTSLPGQlqyecsgqgddLSVGQKQLLCL 1411
Cdd:COG1123 85 IGMVFQDPmtQLNPVTVGdqiaealENLGLSRAEARARVLELLEAVGLERRLDRYPHQ-----------LSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1412 ARALLRKTQILILDEATASVDPGTEIQMQAALERWFAQ--CTVLLIAHRLRSVMNCA-RVLVMDEGQVAESGSPAQLLAQ 1488
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErgTTVLLITHDLGVVAEIAdRVVVMDDGRIVEDGPPEEILAA 233
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1272-1487 |
2.58e-30 |
|
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: 121.06 E-value: 2.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1272 RHRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRITIIPQDPvlf 1351
Cdd:COG1124 12 GQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDP--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1352 PGSL--RMNLD-LLQE--------NTDEGIWAALETVQL-KAFVTSLPGQLqyecSGqgddlsvGQKQLLCLARALLRKT 1419
Cdd:COG1124 89 YASLhpRHTVDrILAEplrihglpDREERIAELLEQVGLpPSFLDRYPHQL----SG-------GQRQRVAIARALILEP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13591916 1420 QILILDEATASVDPGTEIQMQAALERWFAQ--CTVLLIAHRLRSV--MnCARVLVMDEGQVAESGSPAQLLA 1487
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKDLREErgLTYLFVSHDLAVVahL-CDRVAVMQNGRIVEELTVADLLA 228
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1262-1495 |
3.72e-30 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 127.83 E-value: 3.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1262 GQIEFRDFGLRHRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRI 1341
Cdd:PRK11176 340 GDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1342 TIIPQDPVLFPGSLRMNLDLLQEN--TDEGIWAALETVQLKAFVTSLPGQLQYECSGQGDDLSVGQKQLLCLARALLRKT 1419
Cdd:PRK11176 420 ALVSQNVHLFNDTIANNIAYARTEqySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 1420 QILILDEATASVDPGTEIQMQAALERWFAQCTVLLIAHRLRSVMNCARVLVMDEGQVAESGSPAQLLAQKGLFYRL 1495
Cdd:PRK11176 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQL 575
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1264-1480 |
2.01e-29 |
|
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: 117.61 E-value: 2.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1264 IEFRDFGLRHRpelpmAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTL---RSR 1340
Cdd:cd03257 9 VSFPTGGGSVK-----ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1341 ITIIPQDPVlfpGSL--RMN-----LDLLQENTD--------EGIWAALETVQL-KAFVTSLPGQLqyecSGqgddlsvG 1404
Cdd:cd03257 84 IQMVFQDPM---SSLnpRMTigeqiAEPLRIHGKlskkearkEAVLLLLVGVGLpEEVLNRYPHEL----SG-------G 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1405 QKQLLCLARALLRKTQILILDEATASVDPGTEIQMQAAL-----ERwfaQCTVLLIAHRLRSVMNCA-RVLVMDEGQVAE 1478
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLkklqeEL---GLTLLFITHDLGVVAKIAdRVAVMYAGKIVE 226
|
..
gi 13591916 1479 SG 1480
Cdd:cd03257 227 EG 228
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
627-843 |
7.42e-29 |
|
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: 116.43 E-value: 7.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 627 ISIHNGTFAWSQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-------------SVAY 693
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 694 VPQEAWVQNTSVVENVCFRQELdlPWLQEVLEACALGSD---VASFPAGVHTPVGEQGMNLSGGQKQRLSLARAVYRRAA 770
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPG--MSMERVIEAAKLAGAhdfISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13591916 771 VYLMDDPLAALDaHVSQEVFKQVIgpSGLLQGTTRILVTHTLHVLPQADQILVLANGTIAEMGSYQDLLHRNG 843
Cdd:cd03252 159 ILIFDEATSALD-YESEHAIMRNM--HDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENG 228
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
626-834 |
1.04e-28 |
|
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: 115.67 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 626 RISIHNGTFAWSQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-------------SVA 692
Cdd:cd03244 2 DIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 693 YVPQEAWVQNTSVVENVCFRQELDLPWLQEVLEACALGSDVASFPAGVHTPVGEQGMNLSGGQKQRLSLARAVYRRAAVY 772
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13591916 773 LMDDPLAALDaHVSQEVFKQVIgpSGLLQGTTRILVTHTLHVLPQADQILVLANGTIAEMGS 834
Cdd:cd03244 162 VLDEATASVD-PETDALIQKTI--REAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1263-1497 |
1.23e-28 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 122.90 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1263 QIEFRDFglrHRPE-LPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRI 1341
Cdd:PRK10789 315 DVNIRQF---TYPQtDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1342 TIIPQDPVLFPGSLRMNLDLLQEN-TDEGIWAALETVQLKAFVTSLPGQLQYECSGQGDDLSVGQKQLLCLARALLRKTQ 1420
Cdd:PRK10789 392 AVVSQTPFLFSDTVANNIALGRPDaTQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAE 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1421 ILILDEATASVDPGTEIQMQAALERWFAQCTVLLIAHRLRSVMNCARVLVMDEGQVAESGSPAQLLAQKGLF---YRLAQ 1497
Cdd:PRK10789 472 ILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYrdmYRYQQ 551
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
590-841 |
3.85e-28 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 121.39 E-value: 3.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 590 LVQARVSFDRLAAFLCLEEVDPNGMVLSPSrcssKDRISIHNGTFAWSQESPPCLHGINLTVPQGCLLAVVGPVGAGKSS 669
Cdd:COG4618 298 FVSARQAYRRLNELLAAVPAEPERMPLPRP----KGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKST 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 670 LLSALLGELLKVEGSVSIEG-------------SVAYVPQEawVQ--NTSVVENVCFRQELDlPwlQEVLEACALgSDV- 733
Cdd:COG4618 374 LARLLVGVWPPTAGSVRLDGadlsqwdreelgrHIGYLPQD--VElfDGTIAENIARFGDAD-P--EKVVAAAKL-AGVh 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 734 ---ASFPAGVHTPVGEQGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAhvsqevfkqvIGPSGLLQ--------G 802
Cdd:COG4618 448 emiLRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD----------EGEAALAAairalkarG 517
|
250 260 270
....*....|....*....|....*....|....*....
gi 13591916 803 TTRILVTHTLHVLPQADQILVLANGTIAEMGSYQDLLHR 841
Cdd:COG4618 518 ATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
348-854 |
5.53e-28 |
|
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: 121.99 E-value: 5.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 348 WLLAVLMFLSACLQTLFeqQYMYRVKVLQM--RLRTAITGLVYRKVLVLSSGSRKSSAAGDVVN-----------LVSVD 414
Cdd:TIGR03797 176 VQIALALLAAAVGAAAF--QLAQSLAVLRLetRMDASLQAAVWDRLLRLPVSFFRQYSTGDLASramgisqirriLSGST 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 415 VQRLVESILHLNGLWLLFlwiivcfVYLWQLlgpsALTAVAVFLSLLPLNFFITKKRSFHQEEQMRQKASRARLTSSMLR 494
Cdd:TIGR03797 254 LTTLLSGIFALLNLGLMF-------YYSWKL----ALVAVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLIN 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 495 TVRTIKSHGWECAFLERLLHIRGQElgalktSAFLFSVSLVSFQVSTFLVALVVFAVHTLVAednAMDAEKAFVTLTVLS 574
Cdd:TIGR03797 323 GISKLRVAGAENRAFARWAKLFSRQ------RKLELSAQRIENLLTVFNAVLPVLTSAALFA---AAISLLGGAGLSLGS 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 575 ILNKAQAFLPF--SVHCLVQARVS-------FDRLAAFL-CLEEVDPNGMvlSPSRCSSkdRISIHNGTFAWSQESPPCL 644
Cdd:TIGR03797 394 FLAFNTAFGSFsgAVTQLSNTLISilaviplWERAKPILeALPEVDEAKT--DPGKLSG--AIEVDRVTFRYRPDGPLIL 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 645 HGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-------------SVAYVPQEAWVQNTSVVENVCF 711
Cdd:TIGR03797 470 DDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGqdlagldvqavrrQLGVVLQNGRLMSGSIFENIAG 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 712 RQELDLPWLQEVLEACALGSDVASFPAGVHTPVGEQGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALD----AHVSQ 787
Cdd:TIGR03797 550 GAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDnrtqAIVSE 629
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13591916 788 EVFKqvigpsgllQGTTRILVTHTLHVLPQADQILVLANGTIAEMGSYQDLLHRNGALVGLLdgARQ 854
Cdd:TIGR03797 630 SLER---------LKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLA--RRQ 685
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1264-1480 |
1.17e-27 |
|
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: 110.87 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1264 IEFRDFGLRHRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGlHTLRSRITI 1343
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1344 IPQDPVLFPGSLRMNLdllqentdegiwaaletvqlkafvtslpgqlqyecsgqGDDLSVGQKQLLCLARALLRKTQILI 1423
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1424 LDEATASVDPGTEIQMqaaLERWFAQC---TVLLIAHRLRSVMNCARVLVMDEGQVAESG 1480
Cdd:cd03247 122 LDEPTVGLDPITERQL---LSLIFEVLkdkTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
590-843 |
1.89e-27 |
|
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: 120.23 E-value: 1.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 590 LVQARVSFDRLAAFLCLEEVDPNGMVLSPSRCSSKDrISIHNGTFAWSQESPpCLHGINLTVPQGCLLAVVGPVGAGKSS 669
Cdd:TIGR01193 438 LQAARVANNRLNEVYLVDSEFINKKKRTELNNLNGD-IVINDVSYSYGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKST 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 670 LLSALLGELLKVEGSVSIEG-------------SVAYVPQEAWVQNTSVVENVCFRQELDLPwLQEVLEACALG---SDV 733
Cdd:TIGR01193 516 LAKLLVGFFQARSGEILLNGfslkdidrhtlrqFINYLPQEPYIFSGSILENLLLGAKENVS-QDEIWAACEIAeikDDI 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 734 ASFPAGVHTPVGEQGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKQVIGpsglLQGTTRILVTHTLH 813
Cdd:TIGR01193 595 ENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN----LQDKTIIFVAHRLS 670
|
250 260 270
....*....|....*....|....*....|
gi 13591916 814 VLPQADQILVLANGTIAEMGSYQDLLHRNG 843
Cdd:TIGR01193 671 VAKQSDKIIVLDHGKIIEQGSHDELLDRNG 700
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
625-829 |
3.56e-27 |
|
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: 111.14 E-value: 3.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 625 DRISIHNGTFAWSQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-------------SV 691
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 692 AYVPQEAWVQNTSVVENVCF-RQELDLPWLQEVLEACALGSDVASFPAGVHTPVGEQGMNLSGGQKQRLSLARAVYRRAA 770
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLgAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 13591916 771 VYLMDDPLAALDAHVSQEVFKQVigpSGLLQGTTRILVTHTLHVLPQADQILVLANGTI 829
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERL---RQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1280-1488 |
6.67e-27 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 110.92 E-value: 6.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGlHTLRSRITIIPQDPVLFPG-SLRMN 1358
Cdd:COG1131 15 ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP-AEVRRRIGYVPQEPALYPDlTVREN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1359 LDLL-------QENTDEGIWAALETVQLKAFVTSLPGQLqyecSGqgddlsvGQKQLLCLARALLRKTQILILDEATASV 1431
Cdd:COG1131 94 LRFFarlyglpRKEARERIDELLELFGLTDAADRKVGTL----SG-------GMKQRLGLALALLHDPELLILDEPTSGL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 13591916 1432 DPGTEIQMQAALERWFAQ-CTVLLIAHRLRSV-MNCARVLVMDEGQVAESGSPAQLLAQ 1488
Cdd:COG1131 163 DPEARRELWELLRELAAEgKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
647-849 |
1.13e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 117.25 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 647 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELlKVEGSVSIEGS-------VAYVPQEAWV-QNT-----SVVENVCF-R 712
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIelreldpESWRKHLSWVgQNPqlphgTLRDNVLLgN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 713 QELDLPWLQEVLEACALGSDVASFPAGVHTPVGEQGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKQ 792
Cdd:PRK11174 448 PDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQA 527
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 13591916 793 VIGPSgllQGTTRILVTHTLHVLPQADQILVLANGTIAEMGSYQDLLHRNGALVGLL 849
Cdd:PRK11174 528 LNAAS---RRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLL 581
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
626-843 |
1.53e-26 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 116.74 E-value: 1.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 626 RISIHNGTFAWSQESPpCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-------------SVA 692
Cdd:PRK10790 340 RIDIDNVSFAYRDDNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplsslshsvlrqGVA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 693 YVPQEAWVQNTSVVENVCFRQELDLPWLQEVLEACALGSDVASFPAGVHTPVGEQGMNLSGGQKQRLSLARAVYRRAAVY 772
Cdd:PRK10790 419 MVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQIL 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13591916 773 LMDDPLAALDAHVSQEVFKQVigpSGLLQGTTRILVTHTLHVLPQADQILVLANGTIAEMGSYQDLLHRNG 843
Cdd:PRK10790 499 ILDEATANIDSGTEQAIQQAL---AAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQG 566
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1281-1429 |
3.03e-26 |
|
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: 105.81 E-value: 3.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1281 VQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRITIIPQDPVLFPG-SLRMNL 1359
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13591916 1360 -------DLLQENTDEGIWAALETVQLKAFVTSLPGQlqyecsgQGDDLSVGQKQLLCLARALLRKTQILILDEATA 1429
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEKLGLGDLADRPVGE-------RPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1264-1476 |
3.10e-26 |
|
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: 106.92 E-value: 3.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1264 IEFRDFGLRHRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRITI 1343
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1344 IPQDPVLFPGSLRMNLdllqentdegiwaaletvqlkafvtslpgqlqyecsgqgddLSVGQKQLLCLARALLRKTQILI 1423
Cdd:cd03246 81 LPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 13591916 1424 LDEATASVDPGTEIQMQAALERWFAQ-CTVLLIAHRLRSVMNCARVLVMDEGQV 1476
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKAAgATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
378-812 |
1.60e-25 |
|
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: 112.84 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 378 RLRTAitglVYRKVLVLSSGSRKSSAAGDVVNLVSVDVQRLVESILH--LNGLWLLFLWIIVCFVYLWqLLGPSALTAVA 455
Cdd:TIGR02868 87 ALRVR----VYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRviVPAGVALVVGAAAVAAIAV-LSVPAALILAA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 456 ---VFLSLLPLnFFITKKRSFHQeeqmRQKASRARLTSSMLRTVR---TIKSHGWECAFLERLLHIRGQELGALKTSAFL 529
Cdd:TIGR02868 162 gllLAGFVAPL-VSLRAARAAEQ----ALARLRGELAAQLTDALDgaaELVASGALPAALAQVEEADRELTRAERRAAAA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 530 FSVSlvsfQVSTFLVALVVFAVHTLVAEDNAMDAEKAFVTLTVLSILN----KAQAFLPFSVHCLVQARVSFDRLAAFLC 605
Cdd:TIGR02868 237 TALG----AALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPlaafEAFAALPAAAQQLTRVRAAAERIVEVLD 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 606 LEEVDPNGMVLSPSRCSSKD-RISIHNGTFAWSQeSPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGS 684
Cdd:TIGR02868 313 AAGPVAEGSAPAAGAVGLGKpTLELRDLSAGYPG-APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGE 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 685 VSIEGS-------------VAYVPQEAWVQNTSVVENVCF-RQELDLPWLQEVLEACALGSDVASFPAGVHTPVGEQGMN 750
Cdd:TIGR02868 392 VTLDGVpvssldqdevrrrVSVCAQDAHLFDTTVRENLRLaRPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGAR 471
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13591916 751 LSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKQVIGPsglLQGTTRILVTHTL 812
Cdd:TIGR02868 472 LSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAA---LSGRTVVLITHHL 530
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
309-577 |
2.40e-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: 107.34 E-value: 2.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 309 FLLGTLSLVISDAFRFAVPKLLSLFLEFM---GDLESSAWTGWLLAVLMFLSACLQTLFEQQYMYrvKVLQMRLRTAITG 385
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLlpdGDPETQALNVYSLALLLLGLAQFILSFLQSYLL--NHTGERLSRRLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 386 LVYRKVLVLSSGSRKSSAAGDVVNLVSVDVQRLVESILHLNGLWLLFLWIIVC-----FVYLWQLlgpsALTAVAVFLSL 460
Cdd:pfam00664 79 KLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGgiivmFYYGWKL----TLVLLAVLPLY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 461 LPLNFFITKKRSFHQEEQMRQKASRARLTSSMLRTVRTIKSHGWECAFLERLLHIRGQELGALKTSAFLFSVSLVSFQVS 540
Cdd:pfam00664 155 ILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFI 234
|
250 260 270
....*....|....*....|....*....|....*..
gi 13591916 541 TFLVALVVFAVHTLVAEDNAMDAEKAFVTLTVLSILN 577
Cdd:pfam00664 235 GYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLF 271
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
950-1215 |
3.93e-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: 106.96 E-value: 3.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 950 LFLFLCQQVASFCQGYWLSLWADDPVVDGKQ--MHSALRGSIFGLLGCLQAIGLFASMAAVFLGGARASCLLFRSLLWDV 1027
Cdd:pfam00664 5 ILLAILSGAISPAFPLVLGRILDVLLPDGDPetQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1028 ARSPIGFFERTPVGNLLNRFSKETDIVDVDIPDKMRTLLTYAF---GLLEVGLAVSMATPLAIVAILPLMLLyagFQSLY 1104
Cdd:pfam00664 85 LRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLAtivGGIIVMFYYGWKLTLVLLAVLPLYIL---VSAVF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1105 VATCCQLRRLESASYSSVCSHLAETFQGSQVVRAFQAQGPFTAQHDALMDENQRISFPRLVADRWLAANLELLGNGLVFV 1184
Cdd:pfam00664 162 AKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYAL 241
|
250 260 270
....*....|....*....|....*....|...
gi 13591916 1185 AA-TCAVLSKAH-LSAGLAGFSVSAALQVTQTL 1215
Cdd:pfam00664 242 ALwFGAYLVISGeLSVGDLVAFLSLFAQLFGPL 274
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
642-866 |
5.51e-25 |
|
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: 111.84 E-value: 5.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 642 PCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-------------SVAYVPQEAWVQNTSVVEN 708
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdirdvtqaslraAIGIVPQDTVLFNDTIAYN 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 709 VCF-RQELDLPWLQEVLEACALGSDVASFPAGVHTPVGEQGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQ 787
Cdd:COG5265 452 IAYgRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTER 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 788 EV---FKQVIgpsgllQGTTRILVTHTLHVLPQADQILVLANGTIAEMGSYQDLLHRNGALVGLLdgARQPAGEGEGEAH 864
Cdd:COG5265 532 AIqaaLREVA------RGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMW--ARQQEEEEAEEAL 603
|
..
gi 13591916 865 AA 866
Cdd:COG5265 604 AA 605
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1270-1475 |
7.18e-25 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 102.32 E-value: 7.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1270 GLRHRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRITIIPQdpv 1349
Cdd:cd00267 4 NLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1350 lfpgslrmnldllqentdegiwaaletvqlkafvtslpgqlqyecsgqgddLSVGQKQLLCLARALLRKTQILILDEATA 1429
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 13591916 1430 SVDPGTEIQMQAALERWFAQ-CTVLLIAHRLRSVMN-CARVLVMDEGQ 1475
Cdd:cd00267 110 GLDPASRERLLELLRELAEEgRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1264-1488 |
4.61e-24 |
|
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: 102.27 E-value: 4.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1264 IEFRD----FGLRHRPELpmAVQGVSLKIHAGEKVGIVGRTGAGKSSltwgLLR----LQEATEGGIWIDGVPITDM--- 1332
Cdd:cd03258 2 IELKNvskvFGDTGGKVT--ALKDVSLSVPKGEIFGIIGRSGAGKST----LIRcingLERPTSGSVLVDGTDLTLLsgk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1333 GLHTLRSRITIIPQ-----------DPVLFPgslrmnLDLL---QENTDEGIWAALETVQLKAFVTSLPGQLqyecSGqg 1398
Cdd:cd03258 76 ELRKARRRIGMIFQhfnllssrtvfENVALP------LEIAgvpKAEIEERVLELLELVGLEDKADAYPAQL----SG-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1399 ddlsvGQKQLLCLARALLRKTQILILDEATASVDPGT---------EIQMQAALerwfaqcTVLLIAHRLRSVMN-CARV 1468
Cdd:cd03258 144 -----GQKQRVGIARALANNPKVLLCDEATSALDPETtqsilallrDINRELGL-------TIVLITHEMEVVKRiCDRV 211
|
250 260
....*....|....*....|
gi 13591916 1469 LVMDEGQVAESGSPAQLLAQ 1488
Cdd:cd03258 212 AVMEKGEVVEEGTVEEVFAN 231
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
566-861 |
4.81e-24 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 108.90 E-value: 4.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 566 AFVTLTVLSI--LNKAQAFlpfsVHCLVQARVsfdRLAAFLCLEEV-----DPNGMVlSPSRCssKDRISIHNGTFAWSQ 638
Cdd:PRK13657 277 AFVGFATLLIgrLDQVVAF----INQVFMAAP---KLEEFFEVEDAvpdvrDPPGAI-DLGRV--KGAVEFDDVSFSYDN 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 639 eSPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-------------SVAYVPQEAWVQNTSV 705
Cdd:PRK13657 347 -SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdirtvtraslrrNIAVVFQDAGLFNRSI 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 706 VENVCF-RQELDLPWLQEVLEACALGSDVASFPAGVHTPVGEQGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAh 784
Cdd:PRK13657 426 EDNIRVgRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDV- 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 785 VSQEVFKQVIgpSGLLQGTTRILVTHTLHVLPQADQILVLANGTIAEMGSYQDLLHRNGALVGLL---------DGARQP 855
Cdd:PRK13657 505 ETEAKVKAAL--DELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLraqgmlqedERRKQP 582
|
....*.
gi 13591916 856 AGEGEG 861
Cdd:PRK13657 583 AAEGAN 588
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1280-1475 |
6.54e-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: 100.34 E-value: 6.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHT--LRSRITIIPQDPVLFPgslRM 1357
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIGMVFQDFALFP---HL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1358 NldllqentdegiwaALETVQLKafvtslpgqlqyecsgqgddLSVGQKQLLCLARALLRKTQILILDEATASVDPGTEI 1437
Cdd:cd03229 92 T--------------VLENIALG--------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 13591916 1438 QMQAALERWFAQ--CTVLLIAHRLRSVMNCA-RVLVMDEGQ 1475
Cdd:cd03229 138 EVRALLKSLQAQlgITVVLVTHDLDEAARLAdRVVVLRDGK 178
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1264-1487 |
5.57e-23 |
|
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: 99.50 E-value: 5.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1264 IEFRD--FGLRHRPELpmavQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMG---LHTLR 1338
Cdd:cd03261 1 IELRGltKSFGGRTVL----KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1339 SRITIIPQDPVLF-----------PgsLRMNLDLLQENTDEGIWAALETVQLKAFVTSLPGQLqyecSGqgddlsvGQKQ 1407
Cdd:cd03261 77 RRMGMLFQSGALFdsltvfenvafP--LREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAEL----SG-------GMKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1408 LLCLARALLRKTQILILDEATASVDP--GTEIQ-----MQAALerwfaQCTVLLIAHRLRSVMNCA-RVLVMDEGQVAES 1479
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPiaSGVIDdlirsLKKEL-----GLTSIMVTHDLDTAFAIAdRIAVLYDGKIVAE 218
|
....*...
gi 13591916 1480 GSPAQLLA 1487
Cdd:cd03261 219 GTPEELRA 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
627-829 |
6.74e-23 |
|
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: 97.29 E-value: 6.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 627 ISIHNGTFAWSQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGS-------------VAY 693
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdpnelgdhVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 694 VPQEAWVQNTSVVENVcfrqeldlpwlqevleacalgsdvasfpagvhtpvgeqgmnLSGGQKQRLSLARAVYRRAAVYL 773
Cdd:cd03246 81 LPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 774 MDDPLAALDAHVSQEVFKQVIGPSglLQGTTRILVTHTLHVLPQADQILVLANGTI 829
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALK--AAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
623-844 |
7.76e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 105.10 E-value: 7.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 623 SKDRISIHNGTFAWSQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG------------- 689
Cdd:PRK11176 338 AKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrdytlaslrn 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 690 SVAYVPQEAWVQNTSVVENVCF-RQELdlpWLQEVLEACALGSDVASF----PAGVHTPVGEQGMNLSGGQKQRLSLARA 764
Cdd:PRK11176 418 QVALVSQNVHLFNDTIANNIAYaRTEQ---YSREQIEEAARMAYAMDFinkmDNGLDTVIGENGVLLSGGQRQRIAIARA 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 765 VYRRAAVYLMDDPLAALDAHvSQEVFKQVIgpSGLLQGTTRILVTHTLHVLPQADQILVLANGTIAEMGSYQDLLHRNGA 844
Cdd:PRK11176 495 LLRDSPILILDEATSALDTE-SERAIQAAL--DELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGV 571
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
627-831 |
1.06e-22 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 99.01 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 627 ISIHNGTFAWSQEspPCLHGINLTVPQGCLLAVVGPVGAGkssllsallgellK-------------VEGSVSIEG---- 689
Cdd:COG1121 7 IELENLTVSYGGR--PVLEDVSLTIPPGEFVAIVGPNGAG-------------KstllkailgllppTSGTVRLFGkppr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 690 ----SVAYVPQEAWVQNT---SVVENV---CFRQeldLPWL--------QEVLEACA-LG-SDVAsfpagvHTPVGEqgm 749
Cdd:COG1121 72 rarrRIGYVPQRAEVDWDfpiTVRDVVlmgRYGR---RGLFrrpsradrEAVDEALErVGlEDLA------DRPIGE--- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 750 nLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHvSQEVFkqvigpSGLL-----QGTTRILVTHTLH-VLPQADQILV 823
Cdd:COG1121 140 -LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAA-TEEAL------YELLrelrrEGKTILVVTHDLGaVREYFDRVLL 211
|
....*...
gi 13591916 824 LANGTIAE 831
Cdd:COG1121 212 LNRGLVAH 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1280-1488 |
1.36e-22 |
|
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: 104.00 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEaTEGGIWIDGVPITDMG---LHTLRSRITIIPQDPVlfpGSL- 1355
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDPF---GSLs 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1356 -RMN--------LDLLQ-----ENTDEGIWAALETVQLKafvtslPGQLQ-Y--ECSGqgddlsvGQKQLLCLARALLRK 1418
Cdd:COG4172 377 pRMTvgqiiaegLRVHGpglsaAERRARVAEALEEVGLD------PAARHrYphEFSG-------GQRQRIAIARALILE 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13591916 1419 TQILILDEATASVDpgTEIQMQ-----AALERWFaQCTVLLIAHRLRSV--MnCARVLVMDEGQVAESGSPAQLLAQ 1488
Cdd:COG4172 444 PKLLVLDEPTSALD--VSVQAQildllRDLQREH-GLAYLFISHDLAVVraL-AHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
633-843 |
3.46e-22 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 102.87 E-value: 3.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 633 TFAWSQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSV-------------SIEGSVAYVPQEAW 699
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrfhdipltklqldSWRSRLAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 700 VQNTSVVENVCFRQELDLPwlQEVLEACALGS---DVASFPAGVHTPVGEQGMNLSGGQKQRLSLARAVYRRAAVYLMDD 776
Cdd:PRK10789 400 LFSDTVANNIALGRPDATQ--QEIEHVARLASvhdDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDD 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13591916 777 PLAALDAHVSQEVFKQVigpSGLLQGTTRILVTHTLHVLPQADQILVLANGTIAEMGSYQDLLHRNG 843
Cdd:PRK10789 478 ALSAVDGRTEHQILHNL---RQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
627-863 |
3.95e-22 |
|
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: 102.29 E-value: 3.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 627 ISIHNGTFAWSQESPPCLHGINLTVPQGCLLAVVGPVGAGK---SSLLSALLGELLKVEGSVSIEG-------------S 690
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKstlALALMGLLPHGGRISGEVLLDGrdllelsealrgrR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 691 VAYVPQEAWVQ--NTSVVENVCFRQEL-DLPWLQ------EVLEACALGSDVASFPAgvhtpvgeqgmNLSGGQKQRLSL 761
Cdd:COG1123 85 IGMVFQDPMTQlnPVTVGDQIAEALENlGLSRAEararvlELLEAVGLERRLDRYPH-----------QLSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 762 ARAVYRRAAVYLMDDPLAALDAHVSQEVFkQVIGPSGLLQGTTRILVTHTLHVLPQ-ADQILVLANGTIAEMGSYQDLLH 840
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEIL-DLLRELQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILA 232
|
250 260
....*....|....*....|....*
gi 13591916 841 RNGAL--VGLLDGARQPAGEGEGEA 863
Cdd:COG1123 233 APQALaaVPRLGAARGRAAPAAAAA 257
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
624-829 |
6.38e-22 |
|
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: 96.00 E-value: 6.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 624 KDRISIHNGTFAWSQESP-PCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGS------------ 690
Cdd:cd03248 9 KGIVKFQNVTFAYPTRPDtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkylhs 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 691 -VAYVPQEAWVQNTSVVENVCF-RQELDLPWLQEVLEACALGSDVASFPAGVHTPVGEQGMNLSGGQKQRLSLARAVYRR 768
Cdd:cd03248 89 kVSLVGQEPVLFARSLQDNIAYgLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13591916 769 AAVYLMDDPLAALDAHvSQEVFKQVIgpSGLLQGTTRILVTHTLHVLPQADQILVLANGTI 829
Cdd:cd03248 169 PQVLILDEATSALDAE-SEQQVQQAL--YDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1264-1488 |
6.43e-22 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 99.00 E-value: 6.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1264 IEFRD----FGLRHRPELpmAVQGVSLKIHAGEKVGIVGRTGAGKSSltwgLLR----LQEATEGGIWIDGVPITDM--- 1332
Cdd:COG1135 2 IELENlsktFPTKGGPVT--ALDDVSLTIEKGEIFGIIGYSGAGKST----LIRcinlLERPTSGSVLVDGVDLTALser 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1333 GLHTLRSRITIIPQ-----------DPVLFPgsLR---MNLDLLQENTDEgiwaALETVQLKAFVTSLPGQLqyecSGqg 1398
Cdd:COG1135 76 ELRAARRKIGMIFQhfnllssrtvaENVALP--LEiagVPKAEIRKRVAE----LLELVGLSDKADAYPSQL----SG-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1399 ddlsvGQKQllclarallrktQILILDEATASVDPGT---------EIQMQAALerwfaqcTVLLIAHRL---RSVmnCA 1466
Cdd:COG1135 144 -----GQKQrvgiaralannpKVLLCDEATSALDPETtrsildllkDINRELGL-------TIVLITHEMdvvRRI--CD 209
|
250 260
....*....|....*....|..
gi 13591916 1467 RVLVMDEGQVAESGSPAQLLAQ 1488
Cdd:COG1135 210 RVAVLENGRIVEQGPVLDVFAN 231
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1270-1490 |
8.51e-22 |
|
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: 96.08 E-value: 8.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1270 GLRHRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHtLRSRITIIPQDPV 1349
Cdd:COG4555 6 NLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVLPDERG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1350 LFPG-SLRMNLDL---LQENTDEGIWAALETVqLKAFvtSLPGQLQYECSGqgddLSVGQKQLLCLARALLRKTQILILD 1425
Cdd:COG4555 85 LYDRlTVRENIRYfaeLYGLFDEELKKRIEEL-IELL--GLEEFLDRRVGE----LSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13591916 1426 EATASVDPGTEIQMQAALERWFAQ-CTVLLIAHRLRSVMN-CARVLVMDEGQVAESGSPAQLLAQKG 1490
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKEgKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
628-830 |
1.12e-21 |
|
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: 94.91 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 628 SIHNGTFAWSQEspPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG--------SVAYVPQEAW 699
Cdd:cd03235 1 EVEDLTVSYGGH--PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQRRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 700 VQNTS------VVENVCFRQELDLPWL-----QEVLEACALG--SDVAsfpagvHTPVGEqgmnLSGGQKQRLSLARAVY 766
Cdd:cd03235 79 IDRDFpisvrdVVLMGLYGHKGLFRRLskadkAKVDEALERVglSELA------DRQIGE----LSGGQQQRVLLARALV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 767 RRAAVYLMDDPLAALDAHvSQEVFKQVIgpSGL-LQGTTRILVTHTLH-VLPQADQILVLANGTIA 830
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPK-TQEDIYELL--RELrREGMTILVVTHDLGlVLEYFDRVLLLNRTVVA 211
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1280-1488 |
1.46e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 96.62 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRITIIPQDP----------- 1348
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQNPdnqfvgatvqd 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1349 -VLFpgSLRMN---LDLLQENTDEgiwaALETVQLKAFVTSLPGQLqyecSGqgddlsvGQKQLLCLARALLRKTQILIL 1424
Cdd:PRK13635 102 dVAF--GLENIgvpREEMVERVDQ----ALRQVGMEDFLNREPHRL----SG-------GQKQRVAIAGVLALQPDIIIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 1425 DEATASVDPGTEIQMQAALERWFAQ--CTVLLIAHRLRSVMNCARVLVMDEGQVAESGSPAQLLAQ 1488
Cdd:PRK13635 165 DEATSMLDPRGRREVLETVRQLKEQkgITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
644-841 |
1.75e-21 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 95.13 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG------------SVAYVPQEAWV-QNTSVVENVC 710
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGYVPQEPALyPDLTVRENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 711 FRQEL-DLP------WLQEVLEACALgSDVAsfpagvHTPVGeqgmNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDA 783
Cdd:COG1131 96 FFARLyGLPrkeareRIDELLELFGL-TDAA------DRKVG----TLSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 784 HVSQEvFKQVIgpSGLL-QGTTRILVTHTLHVLPQ-ADQILVLANGTIAEMGSYQDLLHR 841
Cdd:COG1131 165 EARRE-LWELL--RELAaEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1264-1485 |
1.96e-21 |
|
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: 94.55 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1264 IEFRDFGLRHRPElpMAVQGVSLKIHAGEKVGIVGRTGAGKSSLtwglLRL---------QEATEGGIWIDGVPITDMGL 1334
Cdd:cd03260 1 IELRDLNVYYGDK--HALKDISLDIPKGEITALIGPSGCGKSTL----LRLlnrlndlipGAPDEGEVLLDGKDIYDLDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1335 H--TLRSRITIIPQDPVLFPGSLRMNLDL--------LQENTDEGIWAALETVQLKAFVTSLPGQLqyecsgqgdDLSVG 1404
Cdd:cd03260 75 DvlELRRRVGMVFQKPNPFPGSIYDNVAYglrlhgikLKEELDERVEEALRKAALWDEVKDRLHAL---------GLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1405 QKQLLCLARALLRKTQILILDEATASVDPGTEIQMQAALERWFAQCTVLLIAHRLRSVMNCA-RVLVMDEGQVAESGSPA 1483
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVAdRTAFLLNGRLVEFGPTE 225
|
..
gi 13591916 1484 QL 1485
Cdd:cd03260 226 QI 227
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1280-1484 |
2.13e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 96.27 E-value: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMG--LHTLRSRITIIPQDP--VLFPGSL 1355
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKvkLSDIRKKVGLVFQYPeyQLFEETI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1356 R-------MNLDLLQENTDEGIWAALETVQLKafvtslpgqlqYEcsGQGD----DLSVGQKQLLCLARALLRKTQILIL 1424
Cdd:PRK13637 102 EkdiafgpINLGLSEEEIENRVKRAMNIVGLD-----------YE--DYKDkspfELSGGQKRRVAIAGVVAMEPKILIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13591916 1425 DEATASVDPGT--EI--QMQAALERWfaQCTVLLIAHRLRSVMNCA-RVLVMDEGQVAESGSPAQ 1484
Cdd:PRK13637 169 DEPTAGLDPKGrdEIlnKIKELHKEY--NMTIILVSHSMEDVAKLAdRIIVMNKGKCELQGTPRE 231
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
628-828 |
7.23e-21 |
|
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: 92.53 E-value: 7.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 628 SIHNGTFAWSQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-------------SVAYV 694
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltklslkelrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 695 PQEAWVQ--NTSVVENVCF--------RQELDlpwlQEVLEACALgsdvasfpagvhtpVGEQGM------NLSGGQKQR 758
Cdd:cd03225 81 FQNPDDQffGPTVEEEVAFglenlglpEEEIE----ERVEEALEL--------------VGLEGLrdrspfTLSGGQKQR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13591916 759 LSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKQVIGpsglL--QGTTRILVTHTLH-VLPQADQILVLANGT 828
Cdd:cd03225 143 VAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKK----LkaEGKTIIIVTHDLDlLLELADRVIVLEDGK 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1269-1477 |
9.12e-21 |
|
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: 92.21 E-value: 9.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1269 FGLRHRPelpmAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMglhtlRSRITIIPQDP 1348
Cdd:cd03235 7 VSYGGHP----VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1349 VL---FPGSLR----MNLD----LLQENTDEG---IWAALETVQLKAFVTSLPGQLqyecSGqgddlsvGQKQLLCLARA 1414
Cdd:cd03235 78 SIdrdFPISVRdvvlMGLYghkgLFRRLSKADkakVDEALERVGLSELADRQIGEL----SG-------GQQQRVLLARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13591916 1415 LLRKTQILILDEATASVDPGTEIQMQAALERWFAQ-CTVLLIAHRLRSVMN-CARVLVMDEGQVA 1477
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEyFDRVLLLNRTVVA 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
634-833 |
1.24e-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: 91.81 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 634 FAWSQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-----------SVAYVPQE-AWVQ 701
Cdd:cd03259 6 LSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvtgvpperrNIGMVFQDyALFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 702 NTSVVENVCF--------RQELDLPWLqEVLEACALGSDVASFPAGvhtpvgeqgmnLSGGQKQRLSLARAVYRRAAVYL 773
Cdd:cd03259 86 HLTVAENIAFglklrgvpKAEIRARVR-ELLELVGLEGLLNRYPHE-----------LSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13591916 774 MDDPLAALDAHVSQEVFKQVigpSGLL--QGTTRILVTHTL-HVLPQADQILVLANGTIAEMG 833
Cdd:cd03259 154 LDEPLSALDAKLREELREEL---KELQreLGITTIYVTHDQeEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1264-1488 |
1.60e-20 |
|
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: 91.76 E-value: 1.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1264 IEFRDFGLRHRPELP--MAVQGVSLKIHAGEKVGIVGRTGAGKSSLtwglLR----LQEATEGGIWIDGVPITDmglhtL 1337
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTL----LRiiagLERPTSGEVLVDGEPVTG-----P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1338 RSRITIIPQDPVLFP-GSLRMN--LDLLQENTDEGIW-----AALETVQLKAFVTSLPGQLqyecSGqgddlsvGQKQLL 1409
Cdd:cd03293 72 GPDRGYVFQQDALLPwLTVLDNvaLGLELQGVPKAEAreraeELLELVGLSGFENAYPHQL----SG-------GMRQRV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1410 CLARALLRKTQILILDEATASVDPGTEIQMQAALER-WFAQC-TVLLIAHRLR-SVMNCARVLVMdegqvaeSGSPAQLL 1486
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDALTREQLQEELLDiWRETGkTVLLVTHDIDeAVFLADRVVVL-------SARPGRIV 213
|
..
gi 13591916 1487 AQ 1488
Cdd:cd03293 214 AE 215
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1264-1491 |
2.24e-20 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 92.07 E-value: 2.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1264 IEFRD--FGLRHRPelpmAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMglhtlRSRI 1341
Cdd:COG1121 7 IELENltVSYGGRP----VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1342 TIIPQDPVL---FPGSLR----MNLD-------LLQENTDEGIWAALETVQLKAFVTSLPGQLqyecSGqgddlsvGQKQ 1407
Cdd:COG1121 78 GYVPQRAEVdwdFPITVRdvvlMGRYgrrglfrRPSRADREAVDEALERVGLEDLADRPIGEL----SG-------GQQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1408 llclarallrKT----------QILILDEATASVDPGTEIQMQAALERWFAQ-CTVLLIAHRLRSVMNCA-RVLVMDEGQ 1475
Cdd:COG1121 147 ----------RVllaralaqdpDLLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHDLGAVREYFdRVLLLNRGL 216
|
250
....*....|....*.
gi 13591916 1476 VAeSGSPAQLLAQKGL 1491
Cdd:COG1121 217 VA-HGPPEEVLTPENL 231
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1264-1486 |
2.36e-20 |
|
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: 92.41 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1264 IEFRD--FGLRHRPelpmAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRI 1341
Cdd:COG1120 2 LEAENlsVGYGGRP----VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1342 TIIPQDPVL-FPGSLR----M----NLDLLQENTDEG---IWAALETVQLKAF----VTSLpgqlqyecSGqgddlsvGQ 1405
Cdd:COG1120 78 AYVPQEPPApFGLTVRelvaLgrypHLGLFGRPSAEDreaVEEALERTGLEHLadrpVDEL--------SG-------GE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1406 KQLLCLARALLRKTQILILDEATASVDPGTEIQMQAALERWFAQ--CTVLLIAHRLRSVMNCA-RVLVMDEGQVAESGSP 1482
Cdd:COG1120 143 RQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErgRTVVMVLHDLNLAARYAdRLVLLKDGRIVAQGPP 222
|
....
gi 13591916 1483 AQLL 1486
Cdd:COG1120 223 EEVL 226
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1264-1489 |
2.73e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 92.36 E-value: 2.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1264 IEFRDFGLRHRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRITI 1343
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1344 IPQDP-VLFPGS-----LRMNLDLLQENTDEgIWAALETVQLKafvTSLPGQLQYECSgqgdDLSVGQKQLLCLARALLR 1417
Cdd:PRK13632 88 IFQNPdNQFIGAtveddIAFGLENKKVPPKK-MKDIIDDLAKK---VGMEDYLDKEPQ----NLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13591916 1418 KTQILILDEATASVDP-GTEIQMQAALE-RWFAQCTVLLIAHRLRSVMNCARVLVMDEGQVAESGSPAQLLAQK 1489
Cdd:PRK13632 160 NPEIIIFDESTSMLDPkGKREIKKIMVDlRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
627-833 |
8.43e-20 |
|
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: 88.52 E-value: 8.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 627 ISIHNGTFAWSQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGS------------VAYV 694
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdlekalsslISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 695 PQEAWVQNTSVVENVcfrqeldlpwlqevleacalgsdvasfpagvhtpvgeqGMNLSGGQKQRLSLARAVYRRAAVYLM 774
Cdd:cd03247 81 NQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 13591916 775 DDPLAALDAHVSQEVFKQVIgpsGLLQGTTRILVTHTLHVLPQADQILVLANGTIAEMG 833
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIF---EVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1269-1476 |
1.10e-19 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 88.85 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1269 FGLRHRPELpmaVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPItdmGLHTLRSRITIIPQDP 1348
Cdd:cd03226 7 FSYKKGTEI---LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1349 --VLFPGSLRMNLDLLQENTDEGIWAA---LETVQLKAFVTSLPgqlqyecsgqgDDLSVGQKQLLCLARALLRKTQILI 1423
Cdd:cd03226 81 dyQLFTDSVREELLLGLKELDAGNEQAetvLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 13591916 1424 LDEATASVDPGteiQMQaALERWFAQC-----TVLLIAHRLRSVMNCA-RVLVMDEGQV 1476
Cdd:cd03226 150 FDEPTSGLDYK---NME-RVGELIRELaaqgkAVIVITHDYEFLAKVCdRVLLLANGAI 204
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
644-834 |
1.64e-19 |
|
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: 89.16 E-value: 1.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGK-----SSLLSALLGELLKVEGSVSIEGS---------------VAYVPQEAWVQNT 703
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKstllrLLNRLNDLIPGAPDEGEVLLDGKdiydldvdvlelrrrVGMVFQKPNPFPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 704 SVVENVCF---------RQELDlPWLQEVLEACALGSDVASFPAGVHtpvgeqgmnLSGGQKQRLSLARAVYRRAAVYLM 774
Cdd:cd03260 96 SIYDNVAYglrlhgiklKEELD-ERVEEALRKAALWDEVKDRLHALG---------LSGGQQQRLCLARALANEPEVLLL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13591916 775 DDPLAALDAhVSQEVFKQVIGpsGLLQGTTRILVTHTLHvlpQA----DQILVLANGTIAEMGS 834
Cdd:cd03260 166 DEPTSALDP-ISTAKIEELIA--ELKKEYTIVIVTHNMQ---QAarvaDRTAFLLNGRLVEFGP 223
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
644-831 |
3.16e-19 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 88.18 E-value: 3.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKssllsallgellkvEGSVSIEG-----------------SVAYVPQEA-WVQNTSV 705
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKstllnilggldrptSGEVLIDGqdisslserelarlrrrHIGFVFQFFnLLPELTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 706 VENVCFRQEL-------DLPWLQEVLEACALGSDVASFPAgvhtpvgeqgmNLSGGQKQRLSLARAVYRRAAVYLMDDPL 778
Cdd:COG1136 104 LENVALPLLLagvsrkeRRERARELLERVGLGDRLDHRPS-----------QLSGGQQQRVAIARALVNRPKLILADEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 13591916 779 AALDAHVSQEVFKqvigpsgLLQ------GTTRILVTHTLHVLPQADQILVLANGTIAE 831
Cdd:COG1136 173 GNLDSKTGEEVLE-------LLRelnrelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
633-831 |
4.23e-19 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 88.61 E-value: 4.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 633 TFAWSQESPPCLHGINLTVPQGCLLAVVGPVGAGK----------SSLlsallgellkVEGSVSIEG--------SVAYV 694
Cdd:COG1116 16 RFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKstllrliaglEKP----------TSGEVLVDGkpvtgpgpDRGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 695 PQEA----WvqnTSVVENVCF--------RQELDlPWLQEVLEACALGSDVASFPAgvhtpvgeqgmNLSGGQKQRLSLA 762
Cdd:COG1116 86 FQEPallpW---LTVLDNVALglelrgvpKAERR-ERARELLELVGLAGFEDAYPH-----------QLSGGMRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 763 RAVYRRAAVYLMDDPLAALDA----HVSQEVFKqvigpsgLLQ--GTTRILVTHTLH---VLpqADQILVLAN--GTIAE 831
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDAltreRLQDELLR-------LWQetGKTVLFVTHDVDeavFL--ADRVVVLSArpGRIVE 221
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1280-1487 |
4.78e-19 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 88.61 E-value: 4.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLtwglLR----LQEATEGGIWIDGVPITDMGlhtlrSRITIIPQDPVLFP--- 1352
Cdd:COG1116 26 ALDDVSLTVAAGEFVALVGPSGCGKSTL----LRliagLEKPTSGEVLVDGKPVTGPG-----PDRGVVFQEPALLPwlt 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1353 --GSLRMNLDLLQENTDEG---IWAALETVQLKAFVTSLPGQLqyecSGqgddlsvGQKQLLCLARALLRKTQILILDEA 1427
Cdd:COG1116 97 vlDNVALGLELRGVPKAERrerARELLELVGLAGFEDAYPHQL----SG-------GMRQRVAIARALANDPEVLLMDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13591916 1428 TASVDPGTEIQMQAALERWFAQ--CTVLLIAHRLR-SVMNCARVLVMdegqvaeSGSPAQLLA 1487
Cdd:COG1116 166 FGALDALTRERLQDELLRLWQEtgKTVLFVTHDVDeAVFLADRVVVL-------SARPGRIVE 221
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1279-1480 |
5.47e-19 |
|
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: 87.25 E-value: 5.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1279 MAVQGVSLKIHAGeKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGlHTLRSRITIIPQDPVLFPG-SLRM 1357
Cdd:cd03264 14 RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIGYLPQEFGVYPNfTVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1358 NLDLL-------QENTDEGIWAALETVQLKAFVTSLPGQLqyecSGqgddlsvGQKQLLCLARALLRKTQILILDEATAS 1430
Cdd:cd03264 92 FLDYIawlkgipSKEVKARVDEVLELVNLGDRAKKKIGSL----SG-------GMRRRVGIAQALVGDPSILIVDEPTAG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 13591916 1431 VDPGTEIQMQAALERWFAQCTVLLIAHRLRSV-MNCARVLVMDEGQVAESG 1480
Cdd:cd03264 161 LDPEERIRFRNLLSELGEDRIVILSTHIVEDVeSLCNQVAVLNKGKLVFEG 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1264-1476 |
5.49e-19 |
|
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: 87.20 E-value: 5.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1264 IEFRD----FGLRHrpelpmAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMG--LHTL 1337
Cdd:cd03262 1 IEIKNlhksFGDFH------VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKknINEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1338 RSRITIIPQDPVLFPgslrmNLDLLQENTDEGIWA--------------ALETVQLKAFVTSLPGQLqyecSGqgddlsv 1403
Cdd:cd03262 75 RQKVGMVFQQFNLFP-----HLTVLENITLAPIKVkgmskaeaeeraleLLEKVGLADKADAYPAQL----SG------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1404 GQKQLLCLARALLRKTQILILDEATASVDPGT-----EIQMQAALErwfaQCTVLLIAHRL---RSVMNcaRVLVMDEGQ 1475
Cdd:cd03262 139 GQQQRVAIARALAMNPKVMLFDEPTSALDPELvgevlDVMKDLAEE----GMTMVVVTHEMgfaREVAD--RVIFMDDGR 212
|
.
gi 13591916 1476 V 1476
Cdd:cd03262 213 I 213
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
627-843 |
5.73e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 92.58 E-value: 5.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 627 ISIHNGTFAWSQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-SVAYVPQEAWVQNTSV 705
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGqPIADYSEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 706 VE------NVCFRQELDLP-------WLQEVLEACALGSDVASfPAGVHTPVGEQGMNLSGGQKQRLSLARAVYRRAAVY 772
Cdd:PRK11160 419 VSqrvhlfSATLRDNLLLAapnasdeALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLL 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13591916 773 LMDDPLAALDAHVSQEVFKqvigpsgLL----QGTTRILVTHTLHVLPQADQILVLANGTIAEMGSYQDLLHRNG 843
Cdd:PRK11160 498 LLDEPTEGLDAETERQILE-------LLaehaQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQG 565
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1280-1481 |
7.19e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 89.86 E-value: 7.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPIT---DMGLHTLRSRITIIPQ---------- 1346
Cdd:PRK11153 20 ALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTalsEKELRKARRQIGMIFQhfnllssrtv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1347 -DPVLFPGSL-RMNLDLLQENTDEgiwaALETVQLKAFVTSLPGQLqyecSGqgddlsvGQKQLLCLARALLRKTQILIL 1424
Cdd:PRK11153 100 fDNVALPLELaGTPKAEIKARVTE----LLELVGLSDKADRYPAQL----SG-------GQKQRVAIARALASNPKVLLC 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13591916 1425 DEATASVDPGT---------EIQMQAALerwfaqcTVLLIAHRL---RSVmnCARVLVMDEGQVAESGS 1481
Cdd:PRK11153 165 DEATSALDPATtrsilellkDINRELGL-------TIVLITHEMdvvKRI--CDRVAVIDAGRLVEQGT 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
644-779 |
8.13e-19 |
|
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: 84.62 E-value: 8.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-------------SVAYVPQEAWVQN-TSVVENV 709
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderkslrkEIGYVFQDPQLFPrLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13591916 710 CFRQELDLP-------WLQEVLEACALGSDvasfpagVHTPVGEQGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLA 779
Cdd:pfam00005 81 RLGLLLKGLskrekdaRAEEALEKLGLGDL-------ADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1280-1485 |
8.58e-19 |
|
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: 87.24 E-value: 8.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMG---LHTLRSRITIIPQDPVLFP---- 1352
Cdd:cd03256 16 ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQIGMIFQQFNLIErlsv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1353 ------GSL-RMNL--DLLQENTDEGI---WAALETVQLKAFVTSLPGQLqyecSGqgddlsvGQKQLLCLARALLRKTQ 1420
Cdd:cd03256 96 lenvlsGRLgRRSTwrSLFGLFPKEEKqraLAALERVGLLDKAYQRADQL----SG-------GQQQRVAIARALMQQPK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13591916 1421 ILILDEATASVDPGT-EIQM----QAALERwfaQCTVLLIAHRLRSVM-NCARVLVMDEGQVAESGSPAQL 1485
Cdd:cd03256 165 LILADEPVASLDPASsRQVMdllkRINREE---GITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1281-1488 |
8.79e-19 |
|
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: 92.12 E-value: 8.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1281 VQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRITIIPQDPVLFPGSLRMNLD 1360
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1361 LLQENTDEGIWAALETVQLKAFVTSLP-GqlqYEC--SGQGDDLSVGQKQLLCLARALLRKTQILILDEATASVDPGTEI 1437
Cdd:COG4618 428 RFGDADPEKVVAAAKLAGVHEMILRLPdG---YDTriGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEA 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 13591916 1438 QMQAALERWFAQ-CTVLLIAHRlRSVMNCA-RVLVMDEGQVAESGSPAQLLAQ 1488
Cdd:COG4618 505 ALAAAIRALKARgATVVVITHR-PSLLAAVdKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1280-1476 |
8.86e-19 |
|
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: 85.14 E-value: 8.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDmGLHTLRSRITIIPQDPVLFPG-SLRMN 1358
Cdd:cd03230 15 ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPEEPSLYENlTVREN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1359 LDLlqentdegiwaaletvqlkafvtslpgqlqyecsgqgddlSVGQKQLLCLARALLRKTQILILDEATASVDPGTEIQ 1438
Cdd:cd03230 94 LKL----------------------------------------SGGMKQRLALAQALLHDPELLILDEPTSGLDPESRRE 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 13591916 1439 MQAALERWFAQ-CTVLLIAHRLRSVMN-CARVLVMDEGQV 1476
Cdd:cd03230 134 FWELLRELKKEgKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1281-1488 |
9.51e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 88.25 E-value: 9.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1281 VQGVSLKIHAGEKVGIVGRTGAGKSS---LTWGLLrlqEATEGGIWIDGVPITDMGLHTLRSRITIIPQDP--------- 1348
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGLL---EAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPdnqfvgatv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1349 ---VLFpgSLR---MNLDLLQENTDEgiwaALETVQLKAFVTSLPGQLqyecSGqgddlsvGQKQLLCLARALLRKTQIL 1422
Cdd:PRK13650 100 eddVAF--GLEnkgIPHEEMKERVNE----ALELVGMQDFKEREPARL----SG-------GQKQRVAIAGAVAMRPKII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13591916 1423 ILDEATASVDPGTEIQMQAALE--RWFAQCTVLLIAHRLRSVMNCARVLVMDEGQVAESGSPAQLLAQ 1488
Cdd:PRK13650 163 ILDEATSMLDPEGRLELIKTIKgiRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
644-841 |
1.03e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 89.36 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKssllsallgellkvEGSVSIEG-----------SVAYVPQE-AWVQNTSVVENVCF 711
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKstllrmiagledptSGEILIGGrdvtdlppkdrNIAMVFQSyALYPHMTVYENIAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 712 --------RQELDlPWLQEVLEACALGSDVASFPAgvhtpvgeqgmNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDA 783
Cdd:COG3839 99 plklrkvpKAEID-RRVREAAELLGLEDLLDRKPK-----------QLSGGQRQRVALGRALVREPKVFLLDEPLSNLDA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13591916 784 HVSQEV---FKQvigpsgLLQ--GTTRILVTH------TLhvlpqADQILVLANGTIAEMGSYQDLLHR 841
Cdd:COG3839 167 KLRVEMraeIKR------LHRrlGTTTIYVTHdqveamTL-----ADRIAVMNDGRIQQVGTPEELYDR 224
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1280-1487 |
1.13e-18 |
|
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: 86.72 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSL----TwGLLRlqeATEGGIWIDGVPITDMGLHtLRSRITIIP--QDPVLFPG 1353
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLfnliS-GFLR---PTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1354 -SLRMNLDL-LQENTDEGIWAA----------------LETVQLKAFVTSLPGqlqyecsgqgdDLSVGQKQLLCLARAL 1415
Cdd:cd03219 90 lTVLENVMVaAQARTGSGLLLArarreereareraeelLERVGLADLADRPAG-----------ELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13591916 1416 LRKTQILILDEATASVDPgTEIQMQAALERWFAQ--CTVLLIAHRLRSVMN-CARVLVMDEGQVAESGSPAQLLA 1487
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNP-EETEELAELIRELRErgITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
627-841 |
1.15e-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: 86.62 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 627 ISIHNGTFAWSQEsPPCLHGINLTVPQGCLLAVVGPVGAGK-------------SsllsallgellkvEGSVSIEG---- 689
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKstllrllngllkpT-------------SGEVLVDGkdit 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 690 ---------SVAYVPQEAWVQ--NTSVVENVCF--------RQELDLpWLQEVLEACALgSDVASFPagVHTpvgeqgmn 750
Cdd:COG1122 67 kknlrelrrKVGLVFQNPDDQlfAPTVEEDVAFgpenlglpREEIRE-RVEEALELVGL-EHLADRP--PHE-------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 751 LSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKQVigpSGL-LQGTTRILVTHTL-HVLPQADQILVLANGT 828
Cdd:COG1122 135 LSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELL---KRLnKEGKTVIIVTHDLdLVAELADRVIVLDDGR 211
|
250
....*....|...
gi 13591916 829 IAEMGSYQDLLHR 841
Cdd:COG1122 212 IVADGTPREVFSD 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1280-1488 |
1.50e-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: 87.31 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMG---LHTLRS-RITIIPQDPVLFPgsl 1355
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRkKISMVFQSFALLP--- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1356 rmNLDLLqENTDEGI--------------WAALETVQLKAFVTSLPGQLqyecSGqgddlsvGQKQLLCLARALLRKTQI 1421
Cdd:cd03294 116 --HRTVL-ENVAFGLevqgvpraereeraAEALELVGLEGWEHKYPDEL----SG-------GMQQRVGLARALAVDPDI 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1422 LILDEATASVDPGTEIQMQAALERWFA--QCTVLLIAHRLRSVMNCA-RVLVMDEGQVAESGSPAQLLAQ 1488
Cdd:cd03294 182 LLMDEAFSALDPLIRREMQDELLRLQAelQKTIVFITHDLDEALRLGdRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1280-1487 |
1.71e-18 |
|
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: 85.95 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTlRSR--ITIIPQDPVLFPG-SLR 1356
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE-RARagIGYVPEGRRIFPElTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1357 MNLDL-LQENTDEGIWAALETV-----QLKAFVTSLPGQLqyecSGqgddlsvGQKQLLCLARALLRKTQILILDEATAS 1430
Cdd:cd03224 94 ENLLLgAYARRRAKRKARLERVyelfpRLKERRKQLAGTL----SG-------GEQQMLAIARALMSRPKLLLLDEPSEG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 13591916 1431 VDPGTEIQMQAALERWFAQ-CTVLLIAHRLRSVMNCA-RVLVMDEGQVAESGSPAQLLA 1487
Cdd:cd03224 163 LAPKIVEEIFEAIRELRDEgVTILLVEQNARFALEIAdRAYVLERGRVVLEGTAAELLA 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1204-1458 |
2.16e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 91.02 E-value: 2.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1204 SVSAALQVTQTLQWVVRSWTDLENSMVAVERVQDYVHTPKEAPwRLPSSAAQPLWPCGGQIEFRDFGLRHRPELPMaVQG 1283
Cdd:COG4178 304 AASAFGQVQGALSWFVDNYQSLAEWRATVDRLAGFEEALEAAD-ALPEAASRIETSEDGALALEDLTLRTPDGRPL-LED 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1284 VSLKIHAGEKVGIVGRTGAGKSSLtwglLRlqeaTEGGIW--IDGVPITDMGLHTLrsritIIPQDPVLFPGSLRMNL-- 1359
Cdd:COG4178 382 LSLSLKPGERLLITGPSGSGKSTL----LR----AIAGLWpyGSGRIARPAGARVL-----FLPQRPYLPLGTLREALly 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1360 -DLLQENTDEGIWAALETVQLKAFVTSLpgqlqyecsGQGDD----LSVGQKQLLCLARALLRKTQILILDEATASVDPG 1434
Cdd:COG4178 449 pATAEAFSDAELREALEAVGLGHLAERL---------DEEADwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519
|
250 260
....*....|....*....|....
gi 13591916 1435 TEIQMQAALERWFAQCTVLLIAHR 1458
Cdd:COG4178 520 NEAALYQLLREELPGTTVISVGHR 543
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1281-1480 |
2.75e-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: 84.02 E-value: 2.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1281 VQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRITIIPQdpvlfpgslrmnld 1360
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ-------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1361 llqentdegiwaALETVQLKAF----VTSLpgqlqyecSGqgddlsvGQKQLLCLARALLRKTQILILDEATASVDPGTE 1436
Cdd:cd03214 81 ------------ALELLGLAHLadrpFNEL--------SG-------GERQRVLLARALAQEPPILLLDEPTSHLDIAHQ 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 13591916 1437 IQMQAALERWFAQ--CTVLLIAHRLRSVMNCA-RVLVMDEGQVAESG 1480
Cdd:cd03214 134 IELLELLRRLARErgKTVVMVLHDLNLAARYAdRVILLKDGRIVAQG 180
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1280-1480 |
3.18e-18 |
|
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: 84.88 E-value: 3.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLtwglLR----LQEATEGGIWIDGVPITDMGLHtlRSRITIIPQDPVLFP--- 1352
Cdd:cd03259 15 ALDDLSLTVEPGEFLALLGPSGCGKTTL----LRliagLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFPhlt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1353 -------GsLRMNLdLLQENTDEGIWAALETVQLKAFVTSLPGQLqyecSGqgddlsvGQKQLLCLARALLRKTQILILD 1425
Cdd:cd03259 89 vaeniafG-LKLRG-VPKAEIRARVRELLELVGLEGLLNRYPHEL----SG-------GQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 13591916 1426 EATASVDPGTEIQMQAALERWFAQ--CTVLLIAHRLRSVMNCA-RVLVMDEGQVAESG 1480
Cdd:cd03259 156 EPLSALDAKLREELREELKELQRElgITTIYVTHDQEEALALAdRIAVMNEGRIVQVG 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
644-840 |
4.29e-18 |
|
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: 85.25 E-value: 4.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGS----------------VAYVPQE-AWVQNTSVV 706
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlrrrMGMLFQSgALFDSLTVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 707 ENVCF--RQELDLP--WLQEV----LEACALGSDVASFPAgvhtpvgeqgmNLSGGQKQRLSLARAVYRRAAVYLMDDPL 778
Cdd:cd03261 96 ENVAFplREHTRLSeeEIREIvlekLEAVGLRGAEDLYPA-----------ELSGGMKKRVALARALALDPELLLYDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 779 AALDAhVSQEVFKQVIgpsGLLQ---GTTRILVTHTLH-VLPQADQILVLANGTIAEMGSYQDLLH 840
Cdd:cd03261 165 AGLDP-IASGVIDDLI---RSLKkelGLTSIMVTHDLDtAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
626-834 |
4.50e-18 |
|
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: 84.39 E-value: 4.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 626 RISIHNGTFAWSQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-------------SVA 692
Cdd:cd03369 6 EIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 693 YVPQEAWVQNTSVVENVCFRQELDLPWLQEVLEacalgsdvasfpagvhtpVGEQGMNLSGGQKQRLSLARAVYRRAAVY 772
Cdd:cd03369 86 IIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13591916 773 LMDDPLAALDAHVSQEVFKQVigpSGLLQGTTRILVTHTLHVLPQADQILVLANGTIAEMGS 834
Cdd:cd03369 148 VLDEATASIDYATDALIQKTI---REEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1262-1492 |
5.80e-18 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 90.86 E-value: 5.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1262 GQIEFRDFGLRH--RPELPMaVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLR-------------------------- 1313
Cdd:PTZ00265 1164 GKIEIMDVNFRYisRPNVPI-YKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfydlkndhhivfknehtndmtneqdy 1242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1314 ---------LQEATE-------------------GGIWIDGVPITDMGLHTLRSRITIIPQDPVLFPGSLRMNLDLLQEN 1365
Cdd:PTZ00265 1243 qgdeeqnvgMKNVNEfsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKED 1322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1366 -TDEGIWAALETVQLKAFVTSLPGQLQYECSGQGDDLSVGQKQLLCLARALLRKTQILILDEATASVDPGTEIQMQAALE 1444
Cdd:PTZ00265 1323 aTREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1402
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 1445 --RWFAQCTVLLIAHRLRSVMNCARVLVMDEGQ-----VAESGSPAQLL-AQKGLF 1492
Cdd:PTZ00265 1403 diKDKADKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLsVQDGVY 1458
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
644-841 |
5.90e-18 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 87.12 E-value: 5.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLsallgellKV--------EGSVSIEGSVAYV---PQE---AWV-QN------ 702
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLL--------RIiagletpdSGRIVLNGRDLFTnlpPRErrvGFVfQHyalfph 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 703 TSVVENVCF-----------RQELDLPWLQEV-LEACAlgsdvASFPAgvhtpvgeqgmNLSGGQKQRLSLARAVYRRAA 770
Cdd:COG1118 90 MTVAENIAFglrvrppskaeIRARVEELLELVqLEGLA-----DRYPS-----------QLSGGQRQRVALARALAVEPE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13591916 771 VYLMDDPLAALDAHVSQEVFKQVigpSGLLQ--GTTRILVTHTL-HVLPQADQILVLANGTIAEMGSYQDLLHR 841
Cdd:COG1118 154 VLLLDEPFGALDAKVRKELRRWL---RRLHDelGGTTVFVTHDQeEALELADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
644-829 |
6.07e-18 |
|
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: 84.08 E-value: 6.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-----------------SVAYVPQE-AWVQNTSV 705
Cdd:cd03255 20 LKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGtdisklsekelaafrrrHIGFVFQSfNLLPDLTA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 706 VENV-------CFRQELDLPWLQEVLEACALGSDVASFPAgvhtpvgeqgmNLSGGQKQRLSLARAVYRRAAVYLMDDPL 778
Cdd:cd03255 100 LENVelplllaGVPKKERRERAEELLERVGLGDRLNHYPS-----------ELSGGQQQRVAIARALANDPKIILADEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 13591916 779 AALDAHVSQEVFKqvigpsgLLQ------GTTRILVTHTLHVLPQADQILVLANGTI 829
Cdd:cd03255 169 GNLDSETGKEVME-------LLRelnkeaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1264-1484 |
6.13e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 84.33 E-value: 6.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1264 IEFRDFGLRHRPElPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDM---GLHTLRSR 1340
Cdd:COG2884 2 IRFENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1341 ITIIPQDP-----------VLFPgsLR---MNLDLLQENTDEgiwaALETVQLKAFVTSLPGQLqyecSGqgddlsvGQK 1406
Cdd:COG2884 81 IGVVFQDFrllpdrtvyenVALP--LRvtgKSRKEIRRRVRE----VLDLVGLSDKAKALPHEL----SG-------GEQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1407 QLLCLARALLRKTQILILDEATASVDPGT--EIqMQaALERwFAQ--CTVLLIAHRLRSVMNC-ARVLVMDEGQVAESGS 1481
Cdd:COG2884 144 QRVAIARALVNRPELLLADEPTGNLDPETswEI-ME-LLEE-INRrgTTVLIATHDLELVDRMpKRVLELEDGRLVRDEA 220
|
...
gi 13591916 1482 PAQ 1484
Cdd:COG2884 221 RGV 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
644-833 |
7.66e-18 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 83.84 E-value: 7.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGS-VAYVPQE----AWV-QN------TSVVENVCF 711
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdVTDLPPKdrdiAMVfQNyalyphMTVYDNIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 712 --------RQELDlpwlQEVLEACALgsdvasfpAGVHTPVGEQGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDA 783
Cdd:cd03301 96 glklrkvpKDEID----ERVREVAEL--------LQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 13591916 784 HVSQEVFKQVigpSGLLQ--GTTRILVTH-TLHVLPQADQILVLANGTIAEMG 833
Cdd:cd03301 164 KLRVQMRAEL---KRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1264-1482 |
9.64e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 85.19 E-value: 9.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1264 IEFRDFGLRHRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRITI 1343
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1344 IPQDPV-LFPGSLRM--------NLDLLQENTDEGIWAALETVQLKAFVTSLPgqlqyecsgqgDDLSVGQKQLLCLARA 1414
Cdd:PRK13648 88 VFQNPDnQFVGSIVKydvafgleNHAVPYDEMHRRVSEALKQVDMLERADYEP-----------NALSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1415 LLRKTQILILDEATASVDPGTEIQMQAALERWFAQ--CTVLLIAHRLRSVMNCARVLVMDEGQVAESGSP 1482
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhnITIISITHDLSEAMEADHVIVMNKGTVYKEGTP 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
627-831 |
9.68e-18 |
|
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: 83.68 E-value: 9.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 627 ISIHNGTFAWSQESPPC--LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG--------SVAYVPQ 696
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGepvtgpgpDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 697 EA----WvqnTSVVENVCFRqeLDLPWL---------QEVLEACALGSDVASFPAgvhtpvgeqgmNLSGGQKQRLSLAR 763
Cdd:cd03293 81 QDallpW---LTVLDNVALG--LELQGVpkaeareraEELLELVGLSGFENAYPH-----------QLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13591916 764 AVYRRAAVYLMDDPLAALDA----HVSQEVFKQVIGpsgllQGTTRILVTHTLH---VLpqADQILVLAN--GTIAE 831
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDAltreQLQEELLDIWRE-----TGKTVLLVTHDIDeavFL--ADRVVVLSArpGRIVA 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1285-1488 |
1.08e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 84.04 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1285 SLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTlrsR-ITIIPQDPVLFPG-SLRMNLDL- 1361
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE---RpVSMLFQENNLFPHlTVAQNIGLg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1362 ------LQENTDEGIWAALETVQLKAFVTSLPGQLqyecSGqgddlsvGQKQLLCLARALLRKTQILILDEATASVDPGT 1435
Cdd:COG3840 96 lrpglkLTAEQRAQVEQALERVGLAGLLDRLPGQL----SG-------GQRQRVALARCLVRKRPILLLDEPFSALDPAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 13591916 1436 EIQM-----QAALERwfaQCTVLLIAHRLRSVMN-CARVLVMDEGQVAESGSPAQLLAQ 1488
Cdd:COG3840 165 RQEMldlvdELCRER---GLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDG 220
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1266-1478 |
1.28e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 84.74 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1266 FRDFGLRHRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDM---GLHTLRSRIT 1342
Cdd:PRK10419 13 YAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1343 IIPQDPvlfPGS--------------LRMNLDLLQENTDEGIWAALETVQLKAFVTS-LPGQLqyecSGqgddlsvGQKQ 1407
Cdd:PRK10419 93 MVFQDS---ISAvnprktvreiirepLRHLLSLDKAERLARASEMLRAVDLDDSVLDkRPPQL----SG-------GQLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13591916 1408 LLCLARALLRKTQILILDEATASVDPGTEIQMQAALERWFAQ--CTVLLIAHRLRSVMN-CARVLVMDEGQVAE 1478
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfgTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
644-829 |
2.19e-17 |
|
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: 81.33 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGS-------------VAYVPQeawvqntsvvenvc 710
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKdlaslspkelarkIAYVPQ-------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 711 frqeldlpwlqeVLEACalgsDVASFpagVHTPVGEqgmnLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVF 790
Cdd:cd03214 81 ------------ALELL----GLAHL---ADRPFNE----LSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 13591916 791 KQVIGPSGlLQGTTRILVTHTL-HVLPQADQILVLANGTI 829
Cdd:cd03214 138 ELLRRLAR-ERGKTVVMVLHDLnLAARYADRVILLKDGRI 176
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
644-829 |
2.84e-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: 80.90 E-value: 2.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG------------SVAYVPQEAWV-QNTSVVENVc 710
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGkdikkepeevkrRIGYLPEEPSLyENLTVRENL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 711 frqeldlpwlqevleacalgsdvasfpagvhtpvgeqgmNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAhVSQEVF 790
Cdd:cd03230 95 ---------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDP-ESRREF 134
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 13591916 791 KQVIgpSGLL-QGTTRILVTHTLHVLPQ-ADQILVLANGTI 829
Cdd:cd03230 135 WELL--RELKkEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
628-828 |
3.06e-17 |
|
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: 80.37 E-value: 3.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 628 SIHNGTFAWsqESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-SVAYVPQEAWVQNTSVV 706
Cdd:cd00267 1 EIENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGkDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 707 envcfrqeldlpwLQevleacalgsdvasfpagvhtpvgeqgmnLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVS 786
Cdd:cd00267 79 -------------PQ-----------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 13591916 787 QEVFKQVigpSGLLQ-GTTRILVTHTL-HVLPQADQILVLANGT 828
Cdd:cd00267 117 ERLLELL---RELAEeGRTVIIVTHDPeLAELAADRVIVLKDGK 157
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1264-1487 |
4.41e-17 |
|
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: 82.35 E-value: 4.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1264 IEFRDFGLRhRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRITI 1343
Cdd:cd03295 1 IEFENVTKR-YGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1344 IPQDPVLFPG-SLRMNLDLL-------QENTDEGIWAALETVQL--KAFVTSLPGQLqyecSGqgddlsvGQKQLLCLAR 1413
Cdd:cd03295 80 VIQQIGLFPHmTVEENIALVpkllkwpKEKIRERADELLALVGLdpAEFADRYPHEL----SG-------GQQQRVGVAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13591916 1414 ALLRKTQILILDEATASVDPGTEIQMQAALERWFAQC--TVLLIAHRLRSVMNCA-RVLVMDEGQVAESGSPAQLLA 1487
Cdd:cd03295 149 ALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELgkTIVFVTHDIDEAFRLAdRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
644-828 |
5.91e-17 |
|
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: 80.31 E-value: 5.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-SVAYVPQEAWVQNTSVveNVCFRQELDLPWLqE 722
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGeDLTDLEDELPPLRRRI--GMVFQDFALFPHL-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 723 VLEACALGsdvasfpagvhtpvgeqgmnLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKQVigpSGLLQ- 801
Cdd:cd03229 93 VLENIALG--------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALL---KSLQAq 149
|
170 180
....*....|....*....|....*....
gi 13591916 802 -GTTRILVTHTLH-VLPQADQILVLANGT 828
Cdd:cd03229 150 lGITVVLVTHDLDeAARLADRVVVLRDGK 178
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
1014-1235 |
7.59e-17 |
|
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: 83.31 E-value: 7.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1014 RASCLLFRSLLWDVARSPIGFFERTPVGNLLNRFSKETDIVDVDIPDKMRTLLTYAFGLLEVGLAVSMATPLAIVAILPL 1093
Cdd:cd18600 100 TVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIGAITVVSILQPYIFLATVPV 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1094 MLLYAGFQSLYVATCCQLRRLESASYSSVCSHLAETFQGSQVVRAFQAQGPFTAQHDALMDENQRISFPRLVADRWLAAN 1173
Cdd:cd18600 180 IIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMR 259
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13591916 1174 LELLGNgLVFVAATCAVLSKAHLSAGLAGFSVSAALQVTQTLQWVVRSWTDLENSMVAVERV 1235
Cdd:cd18600 260 IEMIFV-IFFTAVTFISIGTTGDGEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSRI 320
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
634-829 |
7.81e-17 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 80.63 E-value: 7.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 634 FAWSQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-------------SVAYVPQE-AW 699
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplsampppewrrQVAYVPQEpAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 700 VQNTsVVENVCF-----RQELDLPWLQEVLEACALGSDVASFPAGvhtpvgeqgmNLSGGQKQRLSLARAVYRRAAVYLM 774
Cdd:COG4619 86 WGGT-VRDNLPFpfqlrERKFDRERALELLERLGLPPDILDKPVE----------RLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13591916 775 DDPLAALDAHVSQEVFKqvigpsgLLQ------GTTRILVTHTLHVLPQ-ADQILVLANGTI 829
Cdd:COG4619 155 DEPTSALDPENTRRVEE-------LLReylaeeGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1273-1489 |
8.32e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 82.59 E-value: 8.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1273 HRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPI--TDMGLHTLRSRITIIPQDP-- 1348
Cdd:PRK13636 14 NYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLRESVGMVFQDPdn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1349 VLFPGSLR-------MNLDLLQENTDEGIWAALEtvqlKAFVTSLPGQLQYEcsgqgddLSVGQKQLLCLARALLRKTQI 1421
Cdd:PRK13636 94 QLFSASVYqdvsfgaVNLKLPEDEVRKRVDNALK----RTGIEHLKDKPTHC-------LSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13591916 1422 LILDEATASVDP-GTEIQMQAALERWFAQCTVLLIA-HRLRSV-MNCARVLVMDEGQVAESGSPAQLLAQK 1489
Cdd:PRK13636 163 LVLDEPTAGLDPmGVSEIMKLLVEMQKELGLTIIIAtHDIDIVpLYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1264-1475 |
8.94e-17 |
|
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: 80.59 E-value: 8.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1264 IEFRDFGLRHRP---ELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGvpitdmglhtlrsR 1340
Cdd:cd03250 1 ISVEDASFTWDSgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1341 ITIIPQDPVLFPGSLRMNLDLLQENTDEGIWAALETVQLKAFVTSLPGQLQYECSGQGDDLSVGQKQLLCLARALLRKTQ 1420
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDAD 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13591916 1421 ILILDEATASVDPGTeiqmqaalERW-FAQC---------TVLLIAHRLRSVMNCARVLVMDEGQ 1475
Cdd:cd03250 148 IYLLDDPLSAVDAHV--------GRHiFENCilglllnnkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1280-1485 |
9.48e-17 |
|
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: 81.01 E-value: 9.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSlTWGLLR-LQEATEGGIWIDGVPI-TDMglHTLRSRITIIPQDPVLFPG-SLR 1356
Cdd:cd03263 17 AVDDLSLNVYKGEIFGLLGHNGAGKTT-TLKMLTgELRPTSGTAYINGYSIrTDR--KAARQSLGYCPQFDALFDElTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1357 MNLDLL-------QENTDEGIWAALETVQLKAFVTSLPGQLqyecSGqgddlsvGQKQLLCLARALLRKTQILILDEATA 1429
Cdd:cd03263 94 EHLRFYarlkglpKSEIKEEVELLLRVLGLTDKANKRARTL----SG-------GMKRKLSLAIALIGGPSVLLLDEPTS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 13591916 1430 SVDPGTEIQMQAALERWFAQCTVLLIAHRLRSVMN-CARVLVMDEGQVAESGSPAQL 1485
Cdd:cd03263 163 GLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1282-1473 |
9.74e-17 |
|
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: 80.60 E-value: 9.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1282 QGVSLKIHAGEKVGIVGRTGAGKSSLtwglLR----LQEATEGGIWIDGVPITDMGLHtLRSRITIIPQDPVLFPG-SLR 1356
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTL----LRilagLLPPSAGEVLWNGEPIRDARED-YRRRLAYLGHADGLKPElTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1357 MNLDLLQ-----ENTDEGIWAALETVQLKAFVTSLPGQLqyecsgqgddlSVGQKQLLCLARALLRKTQILILDEATASV 1431
Cdd:COG4133 94 ENLRFWAalyglRADREAIDEALEAVGLAGLADLPVRQL-----------SAGQKRRVALARLLLSPAPLWLLDEPFTAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 13591916 1432 DPgteiQMQAALERWFAQ-----CTVLLIAHRLRSVmNCARVLVMDE 1473
Cdd:COG4133 163 DA----AGVALLAELIAAhlargGAVLLTTHQPLEL-AAARVLDLGD 204
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1264-1501 |
1.01e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 82.09 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1264 IEFRDFGLRHRpELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRITI 1343
Cdd:PRK13647 5 IEVEDLHFRYK-DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1344 IPQDP--VLFPGSL-------RMNLDLLQENTDEGIWAALETVQLKAFVTSLPGQLQYecsgqgddlsvGQKQLLCLARA 1414
Cdd:PRK13647 84 VFQDPddQVFSSTVwddvafgPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSY-----------GQKKRVAIAGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1415 LLRKTQILILDEATASVDPGTEIQMQAALERWFAQCTVLLIA-HRLRSVMNCA-RVLVMDEGQVAESGSPAQLLAQKglf 1492
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEWAdQVIVLKEGRVLAEGDKSLLTDED--- 229
|
....*....
gi 13591916 1493 yrLAQESGL 1501
Cdd:PRK13647 230 --IVEQAGL 236
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1280-1487 |
1.11e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 85.14 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQeATEGGIWIDGVPITDMG---LHTLRSRITIIPQDPvlfPGSLR 1356
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDP---NSSLN 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1357 MNLDLLQ---------------ENTDEGIWAALETVQLKAfvtslPGQLQY--ECSGqgddlsvGQKQLLCLARALLRKT 1419
Cdd:PRK15134 377 PRLNVLQiieeglrvhqptlsaAQREQQVIAVMEEVGLDP-----ETRHRYpaEFSG-------GQRQRIAIARALILKP 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13591916 1420 QILILDEATASVDPGTEIQMQAALERWFA--QCTVLLIAHRLRSVMN-CARVLVMDEGQVAESGSPAQLLA 1487
Cdd:PRK15134 445 SLIILDEPTSSLDKTVQAQILALLKSLQQkhQLAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1280-1477 |
1.18e-16 |
|
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: 79.01 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMG-LHTLRSRITIIPQdpvlfpgslrmn 1358
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGIAMVYQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1359 ldllqentdegiwaaletvqlkafvtslpgqlqyecsgqgddLSVGQKQLLCLARALLRKTQILILDEATASVDPGTEIQ 1438
Cdd:cd03216 83 ------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVER 120
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 13591916 1439 MQAALERWFAQ-CTVLLIAHRLRSVMN-CARVLVMDEGQVA 1477
Cdd:cd03216 121 LFKVIRRLRAQgVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1280-1488 |
1.45e-16 |
|
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: 82.41 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEA---TEGGIWIDGVPITDMGLHTLR----SRITIIPQDPVlfp 1352
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRkirgREIQMIFQDPM--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1353 GSL--RMN--------LDLLQENTDEGIWA----ALETVQL---KAFVTSLPGQLqyecSGqgddlsvGQKQLLCLARAL 1415
Cdd:COG0444 97 TSLnpVMTvgdqiaepLRIHGGLSKAEAREraieLLERVGLpdpERRLDRYPHEL----SG-------GMRQRVMIARAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1416 LRKTQILILDEATASVDPgtEIQMQ-----AALERWFaQCTVLLIAHRLrSVMN--CARVLVMDEGQVAESGSPAQLLAQ 1488
Cdd:COG0444 166 ALEPKLLIADEPTTALDV--TIQAQilnllKDLQREL-GLAILFITHDL-GVVAeiADRVAVMYAGRIVEEGPVEELFEN 241
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
644-839 |
2.00e-16 |
|
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: 80.86 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGK---------SSLLSallgellkvEGSVSIEG-------------SVAYVPQEAWVQ 701
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKstllralagLLKPS---------SGEVLLDGrdlaslsrrelarRIAYVPQEPPAP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 702 -NTSVVENVCF-RqeldLPWL--------------QEVLEACalgsDVASFpagVHTPVGEqgmnLSGGQKQRLSLARAV 765
Cdd:COG1120 88 fGLTVRELVALgR----YPHLglfgrpsaedreavEEALERT----GLEHL---ADRPVDE----LSGGERQRVLIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13591916 766 YRRAAVYLMDDPLAALDAHVSQEVFKQVigpSGL--LQGTTRILVTHTL-HVLPQADQILVLANGTIAEMGSYQDLL 839
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELL---RRLarERGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
633-839 |
2.29e-16 |
|
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: 79.93 E-value: 2.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 633 TFAWSQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG----------------SVAYVPQ 696
Cdd:cd03258 10 VFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGtdltllsgkelrkarrRIGMIFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 697 E-AWVQNTSVVENVCFRQELD-LPWLQ------EVLEACALGSDVASFPAgvhtpvgeqgmNLSGGQKQRLSLARAVYRR 768
Cdd:cd03258 90 HfNLLSSRTVFENVALPLEIAgVPKAEieervlELLELVGLEDKADAYPA-----------QLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13591916 769 AAVYLMDDPLAALDAHVSQEVFKqvigpsgLLQ------GTTRILVTHTLHVLPQ-ADQILVLANGTIAEMGSYQDLL 839
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILA-------LLRdinrelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVF 229
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1266-1488 |
3.61e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 80.27 E-value: 3.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1266 FRD-FGLRHRPELpMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRITII 1344
Cdd:COG4167 14 FKYrTGLFRRQQF-EAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1345 PQDPV--LFPGS---------LRMNLDLLQENTDEGIWAALETVQLkafvtsLPGQLQYECSgqgdDLSVGQKQLLCLAR 1413
Cdd:COG4167 93 FQDPNtsLNPRLnigqileepLRLNTDLTAEEREERIFATLRLVGL------LPEHANFYPH----MLSSGQKQRVALAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1414 ALLRKTQILILDEATASVDPGTEIQM-------QAALerwfaQCTVLLIAHRLRSVMNCA-RVLVMDEGQVAESGSPAQL 1485
Cdd:COG4167 163 ALILQPKIIIADEALAALDMSVRSQIinlmlelQEKL-----GISYIYVSQHLGIVKHISdKVLVMHQGEVVEYGKTAEV 237
|
...
gi 13591916 1486 LAQ 1488
Cdd:COG4167 238 FAN 240
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1277-1486 |
3.76e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 82.39 E-value: 3.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1277 LPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGV---PITDMGLHTL-RSRITIIPQDPVLFP 1352
Cdd:PRK10070 40 LSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVdiaKISDAELREVrRKKIAMVFQSFALMP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1353 gslrmNLDLLqENTDEGIWAA---LETVQLKAFVTSLPGQLQYECSGQGDDLSVGQKQLLCLARALLRKTQILILDEATA 1429
Cdd:PRK10070 120 -----HMTVL-DNTAFGMELAginAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1430 SVDPGTEIQMQAALERWFA--QCTVLLIAHRLRSVMNCA-RVLVMDEGQVAESGSPAQLL 1486
Cdd:PRK10070 194 ALDPLIRTEMQDELVKLQAkhQRTIVFISHDLDEAMRIGdRIAIMQNGEVVQVGTPDEIL 253
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
644-841 |
4.40e-16 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 81.68 E-value: 4.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKssllsallgellkvEGSVSIEG-SVAYVPQE----AWV-QN------TSVVENVCF 711
Cdd:COG3842 21 LDDVSLSIEPGEFVALLGPSGCGKttllrmiagfetpdSGRILLDGrDVTGLPPEkrnvGMVfQDyalfphLTVAENVAF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 712 --------RQELDlpwlQEVLEACALgsdvasfpagvhtpVGEQGM------NLSGGQKQRLSLARAVYRRAAVYLMDDP 777
Cdd:COG3842 101 glrmrgvpKAEIR----ARVAELLEL--------------VGLEGLadryphQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 778 LAALDA----HVSQEVFKqvigpsgLLQ--GTTRILVTH------TLhvlpqADQILVLANGTIAEMGSYQDLLHR 841
Cdd:COG3842 163 LSALDAklreEMREELRR-------LQRelGITFIYVTHdqeealAL-----ADRIAVMNDGRIEQVGTPEEIYER 226
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1280-1487 |
1.35e-15 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 78.54 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSL----TwGLLRlqeATEGGIWIDGVPITDMGLHTL-RSRITIIPQDPVLFPG- 1353
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLfnliT-GFYR---PTSGRILFDGRDITGLPPHRIaRLGIARTFQNPRLFPEl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1354 SLRMNLDL-LQENTDEGIWAA---------------------LETVQLKAFVTSLPGqlqyecsgqgdDLSVGQKQLLCL 1411
Cdd:COG0411 95 TVLENVLVaAHARLGRGLLAAllrlprarreereareraeelLERVGLADRADEPAG-----------NLSYGQQRRLEI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1412 ARALLRKTQILILDEATASVDPgTEIQ-MQAALERWFAQ--CTVLLIAHRLRSVMN-CARVLVMDEGQVAESGSPAQLLA 1487
Cdd:COG0411 164 ARALATEPKLLLLDEPAAGLNP-EETEeLAELIRRLRDErgITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAEVRA 242
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1278-1488 |
1.50e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 78.59 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1278 PMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMG-LHTLRSRITIIPQDP-------- 1348
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIRNKAGMVFQNPdnqivati 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1349 ----VLF-PGSLRMNLDLLQENTDEgiwaALETVQLKAFVTSLPGQLqyecSGqgddlsvGQKQLLCLARALLRKTQILI 1423
Cdd:PRK13633 103 veedVAFgPENLGIPPEEIRERVDE----SLKKVGMYEYRRHAPHLL----SG-------GQKQRVAIAGILAMRPECII 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13591916 1424 LDEATASVDPGTEIQMQAALERWFAQ--CTVLLIAHRLRSVMNCARVLVMDEGQVAESGSPAQLLAQ 1488
Cdd:PRK13633 168 FDEPTAMLDPSGRREVVNTIKELNKKygITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1280-1476 |
1.62e-15 |
|
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: 77.14 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSltwgLLR----LQEATEGGIWIDGVPITDMGLHTL----RSRITIIPQDPVLF 1351
Cdd:cd03255 19 ALKGVSLSIEKGEFVAIVGPSGSGKST----LLNilggLDRPTSGEVRVDGTDISKLSEKELaafrRRHIGFVFQSFNLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1352 PG-SLRMNLDL-------LQENTDEGIWAALETVQLKAFVTSLPGQLqyecSGqgddlsvGQKQLLCLARALLRKTQILI 1423
Cdd:cd03255 95 PDlTALENVELplllagvPKKERRERAEELLERVGLGDRLNHYPSEL----SG-------GQQQRVAIARALANDPKIIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 1424 LDEATASVDPGTEIQMQAALERwFAQ---CTVLLIAHRLRSVMNCARVLVMDEGQV 1476
Cdd:cd03255 164 ADEPTGNLDSETGKEVMELLRE-LNKeagTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1281-1487 |
1.91e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 78.60 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1281 VQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRITIIPQDP-VLFPGSL---- 1355
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPdNQFVGATvedd 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1356 ----RMNLDLLQENTDEGIWAALETVQLKAFVTSLPGQlqyecsgqgddLSVGQKQLLCLARALLRKTQILILDEATASV 1431
Cdd:PRK13642 103 vafgMENQGIPREEMIKRVDEALLAVNMLDFKTREPAR-----------LSGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 13591916 1432 DPGTEIQMQAALERWFAQ--CTVLLIAHRLRSVMNCARVLVMDEGQVAESGSPAQLLA 1487
Cdd:PRK13642 172 DPTGRQEIMRVIHEIKEKyqLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1281-1487 |
2.17e-15 |
|
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: 77.20 E-value: 2.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1281 VQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTlRSRITII--PQDPVLFPG-SLRM 1357
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLGIGylPQEASIFRKlTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1358 NLDL---LQENTDEGIWAALETVqLKAF-VTSLPGQLQYECSGqgddlsvGQKQLLCLARALLRKTQILILDEATASVDP 1433
Cdd:cd03218 95 NILAvleIRGLSKKEREEKLEEL-LEEFhITHLRKSKASSLSG-------GERRRVEIARALATNPKFLLLDEPFAGVDP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 13591916 1434 GT--EIQ-MQAALERWfaQCTVLLIAHRLRSVMN-CARVLVMDEGQVAESGSPAQLLA 1487
Cdd:cd03218 167 IAvqDIQkIIKILKDR--GIGVLITDHNVRETLSiTDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1264-1476 |
2.36e-15 |
|
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: 76.68 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1264 IEFRDFGLRHRPELPmAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDM---GLHTLRSR 1340
Cdd:cd03292 1 IEFINVTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1341 ITIIPQDPVLFPG-SLRMNLDLLQENTDEG-------IWAALETVQLKAFVTSLPGQlqyecsgqgddLSVGQKQLLCLA 1412
Cdd:cd03292 80 IGVVFQDFRLLPDrNVYENVAFALEVTGVPpreirkrVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 1413 RALLRKTQILILDEATASVDPGTEIQMQAALERWFAQCTVLLIAHRLRSVMNCA--RVLVMDEGQV 1476
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTrhRVIALERGKL 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
642-838 |
3.05e-15 |
|
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: 76.99 E-value: 3.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 642 PCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-----------SVAYVPQE-AWVQNTSVVENV 709
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedatdvpvqerNVGFVFQHyALFRHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 710 CF----RQELDLP-------WLQEVLEACALGSDVASFPAgvhtpvgeqgmNLSGGQKQRLSLARAVYRRAAVYLMDDPL 778
Cdd:cd03296 96 AFglrvKPRSERPpeaeiraKVHELLKLVQLDWLADRYPA-----------QLSGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13591916 779 AALDAHVSQEV---FKQVIGPSGLlqgtTRILVTHTL-HVLPQADQILVLANGTIAEMGSYQDL 838
Cdd:cd03296 165 GALDAKVRKELrrwLRRLHDELHV----TTVFVTHDQeEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
642-840 |
6.48e-15 |
|
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: 75.55 E-value: 6.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 642 PCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGS--------------VAYVPQEAWV-QNTSVV 706
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEGRRIfPELTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 707 ENV----CFRQELDLPW-LQEVLEAcalgsdvasFPA---GVHTPVGeqgmNLSGGQKQRLSLARAVYRRAAVYLMDDPL 778
Cdd:cd03224 94 ENLllgaYARRRAKRKArLERVYEL---------FPRlkeRRKQLAG----TLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13591916 779 AALDAHVSQEVFKQVIGPSGllQGTTRILVTHTLH-VLPQADQILVLANGTIAEMGSYQDLLH 840
Cdd:cd03224 161 EGLAPKIVEEIFEAIRELRD--EGVTILLVEQNARfALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
626-849 |
7.46e-15 |
|
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: 76.10 E-value: 7.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 626 RISIHNGTFAWSQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-SVAYVPQEAWVQNTS 704
Cdd:cd03288 19 EIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGiDISKLPLHTLRSRLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 705 VV--ENVCF----RQELDlP-------WLQEVLEACALGSDVASFPAGVHTPVGEQGMNLSGGQKQRLSLARAVYRRAAV 771
Cdd:cd03288 99 IIlqDPILFsgsiRFNLD-PeckctddRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13591916 772 YLMDDPLAALDAhVSQEVFKQVIGPSglLQGTTRILVTHTLHVLPQADQILVLANGTIAEMGSYQDLLHRNGALVGLL 849
Cdd:cd03288 178 LIMDEATASIDM-ATENILQKVVMTA--FADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASL 252
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
644-838 |
1.05e-14 |
|
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: 75.35 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-SVAYVPQEAWVQNT-----------SVVENVCF 711
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkDITNLPPHKRPVNTvfqnyalfphlTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 712 --------RQELDlpwlQEVLEA---CALGSDVASFPAgvhtpvgeqgmNLSGGQKQRLSLARAVYRRAAVYLMDDPLAA 780
Cdd:cd03300 96 glrlkklpKAEIK----ERVAEAldlVQLEGYANRKPS-----------QLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13591916 781 LDAHVSQEV---FKQvigpsglLQ---GTTRILVTHTL-HVLPQADQILVLANGTIAEMGSYQDL 838
Cdd:cd03300 161 LDLKLRKDMqleLKR-------LQkelGITFVFVTHDQeEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1280-1476 |
1.62e-14 |
|
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: 74.24 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGlhtlRSRITIIPQDPVLFP------- 1352
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLPEERGLYPkmkvidq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1353 ----GSLR-MNLDLLQENTDEgiWaaLETVQLkafvtslpGQLQYEcsgQGDDLSVGQKQLLCLARALLRKTQILILDEA 1427
Cdd:cd03269 91 lvylAQLKgLKKEEARRRIDE--W--LERLEL--------SEYANK---RVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 13591916 1428 TASVDP-GTEIQMQAALERWFAQCTVLLIAHRLRSVMN-CARVLVMDEGQV 1476
Cdd:cd03269 156 FSGLDPvNVELLKDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKGRA 206
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
627-839 |
1.69e-14 |
|
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: 74.64 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 627 ISIHNGTFAWSqESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-------------SVAY 693
Cdd:cd03295 1 IEFENVTKRYG-GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 694 VPQEAWV-QNTSVVENVCFRQELdLPWLQE-----VLEACAL-GSDVASFpagvhtpVGEQGMNLSGGQKQRLSLARAVY 766
Cdd:cd03295 80 VIQQIGLfPHMTVEENIALVPKL-LKWPKEkirerADELLALvGLDPAEF-------ADRYPHELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 767 RRAAVYLMDDPLAALDAHVS---QEVFKQvigpsglLQ---GTTRILVTHTL-HVLPQADQILVLANGTIAEMGSYQDLL 839
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRdqlQEEFKR-------LQqelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1264-1489 |
2.01e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 75.64 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1264 IEFRDFGLRHRPELPMAVQG---VSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPIT----DMGLHT 1336
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKGldnISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1337 LRSRITIIPQDP--VLFPGSLRMNLDLLQEN----TDEGIWAALETVQLKAFVTSLPGQLQYECSGqgddlsvGQKQLLC 1410
Cdd:PRK13641 83 LRKKVSLVFQFPeaQLFENTVLKDVEFGPKNfgfsEDEAKEKALKWLKKVGLSEDLISKSPFELSG-------GQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1411 LARALLRKTQILILDEATASVDP-GTEIQMQAALERWFAQCTVLLIAHRLRSVMNCAR-VLVMDEGQVAESGSPAQLLAQ 1488
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPeGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADdVLVLEHGKLIKHASPKEIFSD 235
|
.
gi 13591916 1489 K 1489
Cdd:PRK13641 236 K 236
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
647-833 |
2.52e-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: 73.48 E-value: 2.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 647 INLTVPQGcLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGS-----------------VAYVPQE-AWVQNTSVVEN 708
Cdd:cd03297 17 IDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsrkkinlppqqrkIGLVFQQyALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 709 VCF-----RQELDLPWLQEVLEACALGSDVASFPAGvhtpvgeqgmnLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDA 783
Cdd:cd03297 96 LAFglkrkRNREDRISVDELLDLLGLDHLLNRYPAQ-----------LSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 13591916 784 HVSQEVFKQVIGPSGLLQGTTrILVTHTL-HVLPQADQILVLANGTIAEMG 833
Cdd:cd03297 165 ALRLQLLPELKQIKKNLNIPV-IFVTHDLsEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1276-1480 |
3.62e-14 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 73.30 E-value: 3.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1276 ELPMAVqgvSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVpitDMGLHTLRSR-ITIIPQDPVLFPG- 1353
Cdd:cd03298 12 EQPMHF---DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV---DVTAAPPADRpVSMLFQENNLFAHl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1354 SLRMNLDL-------LQENTDEGIWAALETVQLKAFVTSLPGQLqyecsgqgddlSVGQKQLLCLARALLRKTQILILDE 1426
Cdd:cd03298 86 TVEQNVGLglspglkLTAEDRQAIEVALARVGLAGLEKRLPGEL-----------SGGERQRVALARVLVRDKPVLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 13591916 1427 ATASVDPGTEIQMQAALERWFAQ--CTVLLIAHRLRSVMNCA-RVLVMDEGQVAESG 1480
Cdd:cd03298 155 PFAALDPALRAEMLDLVLDLHAEtkMTVLMVTHQPEDAKRLAqRVVFLDNGRIAAQG 211
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
633-854 |
3.71e-14 |
|
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: 74.07 E-value: 3.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 633 TFAWSQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGS-------------VAYVPQEAW 699
Cdd:COG1124 10 SYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRpvtrrrrkafrrrVQMVFQDPY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 700 vqnTSVveNVCF--RQELDLPwLQ------------EVLEACALGSDVAS-FPagvHTpvgeqgmnLSGGQKQRLSLARA 764
Cdd:COG1124 90 ---ASL--HPRHtvDRILAEP-LRihglpdreeriaELLEQVGLPPSFLDrYP---HQ--------LSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 765 VYRRAAVYLMDDPLAALDAHVSQEVFkqvigpsGLLQ------GTTRILVTHTLHVLPQ-ADQILVLANGTIAEMGSYQD 837
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEIL-------NLLKdlreerGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVAD 225
|
250
....*....|....*....
gi 13591916 838 LL--HRNGALVGLLDGARQ 854
Cdd:COG1124 226 LLagPKHPYTRELLAASLA 244
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
644-826 |
4.65e-14 |
|
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: 72.51 E-value: 4.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG------------SVAYV-PQEAWVQNTSVVENVC 710
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaredyrrRLAYLgHADGLKPELTVRENLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 711 FRQEL-----DLPWLQEVLEACALGsDVASFPAGvhtpvgeqgmNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHv 785
Cdd:COG4133 98 FWAALyglraDREAIDEALEAVGLA-GLADLPVR----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA- 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 13591916 786 SQEVFKQVIGpSGLLQGTTRILVTHTLHVLPqADQILVLAN 826
Cdd:COG4133 166 GVALLAELIA-AHLARGGAVLLTTHQPLELA-AARVLDLGD 204
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1270-1487 |
4.72e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 74.06 E-value: 4.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1270 GLRHRPELPmAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITdMGLHTLRS-RITIIPQDP 1348
Cdd:PRK15112 19 GWFRRQTVE-AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-FGDYSYRSqRIRMIFQDP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1349 -------------VLFPgsLRMNLDLLQENTDEGIWAALETVQLkafvtsLPGQLQYecsgQGDDLSVGQKQLLCLARAL 1415
Cdd:PRK15112 97 stslnprqrisqiLDFP--LRLNTDLEPEQREKQIIETLRQVGL------LPDHASY----YPHMLAPGQKQRLGLARAL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13591916 1416 LRKTQILILDEATASVDPGTEIQM-QAALERWFAQCTVLLIAHRLRSVMN--CARVLVMDEGQVAESGSPAQLLA 1487
Cdd:PRK15112 165 ILRPKVIIADEALASLDMSMRSQLiNLMLELQEKQGISYIYVTQHLGMMKhiSDQVLVMHQGEVVERGSTADVLA 239
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1280-1485 |
5.07e-14 |
|
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: 73.04 E-value: 5.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLtwglLRL----QEATEGGIWIDGVPITDMGLHtlRSRITIIPQDPVLFPG-- 1353
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTL----LRLiagfETPTSGEILLDGKDITNLPPH--KRPVNTVFQNYALFPHlt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1354 -------SLRMnLDLLQENTDEGIWAALETVQLKAFVTSLPGQLqyecSGqgddlsvGQKQLLCLARALLRKTQILILDE 1426
Cdd:cd03300 89 vfeniafGLRL-KKLPKAEIKERVAEALDLVQLEGYANRKPSQL----SG-------GQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13591916 1427 ATASVDPGTEIQMQAALERWFAQC--TVLLIAHRLRSVMNCA-RVLVMDEGQVAESGSPAQL 1485
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKELgiTFVFVTHDQEEALTMSdRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1280-1480 |
6.53e-14 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 72.57 E-value: 6.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDG--VPITDMGlhtlrsritiipqdpVLFPGSL-- 1355
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrvSSLLGLG---------------GGFNPELtg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1356 RMNLDLLqentdeGIWAALETVQLKAFVTSLpgqlqYECSGQGDDL-------SVGQKQLLCLARALLRKTQILILDEAT 1428
Cdd:cd03220 102 RENIYLN------GRLLGLSRKEIDEKIDEI-----IEFSELGDFIdlpvktySSGMKARLAFAIATALEPDILLIDEVL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 13591916 1429 ASVDPGTEIQMQAALERWFAQC-TVLLIAHRLRSVMN-CARVLVMDEGQVAESG 1480
Cdd:cd03220 171 AVGDAAFQEKCQRRLRELLKQGkTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1264-1489 |
8.44e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 73.57 E-value: 8.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1264 IEFRDFGLRHrPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPIT--DMGLHTLRSRI 1341
Cdd:PRK13639 2 LETRDLKYSY-PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1342 TIIPQDP--VLFPGSLR-------MNLDLLQENTDEGIWAALETVQLKAFVTSLPGQLqyecsgqgddlSVGQKQLLCLA 1412
Cdd:PRK13639 81 GIVFQNPddQLFAPTVEedvafgpLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHL-----------SGGQKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13591916 1413 RALLRKTQILILDEATASVDPGTEIQMQAALERWFAQ-CTVLLIAHRLRSVMNCA-RVLVMDEGQVAESGSPAQLLAQK 1489
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEgITIIISTHDVDLVPVYAdKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1280-1489 |
9.14e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 73.66 E-value: 9.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPIT----DMGLHTLRSRITIIPQDP------- 1348
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkDKYIRPVRKRIGMVFQFPesqlfed 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1349 -----VLF-PGSLRMNLDLLQENtdegiwaALETVQLKAFVTSLPGQLQYECSGqgddlsvGQKQLLCLARALLRKTQIL 1422
Cdd:PRK13646 102 tvereIIFgPKNFKMNLDEVKNY-------AHRLLMDLGFSRDVMSQSPFQMSG-------GQMRKIAIVSILAMNPDII 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1423 ILDEATASVDPGTEIQMQAALERWFAQ--CTVLLIAHRLRSVMNCA-RVLVMDEGQVAESGSPAQLLAQK 1489
Cdd:PRK13646 168 VLDEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVARYAdEVIVMKEGSIVSQTSPKELFKDK 237
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
644-838 |
1.06e-13 |
|
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: 72.60 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGS----------------VAYVPQE-AWVQNTSVV 706
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlrrqIGMIFQQfNLIERLSVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 707 ENVC---------FRQELDLPWLQEVLEACALGSDV--ASFpagVHTPVGEqgmnLSGGQKQRLSLARAVYRRAAVYLMD 775
Cdd:cd03256 97 ENVLsgrlgrrstWRSLFGLFPKEEKQRALAALERVglLDK---AYQRADQ----LSGGQQQRVAIARALMQQPKLILAD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 776 DPLAALDAHVSQEVFkqvigpsGLL------QGTTRILVTHTLHV-LPQADQILVLANGTIAEMGSYQDL 838
Cdd:cd03256 170 EPVASLDPASSRQVM-------DLLkrinreEGITVIVSLHQVDLaREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1280-1478 |
1.13e-13 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 72.00 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTW---GLLRlqeATEGGIWIDGVPITDMG---LHTLRSR-ITIIPQDPVLFP 1352
Cdd:COG1136 23 ALRGVSLSIEAGEFVAIVGPSGSGKSTLLNilgGLDR---PTSGEVLIDGQDISSLSereLARLRRRhIGFVFQFFNLLP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1353 gslrmNLDLLqEN--------------TDEGIWAALETVQLKAFVTSLPGQLqyecsgqgddlSVGQKQLLCLARALLRK 1418
Cdd:COG1136 100 -----ELTAL-ENvalplllagvsrkeRRERARELLERVGLGDRLDHRPSQL-----------SGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13591916 1419 TQILILDEATASVDPGTEIQMQAALERWFAQ--CTVLLIAHRLRSVMNCARVLVMDEGQVAE 1478
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1280-1485 |
1.42e-13 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 71.99 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMglhTLRSR-ITIIPQDPVLF------- 1351
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDV---PVQERnVGFVFQHYALFrhmtvfd 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1352 ---------PGSLRMNLDLLQENTDEgiwaALETVQLKAFVTSLPGQLqyecSGqgddlsvGQKQLLCLARALLRKTQIL 1422
Cdd:cd03296 94 nvafglrvkPRSERPPEAEIRAKVHE----LLKLVQLDWLADRYPAQL----SG-------GQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1423 ILDEATASVDPgteiQMQAALERWFAQ------CTVLLIAHRLRSVMNCA-RVLVMDEGQVAESGSPAQL 1485
Cdd:cd03296 159 LLDEPFGALDA----KVRKELRRWLRRlhdelhVTTVFVTHDQEEALEVAdRVVVMNKGRIEQVGTPDEV 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1281-1486 |
1.42e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 72.50 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1281 VQGVSLKIHAGEKVGIVGRTGAGKSSltwgLLRL----QEATEGGIWIDGVPITDMGLHTLRSRITIIPQDPVL-FPGS- 1354
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKST----LLRAlsgeLSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1355 ---LRMNLDLLQENTDEG---IWAALETVQLKAFVTSLPGQLqyecSGqgddlsvGQKQ------LLCLARALLRKTQIL 1422
Cdd:PRK13548 94 eevVAMGRAPHGLSRAEDdalVAAALAQVDLAHLAGRDYPQL----SG-------GEQQrvqlarVLAQLWEPDGPPRWL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13591916 1423 ILDEATASVDPGTEIQ-MQAAleRWFAQ---CTVLLIAHRLR-SVMNCARVLVMDEGQVAESGSPAQLL 1486
Cdd:PRK13548 163 LLDEPTSALDLAHQHHvLRLA--RQLAHergLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
644-837 |
1.87e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 73.83 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-SVAYVPQEAWVQNT-----------SVVENVCF 711
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGqDITHVPAENRHVNTvfqsyalfphmTVFENVAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 712 --------RQELDlpwlQEVLEACALgsdvasfpagvhtpVGEQGM------NLSGGQKQRLSLARAVYRRAAVYLMDDP 777
Cdd:PRK09452 110 glrmqktpAAEIT----PRVMEALRM--------------VQLEEFaqrkphQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13591916 778 LAALDAHVSQEV---FKQvigpsglLQ---GTTRILVTHTL-HVLPQADQILVLANGTIAEMGSYQD 837
Cdd:PRK09452 172 LSALDYKLRKQMqneLKA-------LQrklGITFVFVTHDQeEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1280-1488 |
2.21e-13 |
|
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: 74.84 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWI----DGVPITDMGLhTLRSRIT----IIPQDPVLF 1351
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGP-DGRGRAKryigILHQEYDLY 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1352 PGSlrmnlDLLqENTDEGIWAAL--ETVQLKAFVTSLPGQLQYECSGQ-----GDDLSVGQKQLLCLARALLRKTQILIL 1424
Cdd:TIGR03269 378 PHR-----TVL-DNLTEAIGLELpdELARMKAVITLKMVGFDEEKAEEildkyPDELSEGERHRVALAQVLIKEPRIVIL 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13591916 1425 DEATASVDPGTEIQMQAAL--ERWFAQCTVLLIAHRLRSVMN-CARVLVMDEGQVAESGSPAQLLAQ 1488
Cdd:TIGR03269 452 DEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1280-1485 |
2.22e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 74.67 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSL----TwGLLRlqeATEGGIWIDGVPITDMG-LHTLRSRITIIPQDPVLFPG- 1353
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLmkilS-GVYQ---PDSGEILLDGEPVRFRSpRDAQAAGIAIIHQELNLVPNl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1354 SLRMNLDLLQENTDEGI--WAA--------LETVQLKAFVTSLPGqlqyecsgqgdDLSVGQKQLLCLARALLRKTQILI 1423
Cdd:COG1129 95 SVAENIFLGREPRRGGLidWRAmrrrarelLARLGLDIDPDTPVG-----------DLSVAQQQLVEIARALSRDARVLI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13591916 1424 LDEATASVDPgTEIqmqaalERWFAQ--------CTVLLIAHRLRSVMN-CARVLVMDEGQVAESGSPAQL 1485
Cdd:COG1129 164 LDEPTASLTE-REV------ERLFRIirrlkaqgVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
644-841 |
2.26e-13 |
|
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: 74.55 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG----------------SVAYVPQEAwvqNTSVVE 707
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGkdltklsrrslrelrrRVQMVFQDP---YSSLNP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 708 NVCFRQELDLPWL--------------QEVLEACALGSDVAS-FPagvHTpvgeqgmnLSGGQKQRLSLARAVYRRAAVY 772
Cdd:COG1123 358 RMTVGDIIAEPLRlhgllsraerrervAELLERVGLPPDLADrYP---HE--------LSGGQRQRVAIARALALEPKLL 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 773 LMDDPLAALDAHVSQEVFKqvigpsgLLQ------GTTRILVTHTLHVLPQ-ADQILVLANGTIAEMGSYQDLLHR 841
Cdd:COG1123 427 ILDEPTSALDVSVQAQILN-------LLRdlqrelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1277-1489 |
2.37e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 71.15 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1277 LPMAVqgvSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITdmglHTLRSR--ITIIPQDPVLFPG- 1353
Cdd:PRK10771 14 LPMRF---DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHT----TTPPSRrpVSMLFQENNLFSHl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1354 SLRMNLDL-------LQENTDEGIWAALETVQLKAFVTSLPGQLqyecSGqgddlsvGQKQLLCLARALLRKTQILILDE 1426
Cdd:PRK10771 87 TVAQNIGLglnpglkLNAAQREKLHAIARQMGIEDLLARLPGQL----SG-------GQRQRVALARCLVREQPILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13591916 1427 ATASVDPGTEIQM-----QAALERwfaQCTVLLIAHRLRSVMNCA-RVLVMDEGQVAESGSPAQLLAQK 1489
Cdd:PRK10771 156 PFSALDPALRQEMltlvsQVCQER---QLTLLMVSHSLEDAARIApRSLVVADGRIAWDGPTDELLSGK 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
642-810 |
2.38e-13 |
|
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: 70.90 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 642 PCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG---------SVAYVPQEAWV--------QNTS 704
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgrAIPYLRRKIGVvfqdfrllPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 705 VVENVCFRQEL-DLP------WLQEVLEACALGSDVASFPAGvhtpvgeqgmnLSGGQKQRLSLARAVYRRAAVYLMDDP 777
Cdd:cd03292 95 VYENVAFALEVtGVPpreirkRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 13591916 778 LAALDAHVSQEV---FKQVIgpsglLQGTTRILVTH 810
Cdd:cd03292 164 TGNLDPDTTWEImnlLKKIN-----KAGTTVVVATH 194
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1280-1485 |
3.05e-13 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 72.82 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLtwglLR----LQEATEGGIWIDGVPITDMGLHtlRSRITIIPQDPVLFP--- 1352
Cdd:COG3842 20 ALDDVSLSIEPGEFVALLGPSGCGKTTL----LRmiagFETPDSGRILLDGRDVTGLPPE--KRNVGMVFQDYALFPhlt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1353 -------GsLRMnLDLLQENTDEGIWAALETVQLKAFVTSLPGQLqyecSGqgddlsvGQKQ---------Llclarall 1416
Cdd:COG3842 94 vaenvafG-LRM-RGVPKAEIRARVAELLELVGLEGLADRYPHQL----SG-------GQQQrvalaralaP-------- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13591916 1417 rKTQILILDEATASVDPGTEIQMQAALERWFAQC--TVLLIAHRLRSVMNCA-RVLVMDEGQVAESGSPAQL 1485
Cdd:COG3842 153 -EPRVLLLDEPLSALDAKLREEMREELRRLQRELgiTFIYVTHDQEEALALAdRIAVMNDGRIEQVGTPEEI 223
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1275-1493 |
3.29e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 71.56 E-value: 3.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1275 PELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMG-LHTLRSRITIIPQDP-VLFP 1352
Cdd:PRK13644 12 PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGIVFQNPeTQFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1353 G-SLRMNLDLLQENTdegiwaALETVQLKAFVTSLPGQLQYEC--SGQGDDLSVGQKQLLCLARALLRKTQILILDEATA 1429
Cdd:PRK13644 92 GrTVEEDLAFGPENL------CLPPIEIRKRVDRALAEIGLEKyrHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13591916 1430 SVDPGTEIQMQAALERWFAQC-TVLLIAHRLRSVMNCARVLVMDEGQVAESGSPAQLLAQKGLFY 1493
Cdd:PRK13644 166 MLDPDSGIAVLERIKKLHEKGkTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQT 230
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
644-811 |
3.48e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 70.29 E-value: 3.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG----------SVAYV-PQEAWVQNTSVVENVCFR 712
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiddpdvaeACHYLgHRNAMKPALTVAENLEFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 713 QEL---DLPWLQEVLEACALGsDVASFPAGvhtpvgeqgmNLSGGQKQRLSLAR--AVYRRaaVYLMDDPLAALDAHvSQ 787
Cdd:PRK13539 98 AAFlggEELDIAAALEAVGLA-PLAHLPFG----------YLSAGQKRRVALARllVSNRP--IWILDEPTAALDAA-AV 163
|
170 180
....*....|....*....|....
gi 13591916 788 EVFKQVIGpSGLLQGTTRILVTHT 811
Cdd:PRK13539 164 ALFAELIR-AHLAQGGIVIAATHI 186
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1281-1489 |
3.57e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 71.08 E-value: 3.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1281 VQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTlRSR--ITIIPQDPVLFP------ 1352
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA-RARrgIGYLPQEASIFRrlsvyd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1353 ---GSLRMNLDLLQENTDEGIWAALETVQLKAFVTSLpgqlqyecsgqGDDLSVGQKQLLCLARALLRKTQILILDEATA 1429
Cdd:PRK10895 98 nlmAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSM-----------GQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13591916 1430 SVDPGTEIQMQAALERWF-AQCTVLLIAHRLRSVMN-CARVLVMDEGQVAESGSPAQLLAQK 1489
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLRdSGLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1280-1481 |
4.10e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 72.43 E-value: 4.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGI-WIdGVPITDMG---LHTLRSRITIIPQDPVlfpGSL 1355
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVaWL-GKDLLGMKddeWRAVRSDIQMIFQDPL---ASL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1356 --RMNL-DLLQEN--------TDEGIWAALETVQLKafVTSLPGQLQ---YECSGqgddlsvGQKQLLCLARALLRKTQI 1421
Cdd:PRK15079 112 npRMTIgEIIAEPlrtyhpklSRQEVKDRVKAMMLK--VGLLPNLINrypHEFSG-------GQCQRIGIARALILEPKL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 1422 LILDEATASVDpgTEIQMQA-----ALERWFAqCTVLLIAHRLRSVMNCA-RVLVMDEGQVAESGS 1481
Cdd:PRK15079 183 IICDEPVSALD--VSIQAQVvnllqQLQREMG-LSLIFIAHDLAVVKHISdRVLVMYLGHAVELGT 245
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
644-841 |
4.58e-13 |
|
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: 70.44 E-value: 4.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGS-----------VAYVPQE-AWVQNTSVVENVCF 711
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQNyALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 712 --------RQELDlpwlQEVLE-ACALGSD--VASFPAgvhtpvgeqgmNLSGGQKQRLSLARAVYRRAAVYLMDDPLAA 780
Cdd:cd03299 95 glkkrkvdKKEIE----RKVLEiAEMLGIDhlLNRKPE-----------TLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13591916 781 LDAHVsQEVFKQVIGPSGLLQGTTRILVTHTL-HVLPQADQILVLANGTIAEMGSYQDLLHR 841
Cdd:cd03299 160 LDVRT-KEKLREELKKIRKEFGVTVLHVTHDFeEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1264-1498 |
5.09e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 71.37 E-value: 5.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1264 IEFRDFGLRHRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSS---LTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSR 1340
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1341 ITIIPQDP-VLFPG-SLRMNLDLLQENtdEGIwAALETVQLKAFVTSLPGQLQYECSgQGDDLSVGQKQLLCLARALLRK 1418
Cdd:PRK13640 86 VGIVFQNPdNQFVGaTVGDDVAFGLEN--RAV-PRPEMIKIVRDVLADVGMLDYIDS-EPANLSGGQKQRVAIAGILAVE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1419 TQILILDEATASVDPGTEIQMQAALERWFA--QCTVLLIAHRLRSVMNCARVLVMDEGQVAESGSPAQ------LLAQKG 1490
Cdd:PRK13640 162 PKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEifskveMLKEIG 241
|
250
....*....|..
gi 13591916 1491 L----FYRLAQE 1498
Cdd:PRK13640 242 LdipfVYKLKNK 253
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1280-1487 |
5.26e-13 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 70.40 E-value: 5.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTL-RSRITIIPQDPVLFPG-SLRM 1357
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSlTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1358 NLDL--LQENTDEGIWAALETV-----QLKAFVTSLPGQLqyecSGqgddlsvGQKQLLCLARALLRKTQILILDEATAS 1430
Cdd:COG0410 98 NLLLgaYARRDRAEVRADLERVyelfpRLKERRRQRAGTL----SG-------GEQQMLAIGRALMSRPKLLLLDEPSLG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13591916 1431 VDPgteiQMQAALERWFAQ-----CTVLLIAHRLRSVMNCA-RVLVMDEGQVAESGSPAQLLA 1487
Cdd:COG0410 167 LAP----LIVEEIFEIIRRlnregVTILLVEQNARFALEIAdRAYVLERGRIVLEGTAAELLA 225
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1268-1487 |
5.53e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 70.81 E-value: 5.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1268 DFGLRHRPElpMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPI--TDMGLHTLRSRITIIP 1345
Cdd:PRK13638 6 DLWFRYQDE--PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdySKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1346 QDP------------VLFpgSLRmNLDLLQENTDEGIWAALETVQLKAFvtslpGQLQYECsgqgddLSVGQKQLLCLAR 1413
Cdd:PRK13638 84 QDPeqqifytdidsdIAF--SLR-NLGVPEAEITRRVDEALTLVDAQHF-----RHQPIQC------LSHGQKKRVAIAG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 1414 ALLRKTQILILDEATASVDPGTEIQMQAALERWFAQCT-VLLIAHRLRSVMNCA-RVLVMDEGQVAESGSPAQLLA 1487
Cdd:PRK13638 150 ALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNhVIISSHDIDLIYEISdAVYVLRQGQILTHGAPGEVFA 225
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
644-833 |
8.04e-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: 69.46 E-value: 8.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG----------------SVAYVPQEAwvqNTS--- 704
Cdd:cd03257 21 LDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkirrkEIQMVFQDP---MSSlnp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 705 -------VVENVCFRQELDLPWLQEVLEACALgsdvasfpAGVHTPvgEQGMN-----LSGGQKQRLSLARAVYRRAAVY 772
Cdd:cd03257 98 rmtigeqIAEPLRIHGKLSKKEARKEAVLLLL--------VGVGLP--EEVLNrypheLSGGQRQRVAIARALALNPKLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13591916 773 LMDDPLAALDAHVSQEVFKqvigpsgLLQ------GTTRILVTHTLHVLPQ-ADQILVLANGTIAEMG 833
Cdd:cd03257 168 IADEPTSALDVSVQAQILD-------LLKklqeelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
642-783 |
8.43e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 70.11 E-value: 8.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 642 PCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGsvayVPqeawVQNTSVVENVCFRQELDLPWlQ 721
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG----KP----VEGPGAERGVVFQNEGLLPW-R 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 722 EVLEACALGSDVASFPAGVHTPVGEQGMN--------------LSGGQKQRLSLARAVYRRAAVYLMDDPLAALDA 783
Cdd:PRK11248 86 NVQDNVAFGLQLAGVEKMQRLEIAHQMLKkvglegaekryiwqLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
644-833 |
1.25e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 69.27 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGS-------------------VAYVPQE--AWVQN 702
Cdd:PRK11124 18 LFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdfsktpsdkairelrrnVGMVFQQynLWPHL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 703 TsVVENV----CFRQELDLPWLQ----EVLEACALGSDVASFPagvhtpvgeqgMNLSGGQKQRLSLARAVYRRAAVYLM 774
Cdd:PRK11124 98 T-VQQNLieapCRVLGLSKDQALaraeKLLERLRLKPYADRFP-----------LHLSGGQQQRVAIARALMMEPQVLLF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13591916 775 DDPLAALDAhvsqEVFKQVIGPSGLLQGT--TRILVTHTLHVLPQ-ADQILVLANGTIAEMG 833
Cdd:PRK11124 166 DEPTAALDP----EITAQIVSIIRELAETgiTQVIVTHEVEVARKtASRVVYMENGHIVEQG 223
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1280-1485 |
1.34e-12 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 68.55 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGlHTLRSRITIIPQDPVLFPG-SLRMN 1358
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP-REVRRRIGIVFQDLSVDDElTGWEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1359 L-----------DLLQENTDEgiwaALETVQLKAFVTSLpgqLQYECSGQGDDLSVGQkqllclarALLRKTQILILDEA 1427
Cdd:cd03265 94 LyiharlygvpgAERRERIDE----LLDFVGLLEAADRL---VKTYSGGMRRRLEIAR--------SLVHRPEVLFLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13591916 1428 TASVDPGTEIQMQ---AALERWFAQcTVLLIAHRLRSV-MNCARVLVMDEGQVAESGSPAQL 1485
Cdd:cd03265 159 TIGLDPQTRAHVWeyiEKLKEEFGM-TILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
644-833 |
1.37e-12 |
|
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: 69.03 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGSVAYVP---QEAWVQNTS------VVENV----- 709
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgpdRMVVFQNYSllpwltVRENIalavd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 710 CFRQELDLPWLQEVLEACAlgsDVASFPAGVHTPVGEqgmnLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEV 789
Cdd:TIGR01184 81 RVLPDLSKSERRAIVEEHI---ALVGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 13591916 790 FKQvigpsgLLQ-----GTTRILVTHTL-HVLPQADQILVLANGTIAEMG 833
Cdd:TIGR01184 154 QEE------LMQiweehRVTVLMVTHDVdEALLLSDRVVMLTNGPAANIG 197
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
649-833 |
1.42e-12 |
|
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: 68.29 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 649 LTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG------SVAYVPQEAWVQNTSVVENVCFRQELDL---PW 719
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvtaaPPADRPVSMLFQENNLFAHLTVEQNVGLglsPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 720 L------QEVLEACALGSDVASFPAgvhtpvgEQGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKQV 793
Cdd:cd03298 99 LkltaedRQAIEVALARVGLAGLEK-------RLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 13591916 794 IGpSGLLQGTTRILVTHTLH-VLPQADQILVLANGTIAEMG 833
Cdd:cd03298 172 LD-LHAETKMTVLMVTHQPEdAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
627-813 |
1.44e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 69.68 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 627 ISIHNgtFAWSQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELlKVEGSVSIEGSVAYVPQEAWVQNT--- 703
Cdd:PRK14258 8 IKVNN--LSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMN-ELESEVRVEGRVEFFNQNIYERRVnln 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 704 ------------------SVVENVCFRQELdLPW-----LQEVLEACALGSDVASfpaGVHTPVGEQGMNLSGGQKQRLS 760
Cdd:PRK14258 85 rlrrqvsmvhpkpnlfpmSVYDNVAYGVKI-VGWrpkleIDDIVESALKDADLWD---EIKHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 13591916 761 LARAVYRRAAVYLMDDPLAALDAHVSQEVfKQVIGPSGLLQGTTRILVTHTLH 813
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKV-ESLIQSLRLRSELTMVIVSHNLH 212
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1280-1484 |
1.47e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 71.98 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLT---WGLLRlqeATEGGIWIDGVPITdmgLHT----LRSRITIIPQDPVLFP 1352
Cdd:COG3845 20 ANDDVSLTVRPGEIHALLGENGAGKSTLMkilYGLYQ---PDSGEILIDGKPVR---IRSprdaIALGIGMVHQHFMLVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1353 gslRM----NLDLLQENTDEGI--WAALET------------VQLKAFVtslpgqlqyecsgqgDDLSVGQKQllclara 1414
Cdd:COG3845 94 ---NLtvaeNIVLGLEPTKGGRldRKAARArirelserygldVDPDAKV---------------EDLSVGEQQ------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1415 llrK----------TQILILDEATASVDPgteiqmQAALE-----RWFAQ--CTVLLIAHRLRSVM-NCARVLVMDEGQV 1476
Cdd:COG3845 149 ---RveilkalyrgARILILDEPTAVLTP------QEADElfeilRRLAAegKSIIFITHKLREVMaIADRVTVLRRGKV 219
|
....*...
gi 13591916 1477 AESGSPAQ 1484
Cdd:COG3845 220 VGTVDTAE 227
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1264-1491 |
1.69e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 69.66 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1264 IEFRDFGLRHRPELPM---AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPIT----DMGLHT 1336
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFerrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkkNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1337 LRSRITIIPQDP--VLFPGSLR-------MNLDLLQENTDEGIWAALETVQLKAFVTSlpgQLQYECSGqgddlsvGQKQ 1407
Cdd:PRK13634 83 LRKKVGIVFQFPehQLFEETVEkdicfgpMNFGVSEEDAKQKAREMIELVGLPEELLA---RSPFELSG-------GQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1408 LLCLARALLRKTQILILDEATASVDPG--TEI-QMQAALERWfAQCTVLLIAHRLRSVMNCA-RVLVMDEGQVAESGSPA 1483
Cdd:PRK13634 153 RVAIAGVLAMEPEVLVLDEPTAGLDPKgrKEMmEMFYKLHKE-KGLTTVLVTHSMEDAARYAdQIVVMHKGTVFLQGTPR 231
|
250
....*....|....
gi 13591916 1484 QL------LAQKGL 1491
Cdd:PRK13634 232 EIfadpdeLEAIGL 245
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
642-839 |
1.83e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 71.03 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 642 PCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-------------SVAYVPQEawvqnTSVVEN 708
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraasrRVASVPQD-----TSLSFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 709 VCFRQELDL----------PWLQE---VLEACALGSDVASFpagVHTPVGEqgmnLSGGQKQRLSLARAVYRRAAVYLMD 775
Cdd:PRK09536 92 FDVRQVVEMgrtphrsrfdTWTETdraAVERAMERTGVAQF---ADRPVTS----LSGGERQRVLLARALAQATPVLLLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13591916 776 DPLAALDAH---VSQEVFKQVIGpsgllQGTTRILVTHTLHVLPQ-ADQILVLANGTIAEMGSYQDLL 839
Cdd:PRK09536 165 EPTASLDINhqvRTLELVRRLVD-----DGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVL 227
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1272-1476 |
1.88e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 68.94 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1272 RHRPELPMAVQGVS-------------LKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPitdmgLHTLR 1338
Cdd:PRK11247 6 RLNQGTPLLLNAVSkrygertvlnqldLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAP-----LAEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1339 SRITIIPQDPVLFP-GSLRMNLDL-LQENTDEGIWAALETVQLKAFVTSLPGQLqyecSGqgddlsvGQKQLLCLARALL 1416
Cdd:PRK11247 81 EDTRLMFQDARLLPwKKVIDNVGLgLKGQWRDAALQALAAVGLADRANEWPAAL----SG-------GQKQRVALARALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13591916 1417 RKTQILILDEATASVDPGTEIQMQAALERWFAQ--CTVLLIAHRLRSVMNCA-RVLVMDEGQV 1476
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALTRIEMQDLIESLWQQhgFTVLLVTHDVSEAVAMAdRVLLIEEGKI 212
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
644-830 |
2.06e-12 |
|
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: 66.68 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGsvayvpqeawvqntsvvENVCFRQeldlpwlqeV 723
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG-----------------KEVSFAS---------P 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 724 LEACALGsdVASfpagVHtpvgeQgmnLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKQVigpsGLL--Q 801
Cdd:cd03216 70 RDARRAG--IAM----VY-----Q---LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVI----RRLraQ 131
|
170 180 190
....*....|....*....|....*....|
gi 13591916 802 GTTRILVTHTL-HVLPQADQILVLANGTIA 830
Cdd:cd03216 132 GVAVIFISHRLdEVFEIADRVTVLRDGRVV 161
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
694-841 |
2.13e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 72.37 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 694 VPQEAWVQNTSVVENVCFRQELDLpwLQEVLEAC---ALGSDVASFPAGVHTPVGEQGMNLSGGQKQRLSLARAVYRRAA 770
Cdd:PTZ00265 1301 VSQEPMLFNMSIYENIKFGKEDAT--REDVKRACkfaAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPK 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 771 VYLMDDPLAALDAHvSQEVFKQVIGPSGLLQGTTRILVTHTLHVLPQADQILVLAN-----------GTIAEMGSYQDLL 839
Cdd:PTZ00265 1379 ILLLDEATSSLDSN-SEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNpdrtgsfvqahGTHEELLSVQDGV 1457
|
..
gi 13591916 840 HR 841
Cdd:PTZ00265 1458 YK 1459
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
644-838 |
3.38e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 69.73 E-value: 3.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGS-----------VAYVPQE-AWVQNTSVVENVCF 711
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFVFQHyALFRHMTVFDNIAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 712 -------RQELDLPWLQ----EVLEACALGSDVASFPAgvhtpvgeqgmNLSGGQKQRLSLARAVYRRAAVYLMDDPLAA 780
Cdd:PRK10851 98 gltvlprRERPNAAAIKakvtQLLEMVQLAHLADRYPA-----------QLSGGQKQRVALARALAVEPQILLLDEPFGA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13591916 781 LDAHVSQEVFKQVIGPSGLLQGTTrILVTH----TLHVlpqADQILVLANGTIAEMGSYQDL 838
Cdd:PRK10851 167 LDAQVRKELRRWLRQLHEELKFTS-VFVTHdqeeAMEV---ADRVVVMSQGNIEQAGTPDQV 224
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1284-1471 |
3.66e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 71.60 E-value: 3.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1284 VSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWI-DGVPITDMGLHTLRSRITIIPQDPVLFPGSLRMNL--- 1359
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIkys 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1360 -----------DLLQENT--------------------------------------------DEGIWAALETVQLKAFVT 1384
Cdd:PTZ00265 484 lyslkdlealsNYYNEDGndsqenknkrnscrakcagdlndmsnttdsneliemrknyqtikDSEVVDVSKKVLIHDFVS 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1385 SLPGQLQYECSGQGDDLSVGQKQLLCLARALLRKTQILILDEATASVDPGTEIQMQAALE--RWFAQCTVLLIAHRLRSV 1462
Cdd:PTZ00265 564 ALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTI 643
|
....*....
gi 13591916 1463 MNCARVLVM 1471
Cdd:PTZ00265 644 RYANTIFVL 652
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
644-840 |
3.68e-12 |
|
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: 67.70 E-value: 3.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSsllsallgellkV------------EGSVSIEG-SVAYVPQEAWV---------- 700
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKS------------VllkliigllrpdSGEILVDGqDITGLSEKELYelrrrigmlf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 701 QN----TS--VVENVCF--RQELDLPWLQ------EVLEACALGSDVASFPAgvhtpvgEqgmnLSGGQKQRLSLARAVY 766
Cdd:COG1127 89 QGgalfDSltVFENVAFplREHTDLSEAEirelvlEKLELVGLPGAADKMPS-------E----LSGGMRKRVALARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13591916 767 RRAAVYLMDDPLAALDAHVSQEVFKQVIGpsglLQ---GTTRILVTHTLH-VLPQADQILVLANGTIAEMGSYQDLLH 840
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVIDELIRE----LRdelGLTSVVVTHDLDsAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1279-1485 |
5.12e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.08 E-value: 5.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1279 MAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMG---LHTLRsrITIIPQDPVLFPgsl 1355
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpakAHQLG--IYLVPQEPLLFP--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1356 rmNLDLlQENTDEGIWAALETVQ-LKAFVTSLPGQLQYECsgQGDDLSVGQKQLLCLARALLRKTQILILDEATASVDPg 1434
Cdd:PRK15439 100 --NLSV-KENILFGLPKRQASMQkMKQLLAALGCQLDLDS--SAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTP- 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1435 teiqmqAALERWFAQCTVLL--------IAHRLRSVMNCA-RVLVMDEGQVAESGSPAQL 1485
Cdd:PRK15439 174 ------AETERLFSRIRELLaqgvgivfISHKLPEIRQLAdRISVMRDGTIALSGKTADL 227
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1281-1489 |
5.68e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 69.09 E-value: 5.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1281 VQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGlHTLRSRITIIPQ-DPVLFPGSLRMNL 1359
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA-RLARARIGVVPQfDNLDLEFTVRENL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1360 DLLqentdeGIWAALETVQLKAFVTSLP--GQLQYECSGQGDDLSVGQKQLLCLARALLRKTQILILDEATASVDPGTEI 1437
Cdd:PRK13536 136 LVF------GRYFGMSTREIEAVIPSLLefARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARH 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 13591916 1438 QMQAALERWFAQC-TVLLIAHRLRSVMN-CARVLVMDEGQVAESGSPAQLLAQK 1489
Cdd:PRK13536 210 LIWERLRSLLARGkTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
644-829 |
5.81e-12 |
|
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: 66.51 E-value: 5.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG----------SVAYVPQEAWVQNTSVvenvcfrq 713
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakerrkSIGYVMQDVDYQLFTD-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 714 eldlpwlqEVLEACALGSDVASFPAGV----------HTPVGEQGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDA 783
Cdd:cd03226 88 --------SVREELLLGLKELDAGNEQaetvlkdldlYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDY 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 13591916 784 HVSQEV---FKQVIGpsgllQGTTRILVTHTLHVLPQ-ADQILVLANGTI 829
Cdd:cd03226 160 KNMERVgelIRELAA-----QGKAVIVITHDYEFLAKvCDRVLLLANGAI 204
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
639-829 |
5.91e-12 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 67.36 E-value: 5.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 639 ESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGSVAYVPQEAWVQNTSVVenvcFRQELDLP 718
Cdd:cd03267 32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVV----FGQKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 719 WLQEVLEACALGSDVASFPAG------------------VHTPVgeqgMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAA 780
Cdd:cd03267 108 WDLPVIDSFYLLAAIYDLPPArfkkrldelselldleelLDTPV----RQLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 13591916 781 LDAhVSQEVFKQVIGPSGLLQGTTRILVTHTLHVLPQ-ADQILVLANGTI 829
Cdd:cd03267 184 LDV-VAQENIRNFLKEYNRERGTTVLLTSHYMKDIEAlARRVLVIDKGRL 232
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
309-551 |
8.20e-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: 67.96 E-value: 8.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 309 FLLGTLSLVISDAFRFAVPKLLSLFLEF---MGDLESSAWTGWLLAVLMFLSACLQTLfeQQYMYRVkvLQMRLRTAITG 385
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDvipAGDLSLLLWIALLLLLLALLRALLSYL--RRYLAAR--LGQRVVFDLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 386 LVYRKVLVLSSGSRKSSAAGDVVNLVSVDVQRLVESI-LHLNGLWLLFLWIIVCFVYL----WQLlgpsALTAVAVFLSL 460
Cdd:cd07346 77 DLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVsSGLLQLLSDVLTLIGALVILfylnWKL----TLVALLLLPLY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 461 LPLNFFITKK-RSFHQEEQmrqkASRARLTSSM---LRTVRTIKSHGWECAFLERLLHIRGQELGALKTSAFLFSVSLVS 536
Cdd:cd07346 153 VLILRYFRRRiRKASREVR----ESLAELSAFLqesLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPL 228
|
250
....*....|....*
gi 13591916 537 FQVSTFLVALVVFAV 551
Cdd:cd07346 229 IGLLTALGTALVLLY 243
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1264-1488 |
8.67e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 67.84 E-value: 8.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1264 IEFRDFGLRHRPELPMAVQG---VSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMG----LHT 1336
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASRAlfdIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1337 LRSRITIIPQDP--VLFPGSL-------RMNLDLLQENTDEGIWAALETVQL-KAFVTSLPgqlqYECSGqgddlsvGQK 1406
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVlkdvafgPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSP----FELSG-------GQM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1407 QLLCLARALLRKTQILILDEATASVDPGTEIQMQAALERWFAQC-TVLLIAHRLRSVMNCAR-VLVMDEGQVAESGSPAQ 1484
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGqTVVLVTHLMDDVADYADyVYLLEKGHIISCGTPSD 230
|
....
gi 13591916 1485 LLAQ 1488
Cdd:PRK13643 231 VFQE 234
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
644-839 |
9.97e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 66.65 E-value: 9.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG--------SVAYVPQEA---------WVQNTSVv 706
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvndpkvDERLIRQEAgmvfqqfylFPHLTAL- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 707 ENVCF--------------RQELDLpwlqevLEACALGSDVASFPAgvhtpvgeqgmNLSGGQKQRLSLARAVYRRAAVY 772
Cdd:PRK09493 96 ENVMFgplrvrgaskeeaeKQAREL------LAKVGLAERAHHYPS-----------ELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 773 LMDDPLAALDAHVSQEVFK--QVIGPSGLlqgtTRILVTHTLHVLPQ-ADQILVLANGTIAEMGSYQDLL 839
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLKvmQDLAEEGM----TMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
625-783 |
1.06e-11 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 66.81 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 625 DRISIHngtFAWSQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGsvayVPqeawVQNTS 704
Cdd:COG4525 7 RHVSVR---YPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDG----VP----VTGPG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 705 VVENVCFRQELDLPWLqEVLEACALGSDVASFPAGVHTPVGEQ-----GM---------NLSGGQKQRLSLARAVYRRAA 770
Cdd:COG4525 76 ADRGVVFQKDALLPWL-NVLDNVAFGLRLRGVPKAERRARAEEllalvGLadfarrriwQLSGGMRQRVGIARALAADPR 154
|
170
....*....|...
gi 13591916 771 VYLMDDPLAALDA 783
Cdd:COG4525 155 FLLMDEPFGALDA 167
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1281-1480 |
1.11e-11 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 65.26 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1281 VQGVSLKIHAGEKVGIVGRTGAGKSSLTWGL--LRLQEATEGGIWIDGVPITdmgLHTLRSRITIIPQDPVLFPgslrmN 1358
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLD---KRSFRKIIGYVPQDDILHP-----T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1359 LdllqentdegiwAALETVQLKAFVTSLPGqlqyecsGQGDDLSVGqkqllclaRALLRKTQILILDEATASVDPGTEIQ 1438
Cdd:cd03213 97 L------------TVRETLMFAAKLRGLSG-------GERKRVSIA--------LELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 13591916 1439 MQAALERwFAQ--CTVLLIAHRLRSVM--NCARVLVMDEGQVAESG 1480
Cdd:cd03213 150 VMSLLRR-LADtgRTIICSIHQPSSEIfeLFDKLLLLSQGRVIYFG 194
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
625-839 |
1.52e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 65.93 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 625 DRISIHNGTFAWSqesppclhgINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-SVAYVP-------- 695
Cdd:COG3840 5 DDLTYRYGDFPLR---------FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqDLTALPpaerpvsm 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 696 --QEawvqNT-----SVVENVCF------------RQELdlpwlQEVLEACALGSDVASFPAgvhtpvgeqgmNLSGGQK 756
Cdd:COG3840 76 lfQE----NNlfphlTVAQNIGLglrpglkltaeqRAQV-----EQALERVGLAGLLDRLPG-----------QLSGGQR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 757 QRLSLARAVYRRAAVYLMDDPLAALD-----------AHVSQEvfkqvigpsgllQGTTRILVTHTLH-VLPQADQILVL 824
Cdd:COG3840 136 QRVALARCLVRKRPILLLDEPFSALDpalrqemldlvDELCRE------------RGLTVLMVTHDPEdAARIADRVLLV 203
|
250
....*....|....*
gi 13591916 825 ANGTIAEMGSYQDLL 839
Cdd:COG3840 204 ADGRIAADGPTAALL 218
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
644-829 |
1.63e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 66.24 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVsIEGSVAYVP---------QEA----WvqnTSVVENVc 710
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEaredtrlmfQDArllpW---KKVIDNV- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 711 frqELDL-----PWLQEVLEACALGSDVASFPAGvhtpvgeqgmnLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHV 785
Cdd:PRK11247 103 ---GLGLkgqwrDAALQALAAVGLADRANEWPAA-----------LSGGQKQRVALARALIHRPGLLLLDEPLGALDALT 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 13591916 786 SQEVfKQVIGPSGLLQGTTRILVTHTL-HVLPQADQILVLANGTI 829
Cdd:PRK11247 169 RIEM-QDLIESLWQQHGFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1264-1494 |
1.90e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 66.36 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1264 IEFRDFGLRHRPELPmAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRITI 1343
Cdd:PRK13652 4 IETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1344 I---PQDPVLFP--------GSLRMNLDllQENTDEGIWAALETVQLKAFVTSLPGQLqyecsgqgddlSVGQKQLLCLA 1412
Cdd:PRK13652 83 VfqnPDDQIFSPtveqdiafGPINLGLD--EETVAHRVSSALHMLGLEELRDRVPHHL-----------SGGEKKRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1413 RALLRKTQILILDEATASVDPGTEIQMQAALERWFAQ--CTVLLIAHRLRSVMNCAR-VLVMDEGQVAESGSPAQLLAQK 1489
Cdd:PRK13652 150 GVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEMADyIYVMDKGRIVAYGTVEEIFLQP 229
|
....*
gi 13591916 1490 GLFYR 1494
Cdd:PRK13652 230 DLLAR 234
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
983-1235 |
2.01e-11 |
|
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: 66.43 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 983 SALRGSIFGLLGCLQAIGLFASMAAVFLGGA------RASCLLFRSLLwdvaRSPIGFFERTPVGNLLNRFSKET----D 1052
Cdd:cd18557 33 DVLNELALILLAIYLLQSVFTFVRYYLFNIAgerivaRLRRDLFSSLL----RQEIAFFDKHKTGELTSRLSSDTsvlqS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1053 IVDVDIPDKMRTLLTYAFGLlevGLAVSMATPLAIVaILPLMLLYAGFQSLYVATCCQLRRLESASYSSVCSHLAETFQG 1132
Cdd:cd18557 109 AVTDNLSQLLRNILQVIGGL---IILFILSWKLTLV-LLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1133 SQVVRAFQAQGPFTAQHDALMDENQRISFPRLVADRWLAANLELLGNGLVFVAATCA---VLSKaHLSAG-LAGFSVsAA 1208
Cdd:cd18557 185 IRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGgylVLSG-QLTVGeLTSFIL-YT 262
|
250 260
....*....|....*....|....*..
gi 13591916 1209 LQVTQTLQWVVRSWTDLENSMVAVERV 1235
Cdd:cd18557 263 IMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
627-850 |
2.07e-11 |
|
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: 66.30 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 627 ISIHNGTFAWSQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGSVAYVPQEAW------- 699
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeirkkvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 700 -V-QN-------TSVVENVCFRQE-LDLPW------LQEVLEACALgSDVASfpagvHTPVgeqgmNLSGGQKQRLSLAR 763
Cdd:TIGR04520 81 mVfQNpdnqfvgATVEDDVAFGLEnLGVPReemrkrVDEALKLVGM-EDFRD-----REPH-----LLSGGQKQRVAIAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 764 AVYRRAAVYLMDDPLAALDAHVSQEVFKQVigpsglLQ-----GTTRILVTHTLHVLPQADQILVLANGTIAEMGSYQDL 838
Cdd:TIGR04520 150 VLAMRPDIIILDEATSMLDPKGRKEVLETI------RKlnkeeGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREI 223
|
250
....*....|...
gi 13591916 839 LHRNGALVGL-LD 850
Cdd:TIGR04520 224 FSQVELLKEIgLD 236
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
750-841 |
2.08e-11 |
|
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: 67.43 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 750 NLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEV---FKQvigpsglLQGTTRI---LVTHTLH-VLPQADQIL 822
Cdd:COG4148 133 TLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEIlpyLER-------LRDELDIpilYVSHSLDeVARLADHVV 205
|
90
....*....|....*....
gi 13591916 823 VLANGTIAEMGSYQDLLHR 841
Cdd:COG4148 206 LLEQGRVVASGPLAEVLSR 224
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
644-833 |
2.44e-11 |
|
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: 64.91 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGcLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGS------------VAYVPQE-AWVQNTSVVENVC 710
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqpqklrrrIGYLPQEfGVYPNFTVREFLD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 711 FrqeldLPWL------------QEVLEACALGsDVAsfpagvHTPVGEqgmnLSGGQKQRLSLARAVYRRAAVYLMDDPL 778
Cdd:cd03264 95 Y-----IAWLkgipskevkarvDEVLELVNLG-DRA------KKKIGS----LSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 779 AALDAhVSQEVFKQVIgpSGLLQGTTRILVTHTLH-VLPQADQILVLANGTIAEMG 833
Cdd:cd03264 159 AGLDP-EERIRFRNLL--SELGEDRIVILSTHIVEdVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1264-1487 |
2.61e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 66.37 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1264 IEFRdfGLRHRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTlRSRITI 1343
Cdd:PRK13537 8 IDFR--NVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1344 IPQDPVLFPG-SLRMNLDLLqentdeGIWAALETVQLKAFVTSLP--GQLQYECSGQGDDLSVGQKQLLCLARALLRKTQ 1420
Cdd:PRK13537 85 VPQFDNLDPDfTVRENLLVF------GRYFGLSAAAARALVPPLLefAKLENKADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13591916 1421 ILILDEATASVDPGTEIQMQAALERWFAQC-TVLLIAHRLRSVMN-CARVLVMDEGQVAESGSPAQLLA 1487
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLARGkTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
644-831 |
2.77e-11 |
|
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: 65.15 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-----------------SVAYVPQ-EAWVQNTSV 705
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGqdlfaldedararlrarHVGFVFQsFQLLPTLTA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 706 VENVCfrqeldLP-WL----------QEVLEACALGSDVASFPAGvhtpvgeqgmnLSGGQKQRLSLARAVYRRAAVYLM 774
Cdd:COG4181 108 LENVM------LPlELagrrdararaRALLERVGLGHRLDHYPAQ-----------LSGGEQQRVALARAFATEPAILFA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13591916 775 DDPLAALDAHVSQevfkQVIgpsGLL------QGTTRILVTHTLHVLPQADQILVLANGTIAE 831
Cdd:COG4181 171 DEPTGNLDAATGE----QII---DLLfelnreRGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1280-1480 |
3.34e-11 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 64.58 E-value: 3.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLtwglLR----LQEATEGGIWIDGVPITDmgLHTLRSRITIIPQDPVLFPG-- 1353
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTT----LRmiagLEEPTSGRIYIGGRDVTD--LPPKDRDIAMVFQNYALYPHmt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1354 -------SLRMNlDLLQENTDEGIWAALETVQLKAFVTSLPGQLqyecSGqgddlsvGQKQLLCLARALLRKTQILILDE 1426
Cdd:cd03301 89 vydniafGLKLR-KVPKDEIDERVREVAELLQIEHLLDRKPKQL----SG-------GQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 13591916 1427 ATASVDPGTEIQMQAALERWFAQ--CTVLLIAHRLRSVMNCA-RVLVMDEGQVAESG 1480
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLQQRlgTTTIYVTHDQVEAMTMAdRIAVMNDGQIQQIG 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1280-1485 |
5.39e-11 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 65.86 E-value: 5.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLtwglLR----LQEATEGGIWIDGVPITDmgLHTLRSRITIIPQDPVLFPG-- 1353
Cdd:COG3839 18 ALKDIDLDIEDGEFLVLLGPSGCGKSTL----LRmiagLEDPTSGEILIGGRDVTD--LPPKDRNIAMVFQSYALYPHmt 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1354 -------SLRMNlDLLQENTDEGIWAALETVQLKAFVTSLPGQLqyecSGqgddlsvGQKQllclarallRKTQILILDE 1426
Cdd:COG3839 92 vyeniafPLKLR-KVPKAEIDRRVREAAELLGLEDLLDRKPKQL----SG-------GQRQrvalgralvREPKVFLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13591916 1427 ATASVDPGTEIQMQAALERWFAQ--CTVLLIAHRLRSVMNCA-RVLVMDEGQVAESGSPAQL 1485
Cdd:COG3839 160 PLSNLDAKLRVEMRAEIKRLHRRlgTTTIYVTHDQVEAMTLAdRIAVMNDGRIQQVGTPEEL 221
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1279-1485 |
5.50e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 66.40 E-value: 5.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1279 MAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHtlRSRITIIPQDPVLFPG-SLRM 1357
Cdd:PRK11607 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY--QRPINMMFQSYALFPHmTVEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1358 NL--DLLQENTDEGIWAA-----LETVQLKAFVTSLPGQlqyecsgqgddLSVGQKQLLCLARALLRKTQILILDEATAS 1430
Cdd:PRK11607 111 NIafGLKQDKLPKAEIASrvnemLGLVHMQEFAKRKPHQ-----------LSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1431 VDPGTEIQMQAA----LERWFAQCtvLLIAHRLRSVMNCA-RVLVMDEGQVAESGSPAQL 1485
Cdd:PRK11607 180 LDKKLRDRMQLEvvdiLERVGVTC--VMVTHDQEEAMTMAgRIAIMNRGKFVQIGEPEEI 237
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
644-829 |
6.17e-11 |
|
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: 63.70 E-value: 6.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGSVAYVPQEAWVQ----------------NTSVVE 707
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElrqkvgmvfqqfnlfpHLTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 708 NVCfrqeLDLPWLQ------------EVLEACALGSDVASFPAgvhtpvgeqgmNLSGGQKQRLSLARAVYRRAAVYLMD 775
Cdd:cd03262 96 NIT----LAPIKVKgmskaeaeeralELLEKVGLADKADAYPA-----------QLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 13591916 776 DPLAALDAHVSQEVFkQVIgpSGLLQ-GTTRILVTHTL----HVlpqADQILVLANGTI 829
Cdd:cd03262 161 EPTSALDPELVGEVL-DVM--KDLAEeGMTMVVVTHEMgfarEV---ADRVIFMDDGRI 213
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1281-1487 |
6.86e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 63.89 E-value: 6.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1281 VQGVSLKIHAGEKVGIVGRTGAGKS---SLTWGLLRlqeATEGGIWIDGVPITDMGLHtLRSR--ITIIPQDPVLFpgsl 1355
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTttfYMIVGLVK---PDSGRIFLDGEDITHLPMH-KRARlgIGYLPQEASIF---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1356 RmnlDL-LQENtdegIWAALETVQL-----KAFVTSLPGQLQYE--CSGQGDDLSVGQKQllclarallrKTQI------ 1421
Cdd:COG1137 91 R---KLtVEDN----ILAVLELRKLskkerEERLEELLEEFGIThlRKSKAYSLSGGERR----------RVEIaralat 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13591916 1422 ----LILDEATASVDPGT--EIQ-MQAAL-ERWFAqctVLLIAHRLRSVMN-CARVLVMDEGQVAESGSPAQLLA 1487
Cdd:COG1137 154 npkfILLDEPFAGVDPIAvaDIQkIIRHLkERGIG---VLITDHNVRETLGiCDRAYIISEGKVLAEGTPEEILN 225
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
644-833 |
6.94e-11 |
|
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: 62.95 E-value: 6.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALL--GELLKVEGSVSIEG----------SVAYVPQEAWVQNT-SVVENVC 710
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGrpldkrsfrkIIGYVPQDDILHPTlTVRETLM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 711 FRQELdlpwlqevleacalgsdvasfpagvhtpvgeQGmnLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVF 790
Cdd:cd03213 105 FAAKL-------------------------------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 13591916 791 KQVIGPSglLQGTTRILVTHTL--HVLPQADQILVLANGTIAEMG 833
Cdd:cd03213 152 SLLRRLA--DTGRTIICSIHQPssEIFELFDKLLLLSQGRVIYFG 194
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1281-1476 |
7.20e-11 |
|
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: 66.39 E-value: 7.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1281 VQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQE-ATEGGIWIDGVPI-TDMGLHTLRSRITIIPQD-------PVLF 1351
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVdIRNPAQAIRAGIAMVPEDrkrhgivPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1352 PG-----------SLRMNLDLLQEntDEGIWAALETVQLKAFVTSLPGQlqyecsgqgdDLSVGQKQLLCLARALLRKTQ 1420
Cdd:TIGR02633 356 VGknitlsvlksfCFKMRIDAAAE--LQIIGSAIQRLKVKTASPFLPIG----------RLSGGNQQKAVLAKMLLTNPR 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 13591916 1421 ILILDEATASVDPGTEIQMQAALERWFAQ-CTVLLIAHRLRSVMNCA-RVLVMDEGQV 1476
Cdd:TIGR02633 424 VLILDEPTRGVDVGAKYEIYKLINQLAQEgVAIIVVSSELAEVLGLSdRVLVIGEGKL 481
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1281-1486 |
7.68e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 66.02 E-value: 7.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1281 VQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRITIIPQDPVL-FPGSLRM-- 1357
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRQvv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1358 ---------NLDLLQENTDEGIWAALETVQLKAF----VTSLPGqlqyecsgqgddlsvGQKQLLCLARALLRKTQILIL 1424
Cdd:PRK09536 99 emgrtphrsRFDTWTETDRAAVERAMERTGVAQFadrpVTSLSG---------------GERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13591916 1425 DEATASVDPGTEIQMQAALERWFAQC-TVLLIAHRLR-SVMNCARVLVMDEGQVAESGSPAQLL 1486
Cdd:PRK09536 164 DEPTASLDINHQVRTLELVRRLVDDGkTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
744-829 |
1.18e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 66.29 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 744 VGEQGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEV---FKQVIGpsgllQGTTRILVTHTLHVLPQADQ 820
Cdd:PRK10535 138 VEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVmaiLHQLRD-----RGHTVIIVTHDPQVAAQAER 212
|
....*....
gi 13591916 821 ILVLANGTI 829
Cdd:PRK10535 213 VIEIRDGEI 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1263-1488 |
1.24e-10 |
|
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: 65.86 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1263 QIEFRDFGLRHRpelpmAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRL----QEATEGGIWIDGVPITDMGLHTLR 1338
Cdd:COG4172 13 SVAFGQGGGTVE-----AVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILFDGQDLLGLSERELR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1339 ----SRITIIPQDPV--LFP----G-----SLRMNLDLLQENTDEGIWAALETVQL---KAFVTSLPGQLqyecSGqgdd 1400
Cdd:COG4172 88 rirgNRIAMIFQEPMtsLNPlhtiGkqiaeVLRLHRGLSGAAARARALELLERVGIpdpERRLDAYPHQL----SG---- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1401 lsvGQKQLLCLARALLRKTQILILDEATASVDpgTEIQMQ-----AALERWFaQCTVLLIAHRLRSVMNCA-RVLVMDEG 1474
Cdd:COG4172 160 ---GQRQRVMIAMALANEPDLLIADEPTTALD--VTVQAQildllKDLQREL-GMALLLITHDLGVVRRFAdRVAVMRQG 233
|
250
....*....|....
gi 13591916 1475 QVAESGSPAQLLAQ 1488
Cdd:COG4172 234 EIVEQGPTAELFAA 247
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
641-831 |
1.24e-10 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 63.15 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 641 PPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG---------SVAY-------VPQEAW-VQNT 703
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsrlkrrEIPYlrrrigvVFQDFRlLPDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 704 SVVENVCF--------RQELDlPWLQEVLEACALGSDVASFPagvhtpvgeqgMNLSGGQKQRLSLARAVYRRAAVYLMD 775
Cdd:COG2884 95 TVYENVALplrvtgksRKEIR-RRVREVLDLVGLSDKAKALP-----------HELSGGEQQRVAIARALVNRPELLLAD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13591916 776 DPLAALDAHVSQEVFKqvigpsgLLQ-----GTTRILVTHTLHVLPQADQ-ILVLANGTIAE 831
Cdd:COG2884 163 EPTGNLDPETSWEIME-------LLEeinrrGTTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1280-1488 |
2.06e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 63.59 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHT---------LRSRITIIPQdpVL 1350
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigylpeergLYPKMKVGEQ--LV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1351 FPGSLR-MNLDLLQENTDEgiWaaLETVQLKAFVTSlpgqlqyecsgQGDDLSVGQKQllclarallrKTQI-------- 1421
Cdd:COG4152 94 YLARLKgLSKAEAKRRADE--W--LERLGLGDRANK-----------KVEELSKGNQQ----------KVQLiaallhdp 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13591916 1422 --LILDEATASVDP-GTEIQMQAALERWFAQCTVLLIAHRLRSVMN-CARVLVMDEGQVAESGSPAQLLAQ 1488
Cdd:COG4152 149 elLILDEPFSGLDPvNVELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
646-810 |
2.46e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.28 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 646 GINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEgsvayVPQEAWVQNTSVVEnvCFRQELDLPWLQEVLE 725
Cdd:COG2401 48 DLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----VPDNQFGREASLID--AIGRKGDFKDAVELLN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 726 ACALgSDVASFPAGVHtpvgeqgmNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKQVigpSGLLQ--GT 803
Cdd:COG2401 121 AVGL-SDAVLWLRRFK--------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNL---QKLARraGI 188
|
....*..
gi 13591916 804 TRILVTH 810
Cdd:COG2401 189 TLVVATH 195
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
644-841 |
2.47e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 62.62 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSAL-----LGELLKVEGSVSIEGS----------------VAYVPQEawVQN 702
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlieLYPEARVSGEVYLDGQdifkmdvielrrrvqmVFQIPNP--IPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 703 TSVVENVCF----------RQELDlPWLQEVLEACALGSDVAS---FPAGvhtpvgeqgmNLSGGQKQRLSLARAVYRRA 769
Cdd:PRK14247 97 LSIFENVALglklnrlvksKKELQ-ERVRWALEKAQLWDEVKDrldAPAG----------KLSGGQQQRLCIARALAFQP 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13591916 770 AVYLMDDPLAALDAHVS---QEVFKQvigpsgLLQGTTRILVThtlHVLPQA----DQILVLANGTIAEMGSYQDLLHR 841
Cdd:PRK14247 166 EVLLADEPTANLDPENTakiESLFLE------LKKDMTIVLVT---HFPQQAarisDYVAFLYKGQIVEWGPTREVFTN 235
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1281-1486 |
2.67e-10 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 62.35 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1281 VQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDmgLHTLRSRITIIPQDPVLFPgslRMNLd 1360
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN--LPPEKRDISYVPQNYALFP---HMTV- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1361 llQENTDEGIWAALET-VQLKAFVTSLPGQLQYE--CSGQGDDLSVGQKQLLCLARALLRKTQILILDEATASVDPGTEI 1437
Cdd:cd03299 89 --YKNIAYGLKKRKVDkKEIERKVLEIAEMLGIDhlLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 13591916 1438 QMQAALERWFAQ--CTVLLIAHRLRSVMNCA-RVLVMDEGQVAESGSPAQLL 1486
Cdd:cd03299 167 KLREELKKIRKEfgVTVLHVTHDFEEAWALAdKVAIMLNGKLIQVGKPEEVF 218
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
644-831 |
3.06e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 62.83 E-value: 3.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGSVAYVPQEAWVQN---------------TSVVEN 708
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSkvglvfqdpddqvfsSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 709 VCF---RQELDLPWLQEVLEACALGSDVASFPagvHTPvgeqGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHV 785
Cdd:PRK13647 101 VAFgpvNMGLDKDEVERRVEEALKAVRMWDFR---DKP----PYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 13591916 786 SQEVFKQVIGPSGllQGTTRILVTHTLHVLPQ-ADQILVLANG-TIAE 831
Cdd:PRK13647 174 QETLMEILDRLHN--QGKTVIVATHDVDLAAEwADQVIVLKEGrVLAE 219
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
647-838 |
3.37e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 63.59 E-value: 3.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 647 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGS-----------VAYVPQE-AWVQNTSVVENVCF--- 711
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEdvthrsiqqrdICMVFQSyALFPHMSLGENVGYglk 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 712 -----RQELDlpwlQEVLEACALgSDVASFpagvhtpvGEQGMN-LSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHV 785
Cdd:PRK11432 105 mlgvpKEERK----QRVKEALEL-VDLAGF--------EDRYVDqISGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 786 SQEVFKQVigpSGLLQ--GTTRILVTH-TLHVLPQADQILVLANGTIAEMGSYQDL 838
Cdd:PRK11432 172 RRSMREKI---RELQQqfNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1291-1480 |
3.65e-10 |
|
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: 61.54 E-value: 3.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1291 GEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITD----MGLHTLRSRITIIPQDPVLFPgslRMNLdllQENT 1366
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkINLPPQQRKIGLVFQQYALFP---HLNV---RENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1367 DEGIwAALETVQLKAFVTSLP-----GQLQYECSGQgddLSVGQKQLLCLARALLRKTQILILDEATASVDPGTEIQMQA 1441
Cdd:cd03297 97 AFGL-KRKRNREDRISVDELLdllglDHLLNRYPAQ---LSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 13591916 1442 ALERWFA--QCTVLLIAHRLRSV-MNCARVLVMDEGQVAESG 1480
Cdd:cd03297 173 ELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1264-1486 |
3.84e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 62.03 E-value: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1264 IEFRD----FGlrhrpelPMAV-QGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITD--MGLHT 1336
Cdd:PRK09493 2 IEFKNvskhFG-------PTQVlHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1337 LRSRITIIPQDPVLFP----------GSLRMNlDLLQENTDEGIWAALETVQLKAFVTSLPGQLqyecSGqgddlsvGQK 1406
Cdd:PRK09493 75 IRQEAGMVFQQFYLFPhltalenvmfGPLRVR-GASKEEAEKQARELLAKVGLAERAHHYPSEL----SG-------GQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1407 QLLCLARALLRKTQILILDEATASVDPgtEIQ------MQAALERWFaqcTVLLIAHRL---RSVmnCARVLVMDEGQVA 1477
Cdd:PRK09493 143 QRVAIARALAVKPKLMLFDEPTSALDP--ELRhevlkvMQDLAEEGM---TMVIVTHEIgfaEKV--ASRLIFIDKGRIA 215
|
....*....
gi 13591916 1478 ESGSPAQLL 1486
Cdd:PRK09493 216 EDGDPQVLI 224
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1281-1490 |
5.30e-10 |
|
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: 60.62 E-value: 5.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1281 VQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQ--EATEGGIWIDGVPITDMGLHtLRSR--ITIIPQDPVLFPGslr 1356
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPE-ERARlgIFLAFQYPPEIPG--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1357 mnldllqentdegiwaaletVQLKAFVTSLpgqlqyecsgqGDDLSVGQKQLLCLARALLRKTQILILDEatasVDPGTE 1436
Cdd:cd03217 92 --------------------VKNADFLRYV-----------NEGFSGGEKKRNEILQLLLLEPDLAILDE----PDSGLD 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13591916 1437 I----QMQAALERWFAQ-CTVLLIAH--RLRSVMNCARVLVMDEGQVAESGSP--AQLLAQKG 1490
Cdd:cd03217 137 IdalrLVAEVINKLREEgKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKelALEIEKKG 199
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1280-1480 |
6.58e-10 |
|
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: 60.84 E-value: 6.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTlRSRITIIPQDPVLFPG-SLRMN 1358
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEA-RRRLGFVSDSTGLYDRlTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1359 LDLLqentdeGIWAALETVQLKAFVTSLPGQLQYE--CSGQGDDLSVGQKQLLCLARALLRKTQILILDEATASVD-PGT 1435
Cdd:cd03266 99 LEYF------AGLYGLKGDELTARLEELADRLGMEelLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDvMAT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 13591916 1436 EIQMQAALERWFAQCTVLLIAHRLRSVMN-CARVLVMDEGQVAESG 1480
Cdd:cd03266 173 RALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
644-833 |
6.73e-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: 61.01 E-value: 6.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGSVAYV--PQEAWVQNTSVVENVCF--------RQ 713
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLlgLGGGFNPELTGRENIYLngrllglsRK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 714 ELDLpWLQEVLEACALGSDvasfpagVHTPVGeqgmNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHV---SQEVF 790
Cdd:cd03220 118 EIDE-KIDEIIEFSELGDF-------IDLPVK----TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFqekCQRRL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 13591916 791 KQVIgpsglLQGTTRILVTHTLHVLPQ-ADQILVLANGTIAEMG 833
Cdd:cd03220 186 RELL-----KQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1296-1492 |
6.93e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 62.18 E-value: 6.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1296 IVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHT----------------LRSRITIIPQDP--VLFPGSLR- 1356
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHelitnpyskkiknfkeLRRRVSMVFQFPeyQLFKDTIEk 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1357 ------MNLDLLQENTDEGIWAALETVQLK-AFVTSLPgqlqYECSGqgddlsvGQKQLLCLARALLRKTQILILDEATA 1429
Cdd:PRK13631 137 dimfgpVALGVKKSEAKKLAKFYLNKMGLDdSYLERSP----FGLSG-------GQKRRVAIAGILAIQPEILIFDEPTA 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13591916 1430 SVDP-GTEIQMQAALERWFAQCTVLLIAHRLRSVMNCA-RVLVMDEGQVAESGSPAQLLAQKGLF 1492
Cdd:PRK13631 206 GLDPkGEHEMMQLILDAKANNKTVFVITHTMEHVLEVAdEVIVMDKGKILKTGTPYEIFTDQHII 270
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
644-833 |
7.29e-10 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 61.21 E-value: 7.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGK----------------SsllsallgellKVEGSVSIEG---------------SVA 692
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKstllrclnrmndlipgA-----------RVEGEILLDGediydpdvdvvelrrRVG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 693 YVPQEAwvqN---TSVVENVCF---------RQELDlpwlqEV----LEACALGSDVAsfpAGVHTPvgeqGMNLSGGQK 756
Cdd:COG1117 96 MVFQKP---NpfpKSIYDNVAYglrlhgiksKSELD-----EIveesLRKAALWDEVK---DRLKKS----ALGLSGGQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 757 QRLSLARAVYRRAAVYLMDDPLAALD----AHV---SQEVFKQVigpsgllqgtTRILVTHTLHvlpQA----DQILVLA 825
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALDpistAKIeelILELKKDY----------TIVIVTHNMQ---QAarvsDYTAFFY 227
|
....*...
gi 13591916 826 NGTIAEMG 833
Cdd:COG1117 228 LGELVEFG 235
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
644-833 |
7.71e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 61.40 E-value: 7.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSA-----LLGELLKVEGSVSIEGSVAYVPQEAWVQ----------------N 702
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrllELNEEARVEGEVRLFGRNIYSPDVDPIEvrrevgmvfqypnpfpH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 703 TSVVENVCF----------RQELD--LPWlqeVLEACALGSDVAS----FPAgvhtpvgeqgmNLSGGQKQRLSLARAVY 766
Cdd:PRK14267 100 LTIYDNVAIgvklnglvksKKELDerVEW---ALKKAALWDEVKDrlndYPS-----------NLSGGQRQRLVIARALA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13591916 767 RRAAVYLMDDPLAALD----AHVSQEVFKqvigpsgLLQGTTRILVTHT-LHVLPQADQILVLANGTIAEMG 833
Cdd:PRK14267 166 MKPKILLMDEPTANIDpvgtAKIEELLFE-------LKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1277-1476 |
7.93e-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: 59.75 E-value: 7.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1277 LPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHT-LRSRITIIPQDPV---LFP 1352
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVPEDRKregLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1353 G-SLRMNLdllqentdegiwaaletvqlkafvtSLPGQLqyecSGqgddlsvGQKQLLCLARALLRKTQILILDEATASV 1431
Cdd:cd03215 92 DlSVAENI-------------------------ALSSLL----SG-------GNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 13591916 1432 DPGT--EI--QMQAALERwfaQCTVLLIAHRLRSVMNCA-RVLVMDEGQV 1476
Cdd:cd03215 136 DVGAkaEIyrLIRELADA---GKAVLLISSELDELLGLCdRILVMYEGRI 182
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
644-839 |
8.46e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 61.22 E-value: 8.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGSVAYVPQEAW--------------------VQNT 703
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFqidaiklrkevgmvfqqpnpFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 704 SVVENVCF---------RQELDlPWLQEVLEACALGSDVasfpagvHTPVGEQGMNLSGGQKQRLSLARAVYRRAAVYLM 774
Cdd:PRK14246 106 SIYDNIAYplkshgikeKREIK-KIVEECLRKVGLWKEV-------YDRLNSPASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 775 DDPLAALDAHVSQEVFKQVigpSGLLQGTTRILVTHTlhvlPQ-----ADQILVLANGTIAEMGSYQDLL 839
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLI---TELKNEIAIVIVSHN----PQqvarvADYVAFLYNGELVEWGSSNEIF 240
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
626-839 |
8.58e-10 |
|
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: 61.41 E-value: 8.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 626 RISIHNGTFAWSQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELlKVEGSVSIEG-SVAYVPQEAWVQNTS 704
Cdd:cd03289 2 QMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGvSWNSVPLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 705 VVENVCF------RQELDlPW-------LQEVLEACALGSDVASFPAGVHTPVGEQGMNLSGGQKQRLSLARAVYRRAAV 771
Cdd:cd03289 81 VIPQKVFifsgtfRKNLD-PYgkwsdeeIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13591916 772 YLMDDPLAALDAhVSQEVFKQVIGPSglLQGTTRILVTHTLHVLPQADQILVLANGTIAEMGSYQDLL 839
Cdd:cd03289 160 LLLDEPSAHLDP-ITYQVIRKTLKQA--FADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLL 224
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1282-1478 |
8.99e-10 |
|
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: 60.53 E-value: 8.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1282 QGVSLKIHAGEKVGIVGRTGAGKSSLTwGLLR-LQEATEGGIWIDGVPITDM---GLHTLRSR-ITIIPQ---------- 1346
Cdd:COG4181 29 KGISLEVEAGESVAIVGASGSGKSTLL-GLLAgLDRPTSGTVRLAGQDLFALdedARARLRARhVGFVFQsfqllptlta 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1347 -DPVLFPGSLRMNLDLLQENTdegiwAALETVQLKAFVTSLPGQLqyecSGqgddlsvGQKQLLCLARALLRKTQILILD 1425
Cdd:COG4181 108 lENVMLPLELAGRRDARARAR-----ALLERVGLGHRLDHYPAQL----SG-------GEQQRVALARAFATEPAILFAD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 13591916 1426 EATASVDPGTEIQMQAALERWFAQ--CTVLLIAHRLRSVMNCARVLVMDEGQVAE 1478
Cdd:COG4181 172 EPTGNLDAATGEQIIDLLFELNRErgTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1280-1488 |
1.40e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 60.10 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSltwgLLRL----QEATEGGIWIDG--VPITDM--GLH---TLRsritiipqDP 1348
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKST----LLKLiagiLEPTSGRVEVNGrvSALLELgaGFHpelTGR--------EN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1349 VLFPGS-LRMNLDLLQENTDE-----GIWAALET----------VQLkAFVTSLpgqlqyecsgqgddlsvgqkqllcla 1412
Cdd:COG1134 109 IYLNGRlLGLSRKEIDEKFDEivefaELGDFIDQpvktyssgmrARL-AFAVAT-------------------------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1413 ralLRKTQILILDEATASVDPgtEIQ---MQAALERWFAQCTVLLIAHRLRSVMN-CARVLVMDEGQVAESGSPAQLLAQ 1488
Cdd:COG1134 162 ---AVDPDILLVDEVLAVGDA--AFQkkcLARIRELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
644-829 |
1.53e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 62.34 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKssllsallgellKV--------EGSVSIEGS--------------VAYVPQE-AWV 700
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKst--------lmKIlsgvyqpdSGEILLDGEpvrfrsprdaqaagIAIIHQElNLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 701 QNTSVVENVCFRQELDLPWL----------QEVLEAcaLGSDVAsfpagVHTPVGEqgmnLSGGQKQRLSLARAVYRRAA 770
Cdd:COG1129 92 PNLSVAENIFLGREPRRGGLidwramrrraRELLAR--LGLDID-----PDTPVGD----LSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13591916 771 VYLMDDPLAALDAHVSQEVFKQVigpsGLL--QGTTRILVTHTLH-VLPQADQILVLANGTI 829
Cdd:COG1129 161 VLILDEPTASLTEREVERLFRII----RRLkaQGVAIIYISHRLDeVFEIADRVTVLRDGRL 218
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
644-839 |
1.70e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 60.15 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSAL------LGELLKVeGSVSIEGSVAYVPQEAWVQNtsVVENVCFR-QELD 716
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpEAGTIRV-GDITIDTARSLSQQKGLIRQ--LRQHVGFVfQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 717 LPWLQEVLE----------------ACALGSDVASfpagvhtPVGEQGMN------LSGGQKQRLSLARAVYRRAAVYLM 774
Cdd:PRK11264 96 LFPHRTVLEniiegpvivkgepkeeATARARELLA-------KVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEVILF 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13591916 775 DDPLAALDAHVSQEVFKQVigpSGLLQ-GTTRILVTHTLHVLPQ-ADQILVLANGTIAEMGSYQDLL 839
Cdd:PRK11264 169 DEPTSALDPELVGEVLNTI---RQLAQeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALF 232
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
644-856 |
1.71e-09 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 61.25 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKssllsallgellkvEGSVSIEG----------------SVAYVPQEAwvqN----- 702
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKstlircinllerptSGSVLVDGvdltalserelraarrKIGMIFQHF---Nllssr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 703 TsVVENVCF-----------RQE-----LDLpwlqeV-LEACAlgsdvASFPAgvhtpvgeqgmNLSGGQKQRLSLARAV 765
Cdd:COG1135 98 T-VAENVALpleiagvpkaeIRKrvaelLEL-----VgLSDKA-----DAYPS-----------QLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 766 YRRAAVYLMDDPLAALDAHVSQEVFKqvigpsgLLQ------GTTRILVTHTLHVLPQ-ADQILVLANGTIAEMGSYQDL 838
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSILD-------LLKdinrelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGPVLDV 228
|
250 260
....*....|....*....|...
gi 13591916 839 LHRNG-----ALVGLLDGARQPA 856
Cdd:COG1135 229 FANPQseltrRFLPTVLNDELPE 251
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
644-840 |
1.83e-09 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 59.61 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGS--------------VAYVPQEAWV-QNTSVVEN 708
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditglpphriarlgIGYVPEGRRIfPSLTVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 709 -----VCFRQELDLPW-LQEVLEAcalgsdvasFPAgvhtpVGE----QGMNLSGGQKQRLSLARAVYRRAAVYLMDDPL 778
Cdd:COG0410 99 lllgaYARRDRAEVRAdLERVYEL---------FPR-----LKErrrqRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13591916 779 AALDAHVSQEVFKQVigpsGLL--QGTTRILVTHTLH-VLPQADQILVLANGTIAEMGSYQDLLH 840
Cdd:COG0410 165 LGLAPLIVEEIFEII----RRLnrEGVTILLVEQNARfALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
950-1235 |
1.85e-09 |
|
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: 60.64 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 950 LFLFLCQQVASFCQ--GYWLSLWADDPVVDGKQMHSALR-GSIFGLLGCLQAIGLFASMAAVFLGGARASCLLFRSLLWD 1026
Cdd:cd07346 2 LLALLLLLLATALGlaLPLLTKLLIDDVIPAGDLSLLLWiALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1027 VARSPIGFFERTPVGNLLNRFSKETDIVDVDIPDKMRTLLTYAFGLleVGLAVSMAT---PLAIVAILPLMLLYAGFQSL 1103
Cdd:cd07346 82 LQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTL--IGALVILFYlnwKLTLVALLLLPLYVLILRYF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1104 yvatccqLRRLESASY------SSVCSHLAETFQGSQVVRAFQAQgpfTAQHDALMDENQRISFPRLVADRWLAANLELL 1177
Cdd:cd07346 160 -------RRRIRKASRevreslAELSAFLQESLSGIRVVKAFAAE---EREIERFREANRDLRDANLRAARLSALFSPLI 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 1178 gnGLVFVAATCAVL-------SKAHLSAG-LAGFsVSAALQVTQTLQWVVRSWTDLENSMVAVERV 1235
Cdd:cd07346 230 --GLLTALGTALVLlyggylvLQGSLTIGeLVAF-LAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
646-838 |
1.96e-09 |
|
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: 59.31 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 646 GINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG------------SVAYVPQEAWVQNT-SVVENVCFR 712
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIGIVFQDLSVDDElTGWENLYIH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 713 QEL-DLPW------LQEVLEACALGsDVAsfpagvHTPVGeqgmNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHV 785
Cdd:cd03265 98 ARLyGVPGaerrerIDELLDFVGLL-EAA------DRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 786 SQEVFKQVigpSGLL--QGTTRILVTHTLHVLPQ-ADQILVLANGTIAEMGSYQDL 838
Cdd:cd03265 167 RAHVWEYI---EKLKeeFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1281-1439 |
2.79e-09 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 58.65 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1281 VQGVSLKIHAGEKVGIVGRTGAGKSS-LTW--GLLRLQEATEGGIWIDGVPITDmgLHTLRSRITIIPQDPVLFP----- 1352
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTlLAAiaGTLSPAFSASGEVLLNGRRLTA--LPAEQRRIGILFQDDLLFPhlsvg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1353 GSLRMNL--DLLQENTDEGIWAALETVQLKAFVTSLPGQLqyecSGqgddlsvGQKQLLCLARALLRKTQILILDEATAS 1430
Cdd:COG4136 95 ENLAFALppTIGRAQRRARVEQALEEAGLAGFADRDPATL----SG-------GQRARVALLRALLAEPRALLLDEPFSK 163
|
....*....
gi 13591916 1431 VDPGTEIQM 1439
Cdd:COG4136 164 LDAALRAQF 172
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1280-1491 |
3.81e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 58.74 E-value: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITD-MGLHTLRSRITIIPQDPVLFPgslRMN 1358
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKIMREAVAIVPEGRRVFS---RMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1359 ldlLQENTDE-GIWAALETVQLK-AFVTSLPGQLQYECSGQGDDLSVGQKQLLCLARALLRKTQILILDEATASVDPGTE 1436
Cdd:PRK11614 97 ---VEENLAMgGFFAERDQFQERiKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 13591916 1437 IQMQAALERWFAQ-CTVLLIAHRLRSVMNCA-RVLVMDEGQVAESGSPAQLLAQKGL 1491
Cdd:PRK11614 174 QQIFDTIEQLREQgMTIFLVEQNANQALKLAdRGYVLENGHVVLEDTGDALLANEAV 230
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
627-850 |
4.20e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 59.26 E-value: 4.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 627 ISIHNGTFAWSQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGSVaYVPQEAW------- 699
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV-LSEETVWdvrrqvg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 700 --VQN-------TSVVENVCF--------RQELdLPWLQEVLEACALGSDVASFPAgvhtpvgeqgmNLSGGQKQRLSLA 762
Cdd:PRK13635 85 mvFQNpdnqfvgATVQDDVAFglenigvpREEM-VERVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 763 RAVYRRAAVYLMDDPLAALDAHVSQEVFKQVigpsGLL---QGTTRILVTHTLHVLPQADQILVLANGTIAEMGSYQDLL 839
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVLETV----RQLkeqKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIF 228
|
250
....*....|..
gi 13591916 840 HRNGALVGL-LD 850
Cdd:PRK13635 229 KSGHMLQEIgLD 240
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1270-1488 |
5.31e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 59.59 E-value: 5.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1270 GLRHRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITD---MGLHTLRSRITIIPQ 1346
Cdd:PRK11308 20 GLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpEAQKLLRQKIQIVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1347 DPVlfpGSL--RMNL-DLLQE----NTD-------EGIWAALETVQLKA-FVTSLPGQLqyecSGqgddlsvGQKQLLCL 1411
Cdd:PRK11308 100 NPY---GSLnpRKKVgQILEEplliNTSlsaaerrEKALAMMAKVGLRPeHYDRYPHMF----SG-------GQRQRIAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1412 ARALLRKTQILILDEATASVDpgTEIQMQ-----AALERWFaQCTVLLIAHRLRSVMNCA-RVLVMDEGQVAESGSPAQL 1485
Cdd:PRK11308 166 ARALMLDPDVVVADEPVSALD--VSVQAQvlnlmMDLQQEL-GLSYVFISHDLSVVEHIAdEVMVMYLGRCVEKGTKEQI 242
|
...
gi 13591916 1486 LAQ 1488
Cdd:PRK11308 243 FNN 245
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
644-846 |
5.43e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 59.03 E-value: 5.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSvSIEGSVAYVPQEAWVQNTSVVEnvcFRQELDL------ 717
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGF-RVEGKVTFHGKNLYAPDVDPVE---VRRRIGMvfqkpn 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 718 PWLQEVLEACALGSDVASFPAG-----------------VHTPVGEQGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAA 780
Cdd:PRK14243 102 PFPKSIYDNIAYGARINGYKGDmdelverslrqaalwdeVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 781 LDAhVS----QEVFKQvigpsgLLQGTTRILVTHTLHVLPQADQILVLANGTIAEMGSyqdllhRNGALV 846
Cdd:PRK14243 182 LDP-IStlriEELMHE------LKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGG------RYGYLV 238
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1281-1462 |
5.69e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 58.89 E-value: 5.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1281 VQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQE-----ATEGGIWIDGVPITD--MGLHTLRSRITIIPQDPVLFPG 1353
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIYErrVNLNRLRRQVSMVHPKPNLFPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1354 SLrmnldllQENTDEGI----WAAleTVQLKAFVTS------LPGQLQYECSGQGDDLSVGQKQLLCLARALLRKTQILI 1423
Cdd:PRK14258 103 SV-------YDNVAYGVkivgWRP--KLEIDDIVESalkdadLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 13591916 1424 LDEATASVDPGTEIQMQAALE--RWFAQCTVLLIAHRLRSV 1462
Cdd:PRK14258 174 MDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQV 214
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1245-1478 |
6.02e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 60.37 E-value: 6.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1245 APWR--LPSSAAQPLWPcggQIEFRDFGLrHRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGI 1322
Cdd:PRK10522 305 APYKaeFPRPQAFPDWQ---TLELRNVTF-AYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1323 WIDGVPITDMGLHTLRSRITIIPQDPVLFPgslRMNLDLLQENTDEGIWAALETVQLKAFVTSLPGQLqyecsgQGDDLS 1402
Cdd:PRK10522 381 LLDGKPVTAEQPEDYRKLFSAVFTDFHLFD---QLLGPEGKPANPALVEKWLERLKMAHKLELEDGRI------SNLKLS 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1403 VGQKQLLCLARALLRKTQILILDEATASVDPgteiqmqaALERWFAQC----------TVLLIAHRLRSVMNCARVLVMD 1472
Cdd:PRK10522 452 KGQKKRLALLLALAEERDILLLDEWAADQDP--------HFRREFYQVllpllqemgkTIFAISHDDHYFIHADRLLEMR 523
|
....*.
gi 13591916 1473 EGQVAE 1478
Cdd:PRK10522 524 NGQLSE 529
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1282-1353 |
6.31e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 60.46 E-value: 6.31e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 1282 QGVSLKIHAGEKVGIVGRTGAGKSSltwgLLRL----QEATEGGIWIDGvpitdmGLhtlrsRITIIPQDPVLFPG 1353
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKST----LLKIlageLEPDSGEVSIPK------GL-----RIGYLPQEPPLDDD 75
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1284-1485 |
7.38e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 59.33 E-value: 7.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1284 VSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGvpiTDMG-LHTLRSRITIIPQDPVLF----------- 1351
Cdd:PRK10851 21 ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG---TDVSrLHARDRKVGFVFQHYALFrhmtvfdniaf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1352 -----PGSLRMNLDLLqentDEGIWAALETVQLKAFVTSLPGQLqyecSGqgddlsvGQKQLLCLARALLRKTQILILDE 1426
Cdd:PRK10851 98 gltvlPRRERPNAAAI----KAKVTQLLEMVQLAHLADRYPAQL----SG-------GQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 1427 ATASVDPgteiQMQAALERWFAQC------TVLLIAHRLRSVMNCA-RVLVMDEGQVAESGSPAQL 1485
Cdd:PRK10851 163 PFGALDA----QVRKELRRWLRQLheelkfTSVFVTHDQEEAMEVAdRVVVMSQGNIEQAGTPDQV 224
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
647-838 |
7.77e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 59.46 E-value: 7.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 647 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-SVAYVP-----------QEAWVQNTSVVENVCFRQE 714
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvDLSHVPpyqrpinmmfqSYALFPHMTVEQNIAFGLK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 715 ldlpwlQEVLEACALGSDVASFPAGVHTP--VGEQGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKQ 792
Cdd:PRK11607 118 ------QDKLPKAEIASRVNEMLGLVHMQefAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLE 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 13591916 793 VIgpsGLLQ--GTTRILVTHTL-HVLPQADQILVLANGTIAEMGSYQDL 838
Cdd:PRK11607 192 VV---DILErvGVTCVMVTHDQeEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
996-1351 |
8.21e-09 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 60.20 E-value: 8.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 996 LQAIGLFASMAAVFLGGARASCLLF------------RSLLWDVARSPIGFFERTPVGNLLNRFSKETDIVdvdipdkmr 1063
Cdd:COG4615 48 ARLLLLFAGLLVLLLLSRLASQLLLtrlgqhavarlrLRLSRRILAAPLERLERIGAARLLAALTEDVRTI--------- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1064 tllTYAFGLLeVGLAVSMAT-------------PLAIVAILPLMLLYAGFQSLYVATccqLRRLESAS--YSSVCSHLAE 1128
Cdd:COG4615 119 ---SQAFVRL-PELLQSVALvlgclaylawlspPLFLLTLVLLGLGVAGYRLLVRRA---RRHLRRAReaEDRLFKHFRA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1129 TFQGSQVV------RAFQAQGPFTAQHDALMDENQRisfprlvADRWLAANlELLGNGLVFVAATCAVLSKAHLSAG--- 1199
Cdd:COG4615 192 LLEGFKELklnrrrRRAFFDEDLQPTAERYRDLRIR-------ADTIFALA-NNWGNLLFFALIGLILFLLPALGWAdpa 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1200 -LAGFsVSAALQVTQTLQWVVRSWTDLENSMVAVERVQDYVHTPKEAPWRLPSSAAQPLWPCGGQIEFRDFGLRHRPEL- 1277
Cdd:COG4615 264 vLSGF-VLVLLFLRGPLSQLVGALPTLSRANVALRKIEELELALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDg 342
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 1278 --PMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRITIIPQDPVLF 1351
Cdd:COG4615 343 deGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF 418
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1281-1457 |
8.72e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 58.00 E-value: 8.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1281 VQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQE-----ATEGGIWIDGVPITDMGLHTLRSRITIIPQDPVLFPG-- 1353
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIPNls 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1354 -----SLRMNLDLLQENTDE---GIWAALETVQLKAfvtslpgQLQYECSGQGDDLSVGQKQLLCLARALLRKTQILILD 1425
Cdd:PRK14247 99 ifenvALGLKLNRLVKSKKElqeRVRWALEKAQLWD-------EVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190
....*....|....*....|....*....|..
gi 13591916 1426 EATASVDPGTEIQMQAALERWFAQCTVLLIAH 1457
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLELKKDMTIVLVTH 203
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
647-841 |
1.13e-08 |
|
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: 58.97 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 647 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-----------------SVAYVPQEAWV-QNTSVVEN 708
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrkgiflppekrRIGYVFQEARLfPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 709 VCF-----RQELDLPWLQEVLEACALGSDVASFPAgvhtpvgeqgmNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDa 783
Cdd:TIGR02142 96 LRYgmkraRPSERRISFERVIELLGIGHLLGRLPG-----------RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD- 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13591916 784 hvsqEVFKQVIGPsgLLQGTTR------ILVTHTL-HVLPQADQILVLANGTIAEMGSYQDLLHR 841
Cdd:TIGR02142 164 ----DPRKYEILP--YLERLHAefgipiLYVSHSLqEVLRLADRVVVLEDGRVAAAGPIAEVWAS 222
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
644-836 |
1.14e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 57.72 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELL--KVEGS--------VSIEGSVA-----------YVPQE-AWVQ 701
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdKSAGShiellgrtVQREGRLArdirksrantgYIFQQfNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 702 NTSVVENV-------------CFRqeldlpWLQEVLEACALGsdvASFPAGVHTPVGEQGMNLSGGQKQRLSLARAVYRR 768
Cdd:PRK09984 100 RLSVLENVligalgstpfwrtCFS------WFTREQKQRALQ---ALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQ 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13591916 769 AAVYLMDDPLAALD---AHVSQEVFKQVIGPSGllqgttrILVTHTLH----VLPQADQILVLANGTIAEMGSYQ 836
Cdd:PRK09984 171 AKVILADEPIASLDpesARIVMDTLRDINQNDG-------ITVVVTLHqvdyALRYCERIVALRQGHVFYDGSSQ 238
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
751-840 |
1.15e-08 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 57.93 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 751 LSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHV-SQEVfkqvigpsGLL------QGTTRILVTHTL----HVlpqAD 819
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVrSQII--------NLMlelqekLGISYIYVSQHLgivkHI---SD 218
|
90 100
....*....|....*....|.
gi 13591916 820 QILVLANGTIAEMGSYQDLLH 840
Cdd:COG4167 219 KVLVMHQGEVVEYGKTAEVFA 239
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
644-827 |
1.40e-08 |
|
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: 56.52 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGS---------VAYVPQE-AWVQNTSVVENVCFRQ 713
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpldiaarnrIGYLPEErGLYPKMKVIDQLVYLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 714 ELD-------LPWLQEVLEACALgSDVASFPAgvhtpvgEQgmnLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAhVS 786
Cdd:cd03269 96 QLKglkkeeaRRRIDEWLERLEL-SEYANKRV-------EE---LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 13591916 787 QEVFKQVIgpSGLL-QGTTRILVTHTL-HVLPQADQILVLANG 827
Cdd:cd03269 164 VELLKDVI--RELArAGKTVILSTHQMeLVEELCDRVLLLNKG 204
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
646-831 |
1.48e-08 |
|
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: 57.06 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 646 GINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-SVAYVPQEAWV--------QNT------SVVENV- 709
Cdd:cd03219 18 DVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGeDITGLPPHEIArlgigrtfQIPrlfpelTVLENVm 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 710 ----CFRQELDLPWL------------QEVLEACALGsDVASFPAGvhtpvgeqgmNLSGGQKQRLSLARAVYRRAAVYL 773
Cdd:cd03219 98 vaaqARTGSGLLLARarreereareraEELLERVGLA-DLADRPAG----------ELSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13591916 774 MDDPLAALDAHVSQEVfkqvigpSGLL-----QGTTRILVTHTLH-VLPQADQILVLANGT-IAE 831
Cdd:cd03219 167 LDEPAAGLNPEETEEL-------AELIrelreRGITVLLVEHDMDvVMSLADRVTVLDQGRvIAE 224
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
623-833 |
1.51e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 57.59 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 623 SKDRISIHNGTFAWsQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGS----------VA 692
Cdd:PRK15056 3 QQAGIVVNDVTVTW-RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 693 YVPQEAWVQNT--SVVENVCFRQEL-DLPWL-------QEVLEACALGSDVASFPagvHTPVGEqgmnLSGGQKQRLSLA 762
Cdd:PRK15056 82 YVPQSEEVDWSfpVLVEDVVMMGRYgHMGWLrrakkrdRQIVTAALARVDMVEFR---HRQIGE----LSGGQKKRVFLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13591916 763 RAVYRRAAVYLMDDPLAALDahVSQEVfkQVIGPSGLL--QGTTRILVTHTLHVLPQADQILVLANGTIAEMG 833
Cdd:PRK15056 155 RAIAQQGQVILLDEPFTGVD--VKTEA--RIISLLRELrdEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1280-1495 |
1.76e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 57.71 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSS---LTWGLLrlqeATEGGIWIDGVPITDMGLHT------LRSRITIIPQDP-- 1348
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTmiqLTNGLI----ISETGQTIVGDYAIPANLKKikevkrLRKEIGLVFQFPey 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1349 VLFPGSLRMNLDL----LQENTDEGIWAALETVQLKAFVTSLPGQLQYECSGqgddlsvGQKQLLCLARALLRKTQILIL 1424
Cdd:PRK13645 102 QLFQETIEKDIAFgpvnLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSG-------GQKRRVALAGIIAMDGNTLVL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13591916 1425 DEATASVDPGTEIQMQAALERWFAQCT--VLLIAHRLRSVMNCA-RVLVMDEGQVAESGSPAQLLAQKGLFYRL 1495
Cdd:PRK13645 175 DEPTGGLDPKGEEDFINLFERLNKEYKkrIIMVTHNMDQVLRIAdEVIVMHEGKVISIGSPFEIFSNQELLTKI 248
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
644-833 |
1.79e-08 |
|
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: 56.51 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSS---LLSALLGELLKVEGSVSIEG----------SVAYVPQ-EAWVQNTSVVENV 709
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTlldAISGRVEGGGTTSGQILFNGqprkpdqfqkCVAYVRQdDILLPGLTVRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 710 CFRQELDLPWLQ-----EVLEACALGSDVAsfpagvHTPVGEQGM-NLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDA 783
Cdd:cd03234 103 TYTAILRLPRKSsdairKKRVEDVLLRDLA------LTRIGGNLVkGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 13591916 784 HVSQEVFKQVigpSGLLQGTTRILVthTLH-----VLPQADQILVLANGTIAEMG 833
Cdd:cd03234 177 FTALNLVSTL---SQLARRNRIVIL--TIHqprsdLFRLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1280-1485 |
1.81e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 57.45 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPIT----DMGLHTLRSRITIIPQdpvlFPGSL 1355
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstskNKDIKQIRKKVGLVFQ----FPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1356 RMNLDLLQE----------NTDEGIWAALETVQLKAFVTSLPGQLQYECSGqgddlsvGQKQLLCLARALLRKTQILILD 1425
Cdd:PRK13649 98 LFEETVLKDvafgpqnfgvSQEEAEALAREKLALVGISESLFEKNPFELSG-------GQMRRVAIAGILAMEPKILVLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13591916 1426 EATASVDP-GTEIQMQAALERWFAQCTVLLIAHRLRSVMNCAR-VLVMDEGQVAESGSPAQL 1485
Cdd:PRK13649 171 EPTAGLDPkGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADfVYVLEKGKLVLSGKPKDI 232
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1275-1474 |
1.82e-08 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 56.57 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1275 PELPmAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSR----ITIIPQDPVL 1350
Cdd:cd03290 12 SGLA-TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1351 FPGSLRMNLDLLQENTDEGIWAALETVQLKAFVTSLPGQLQYECSGQGDDLSVGQKQLLCLARALLRKTQILILDEATAS 1430
Cdd:cd03290 91 LNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 13591916 1431 VDPG-TEIQMQAALERWFA--QCTVLLIAHRLRSVMNCARVLVMDEG 1474
Cdd:cd03290 171 LDIHlSDHLMQEGILKFLQddKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1279-1488 |
1.96e-08 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 57.85 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1279 MAVQGVSLKIHAGEKVGIVGRTGAGKSSLtwglLR----LQEATEGGIWIDG--VPITdmgLHTLRSRITIIPQDPVLFP 1352
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTL----LRiiagLETPDSGRIVLNGrdLFTN---LPPRERRVGFVFQHYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1353 ------------GSLRMNLDLLQENTDEgiWaaLETVQLKAFVTSLPGQLqyecSGqgddlsvGQKQLLCLARALLRKTQ 1420
Cdd:COG1118 89 hmtvaeniafglRVRPPSKAEIRARVEE--L--LELVQLEGLADRYPSQL----SG-------GQRQRVALARALAVEPE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13591916 1421 ILILDEATASVDpgteIQMQAALERWFAQ------CTVLLIAHRLRSVMNCA-RVLVMDEGQVAESGSPAQLLAQ 1488
Cdd:COG1118 154 VLLLDEPFGALD----AKVRKELRRWLRRlhdelgGTTVFVTHDQEEALELAdRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1280-1490 |
2.04e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.98 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSS----LTwGLLrlqEATEGGIWIDGVPITDMGLHTlRSRITIIPQDpvlFpgSL 1355
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTtmkmLT-GLL---PASEGEAWLFGQPVDAGDIAT-RRRVGYMSQA---F--SL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1356 ------RMNLDL------LQENTDEG-IWAALETVQLKAFVTSLPgqlqyecsgqgDDLSVGQKQLLCLARALLRKTQIL 1422
Cdd:NF033858 351 ygeltvRQNLELharlfhLPAAEIAArVAEMLERFDLADVADALP-----------DSLPLGIRQRLSLAVAVIHKPELL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1423 ILDEATASVDPgteiqmqAALERwFAQctvLLIA-HRLRSV--------MN----CARVLVMDEGQVAESGSPAQLLAQK 1489
Cdd:NF033858 420 ILDEPTSGVDP-------VARDM-FWR---LLIElSREDGVtifisthfMNeaerCDRISLMHAGRVLASDTPAALVAAR 488
|
.
gi 13591916 1490 G 1490
Cdd:NF033858 489 G 489
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
646-838 |
2.14e-08 |
|
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: 56.36 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 646 GINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG------------SVAYVPQE-AWVQNTSVVENVCFR 712
Cdd:cd03263 20 DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaarqSLGYCPQFdALFDELTVREHLRFY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 713 QELD-LPWLQE------VLEACALgSDVAsfpagvHTPVGeqgmNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDaHV 785
Cdd:cd03263 100 ARLKgLPKSEIkeevelLLRVLGL-TDKA------NKRAR----TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD-PA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 786 SQEVFKQVIgpSGLLQGTTRILVTHTLH---VLpqADQILVLANGTIAEMGSYQDL 838
Cdd:cd03263 168 SRRAIWDLI--LEVRKGRSIILTTHSMDeaeAL--CDRIAIMSDGKLRCIGSPQEL 219
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
751-840 |
2.21e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 58.12 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 751 LSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKQVigpSGLLQ--GTTRILVTH-TLHVLPQADQILVLANG 827
Cdd:PRK11000 134 LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEI---SRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAG 210
|
90
....*....|...
gi 13591916 828 TIAEMGSYQDLLH 840
Cdd:PRK11000 211 RVAQVGKPLELYH 223
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1267-1476 |
2.29e-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: 56.57 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1267 RDFGLRHRPELPmAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDG-VPITDMGLHtlRSRITII- 1344
Cdd:cd03267 24 KSLFKRKYREVE-ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlVPWKRRKKF--LRRIGVVf 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1345 -PQDPVLFPGSLRMNLDLLQENTDegiwaaLETVQLKAFVTSLPGQLQYE--CSGQGDDLSVGQKQLLCLARALLRKTQI 1421
Cdd:cd03267 101 gQKTQLWWDLPVIDSFYLLAAIYD------LPPARFKKRLDELSELLDLEelLDTPVRQLSLGQRMRAEIAAALLHEPEI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 13591916 1422 LILDEATASVDPGTEIQMQAALERWFA--QCTVLLIAHRLRSVMNCA-RVLVMDEGQV 1476
Cdd:cd03267 175 LFLDEPTIGLDVVAQENIRNFLKEYNRerGTTVLLTSHYMKDIEALArRVLVIDKGRL 232
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
644-818 |
2.33e-08 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 55.96 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGSVAYVPQEAWVQNT-------------SVVENVC 710
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLlylghapgikttlSVLENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 711 FrqeldlpWlqevleaCALGSDVASFPA-------GV-HTPVGEqgmnLSGGQKQRLSLARAVYRRAAVYLMDDPLAALD 782
Cdd:cd03231 96 F-------W-------HADHSDEQVEEAlarvglnGFeDRPVAQ----LSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 13591916 783 AHVSQEVFKQVIGPSGllQGTTRILVTHtlHVLPQA 818
Cdd:cd03231 158 KAGVARFAEAMAGHCA--RGGMVVLTTH--QDLGLS 189
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1281-1480 |
2.52e-08 |
|
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: 56.13 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1281 VQGVSLKIHAGEKVGIVGRTGAGKSSL---TWGLLRLQEATEGGIWIDGVPITDmglHTLRSRITIIPQDPVLFPG---- 1353
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLldaISGRVEGGGTTSGQILFNGQPRKP---DQFQKCVAYVRQDDILLPGltvr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1354 -SLR-MNLDLLQENTDEGIWAAL-ETVQLKAF-VTSLPGQLQYECSGqgddlsvGQKQLLCLARALLRKTQILILDEATA 1429
Cdd:cd03234 100 eTLTyTAILRLPRKSSDAIRKKRvEDVLLRDLaLTRIGGNLVKGISG-------GERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 13591916 1430 SVDPGTEIQMQAALERWFAQ-CTVLLIAHRLRSVM--NCARVLVMDEGQVAESG 1480
Cdd:cd03234 173 GLDSFTALNLVSTLSQLARRnRIVILTIHQPRSDLfrLFDRILLLSSGEIVYSG 226
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
751-841 |
2.75e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 57.55 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 751 LSGGQKQRLSLARAVYRRAAVYLMDDPLAALDA----HVSQEVFKqvigpsglLQ---GTTRILVTH------TLhvlpq 817
Cdd:PRK11650 135 LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAklrvQMRLEIQR--------LHrrlKTTSLYVTHdqveamTL----- 201
|
90 100
....*....|....*....|....
gi 13591916 818 ADQILVLANGTIAEMGSYQDLLHR 841
Cdd:PRK11650 202 ADRVVVMNGGVAEQIGTPVEVYEK 225
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1285-1458 |
2.98e-08 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 54.85 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1285 SLKIHAGEKVGIVGRTGAGKSSLtwglLRlqeaTEGGIWidgvPIT--DMGLHTlRSRITIIPQDPVLFPGSLRmnldll 1362
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSL----FR----ALAGLW----PWGsgRIGMPE-GEDLLFLPQRPYLPLGTLR------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1363 qentdegiwaaletvqlkafvtslpGQLQYEcsgQGDDLSVGQKQLLCLARALLRKTQILILDEATASVDPGTEIQMQAA 1442
Cdd:cd03223 82 -------------------------EQLIYP---WDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQL 133
|
170
....*....|....*.
gi 13591916 1443 LERwfAQCTVLLIAHR 1458
Cdd:cd03223 134 LKE--LGITVISVGHR 147
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
642-837 |
3.11e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 55.88 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 642 PCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGS-VAYVPQEAWVQNTSVvenvCF--------- 711
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdISTLKPEIYRQQVSY----CAqtptlfgdt 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 712 -RQELDLPWL--QEVLEACALGSDVASFpaGVHTPVGEQGMN-LSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQ 787
Cdd:PRK10247 97 vYDNLIFPWQirNQQPDPAIFLDDLERF--ALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKH 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 13591916 788 EVfKQVIGPSGLLQGTTRILVTHTLHVLPQADQILVLAngtiAEMGSYQD 837
Cdd:PRK10247 175 NV-NEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQ----PHAGEMQE 219
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
627-850 |
3.18e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 56.66 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 627 ISIHNGTFAWSQESP-PCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGSvAYVPQEAW------ 699
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD-LLTEENVWdirhki 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 700 ---VQN-------TSVVENVCF---RQELDLPWLQE-VLEACALgsdvasfpagvhtpVGEQGMN------LSGGQKQRL 759
Cdd:PRK13650 84 gmvFQNpdnqfvgATVEDDVAFgleNKGIPHEEMKErVNEALEL--------------VGMQDFKereparLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 760 SLARAVYRRAAVYLMDDPLAALDAHVSQEVFKQVigpSGLLQ--GTTRILVTHTLHVLPQADQILVLANGTIAEMGSYQD 837
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDPEGRLELIKTI---KGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRE 226
|
250
....*....|....
gi 13591916 838 LLHRNGALVGL-LD 850
Cdd:PRK13650 227 LFSRGNDLLQLgLD 240
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
644-839 |
3.36e-08 |
|
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: 56.50 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-----------------SVAYVPQE-AWVQNTSV 705
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaamsrkelrelrrkKISMVFQSfALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 706 VENVCFRQELD-------LPWLQEVLEACALGSDVASFPagvhtpvGEqgmnLSGGQKQRLSLARAVYRRAAVYLMDDPL 778
Cdd:cd03294 120 LENVAFGLEVQgvpraerEERAAEALELVGLEGWEHKYP-------DE----LSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13591916 779 AALDAHVSQEVFKQVIGPSGLLQGTTrILVTHTL-HVLPQADQILVLANGTIAEMGSYQDLL 839
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAELQKTI-VFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1284-1499 |
3.47e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 58.64 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1284 VSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDgvpitdmglhtlRSrITIIPQDPVLFPGSLRMNLDLLQ 1363
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE------------RS-IAYVPQQAWIMNATVRGNILFFD 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1364 ENTDEGIWAALETVQLKAFVTSLPGQLQYECSGQGDDLSVGQKQLLCLARALLRKTQILILDEATASVDP--GTEIQMQA 1441
Cdd:PTZ00243 746 EEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAhvGERVVEEC 825
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 13591916 1442 ALERwFAQCTVLLIAHRLRSVMNCARVLVMDEGQVAESGSPAQlLAQKGLFYRLAQES 1499
Cdd:PTZ00243 826 FLGA-LAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSAD-FMRTSLYATLAAEL 881
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1279-1433 |
4.80e-08 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 55.06 E-value: 4.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1279 MAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPItdmglhtlrSRITIIPQDPVLFPG----- 1353
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL---------AEQRDEPHENILYLGhlpgl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1354 ----SLRMNLDLLQE---NTDEGIWAALETVQLKAFVTSLPGQLqyecsgqgddlSVGQKQLLCLARALLRKTQILILDE 1426
Cdd:TIGR01189 85 kpelSALENLHFWAAihgGAQRTIEDALAAVGLTGFEDLPAAQL-----------SAGQQRRLALARLWLSRRPLWILDE 153
|
....*..
gi 13591916 1427 ATASVDP 1433
Cdd:TIGR01189 154 PTTALDK 160
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1280-1475 |
5.12e-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: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSL-----------TWgllrlqeatEGGIWIDGVPITDMGLH-TLRSRITIIPQD 1347
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLmkilsgvyphgTW---------DGEIYWSGSPLKASNIRdTERAGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1348 PVLFPG-SLRMNLDLLQENTDEGIWAALETVQLKAfvTSLPGQLQYECSGQG---DDLSVGQKQLLCLARALLRKTQILI 1423
Cdd:TIGR02633 87 LTLVPElSVAENIFLGNEITLPGGRMAYNAMYLRA--KNLLRELQLDADNVTrpvGDYGGGQQQLVEIAKALNKQARLLI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 13591916 1424 LDEATASVDPgTEIQMQAALERWFAQCTV--LLIAHRLRSVMN-CARVLVMDEGQ 1475
Cdd:TIGR02633 165 LDEPSSSLTE-KETEILLDIIRDLKAHGVacVYISHKLNEVKAvCDTICVIRDGQ 218
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1284-1479 |
5.47e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.37 E-value: 5.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1284 VSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHT-LRSRITIIPQD---PVLF-PGSLRMN 1358
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEDrqsSGLYlDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1359 LDLLQENtDEGIWaaLETVQLKAFVTSLPGQLQYECSGQGDD---LSVGQKQLLCLARALLRKTQILILDEATASVDPGT 1435
Cdd:PRK15439 362 VCALTHN-RRGFW--IKPARENAVLERYRRALNIKFNHAEQAartLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 13591916 1436 EIQMQAALERWFAQCT-VLLIAHRLRSVMNCA-RVLVMDEGQVAES 1479
Cdd:PRK15439 439 RNDIYQLIRSIAAQNVaVLFISSDLEEIEQMAdRVLVMHQGEISGA 484
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
644-829 |
6.25e-08 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 54.53 E-value: 6.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGSVAYVPQEAWVQ------------NTSVVENV-C 710
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRigalieapgfypNLTARENLrL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 711 FRQELDLPW--LQEVLEACALgSDVAsfpagvHTPVGeqgmNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQE 788
Cdd:cd03268 96 LARLLGIRKkrIDEVLDVVGL-KDSA------KKKVK----GFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 13591916 789 VFKQVIGPSGllQGTTRILVTHTLHVLPQ-ADQILVLANGTI 829
Cdd:cd03268 165 LRELILSLRD--QGITVLISSHLLSEIQKvADRIGIINKGKL 204
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1282-1461 |
6.61e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 54.49 E-value: 6.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1282 QGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLhtlRSRITII-PQD---PVLfpgSLRM 1357
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV---AEACHYLgHRNamkPAL---TVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1358 NLDLLQE---NTDEGIWAALETVQLkAFVTSLPGQlqyecsgqgdDLSVGQKQLLCLARALLRKTQILILDEATASVDPG 1434
Cdd:PRK13539 93 NLEFWAAflgGEELDIAAALEAVGL-APLAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
170 180
....*....|....*....|....*..
gi 13591916 1435 TeiqmQAALERwfaqctvlLIAHRLRS 1461
Cdd:PRK13539 162 A----VALFAE--------LIRAHLAQ 176
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
751-841 |
6.71e-08 |
|
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: 57.00 E-value: 6.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 751 LSGGQKQRLSLARAVYRRAAVYLMDDPLAALDahVSqeVFKQVIgpsGLLQ------GTTRILVTHTLHVLPQ-ADQILV 823
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALD--VS--VQAQIL---DLLRdlqrehGLAYLFISHDLAVVRAlAHRVMV 498
|
90
....*....|....*...
gi 13591916 824 LANGTIAEMGSYQDLLHR 841
Cdd:COG4172 499 MKDGKVVEQGPTEQVFDA 516
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
596-839 |
7.51e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 55.99 E-value: 7.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 596 SFDRLAAFLCLEEVDPNGMVLSPSRCSSKDRISIHNGTFAWSQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALL 675
Cdd:PRK13536 9 EAPRRLELSPIERKHQGISEAKASIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 676 GELLKVEGSVSIEGS------------VAYVPQ------EAWVQNTSVVENVCFRQ-----ELDLPWLQEVleacalgsd 732
Cdd:PRK13536 89 GMTSPDAGKITVLGVpvpararlararIGVVPQfdnldlEFTVRENLLVFGRYFGMstreiEAVIPSLLEF--------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 733 vASFPAGVHTPVGEqgmnLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKQVigPSGLLQGTTRILVTHTL 812
Cdd:PRK13536 160 -ARLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERL--RSLLARGKTILLTTHFM 232
|
250 260
....*....|....*....|....*....
gi 13591916 813 HVLPQ-ADQILVLANG-TIAEmGSYQDLL 839
Cdd:PRK13536 233 EEAERlCDRLCVLEAGrKIAE-GRPHALI 260
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
751-839 |
7.78e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 54.97 E-value: 7.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 751 LSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVF---KQVIGPSGLlqgtTRILVTHTLHVLPQ-ADQILVLAN 826
Cdd:PRK10771 130 LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLtlvSQVCQERQL----TLLMVSHSLEDAARiAPRSLVVAD 205
|
90
....*....|...
gi 13591916 827 GTIAEMGSYQDLL 839
Cdd:PRK10771 206 GRIAWDGPTDELL 218
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
989-1161 |
7.93e-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: 55.56 E-value: 7.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 989 IFGLLGCLQAIGLFASMAAVFLGGARAS----CLLFRSLLwdvaRSPIGFFERTPVGNLLNRFSKETDIVDVDIPDKMRT 1064
Cdd:cd18577 52 YFVYLGIGSFVLSYIQTACWTITGERQArrirKRYLKALL----RQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1065 LLTYAFGLLeVGLAVSMA-----TpLAIVAILPLMLLYAGFQSLYVAtccQLRRLESASYSSVCSHLAETFQGSQVVRAF 1139
Cdd:cd18577 128 LIQSLSTFI-AGFIIAFIyswklT-LVLLATLPLIAIVGGIMGKLLS---KYTKKEQEAYAKAGSIAEEALSSIRTVKAF 202
|
170 180
....*....|....*....|..
gi 13591916 1140 QAQGPFTAQHDALMDENQRISF 1161
Cdd:cd18577 203 GGEEKEIKRYSKALEKARKAGI 224
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
644-838 |
8.08e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 55.80 E-value: 8.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIE--------------------GSVAYVPQEAWVQNT 703
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGervitagkknkklkplrkkvGIVFQFPEHQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 704 sVVENVCF-------RQELDLPWLQEVLEACALGSDVASfpagvHTPvgeqgMNLSGGQKQRLSLARAVYRRAAVYLMDD 776
Cdd:PRK13634 103 -VEKDICFgpmnfgvSEEDAKQKAREMIELVGLPEELLA-----RSP-----FELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 777 PLAALDAHVSQEV---FKQVIGPSGLlqgtTRILVTHTLH-VLPQADQILVLANGTIAEMGSYQDL 838
Cdd:PRK13634 172 PTAGLDPKGRKEMmemFYKLHKEKGL----TTVLVTHSMEdAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
644-829 |
8.33e-08 |
|
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: 53.98 E-value: 8.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGS--------------VAYVP----QEAWVQNTSV 705
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtrrsprdairagIAYVPedrkREGLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 706 VENVCfrqeldLPWLqevleacalgsdvasfpagvhtpvgeqgmnLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHV 785
Cdd:cd03215 96 AENIA------LSSL------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 13591916 786 SQEVFKQVIGPSGllQGTTRILVTHTLH-VLPQADQILVLANGTI 829
Cdd:cd03215 140 KAEIYRLIRELAD--AGKAVLLISSELDeLLGLCDRILVMYEGRI 182
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
745-839 |
9.62e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 54.98 E-value: 9.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 745 GEQGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKqvIGPSGLLQGTTRILVTHTL----HVlpqADQ 820
Cdd:PRK10619 147 GKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR--IMQQLAEEGKTMVVVTHEMgfarHV---SSH 221
|
90
....*....|....*....
gi 13591916 821 ILVLANGTIAEMGSYQDLL 839
Cdd:PRK10619 222 VIFLHQGKIEEEGAPEQLF 240
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
751-834 |
1.07e-07 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 54.61 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 751 LSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFkQVIgpSGL-LQGTTRILVTHTLH----VlpqADQILVLA 825
Cdd:COG1126 137 LSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVL-DVM--RDLaKEGMTMVVVTHEMGfareV---ADRVVFMD 210
|
....*....
gi 13591916 826 NGTIAEMGS 834
Cdd:COG1126 211 GGRIVEEGP 219
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1282-1486 |
1.08e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 54.99 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1282 QGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRITIIPQDPVLfPGSLRmnldl 1361
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATT-PGDIT----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1362 LQENTDEGIW--------------AALETVQLKAFVTSLPGQlqyecsgQGDDLSVGQKQLLCLARALLRKTQILILDEA 1427
Cdd:PRK10253 98 VQELVARGRYphqplftrwrkedeEAVTKAMQATGITHLADQ-------SVDTLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13591916 1428 TASVDPGTEIQMQAAL-----ERWFAQCTVLliaHRLRSVMNCARVLV-MDEGQVAESGSPAQLL 1486
Cdd:PRK10253 171 TTWLDISHQIDLLELLselnrEKGYTLAAVL---HDLNQACRYASHLIaLREGKIVAQGAPKEIV 232
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
644-841 |
1.29e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 54.81 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGS-------------VAYVPQEAWVQ--NTSVVEN 708
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfVGLVFQNPDDQifSPTVEQD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 709 VCFrqeldlpwlqevlEACALGSDVASFPAGVHTPVGEQGM---------NLSGGQKQRLSLARAVYRRAAVYLMDDPLA 779
Cdd:PRK13652 100 IAF-------------GPINLGLDEETVAHRVSSALHMLGLeelrdrvphHLSGGEKKRVAIAGVIAMEPQVLVLDEPTA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13591916 780 ALDAHVSQEVFKqVIGPSGLLQGTTRILVTHTLHVLPQ-ADQILVL------ANGTIAEMGSYQDLLHR 841
Cdd:PRK13652 167 GLDPQGVKELID-FLNDLPETYGMTVIFSTHQLDLVPEmADYIYVMdkgrivAYGTVEEIFLQPDLLAR 234
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1281-1488 |
1.34e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 54.59 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1281 VQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPIT-------------DMGLHTLRSRITIIPQD 1347
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1348 PVLFPgslrmNLDLLqENTDEGIWAALETVQLKAFVTSLP--GQLQYECSGQGD---DLSVGQKQLLCLARALLRKTQIL 1422
Cdd:PRK10619 101 FNLWS-----HMTVL-ENVMEAPIQVLGLSKQEARERAVKylAKVGIDERAQGKypvHLSGGQQQRVSIARALAMEPEVL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13591916 1423 ILDEATASVDPG-----TEIQMQAALErwfaQCTVLLIAHRL---RSVMNcaRVLVMDEGQVAESGSPAQLLAQ 1488
Cdd:PRK10619 175 LFDEPTSALDPElvgevLRIMQQLAEE----GKTMVVVTHEMgfaRHVSS--HVIFLHQGKIEEEGAPEQLFGN 242
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1279-1485 |
1.50e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 54.23 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1279 MAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHT--------------LRSRITII 1344
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiarmgvvrtfqhvrLFREMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1345 pqDPVLFPGSLRMNLDLL---------QENTDEGI-WAA--LETVQLKAFVTSLPGQLQYecsgqgddlsvGQKQLLCLA 1412
Cdd:PRK11300 99 --ENLLVAQHQQLKTGLFsgllktpafRRAESEALdRAAtwLERVGLLEHANRQAGNLAY-----------GQQRRLEIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13591916 1413 RALLRKTQILILDEATASVDPGTEIQMQA---ALERWFaQCTVLLIAHRLRSVMNCA-RVLVMDEGQVAESGSPAQL 1485
Cdd:PRK11300 166 RCMVTQPEILMLDEPAAGLNPKETKELDEliaELRNEH-NVTVLLIEHDMKLVMGISdRIYVVNQGTPLANGTPEEI 241
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
644-839 |
1.69e-07 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 54.35 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGsvayVPQEAW----------V--QNTSvvenvcf 711
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNG----RPLAAWspwelarrraVlpQHSS------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 712 rqeLDLPWLqeVLEACALGSDVASFPAGVHTPVGEQGM--------------NLSGGQKQRLSLARA-------VYRRAA 770
Cdd:COG4559 86 ---LAFPFT--VEEVVALGRAPHGSSAAQDRQIVREALalvglahlagrsyqTLSGGEQQRVQLARVlaqlwepVDGGPR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13591916 771 VYLMDDPLAALDAHVSQEVFKQVigpSGLL-QGTTRILVTHTLHVLPQ-ADQILVLANGTIAEMGSYQDLL 839
Cdd:COG4559 161 WLFLDEPTSALDLAHQHAVLRLA---RQLArRGGGVVAVLHDLNLAAQyADRILLLHQGRLVAQGTPEEVL 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
642-838 |
1.69e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.83 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 642 PCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGS--------------VAYVPQEAWV-QNTSVV 706
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpakahqlgIYLVPQEPLLfPNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 707 ENVCFR---QELDLPWLQEVLEA--CALGSDVasfPAGVhtpvgeqgmnLSGGQKQRLSLARAVYRRAAVYLMDDPLAAL 781
Cdd:PRK15439 105 ENILFGlpkRQASMQKMKQLLAAlgCQLDLDS---SAGS----------LEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 13591916 782 DAHVSQEVFKQVigPSGLLQGTTRILVTHTLHVLPQ-ADQILVLANGTIAEMGSYQDL 838
Cdd:PRK15439 172 TPAETERLFSRI--RELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1281-1491 |
1.82e-07 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 54.25 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1281 VQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRITIIPQDPVlfpgslrmnld 1360
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHL----------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1361 llqenTDEGI----------------WAALeTVQLKAFVTSLPGQLQYECSGQG--DDLSVGQKQLLCLARALLRKTQIL 1422
Cdd:PRK11231 87 -----TPEGItvrelvaygrspwlslWGRL-SAEDNARVNQAMEQTRINHLADRrlTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13591916 1423 ILDEATASVDpgteIQMQAALERWFAQC-----TVLLIAHRL-RSVMNCARVLVMDEGQVAESGSPAQLLAQKGL 1491
Cdd:PRK11231 161 LLDEPTTYLD----INHQVELMRLMRELntqgkTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEVMTPGLL 231
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1280-1480 |
2.15e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 55.63 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPI---TDMGLHTLRSRITIIPQDP-------- 1348
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDPyasldprq 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1349 -----VLFPgsLRMNLDLLQENTDEGIWAALETVQLKAfvtSLPGQLQYECSGqgddlsvGQKQLLCLARALLRKTQILI 1423
Cdd:PRK10261 419 tvgdsIMEP--LRVHGLLPGKAAAARVAWLLERVGLLP---EHAWRYPHEFSG-------GQRQRICIARALALNPKVII 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13591916 1424 LDEATASVD---PGTEIQMQAALERWFAqCTVLLIAHRLRSVMNCA-RVLVMDEGQVAESG 1480
Cdd:PRK10261 487 ADEAVSALDvsiRGQIINLLLDLQRDFG-IAYLFISHDMAVVERIShRVAVMYLGQIVEIG 546
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
751-836 |
2.28e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 54.47 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 751 LSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFkQVIGPSGlLQGTTRILVTHTL-HVLPQADQILVLANGTI 829
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMM-QLILDAK-ANNKTVFVITHTMeHVLEVADEVIVMDKGKI 254
|
....*...
gi 13591916 830 AEMGS-YQ 836
Cdd:PRK13631 255 LKTGTpYE 262
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
637-834 |
2.40e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 53.94 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 637 SQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGSVAYVPQEAW---------VQN----- 702
Cdd:PRK13633 19 ESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdirnkagmvFQNpdnqi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 703 --TSVVENVCFRQE-LDLP------WLQEVLEAcalgsdVASFPAGVHTPvgeqgMNLSGGQKQRLSLARAVYRRAAVYL 773
Cdd:PRK13633 99 vaTIVEEDVAFGPEnLGIPpeeireRVDESLKK------VGMYEYRRHAP-----HLLSGGQKQRVAIAGILAMRPECII 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13591916 774 MDDPLAALDAHVSQEVFKqVIGPSGLLQGTTRILVTHTLHVLPQADQILVLANGTIAEMGS 834
Cdd:PRK13633 168 FDEPTAMLDPSGRREVVN-TIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1253-1488 |
2.46e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 55.10 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1253 AAQPLWpcggQIEFRDFGLRHRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEA-----TEGGIWIDGV 1327
Cdd:PRK15134 1 MTQPLL----AIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSppvvyPSGDIRFHGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1328 PITDMGLHTLR----SRITIIPQDPV--LFP---------GSLRMNLDLLQENTDEGIWAALETV---QLKAFVTSLPGQ 1389
Cdd:PRK15134 77 SLLHASEQTLRgvrgNKIAMIFQEPMvsLNPlhtlekqlyEVLSLHRGMRREAARGEILNCLDRVgirQAAKRLTDYPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1390 LqyecsgqgddlSVGQKQLLCLARALLRKTQILILDEATASVDPGTEIQMQAALE--RWFAQCTVLLIAHRLRSVMNCA- 1466
Cdd:PRK15134 157 L-----------SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVRKLAd 225
|
250 260
....*....|....*....|..
gi 13591916 1467 RVLVMDEGQVAESGSPAQLLAQ 1488
Cdd:PRK15134 226 RVAVMQNGRCVEQNRAATLFSA 247
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
751-841 |
2.54e-07 |
|
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: 54.29 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 751 LSGGQKQRLSLARAVYRRAAVYLMDDPLAALDahVSqeVFKQVIgpsGLLQ------GTTRILVTHTLHVLPQ-ADQILV 823
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALD--VT--IQAQIL---NLLKdlqrelGLAILFITHDLGVVAEiADRVAV 223
|
90
....*....|....*...
gi 13591916 824 LANGTIAEMGSYQDLLHR 841
Cdd:COG0444 224 MYAGRIVEEGPVEELFEN 241
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
751-839 |
2.75e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 53.64 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 751 LSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQevfkQVIGPSGLLQ---GTTRILVTHTLHVLPQ-ADQILVLAN 826
Cdd:PRK15112 150 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRS----QLINLMLELQekqGISYIYVTQHLGMMKHiSDQVLVMHQ 225
|
90
....*....|...
gi 13591916 827 GTIAEMGSYQDLL 839
Cdd:PRK15112 226 GEVVERGSTADVL 238
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
646-810 |
2.92e-07 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 52.75 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 646 GINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGSVAYVPQEAWVQNT-------------SVVENVCFR 712
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENIlylghlpglkpelSALENLHFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 713 QELDLPWLQEVLEACALgsdvASFPAGVHTPVGEqgmnLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHvSQEVFKQ 792
Cdd:TIGR01189 98 AAIHGGAQRTIEDALAA----VGLTGFEDLPAAQ----LSAGQQRRLALARLWLSRRPLWILDEPTTALDKA-GVALLAG 168
|
170
....*....|....*...
gi 13591916 793 VIGpSGLLQGTTRILVTH 810
Cdd:TIGR01189 169 LLR-AHLARGGIVLLTTH 185
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1266-1492 |
3.01e-07 |
|
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: 53.71 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1266 FRDFGLRHRPELpmavQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGvpitdmglhtlrsRITIIP 1345
Cdd:cd03291 42 FSNLCLVGAPVL----KNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1346 QDPVLFPGSLRMNLdLLQENTDEGIW-AALETVQLKAFVTSLPGQLQYECSGQGDDLSVGQKQLLCLARALLRKTQILIL 1424
Cdd:cd03291 105 QFSWIMPGTIKENI-IFGVSYDEYRYkSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13591916 1425 DEATASVDPGTEIQM-QAALERWFAQCTVLLIAHRLRSVMNCARVLVMDEGQVAESGSPAQLLAQKGLF 1492
Cdd:cd03291 184 DSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDF 252
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
750-846 |
3.11e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 53.94 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 750 NLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKqvIGPSGLLQGTTRILVTHTL-HVLPQADQILVLANGT 828
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLNKQGKTIILVTHDLdNVLEWTKRTIFFKDGK 242
|
90
....*....|....*...
gi 13591916 829 IAEMGSYQDLLHRNGALV 846
Cdd:PRK13651 243 IIKDGDTYDILSDNKFLI 260
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1280-1481 |
3.16e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 53.96 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTW---GLLRLQEATEGGIWIDGVPITDM---GLHTLRS-RITIIPQDPV--L 1350
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFalmGLLAANGRIGGSATFNGREILNLpekELNKLRAeQISMIFQDPMtsL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1351 FP----GSLRMNLDLLQENTDEGIwAALETVQLKAFVtSLP------GQLQYECSGqgddlsvGQKQLLCLARALLRKTQ 1420
Cdd:PRK09473 111 NPymrvGEQLMEVLMLHKGMSKAE-AFEESVRMLDAV-KMPearkrmKMYPHEFSG-------GMRQRVMIAMALLCRPK 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13591916 1421 ILILDEATASVDPGTEIQMQA---ALERWFaQCTVLLIAHRLRSVMN-CARVLVMDEGQVAESGS 1481
Cdd:PRK09473 182 LLIADEPTTALDVTVQAQIMTllnELKREF-NTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGN 245
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
591-837 |
4.22e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 54.30 E-value: 4.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 591 VQARVsfDRLAAflcLEEVDPN------GMVLSPSRCSSKDRISIHNGTFAWsqESPPCLHGINLTVPQGCLLAVVGPVG 664
Cdd:COG0488 279 AQSRI--KALEK---LEREEPPrrdktvEIRFPPPERLGKKVLELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 665 AGKssllsallGELLKV--------EGSVSIeGS---VAYVPQEawvqntsvvenvcfRQELDLPW--LQEVLEACALGS 731
Cdd:COG0488 352 AGK--------STLLKLlagelepdSGTVKL-GEtvkIGYFDQH--------------QEELDPDKtvLDELRDGAPGGT 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 732 DV------ASF---PAGVHTPVGeqgmNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHvSQEVFKQvigpsgLLQ- 801
Cdd:COG0488 409 EQevrgylGRFlfsGDDAFKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIE-TLEALEE------ALDd 477
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 13591916 802 --GTTrILVTHTLHVLPQ-ADQILVLANGTIAE-MGSYQD 837
Cdd:COG0488 478 fpGTV-LLVSHDRYFLDRvATRILEFEDGGVREyPGGYDD 516
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
644-839 |
4.28e-07 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 52.85 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGsvayVPQEAW----------V--QNTSV-----V 706
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNG----RPLADWspaelarrraVlpQHSSLsfpftV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 707 ENV---------CFRQELDlPWLQEVLEACALgSDVA--SFPAgvhtpvgeqgmnLSGGQKQRLSLARAVYRRAAV---- 771
Cdd:PRK13548 94 EEVvamgraphgLSRAEDD-ALVAAALAQVDL-AHLAgrDYPQ------------LSGGEQQRVQLARVLAQLWEPdgpp 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13591916 772 -YLM-DDPLAALDAHVSQEVFKqvigpsgLL------QGTTRILVTHTLHVLPQ-ADQILVLANGTIAEMGSYQDLL 839
Cdd:PRK13548 160 rWLLlDEPTSALDLAHQHHVLR-------LArqlaheRGLAVIVVLHDLNLAARyADRIVLLHQGRLVADGTPAEVL 229
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1280-1430 |
4.78e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.16 E-value: 4.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSL-----------TWgllrlqeatEGGIWIDGVPITDMGLH-TLRSRITIIPQD 1347
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLmkvlsgvyphgTY---------EGEIIFEGEELQASNIRdTERAGIAIIHQE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1348 PVLFPG-SLRMNLDLLQENTDEGI--WAA--LETVQLKAFVtslpgQLQYECSGQGDDLSVGQKQLLCLARALLRKTQIL 1422
Cdd:PRK13549 91 LALVKElSVLENIFLGNEITPGGImdYDAmyLRAQKLLAQL-----KLDINPATPVGNLGLGQQQLVEIAKALNKQARLL 165
|
....*...
gi 13591916 1423 ILDEATAS 1430
Cdd:PRK13549 166 ILDEPTAS 173
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
644-831 |
5.13e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 52.47 E-value: 5.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-----------------SVAYVPQE-AWVQNTSV 705
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqplhqmdeearaklrakHVGFVFQSfMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 706 VENVcfrqelDLPWL-------------QEVLEACALGSDVASFPAgvhtpvgeqgmNLSGGQKQRLSLARAVYRRAAVY 772
Cdd:PRK10584 106 LENV------ELPALlrgessrqsrngaKALLEQLGLGKRLDHLPA-----------QLSGGEQQRVALARAFNGRPDVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13591916 773 LMDDPLAALDAHVSQEVfkqvigpSGLL------QGTTRILVTHTLHVLPQADQILVLANGTIAE 831
Cdd:PRK10584 169 FADEPTGNLDRQTGDKI-------ADLLfslnreHGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1280-1348 |
5.16e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 54.26 E-value: 5.16e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSR-ITIIPQDP 1348
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPEDR 342
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
751-827 |
5.21e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 52.51 E-value: 5.21e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13591916 751 LSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFkQVIGPSGLLQGTTRILVTHTLHVLPQADQILVLANG 827
Cdd:PRK11629 146 LSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIF-QLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDG 221
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
749-834 |
5.89e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 53.34 E-value: 5.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 749 MNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVF-------KQVIGPsgllqgttrIL-VTHTL-HVLPQAD 819
Cdd:PRK11144 127 GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLpylerlaREINIP---------ILyVSHSLdEILRLAD 197
|
90
....*....|....*
gi 13591916 820 QILVLANGTIAEMGS 834
Cdd:PRK11144 198 RVVVLEQGKVKAFGP 212
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
750-834 |
6.23e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 53.27 E-value: 6.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 750 NLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKqvigpsgLLQ------GTTRILVTHTLHVLPQ-ADQIL 822
Cdd:PRK11153 140 QLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILE-------LLKdinrelGLTIVLITHEMDVVKRiCDRVA 212
|
90
....*....|..
gi 13591916 823 VLANGTIAEMGS 834
Cdd:PRK11153 213 VIDAGRLVEQGT 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1274-1485 |
6.47e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.09 E-value: 6.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1274 RPELPmAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPI-------------TDMGLHTLR-S 1339
Cdd:PRK10261 26 QQKIA-AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrrsrqvielseqSAAQMRHVRgA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1340 RITIIPQDPV-----LFP------GSLRMNLDLLQENTDEGIWAALETVQL---KAFVTSLPGQlqyecsgqgddLSVGQ 1405
Cdd:PRK10261 105 DMAMIFQEPMtslnpVFTvgeqiaESIRLHQGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQ-----------LSGGM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1406 KQLLCLARALLRKTQILILDEATASVDPGTE---IQMQAALERWFAQcTVLLIAHRLRSVMNCA-RVLVMDEGQVAESGS 1481
Cdd:PRK10261 174 RQRVMIAMALSCRPAVLIADEPTTALDVTIQaqiLQLIKVLQKEMSM-GVIFITHDMGVVAEIAdRVLVMYQGEAVETGS 252
|
....
gi 13591916 1482 PAQL 1485
Cdd:PRK10261 253 VEQI 256
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1279-1443 |
6.97e-07 |
|
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: 51.34 E-value: 6.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1279 MAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRITIIPQDPVLFPGSLRMN 1358
Cdd:cd03231 14 ALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1359 LDLLQE-NTDEGIWAALETVQLKAFVTSLPGQlqyecsgqgddLSVGQKQLLCLARALLRKTQILILDEATASVDPGTEI 1437
Cdd:cd03231 94 LRFWHAdHSDEQVEEALARVGLNGFEDRPVAQ-----------LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
....*.
gi 13591916 1438 QMQAAL 1443
Cdd:cd03231 163 RFAEAM 168
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
648-840 |
7.02e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 53.50 E-value: 7.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 648 NLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGSVAYVPQEAWVQNTSVVENVCFRQELDLPWLQEVLEAC 727
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 728 ALGSDVASFPA--------------GVHTPVGEQGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKQV 793
Cdd:PRK10070 128 AFGMELAGINAeerrekaldalrqvGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDEL 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 13591916 794 IGPSGLLQGTTrILVTHTL-HVLPQADQILVLANGTIAEMGSYQDLLH 840
Cdd:PRK10070 208 VKLQAKHQRTI-VFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
1019-1235 |
7.21e-07 |
|
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: 52.81 E-value: 7.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1019 LFRSLLwdvaRSPIGFFERTPVGNLLNRFSKETDIVDVDIPDKMRTLL---TYAFGLLevGLAVSMATPLAIVA--ILPL 1093
Cdd:cd18552 78 LFDKLL----RLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVrdpLTVIGLL--GVLFYLDWKLTLIAlvVLPL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1094 MLLYAGFQSlyvatccqlRRLESASYSS------VCSHLAETFQGSQVVRAFQAQGPFTAQHDALMDENQRISFPRLVAD 1167
Cdd:cd18552 152 AALPIRRIG---------KRLRKISRRSqesmgdLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARAR 222
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13591916 1168 RWLAANLELLGN---GLVFVAATCAVLSkAHLSAG-LAGFsVSAALQVTQTLQWVVRSWTDLENSMVAVERV 1235
Cdd:cd18552 223 ALSSPLMELLGAiaiALVLWYGGYQVIS-GELTPGeFISF-ITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
644-834 |
7.74e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 53.90 E-value: 7.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSS---LLSALLGELLKVEGSVSIEGSV----------AYVPQ-EAWVQNTSVVENV 709
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTlmnALAFRSPKGVKGSGSVLLNGMPidakemraisAYVQQdDLFIPTLTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 710 CFRQELDLP----------WLQEVLEACALGSdvasfpaGVHTPVGEQGM--NLSGGQKQRLSLARAVYRRAAVYLMDDP 777
Cdd:TIGR00955 121 MFQAHLRMPrrvtkkekreRVDEVLQALGLRK-------CANTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 778 LAALDAHVSQEVFKQVigpSGLLQ-GTTRILVTH--TLHVLPQADQILVLANGTIAEMGS 834
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVL---KGLAQkGKTIICTIHqpSSELFELFDKIILMAEGRVAYLGS 250
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1281-1487 |
9.27e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 52.06 E-value: 9.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1281 VQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPI-TDMGL-------HTLRSRITIIPQDPVLFP 1352
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSLsqqkgliRQLRQHVGFVFQNFNLFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1353 GslRMNLdllqENTDEGiwAALETVQLKAFVTSLPGQL--QYECSGQGDD----LSVGQKQLLCLARALLRKTQILILDE 1426
Cdd:PRK11264 99 H--RTVL----ENIIEG--PVIVKGEPKEEATARARELlaKVGLAGKETSyprrLSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1427 ATASVDPG------TEIQMQAALERwfaqcTVLLIAHRL---RSVMNcaRVLVMDEGQVAESGSPAQLLA 1487
Cdd:PRK11264 171 PTSALDPElvgevlNTIRQLAQEKR-----TMVIVTHEMsfaRDVAD--RAIFMDQGRIVEQGPAKALFA 233
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1281-1486 |
1.05e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 52.10 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1281 VQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRITIIPQDpvlFPGSLRMN-- 1358
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQ---LPAAEGMTvr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1359 -------------LDLLQENTDEGIWAALETVQLKAFVTSLPgqlqyecsgqgDDLSVGQKQLLCLARALLRKTQILILD 1425
Cdd:PRK10575 104 elvaigrypwhgaLGRFGAADREKVEEAISLVGLKPLAHRLV-----------DSLSGGERQRAWIAMLVAQDSRCLLLD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13591916 1426 EATASVDPGTEIQMQAALERWFAQ--CTVLLIAHRLR-SVMNCARVLVMDEGQVAESGSPAQLL 1486
Cdd:PRK10575 173 EPTSALDIAHQVDVLALVHRLSQErgLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELM 236
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
309-548 |
1.13e-06 |
|
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: 52.05 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 309 FLLGTLSLVISDAFRFAVPKLLSLFLEFMGDLESSAWTGWLLAVLMFLSACLQTLfeQQYM-----YRVkVLQMRLRtai 383
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGSSGGLLALLVALFLLQAVLSAL--SSYLlgrtgERV-VLDLRRR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 384 tglVYRKVLVLSSGSRKSSAAGDVVNLVSVD---VQRLVESIL--HLNGLWLLFLWIIVCFVYLWQLLGPSALTAVAVFL 458
Cdd:cd18551 75 ---LWRRLLRLPVSFFDRRRSGDLVSRVTNDttlLRELITSGLpqLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 459 SLLPLNFFItKKRSFHQEEQMrqkasrARLTS---SMLRTVRTIKSHGWECAFLERLL----HIRGQELGALKTSAFLFS 531
Cdd:cd18551 152 IILPLGRRI-RKASKRAQDAL------GELSAaleRALSAIRTVKASNAEERETKRGGeaaeRLYRAGLKAAKIEALIGP 224
|
250
....*....|....*..
gi 13591916 532 VSLVSFQVStFLVALVV 548
Cdd:cd18551 225 LMGLAVQLA-LLVVLGV 240
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
644-841 |
1.15e-06 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 51.62 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSllsallgeLLKV--------EGSVSIEGSVA--------YVPQeawvqnTSVVE 707
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKST--------LLKLiagileptSGRVEVNGRVSallelgagFHPE------LTGRE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 708 NVCF--------RQELDlpwlqEVLEacalgsDVASFpAGV----HTPVGeqgmNLSGGQKQRLSLARAVYRRAAVYLMD 775
Cdd:COG1134 108 NIYLngrllglsRKEID-----EKFD------EIVEF-AELgdfiDQPVK----TYSSGMRARLAFAVATAVDPDILLVD 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13591916 776 DPLAALDAHV---SQEVFKQVIGpsgllQGTTRILVTHTLHVLPQ-ADQILVLANGTIAEMGS-------YQDLLHR 841
Cdd:COG1134 172 EVLAVGDAAFqkkCLARIRELRE-----SGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDpeeviaaYEALLAG 243
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
644-833 |
1.21e-06 |
|
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: 51.21 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-SVAYVPQEA-----WVQNT-------SVVENVC 710
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEArrrlgFVSDStglydrlTARENLE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 711 F--------RQELD--LPWLQEVLEACALgsdvasfpagVHTPVGEqgmnLSGGQKQRLSLARAVYRRAAVYLMDDPLAA 780
Cdd:cd03266 101 YfaglyglkGDELTarLEELADRLGMEEL----------LDRRVGG----FSTGMRQKVAIARALVHDPPVLLLDEPTTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 13591916 781 LDAHVSQ---EVFKQVIGpsgllQGTTRILVTHTLH-VLPQADQILVLANGTIAEMG 833
Cdd:cd03266 167 LDVMATRalrEFIRQLRA-----LGKCILFSTHIMQeVERLCDRVVVLHRGRVVYEG 218
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
598-828 |
1.23e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 52.89 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 598 DRLAAFL-CLEEVDPNGMVLSPSRCSSKDRISIHNGTFAwSQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLsallg 676
Cdd:COG4178 333 DRLAGFEeALEAADALPEAASRIETSEDGALALEDLTLR-TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLL----- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 677 ellKV--------EGSVSI--EGSVAYVPQEAWVQNTSVVENVCF---RQELDLPWLQEVLEACALGSdvasFPAGVHTp 743
Cdd:COG4178 407 ---RAiaglwpygSGRIARpaGARVLFLPQRPYLPLGTLREALLYpatAEAFSDAELREALEAVGLGH----LAERLDE- 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 744 vgEQ--GMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKQVIgpsGLLQGTTRILVTHTLHVLPQADQI 821
Cdd:COG4178 479 --EAdwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLR---EELPGTTVISVGHRSTLAAFHDRV 553
|
....*..
gi 13591916 822 LVLANGT 828
Cdd:COG4178 554 LELTGDG 560
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
645-839 |
1.35e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 51.53 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 645 HGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGS-------------VAYVPQEAWVQNTSVVENVCF 711
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiqhyaskevarrIGLLAQNATTPGDITVQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 712 R-----QELDLPWLQEVLEACAlgsdVASFPAGVHTPVGEQGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDahVS 786
Cdd:PRK10253 104 RgryphQPLFTRWRKEDEEAVT----KAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD--IS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 13591916 787 QEV-FKQVIGPSGLLQGTTRILVTHTLH-VLPQADQILVLANGTIAEMGSYQDLL 839
Cdd:PRK10253 178 HQIdLLELLSELNREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1280-1482 |
1.36e-06 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 52.26 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLtwglLRL----QEATEGGIWIDGVPITDmgLHTLRSRITIIPQDPVLFPG-- 1353
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTV----LRLiagfETPDSGRIMLDGQDITH--VPAENRHVNTVFQSYALFPHmt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1354 -------SLRMNlDLLQENTDEGIWAALETVQLKAFVTSLPGQLqyecSGqgddlsvGQKQLLCLARALLRKTQILILDE 1426
Cdd:PRK09452 103 vfenvafGLRMQ-KTPAAEITPRVMEALRMVQLEEFAQRKPHQL----SG-------GQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 13591916 1427 ATASVDPGTEIQMQAALERWFAQ--CTVLLIAHRLRSVMNCA-RVLVMDEGQVAESGSP 1482
Cdd:PRK09452 171 SLSALDYKLRKQMQNELKALQRKlgITFVFVTHDQEEALTMSdRIVVMRDGRIEQDGTP 229
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
644-821 |
1.41e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 51.31 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGE-----LLKVEGSVSIEGSVAYVPQEAWVQ---------------NT 703
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDTVDlrkeigmvfqqpnpfPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 704 SVVENVCFRQEL----DLPWLQEVLEACALGsdvASFPAGVHTPVGEQGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLA 779
Cdd:PRK14239 101 SIYENVVYGLRLkgikDKQVLDEAVEKSLKG---ASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 13591916 780 ALDAHVSQEVFKQVIgpsGLLQGTTRILVTHTLHvlpQADQI 821
Cdd:PRK14239 178 ALDPISAGKIEETLL---GLKDDYTMLLVTRSMQ---QASRI 213
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
644-834 |
1.47e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 51.62 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGsvayvpQEAWVQNTSVVEnvcFRQELDL----PW 719
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKG------EPIKYDKKSLLE---VRKTVGIvfqnPD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 720 LQevLEACALGSDVASFPAGVHTP--------------VGEQGM------NLSGGQKQRLSLARAVYRRAAVYLMDDPLA 779
Cdd:PRK13639 89 DQ--LFAPTVEEDVAFGPLNLGLSkeevekrvkealkaVGMEGFenkpphHLSGGQKKRVAIAGILAMKPEIIVLDEPTS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13591916 780 ALDAHVSQEVFKqvigpsgLL-----QGTTRILVTHTLHVLP-QADQILVLANGTIAEMGS 834
Cdd:PRK13639 167 GLDPMGASQIMK-------LLydlnkEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGT 220
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1271-1325 |
1.82e-06 |
|
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: 50.51 E-value: 1.82e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 13591916 1271 LRHRPELPmAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWID 1325
Cdd:COG4778 18 LQGGKRLP-VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR 71
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1279-1468 |
1.90e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 51.32 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1279 MAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQE-----ATEGGIWIDGVPITDMGLH--TLRSRITIIPQDPVLF 1351
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1352 PGSLRMNLDL------LQENTDEGIWAALETVQLKAFVTSLPGQlqyecSGQGddLSVGQKQLLCLARALLRKTQILILD 1425
Cdd:PRK14243 104 PKSIYDNIAYgaringYKGDMDELVERSLRQAALWDEVKDKLKQ-----SGLS--LSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 13591916 1426 EATASVDPGTEIQMQAALERWFAQCTVLLIAHRLRSVmncARV 1468
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQA---ARV 216
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1280-1433 |
1.91e-06 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 51.19 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLtwglLR-------LQE--ATEGGIWIDGVPI--TDMGLHTLRSRITIIPQDP 1348
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTL----LRclnrmndLIPgaRVEGEILLDGEDIydPDVDVVELRRRVGMVFQKP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1349 VLFPGS--------LRMNLDLLQENTDE---------GIWaalETV--QLKAFVTSLPGqlqyecsgqgddlsvGQKQLL 1409
Cdd:COG1117 102 NPFPKSiydnvaygLRLHGIKSKSELDEiveeslrkaALW---DEVkdRLKKSALGLSG---------------GQQQRL 163
|
170 180
....*....|....*....|....
gi 13591916 1410 CLARALLRKTQILILDEATASVDP 1433
Cdd:COG1117 164 CIARALAVEPEVLLMDEPTSALDP 187
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1282-1484 |
2.34e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 52.42 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1282 QGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTL----RSRITIIPQDPVLFPgslrm 1357
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLS----- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1358 NLDLLQENTDEGIWAALETVQLKAFVTSLPGQLQYE--CSGQGDDLSVGQKQLLCLARALLRKTQILILDEATASVDPGT 1435
Cdd:PRK10535 100 HLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEdrVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 13591916 1436 EIQMQAALERWFAQC-TVLLIAHRLRSVMNCARVLVMDEGQVAeSGSPAQ 1484
Cdd:PRK10535 180 GEEVMAILHQLRDRGhTVIIVTHDPQVAAQAERVIEIRDGEIV-RNPPAQ 228
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
715-824 |
2.36e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 52.52 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 715 LDLPWLQEVLEA-CALGSDvasfpagvHTPVGEQGMNLSGGQKQRLSLAR---AVYRRAAVYLMDDPLAALDAHVSQEVF 790
Cdd:PRK00635 781 LDEPSIHEKIHAlCSLGLD--------YLPLGRPLSSLSGGEIQRLKLAYellAPSKKPTLYVLDEPTTGLHTHDIKALI 852
|
90 100 110
....*....|....*....|....*....|....
gi 13591916 791 KQVIgpSGLLQGTTRILVTHTLHVLPQADQILVL 824
Cdd:PRK00635 853 YVLQ--SLTHQGHTVVIIEHNMHVVKVADYVLEL 884
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
647-858 |
2.46e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 50.92 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 647 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG--------SVAYVPQE---------AWVQNTSVVENV 709
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGenipamsrSRLYTVRKrmsmlfqsgALFTDMNVFDNV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 710 CF--RQELDLP--WLQEV----LEACALGSDVASFPAgvhtpvgeqgmNLSGGQKQRLSLARAVYRRAAVYLMDDPLAAL 781
Cdd:PRK11831 106 AYplREHTQLPapLLHSTvmmkLEAVGLRGAAKLMPS-----------ELSGGMARRAALARAIALEPDLIMFDEPFVGQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 782 DAhVSQEVFKQVIGPSGLLQGTTRILVTHTL-HVLPQADQILVLANGTIAEMGSYQDLLHRNGALV-----GLLDGA--- 852
Cdd:PRK11831 175 DP-ITMGVLVKLISELNSALGVTCVVVSHDVpEVLSIADHAYIVADKKIVAHGSAQALQANPDPRVrqfldGIADGPvpf 253
|
....*.
gi 13591916 853 RQPAGE 858
Cdd:PRK11831 254 RYPAGD 259
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
752-834 |
2.74e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.12 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 752 SGGQKQRLSLARAVYRRAAVYLMDDPLAALDahVSqeVFKQVIGPSGLLQ---GTTRILVTHTLHVLPQ-ADQILVLANG 827
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALD--VS--VQAQVLNLMMDLQqelGLSYVFISHDLSVVEHiADEVMVMYLG 231
|
....*..
gi 13591916 828 TIAEMGS 834
Cdd:PRK11308 232 RCVEKGT 238
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
627-839 |
3.42e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 50.48 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 627 ISIHNGTFAWSQESP-PCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGSvAYVPQEAW------ 699
Cdd:PRK13642 5 LEVENLVFKYEKESDvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE-LLTAENVWnlrrki 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 700 ---VQN-------TSVVENVCF--------RQELdlpwLQEVLEACaLGSDVASFPAgvhtpvgEQGMNLSGGQKQRLSL 761
Cdd:PRK13642 84 gmvFQNpdnqfvgATVEDDVAFgmenqgipREEM----IKRVDEAL-LAVNMLDFKT-------REPARLSGGQKQRVAV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13591916 762 ARAVYRRAAVYLMDDPLAALDAHVSQEVFKqVIGPSGLLQGTTRILVTHTLHVLPQADQILVLANGTIAEMGSYQDLL 839
Cdd:PRK13642 152 AGIIALRPEIIILDESTSMLDPTGRQEIMR-VIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
623-841 |
3.70e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 50.08 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 623 SKDRISIHNGTFawsQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGEL----LKVEGSVSIEG--------- 689
Cdd:PRK10418 1 MPQQIELRNIAL---QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvRQTAGRVLLDGkpvapcalr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 690 --SVAYV---PQEAW--VQN--TSVVENVCFR-QELDLPWLQEVLEACALGSD---VASFPagvhtpvgeqgMNLSGGQK 756
Cdd:PRK10418 78 grKIATImqnPRSAFnpLHTmhTHARETCLALgKPADDATLTAALEAVGLENAarvLKLYP-----------FEMSGGML 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 757 QRLSLARAVYRRAAVYLMDDPLAALDAhVSQEVFKQVIGPSGLLQGTTRILVTHTLHVLPQ-ADQILVLANGTIAEMGSY 835
Cdd:PRK10418 147 QRMMIALALLCEAPFIIADEPTTDLDV-VAQARILDLLESIVQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQGDV 225
|
....*.
gi 13591916 836 QDLLHR 841
Cdd:PRK10418 226 ETLFNA 231
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1284-1463 |
4.48e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 49.73 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1284 VSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIwidgvpitdmgLHTLRSRITIIPQ----DPVLfPGSLRMNL 1359
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIGYVPQklylDTTL-PLTVNRFL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1360 DLLQENTDEGIWAALETVQlKAFVTSLPGQlqyecsgqgdDLSVGQKQLLCLARALLRKTQILILDEATASVDpgteIQM 1439
Cdd:PRK09544 91 RLRPGTKKEDILPALKRVQ-AGHLIDAPMQ----------KLSGGETQRVLLARALLNRPQLLVLDEPTQGVD----VNG 155
|
170 180 190
....*....|....*....|....*....|
gi 13591916 1440 QAALERWFAQ------CTVLLIAHRLRSVM 1463
Cdd:PRK09544 156 QVALYDLIDQlrreldCAVLMVSHDLHLVM 185
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1252-1458 |
4.51e-06 |
|
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: 51.29 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1252 SAAQPLWPCGGQIEFRDFGLRHR------PELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLlrlqeateGGIWid 1325
Cdd:TIGR00954 433 GRNSNLVPGRGIVEYQDNGIKFEniplvtPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRIL--------GELW-- 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1326 gvPITDmGLHTL--RSRITIIPQDPVLFPGSLR------MNLDLLQEN--TDEGIWAALETVQLKAFVTSlPGQLQYECS 1395
Cdd:TIGR00954 503 --PVYG-GRLTKpaKGKLFYVPQRPYMTLGTLRdqiiypDSSEDMKRRglSDKDLEQILDNVQLTHILER-EGGWSAVQD 578
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13591916 1396 GQgDDLSVGQKQLLCLARALLRKTQILILDEATASVDPGTEIQMQAALERwfAQCTVLLIAHR 1458
Cdd:TIGR00954 579 WM-DVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHR 638
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
1031-1161 |
4.67e-06 |
|
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: 50.09 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1031 PIGFFERTPVGNLLNRFSkeTDIvdvdipDKMRTLLTYAFG------LLEVGLAVSMAT---PLAIVAIL--PLMLLYAG 1099
Cdd:cd18547 92 PLSYFDTHSHGDIMSRVT--NDV------DNISQALSQSLTqlissiLTIVGTLIMMLYispLLTLIVLVtvPLSLLVTK 163
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13591916 1100 F-----QSLYVAtccQLRRLesasySSVCSHLAETFQGSQVVRAFQAQGPFTAQHDALMDENQRISF 1161
Cdd:cd18547 164 FiakrsQKYFRK---QQKAL-----GELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASF 222
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
751-848 |
4.89e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 49.75 E-value: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 751 LSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFkQVIGPSGLLQGTTRILVTHTLHVLPQADQILVLANGTIA 830
Cdd:PRK13648 143 LSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLL-DLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVY 221
|
90 100
....*....|....*....|
gi 13591916 831 EMGSYQDLLHRNGAL--VGL 848
Cdd:PRK13648 222 KEGTPTEIFDHAEELtrIGL 241
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
642-827 |
4.89e-06 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 49.18 E-value: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 642 PCLHGINLTVPQGCLLAVVGPVGAGKSS---LLSALLGELLKVEGSVSI------------EGSVAYVPQEAWVQNTSVV 706
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTllkALANRTEGNVSVEGDIHYngipykefaekyPGEIIYVSEEDVHFPTLTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 707 envcfRQELDLpwlqeVLEACalGSDVASfpaGVhtpvgeqgmnlSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVS 786
Cdd:cd03233 101 -----RETLDF-----ALRCK--GNEFVR---GI-----------SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 13591916 787 QEVFKQvigpsglLQGTTRILVTHTLHVLPQA--------DQILVLANG 827
Cdd:cd03233 155 LEILKC-------IRTMADVLKTTTFVSLYQAsdeiydlfDKVLVLYEG 196
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1281-1476 |
5.16e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.08 E-value: 5.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1281 VQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLL-RLQEATEGGIWIDGVPITDMG-LHTLRSRITIIPQD-------PVLF 1351
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFgAYPGRWEGEIFIDGKPVKIRNpQQAIAQGIAMVPEDrkrdgivPVMG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1352 PG-----------SLRMNLDLLQENTDegIWAALETVQLKAFVTSLP-GQLqyecSGqgddlsvGQKQLLCLARALLRKT 1419
Cdd:PRK13549 358 VGknitlaaldrfTGGSRIDDAAELKT--ILESIQRLKVKTASPELAiARL----SG-------GNQQKAVLAKCLLLNP 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13591916 1420 QILILDEATASVDPGT--EIQ--MQAALERWFAqctVLLIAHRLRSVMN-CARVLVMDEGQV 1476
Cdd:PRK13549 425 KILILDEPTRGIDVGAkyEIYklINQLVQQGVA---IIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1279-1468 |
5.38e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 49.46 E-value: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1279 MAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQE-----ATEGGIWIDGVPI--TDMGLHTLRSRITIIPQDPVLF 1351
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIysPDVDPIEVRREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1352 PG---------SLRMN-LDLLQENTDEGIWAALETVQL----KAFVTSLPGQLqyecsgqgddlSVGQKQLLCLARALLR 1417
Cdd:PRK14267 98 PHltiydnvaiGVKLNgLVKSKKELDERVEWALKKAALwdevKDRLNDYPSNL-----------SGGQRQRLVIARALAM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 13591916 1418 KTQILILDEATASVDPGTEIQMQAALERWFAQCTVLLIAHrlrSVMNCARV 1468
Cdd:PRK14267 167 KPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH---SPAQAARV 214
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
752-840 |
5.80e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 50.09 E-value: 5.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 752 SGGQKQRLSLARAVYRRAAVYLMDDPLAALDahVSQEVfkQVIgpsGLLQ------GTTRILVTHTLHVLPQ-ADQILVL 824
Cdd:PRK15079 163 SGGQCQRIGIARALILEPKLIICDEPVSALD--VSIQA--QVV---NLLQqlqremGLSLIFIAHDLAVVKHiSDRVLVM 235
|
90
....*....|....*.
gi 13591916 825 ANGTIAEMGSYQDLLH 840
Cdd:PRK15079 236 YLGHAVELGTYDEVYH 251
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
751-841 |
6.04e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.01 E-value: 6.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 751 LSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFkQVIgpsGLLQGTTR---ILVTHTLHVLPQ-ADQILVLAN 826
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQIL-QLI---KVLQKEMSmgvIFITHDMGVVAEiADRVLVMYQ 244
|
90
....*....|....*
gi 13591916 827 GTIAEMGSYQDLLHR 841
Cdd:PRK10261 245 GEAVETGSVEQIFHA 259
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
642-829 |
6.16e-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: 51.17 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 642 PCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG------------SVAYVPQEAWV-QNTSVVEN 708
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietnldavrqSLGMCPQHNILfHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 709 VCFRQELD-LPWLQEVLEACALGSDVasfpaGVHTPVGEQGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQ 787
Cdd:TIGR01257 1024 ILFYAQLKgRSWEEAQLEMEAMLEDT-----GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 13591916 788 EVFKQVIgpsGLLQGTTRILVTHTLHVLP-QADQILVLANGTI 829
Cdd:TIGR01257 1099 SIWDLLL---KYRSGRTIIMSTHHMDEADlLGDRIAIISQGRL 1138
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
644-839 |
6.35e-06 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 49.24 E-value: 6.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-------------SVAYVPQEAWV-QNTSVVENV 709
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarRLALLPQHHLTpEGITVRELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 710 CFRQEldlPWL----------QEVLEACALGSDVASFpagVHTPVGEqgmnLSGGQKQRLSLARAVYRRAAVYLMDDPLA 779
Cdd:PRK11231 98 AYGRS---PWLslwgrlsaedNARVNQAMEQTRINHL---ADRRLTD----LSGGQRQRAFLAMVLAQDTPVVLLDEPTT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13591916 780 ALDAHVSQEVFKqvigpsgLL-----QGTTRILVthtLHVLPQA----DQILVLANGTIAEMGSYQDLL 839
Cdd:PRK11231 168 YLDINHQVELMR-------LMrelntQGKTVVTV---LHDLNQAsrycDHLVVLANGHVMAQGTPEEVM 226
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1284-1485 |
7.60e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 50.03 E-value: 7.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1284 VSLKIHAGEKVGIVGRTGAGKSSLtwglLR----LQEATEGGIWIDG-----VPITDMGlhtlrsrITIIPQDPVLFPG- 1353
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTL----LRmiagLEDITSGDLFIGEkrmndVPPAERG-------VGMVFQSYALYPHl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1354 SLRMN----LDLL---QENTDEGIWAALETVQLKAFVTSLPgqlqyecsgqgDDLSVGQKQLLCLARALLRKTQILILDE 1426
Cdd:PRK11000 91 SVAENmsfgLKLAgakKEEINQRVNQVAEVLQLAHLLDRKP-----------KALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13591916 1427 ATASVDPGTEIQMQAALERWFA--QCTVLLIAHRLRSVMNCA-RVLVMDEGQVAESGSPAQL 1485
Cdd:PRK11000 160 PLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHDQVEAMTLAdKIVVLDAGRVAQVGKPLEL 221
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1280-1332 |
8.43e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 49.84 E-value: 8.43e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSltwgLLR----LQEATEGGIWIDGVPITDM 1332
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKST----LLRmvagLERITSGEIWIGGRVVNEL 71
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
751-834 |
8.83e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 49.28 E-value: 8.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 751 LSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKQVigpsGLLQ---GTTRILVTHTLH-VLPQADQILVLAN 826
Cdd:PRK13637 145 LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKI----KELHkeyNMTIILVSHSMEdVAKLADRIIVMNK 220
|
....*...
gi 13591916 827 GTIAEMGS 834
Cdd:PRK13637 221 GKCELQGT 228
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
741-829 |
9.82e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 48.93 E-value: 9.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 741 HTPVGeqgmNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVF---KQVIGPSGLlqgTTrILVTHTLHvlpQ 817
Cdd:COG1101 143 DTKVG----LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLeltEKIVEENNL---TT-LMVTHNME---Q 211
|
90
....*....|....*.
gi 13591916 818 A----DQILVLANGTI 829
Cdd:COG1101 212 AldygNRLIMMHEGRI 227
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
640-829 |
1.09e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.00 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 640 SPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGS--VAYVPQEA----------------WVQ 701
Cdd:PRK10762 264 SGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHevVTRSPQDGlangivyisedrkrdgLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 702 NTSVVEN--VCFRQELDLPW--LQEVLEACALGSDVASFpaGVHTPVGEQGM-NLSGGQKQRLSLARAVYRRAAVYLMDD 776
Cdd:PRK10762 344 GMSVKENmsLTALRYFSRAGgsLKHADEQQAVSDFIRLF--NIKTPSMEQAIgLLSGGNQQKVAIARGLMTRPKVLILDE 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 777 PLAALDAHVSQEV------FKQvigpsgllQGTTRILVTHTL-HVLPQADQILVLANGTI 829
Cdd:PRK10762 422 PTRGVDVGAKKEIyqlinqFKA--------EGLSIILVSSEMpEVLGMSDRILVMHEGRI 473
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1280-1480 |
1.30e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 48.73 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLrsrITIIPQD-------PVLFP 1352
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSeevdwsfPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1353 GSLRMN-------LDLLQENTDEGIWAALETVQLKAFVTSLPGQLqyecsgqgddlSVGQKQLLCLARALLRKTQILILD 1425
Cdd:PRK15056 99 DVVMMGryghmgwLRRAKKRDRQIVTAALARVDMVEFRHRQIGEL-----------SGGQKKRVFLARAIAQQGQVILLD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 1426 EATASVDPGTEIQMQAALERWFAQ-CTVLLIAHRLRSVMNCARVLVMDEGQVAESG 1480
Cdd:PRK15056 168 EPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
627-827 |
1.50e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 48.67 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 627 ISIHNGTFAWSQESP---PCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-------------- 689
Cdd:PRK13641 3 IKFENVDYIYSPGTPmekKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 690 ---SVAYVPQ--EAWVQNTSVVENVCF-----------RQELDLPWLQEVleacALGSDVASfpagvHTPvgeqgMNLSG 753
Cdd:PRK13641 83 lrkKVSLVFQfpEAQLFENTVLKDVEFgpknfgfsedeAKEKALKWLKKV----GLSEDLIS-----KSP-----FELSG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13591916 754 GQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKqvIGPSGLLQGTTRILVTHTL-HVLPQADQILVLANG 827
Cdd:PRK13641 149 GQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQ--LFKDYQKAGHTVILVTHNMdDVAEYADDVLVLEHG 221
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1281-1478 |
1.61e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 47.85 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1281 VQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDM---GLHTLRSR--------ITIIP---- 1345
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARAKLRAKhvgfvfqsFMLIPtlna 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1346 QDPVLFPGSLRMNLDllqENTDEGIWAALETVQLKAFVTSLPGQlqyecsgqgddLSVGQKQLLCLARALLRKTQILILD 1425
Cdd:PRK10584 106 LENVELPALLRGESS---RQSRNGAKALLEQLGLGKRLDHLPAQ-----------LSGGEQQRVALARAFNGRPDVLFAD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 1426 EATASVD--PGTEI-QMQAALERWFAQcTVLLIAHRLRSVMNCARVLVMDEGQVAE 1478
Cdd:PRK10584 172 EPTGNLDrqTGDKIaDLLFSLNREHGT-TLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1284-1480 |
1.64e-05 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 48.09 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1284 VSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDG------VPITDMGLHTLRSRITIIPQDPVLFPG-SLR 1356
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQQYNLWPHlTVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1357 MNL-----DLLQENTDEGIWAA---LETVQLKAFVTSLPGQLqyecSGqgddlsvGQKQLLCLARALLRKTQILILDEAT 1428
Cdd:PRK11124 101 QNLieapcRVLGLSKDQALARAeklLERLRLKPYADRFPLHL----SG-------GQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 1429 ASVDPgtEIQMQ-AALERWFAQC--TVLLIAHRLRSVMNCA-RVLVMDEGQVAESG 1480
Cdd:PRK11124 170 AALDP--EITAQiVSIIRELAETgiTQVIVTHEVEVARKTAsRVVYMENGHIVEQG 223
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1280-1479 |
1.68e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.14 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPI-----TDmglhTLRSRITIIPQDPVLFPG- 1353
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfastTA----ALAAGVAIIYQELHLVPEm 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1354 SLRMNLDLLQENTDEGIwaaLETVQLKAFVTSlpgQLQyecsGQGDD---------LSVGQKQLLCLARALLRKTQILIL 1424
Cdd:PRK11288 95 TVAENLYLGQLPHKGGI---VNRRLLNYEARE---QLE----HLGVDidpdtplkyLSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 13591916 1425 DEATASVDpGTEI-QMQAALERWFAQCTVLL-IAHRLRSVMN-CARVLVMDEGQVAES 1479
Cdd:PRK11288 165 DEPTSSLS-AREIeQLFRVIRELRAEGRVILyVSHRMEEIFAlCDAITVFKDGRYVAT 221
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1280-1488 |
1.76e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 48.54 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSS----LTwGLLRlqeATEGGIWIDG-VPITDmgLHTLRSRITII---------- 1344
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTtikmLT-GILV---PTSGEVRVLGyVPFKR--RKEFARRIGVVfgqrsqlwwd 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1345 --PQDpvlfpgSLRMNLDL-------LQENTDEGIwaalETVQLKAFVTSLPGQLqyecsgqgddlSVGQKQLLCLARAL 1415
Cdd:COG4586 111 lpAID------SFRLLKAIyripdaeYKKRLDELV----ELLDLGELLDTPVRQL-----------SLGQRMRCELAAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1416 LRKTQILILDEATASVDpgteIQMQAALeRWF-------AQCTVLLIAHRLRSVMN-CARVLVMDEGQVAESGSPAQLLA 1487
Cdd:COG4586 170 LHRPKILFLDEPTIGLD----VVSKEAI-REFlkeynreRGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKE 244
|
.
gi 13591916 1488 Q 1488
Cdd:COG4586 245 R 245
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1281-1432 |
1.91e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 47.79 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1281 VQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHTLRSRITIIPQDPVLFPGSLRMNL- 1359
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDNLi 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13591916 1360 ---DLLQENTDEGIWAAletvQLKAFvtSLPGQ-LQYECSgqgdDLSVGQKQLLCLARALLRKTQILILDEATASVD 1432
Cdd:PRK10247 103 fpwQIRNQQPDPAIFLD----DLERF--ALPDTiLTKNIA----ELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1284-1488 |
2.01e-05 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 48.56 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1284 VSLKIHAGEKVGIVGRTGAGKSSLtwglLR----LQEATEGGIWIDGVPITDmglHTLRSR-ITIIPQDPVLFPG----- 1353
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTV----LRlvagLEKPTEGQIFIDGEDVTH---RSIQQRdICMVFQSYALFPHmslge 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1354 ----SLRMnLDLLQENTDEGIWAALETVQLKAFvtslpgQLQYEcsgqgDDLSVGQKQLLCLARALLRKTQILILDEATA 1429
Cdd:PRK11432 98 nvgyGLKM-LGVPKEERKQRVKEALELVDLAGF------EDRYV-----DQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13591916 1430 SVDPGTEIQMQAALeRWFAQ---CTVLLIAHRLRSVMNCA-RVLVMDEGQVAESGSPAQLLAQ 1488
Cdd:PRK11432 166 NLDANLRRSMREKI-RELQQqfnITSLYVTHDQSEAFAVSdTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1284-1487 |
2.17e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 48.17 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1284 VSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEAT-----EGGIWIDGVPITDM-GLHTLRSRITIIPQDPVLFPGSLRM 1357
Cdd:PRK14271 40 VSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVsgyrySGDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPMSIMD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1358 NL-------DLLQENTDEGIwaaletVQLKAFVTSLPGQLQYECSGQGDDLSVGQKQLLCLARALLRKTQILILDEATAS 1430
Cdd:PRK14271 120 NVlagvrahKLVPRKEFRGV------AQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 13591916 1431 VDPGTEIQMQAALERWFAQCTVLLIAHRLRSVMNCA-RVLVMDEGQVAESGSPAQLLA 1487
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISdRAALFFDGRLVEEGPTEQLFS 251
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1281-1486 |
2.25e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 47.73 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1281 VQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGV------PITDMGLHTLRSRITIIPQDPVLFPgS 1354
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFP-H 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1355 LRMNLDLLQENTDEGIwaaLETVQLKAFV------TSLPGQLQYECSGQGDDLSVGQKQLLCLARALLRKTQILILDEAT 1428
Cdd:PRK14246 105 LSIYDNIAYPLKSHGI---KEKREIKKIVeeclrkVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 13591916 1429 ASVDPGTEIQMQAALERWFAQCTVLLIAHRLRSVMNCAR-VLVMDEGQVAESGSPAQLL 1486
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADyVAFLYNGELVEWGSSNEIF 240
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1263-1487 |
2.31e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 47.77 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1263 QIEFRdfGLRHRPELPMaVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEA----TEGGIWIDGVPITdmgLHTLR 1338
Cdd:PRK10418 4 QIELR--NIALQAAQPL-VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVA---PCALR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1339 SR-ITIIPQDP-VLFPGSLRMN-------LDLLQENTDEGIWAALETVQLkAFVTSLPGQLQYECSGqgddlsvGQKQLL 1409
Cdd:PRK10418 78 GRkIATIMQNPrSAFNPLHTMHtharetcLALGKPADDATLTAALEAVGL-ENAARVLKLYPFEMSG-------GMLQRM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1410 CLARALLRKTQILILDEATASVDPGTEIQMQAALERWFAQ--CTVLLIAHRLRSVMNCA-RVLVMDEGQVAESGSPAQLL 1486
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKraLGMLLVTHDMGVVARLAdDVAVMSHGRIVEQGDVETLF 229
|
.
gi 13591916 1487 A 1487
Cdd:PRK10418 230 N 230
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
644-830 |
2.37e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.77 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSllsallgeLLKV----------EGSVSIEGS--------------VAYVPQE-A 698
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKST--------LMKVlsgvyphgtyEGEIIFEGEelqasnirdteragIAIIHQElA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 699 WVQNTSVVENVCFRQELD----LPWLQEVLEACALGSDVaSFPAGVHTPVgeqgMNLSGGQKQRLSLARAVYRRAAVYLM 774
Cdd:PRK13549 93 LVKELSVLENIFLGNEITpggiMDYDAMYLRAQKLLAQL-KLDINPATPV----GNLGLGQQQLVEIAKALNKQARLLIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 775 DDPLAALDAhvsQEVfkqvigpSGLL--------QGTTRILVTHTLH-VLPQADQILVLANG-TIA 830
Cdd:PRK13549 168 DEPTASLTE---SET-------AVLLdiirdlkaHGIACIYISHKLNeVKAISDTICVIRDGrHIG 223
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
740-838 |
2.58e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 47.87 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 740 VHTPVGEQGM---------NLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKQVIGpsglLQ---GTTRIL 807
Cdd:PRK13640 124 VRDVLADVGMldyidsepaNLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRK----LKkknNLTVIS 199
|
90 100 110
....*....|....*....|....*....|.
gi 13591916 808 VTHTLHVLPQADQILVLANGTIAEMGSYQDL 838
Cdd:PRK13640 200 ITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
627-839 |
2.61e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 47.68 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 627 ISIHNGTFAWSQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGSVayVPQEAW------- 699
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGIT--ISKENLkeirkki 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 700 ---VQN-------TSVVENVCFRQE---LDLPWLQEVLEACALGSDVASFpagvhtpVGEQGMNLSGGQKQRLSLARAVY 766
Cdd:PRK13632 86 giiFQNpdnqfigATVEDDIAFGLEnkkVPPKKMKDIIDDLAKKVGMEDY-------LDKEPQNLSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 767 RRAAVYLMDDPLAALDAHVSQEVfKQVIGPsglLQGT---TRILVTHTLHVLPQADQILVLANGTIAEMGSYQDLL 839
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKREI-KKIMVD---LRKTrkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
751-834 |
2.96e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 47.70 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 751 LSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHvSQEVFKQVIGPSGLLQGTTRILVTHTL-HVLPQADQILVLANGTI 829
Cdd:PRK13645 151 LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK-GEEDFINLFERLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKV 229
|
....*
gi 13591916 830 AEMGS 834
Cdd:PRK13645 230 ISIGS 234
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1281-1486 |
3.09e-05 |
|
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: 47.39 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1281 VQGVSLKIHAGEKVGIVGRTGAGKSSLtwglLRLQEA----TEGG-IWIDGVPITDMGLHTLRSRI---------TIIPQ 1346
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTL----LSLITGdlppTYGNdVRLFGERRGGEDVWELRKRIglvspalqlRFPRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1347 DPVL------FPGSLrmnlDLLQENTDEGI---WAALETVQLKAFVTSLPGQLqyecsgqgddlSVGQKQllclarallr 1417
Cdd:COG1119 95 ETVLdvvlsgFFDSI----GLYREPTDEQReraRELLELLGLAHLADRPFGTL-----------SQGEQR---------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1418 KTQI----------LILDEATASVDPGTEIQMQAALERWFAQ--CTVLLIAHRLRSVMNC-ARVLVMDEGQVAESGSPAQ 1484
Cdd:COG1119 150 RVLIaralvkdpelLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEE 229
|
..
gi 13591916 1485 LL 1486
Cdd:COG1119 230 VL 231
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
1019-1235 |
3.28e-05 |
|
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: 47.59 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1019 LFRSLLwdvaRSPIGFFERTPVGNLLNRFSkETDIVDVDIPDKMRTLLT---YAFGLLEVGLAVSMATPLAIVAILPLM- 1094
Cdd:cd18782 81 IIDHLL----RLPLGFFDKRPVGELSTRIS-ELDTIRGFLTGTALTTLLdvlFSVIYIAVLFSYSPLLTLVVLATVPLQl 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1095 LLYAGFQSLYVAtccQLRRLESASySSVCSHLAETFQGSQVVRAFQAQGPFTAQ----HDALMDENQRISFPRLVADRwL 1170
Cdd:cd18782 156 LLTFLFGPILRR---QIRRRAEAS-AKTQSYLVESLTGIQTVKAQNAELKARWRwqnrYARSLGEGFKLTVLGTTSGS-L 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 1171 AANLELLGNGLVFVAATCAVLsKAHLSAG-LAGFSVSAAlQVTQTLQWVVRSWTDLENSMVAVERV 1235
Cdd:cd18782 231 SQFLNKLSSLLVLWVGAYLVL-RGELTLGqLIAFRILSG-YVTGPILRLSTLWQQFQELRVSLERL 294
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1284-1502 |
3.89e-05 |
|
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: 47.79 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1284 VSLKIHAGEKVGIVGRTGAGKSSL---TWGLLRLQEAT---EGGIWIDGVPITDMGLHtlRSRITIIPQDPVLFPG-SLR 1356
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLlraIAGLERPDSGRirlGGEVLQDSARGIFLPPH--RRRIGYVFQEARLFPHlSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1357 MNLDLlqentdeGIW------------AALETVQLKAFVTSLPGQLqyecSGqgddlsvGQKQLLCLARALLRKTQILIL 1424
Cdd:COG4148 96 GNLLY-------GRKrapraerrisfdEVVELLGIGHLLDRRPATL----SG-------GERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1425 DEATASVDPGTEIQMQAALERWFAQ--CTVLLIAHRLRSVMNCA-RVLVMDEGQVAESGSPAQLLAQKGLFyRLAQESGL 1501
Cdd:COG4148 158 DEPLAALDLARKAEILPYLERLRDEldIPILYVSHSLDEVARLAdHVVLLEQGRVVASGPLAEVLSRPDLL-PLAGGEEA 236
|
.
gi 13591916 1502 A 1502
Cdd:COG4148 237 G 237
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1284-1486 |
4.10e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.98 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1284 VSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPIT-DMGLHTLRSRITIIPQD-------PVLfpgSL 1355
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAIRAGIMLCPEDrkaegiiPVH---SV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1356 RMNLD------------LL-----QENTDEGIwaaletvQLKAFVTSLPGQLQYECSGqgddlsvGQKQLLCLARALLRK 1418
Cdd:PRK11288 349 ADNINisarrhhlragcLInnrweAENADRFI-------RSLNIKTPSREQLIMNLSG-------GNQQKAILGRWLSED 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13591916 1419 TQILILDEATASVDPGTEIQMQAALERWFAQ-CTVLLIAHRLRSVMNCA-RVLVMDEGQVA-----ESGSPAQLL 1486
Cdd:PRK11288 415 MKVILLDEPTRGIDVGAKHEIYNVIYELAAQgVAVLFVSSDLPEVLGVAdRIVVMREGRIAgelarEQATERQAL 489
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
642-839 |
4.82e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 46.90 E-value: 4.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 642 PCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGSVAYVPQEawVQNTSVVENVCFRQELDLPWLQ 721
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSK--LQGIRKLVGIVFQNPETQFVGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 722 EVLEACALGSDVASFP-----AGVHTPVGEQGM---------NLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQ 787
Cdd:PRK13644 94 TVEEDLAFGPENLCLPpieirKRVDRALAEIGLekyrhrspkTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 13591916 788 EVFKQVIGPSGllQGTTRILVTHTLHVLPQADQILVLANGTIAEMGSYQDLL 839
Cdd:PRK13644 174 AVLERIKKLHE--KGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
983-1190 |
4.99e-05 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 46.86 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 983 SALRGSIFGLLGCLQAIGLFASM-AAVF-LGG----ARASCLLFRSLLwdvaRSPIGFFERTPVGNLLNRFSKETDI--- 1053
Cdd:cd18780 39 RALNQAVLILLGVVLIGSIATFLrSWLFtLAGervvARLRKRLFSAII----AQEIAFFDVTRTGELLNRLSSDTQVlqn 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1054 -VDVDIPDKMRTLLTyAFGLLEVGLAVSMATPLAIVAILPLMLLYAGFQSLYVATccqLRRL---ESASYSSVCShlaET 1129
Cdd:cd18780 115 aVTVNLSMLLRYLVQ-IIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRK---LSKKfqdALAAASTVAE---ES 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13591916 1130 FQGSQVVRAFQAQGPFTAQHDALMDENQRISFPRLVADRWLaanlellgNGLVFVAATCAV 1190
Cdd:cd18780 188 ISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGF--------NGFMGAAAQLAI 240
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
309-544 |
6.14e-05 |
|
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: 46.64 E-value: 6.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 309 FLLGTLSLVISDAFRFAVPKLLSLFLEFMGDLESSAWTGWLLAVLMFLSACLQTLFeqQYMYRVKV------LQMRLRTA 382
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGTLTASQLLRYALLILLLALLIGIF--RFLWRYLIfgasrrIEYDLRND 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 383 ItglvYRKVLVLSSGSRKSSAAGDVVNLVSVDVQRLVES----ILHL-NGLWLLFLWIIVCFVYLWQllgpsaLTAVAvf 457
Cdd:cd18541 79 L----FAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMAlgpgILYLvDALFLGVLVLVMMFTISPK------LTLIA-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 458 LSLLPLNFFITKK--RSFHQEEQMRQKASrARLTSS---MLRTVRTIKSHGWECAFLERL----LHIRGQELGALKTSAF 528
Cdd:cd18541 147 LLPLPLLALLVYRlgKKIHKRFRKVQEAF-SDLSDRvqeSFSGIRVIKAFVQEEAEIERFdklnEEYVEKNLRLARVDAL 225
|
250
....*....|....*.
gi 13591916 529 LFSVSLVSFQVSTFLV 544
Cdd:cd18541 226 FFPLIGLLIGLSFLIV 241
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
642-819 |
6.93e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 45.71 E-value: 6.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 642 PCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGS------VAYVPQEAWV-QNTSVVENVCFRQE 714
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsikkdlCTYQKQLCFVgHRSGINPYLTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 715 --LDLPWLQ---EVLEACALGS--DVASFPAGVhtpvgeqgmnLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQ 787
Cdd:PRK13540 95 clYDIHFSPgavGITELCRLFSleHLIDYPCGL----------LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180 190
....*....|....*....|....*....|..
gi 13591916 788 EVFKQVigPSGLLQGTTRILVTHTLHVLPQAD 819
Cdd:PRK13540 165 TIITKI--QEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1270-1477 |
7.47e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 47.32 E-value: 7.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1270 GLRHRPelpmAVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITdmgLHT----LRSRITIIP 1345
Cdd:COG1129 261 GLSVGG----VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR---IRSprdaIRAGIAYVP 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1346 QDPV---LFPG-SLRMNLDLlqentdegiwAALETV---------QLKAFVTSLPGQLQYECSGQGD---DLSVGQKQll 1409
Cdd:COG1129 334 EDRKgegLVLDlSIRENITL----------ASLDRLsrgglldrrRERALAEEYIKRLRIKTPSPEQpvgNLSGGNQQ-- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1410 clarallrK----------TQILILDEATASVDPGT--EIQmqaALERWFAQ--CTVLLIAHRLRSVM-NCARVLVMDEG 1474
Cdd:COG1129 402 --------KvvlakwlatdPKVLILDEPTRGIDVGAkaEIY---RLIRELAAegKAVIVISSELPELLgLSDRILVMREG 470
|
...
gi 13591916 1475 QVA 1477
Cdd:COG1129 471 RIV 473
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
644-834 |
7.52e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 46.38 E-value: 7.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG---------------SVAYVPQEAWVQ--NTSVV 706
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpidysrkglmklreSVGMVFQDPDNQlfSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 707 ENVCF-RQELDLP--WLQEVLEACALGSDVASFPagvHTPVgeqgMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDA 783
Cdd:PRK13636 102 QDVSFgAVNLKLPedEVRKRVDNALKRTGIEHLK---DKPT----HCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 13591916 784 HVSQEVFKQVIGPSGLLqGTTRILVTHTLHVLP-QADQILVLANGTIAEMGS 834
Cdd:PRK13636 175 MGVSEIMKLLVEMQKEL-GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGN 225
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
644-840 |
7.58e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 46.27 E-value: 7.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSI-EGSVAYVPQEAWVQNTSVVENVCFRQELDLPWLQE 722
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 723 VLEACALG--------SDVASFPAGVHTPVG-------EQGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQ 787
Cdd:PRK13643 102 VLKDVAFGpqnfgipkEKAEKIAAEKLEMVGladefweKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 13591916 788 EVFKqvIGPSGLLQGTTRILVTHTL-HVLPQADQILVLANGTIAEMGSYQDLLH 840
Cdd:PRK13643 182 EMMQ--LFESIHQSGQTVVLVTHLMdDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
749-827 |
8.01e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 45.64 E-value: 8.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 749 MNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQ------EVFKQVigpsgllqGTTRILVTHTLHVLPQAD-QI 821
Cdd:PRK10908 136 IQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEgilrlfEEFNRV--------GVTVLMATHDIGLISRRSyRM 207
|
....*.
gi 13591916 822 LVLANG 827
Cdd:PRK10908 208 LTLSDG 213
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
627-838 |
9.41e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 45.93 E-value: 9.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 627 ISIHNGTFAWSQESP---PCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-------------- 689
Cdd:PRK13646 3 IRFDNVSYTYQKGTPyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 690 ---SVAYVPQ--EAWVQNTSVVENVCF-RQELDLPwLQEVLE-ACALGSDVAsFPAGVhtpVGEQGMNLSGGQKQRLSLA 762
Cdd:PRK13646 83 vrkRIGMVFQfpESQLFEDTVEREIIFgPKNFKMN-LDEVKNyAHRLLMDLG-FSRDV---MSQSPFQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13591916 763 RAVYRRAAVYLMDDPLAALDAHVSQEVFKqVIGPSGLLQGTTRILVTHTLH-VLPQADQILVLANGTIAEMGSYQDL 838
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMR-LLKSLQTDENKTIILVSHDMNeVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1263-1487 |
9.80e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 46.23 E-value: 9.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1263 QIEFRDFGLRHRPELPM---AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGI-WI--DGVPITDMGLHT 1336
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPTelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIeWIfkDEKNKKKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1337 ---------------------LRSRITIIPQ------------DPVLFpGSLRMNLDllQENTDEGIWAALETVQL-KAF 1382
Cdd:PRK13651 82 kvleklviqktrfkkikkikeIRRRVGVVFQfaeyqlfeqtieKDIIF-GPVSMGVS--KEEAKKRAAKYIELVGLdESY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1383 VTSLPgqlqYECSGqgddlsvGQKQLLCLARALLRKTQILILDEATASVDPGTEIQMQAALERWFAQC-TVLLIAHRLRS 1461
Cdd:PRK13651 159 LQRSP----FELSG-------GQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGkTIILVTHDLDN 227
|
250 260
....*....|....*....|....*..
gi 13591916 1462 VMNCA-RVLVMDEGQVAESGSPAQLLA 1487
Cdd:PRK13651 228 VLEWTkRTIFFKDGKIIKDGDTYDILS 254
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
743-824 |
9.86e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.93 E-value: 9.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 743 PVGEQGMNLSGGQKQRLSLARAVYRRA---AVYLMDDPLAALDAH-VSQ--EVFKQVIGpsgllQGTTRILVTHTLHVLP 816
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLHFDdIKKllEVLQRLVD-----KGNTVVVIEHNLDVIK 896
|
....*...
gi 13591916 817 QADQILVL 824
Cdd:TIGR00630 897 TADYIIDL 904
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1280-1482 |
1.04e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 47.32 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPItDMGLHTLRSRITIIPQDPVLFPGSLRMNL 1359
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1360 DLLQENTDEGIWaalETVQLKAFVTSLPGQLQYECSGQGDDLSVGQKQLLCLARALLRKTQILILDEATASVDPGTEIQM 1439
Cdd:TIGR01257 1024 ILFYAQLKGRSW---EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 13591916 1440 QAALERWFAQCTVLLIAHRLRSV-MNCARVLVMDEGQVAESGSP 1482
Cdd:TIGR01257 1101 WDLLLKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1281-1478 |
1.18e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.70 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1281 VQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMG-LHTLRSRITIIPQ---DPVLFPG-SL 1355
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpLDAVKKGMAYITEsrrDNGFFPNfSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1356 RMNLDLLQENTD---EGIWAALETVQLKAFVTSLPGQLQYECSGQGD---DLSVGQKQLLCLARALLRKTQILILDEATA 1429
Cdd:PRK09700 359 AQNMAISRSLKDggyKGAMGLFHEVDEQRTAENQRELLALKCHSVNQnitELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 13591916 1430 SVDPGTEIQMQaALERWFAQ--CTVLLIAHRLRSVMN-CARVLVMDEGQVAE 1478
Cdd:PRK09700 439 GIDVGAKAEIY-KVMRQLADdgKVILMVSSELPEIITvCDRIAVFCEGRLTQ 489
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1280-1476 |
1.22e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 45.25 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMG---LHTLRSRITIIPQD-PVLFPGSL 1355
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnreVPFLRRQIGMIFQDhHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1356 RMNLDL-------LQENTDEGIWAALETVQLKAFVTSLPGQlqyecsgqgddLSVGQKQLLCLARALLRKTQILILDEAT 1428
Cdd:PRK10908 97 YDNVAIpliiagaSGDDIRRRVSAALDKVGLLDKAKNFPIQ-----------LSGGEQQRVGIARAVVNKPAVLLADEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 13591916 1429 ASVDPgteiQMQAALERWFAQ-----CTVLLIAHRLRSVMN-CARVLVMDEGQV 1476
Cdd:PRK10908 166 GNLDD----ALSEGILRLFEEfnrvgVTVLMATHDIGLISRrSYRMLTLSDGHL 215
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
656-782 |
1.28e-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: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 656 LLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG-SVAYVPQEAWVQNTSVVENVCFRQeldlpwLQEVLEACALGSDVA 734
Cdd:cd03237 27 VIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYIKADYEGTVRDLLSSI------TKDFYTHPYFKTEIA 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 13591916 735 SfPAGVHTPVGEQGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALD 782
Cdd:cd03237 101 K-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1280-1487 |
1.32e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 45.95 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLrlqeategGIWIDGVPIT-------DMGLHTLRSR---------ITI 1343
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAIC--------GVTKDNWRVTadrmrfdDIDLLRLSPRerrklvghnVSM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1344 IPQDP--VLFPgSLRMNLDLLQE---NTDEGIW---------AALETVQL------KAFVTSLPgqlqYEcsgqgddLSV 1403
Cdd:PRK15093 94 IFQEPqsCLDP-SERVGRQLMQNipgWTYKGRWwqrfgwrkrRAIELLHRvgikdhKDAMRSFP----YE-------LTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1404 GQKQLLCLARALLRKTQILILDEATASVDPGTEIQMQAALERWFAQ--CTVLLIAHRLRSVMNCA-RVLVMDEGQVAESG 1480
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnnTTILLISHDLQMLSQWAdKINVLYCGQTVETA 241
|
....*..
gi 13591916 1481 SPAQLLA 1487
Cdd:PRK15093 242 PSKELVT 248
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1280-1479 |
1.42e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.15 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMG-LHTLRSRITIIPQDPVLFPG-SLRM 1357
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGpKSSQEAGIGIIHQELNLIPQlTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1358 NLDLLQENTdeGIWAALETVQLKAFVTSLPGQLQYECSGQG--DDLSVGQKQLLCLARALLRKTQILILDEAT-ASVDPG 1434
Cdd:PRK10762 99 NIFLGREFV--NRFGRIDWKKMYAEADKLLARLNLRFSSDKlvGELSIGEQQMVEIAKVLSFESKVIIMDEPTdALTDTE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 13591916 1435 TEIQMQAALERWFAQCTVLLIAHRLRSVMN-CARVLVMDEGQ-VAES 1479
Cdd:PRK10762 177 TESLFRVIRELKSQGRGIVYISHRLKEIFEiCDDVTVFRDGQfIAER 223
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
743-824 |
1.43e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 45.30 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 743 PVGEQGMNLSGGQKQRLSLARAVYRRA---AVYLMDDPLAAL---DAHVSQEVFKQVIGpsgllQGTTRILVTHTLHVLP 816
Cdd:cd03271 162 KLGQPATTLSGGEAQRIKLAKELSKRStgkTLYILDEPTTGLhfhDVKKLLEVLQRLVD-----KGNTVVVIEHNLDVIK 236
|
....*...
gi 13591916 817 QADQILVL 824
Cdd:cd03271 237 CADWIIDL 244
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
646-839 |
1.50e-04 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 45.57 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 646 GINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGS------------VAYVPQ-EAWVQNTSVVENV-CF 711
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpvpsrarharqrVGVVPQfDNLDPDFTVRENLlVF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 712 RQELDLPwLQEVLEACALGSDVASFPAGVHTPVGEqgmnLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFK 791
Cdd:PRK13537 105 GRYFGLS-AAAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 13591916 792 QVigPSGLLQGTTRILVTHTLHVLPQ-ADQILVLANG-TIAEmGSYQDLL 839
Cdd:PRK13537 180 RL--RSLLARGKTILLTTHFMEEAERlCDRLCVIEEGrKIAE-GAPHALI 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
752-836 |
1.59e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 46.24 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 752 SGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSqevfKQVIGPSGLLQGTTR---ILVTHTLHVLPQ-ADQILVLANG 827
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQ----AQILALLKSLQQKHQlayLFISHDLHVVRAlCHQVIVLRQG 502
|
....*....
gi 13591916 828 TIAEMGSYQ 836
Cdd:PRK15134 503 EVVEQGDCE 511
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
751-841 |
1.70e-04 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 45.49 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 751 LSGGQKQRLSLARAVYRRAAVYLMDDPLAALDahVSqeVFKQVIgpsGLLQ------GTTRILVTHTLHVLPQ-ADQILV 823
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALD--VS--IQAQVL---NLLEdlqdelGLTYLFISHDLSVVRHiSDRVAV 230
|
90
....*....|....*...
gi 13591916 824 LANGTIAEMGSYQDLLHR 841
Cdd:COG4608 231 MYLGKIVEIAPRDELYAR 248
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
752-828 |
1.72e-04 |
|
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: 44.73 E-value: 1.72e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13591916 752 SGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHvSQEVFKQVIGpSGLLQGTTRILVTHTLHVLPQ-ADQILVLANGT 828
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAA-NRAVVVELIE-EAKARGTAIIGIFHDEEVREAvADRVVDVTPFS 229
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1280-1478 |
1.79e-04 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 45.08 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGlhtlrSRITIIPQDPVLFP-----GS 1354
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AERGVVFQNEGLLPwrnvqDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1355 LRMNLDLLQENTDEGIWAALET---VQLKAFVTSLPGQLqyecsgqgddlSVGQKQLLCLARALLRKTQILILDEATASV 1431
Cdd:PRK11248 91 VAFGLQLAGVEKMQRLEIAHQMlkkVGLEGAEKRYIWQL-----------SGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 13591916 1432 DPGTEIQMQAALERWFAQC--TVLLIAHRLRSVMNCARVLVM---DEGQVAE 1478
Cdd:PRK11248 160 DAFTREQMQTLLLKLWQETgkQVLLITHDIEEAVFMATELVLlspGPGRVVE 211
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
977-1165 |
1.86e-04 |
|
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: 45.52 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 977 DGKQMHSALRGS-IFGLLGCLQAIGLFASMAAVFLGGARASC----LLFRSLLwdvaRSPIGFFERTP--VGNLLNRFSK 1049
Cdd:cd18578 44 DDELRSEANFWAlMFLVLAIVAGIAYFLQGYLFGIAGERLTRrlrkLAFRAIL----RQDIAWFDDPEnsTGALTSRLST 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1050 EtdivdvdiPDKMRTLLTYAFGL-------LEVGLAVSMAT--PLAIV--AILPLMLLyAGFQSLYVatccqLRRLES-- 1116
Cdd:cd18578 120 D--------ASDVRGLVGDRLGLilqaivtLVAGLIIAFVYgwKLALVglATVPLLLL-AGYLRMRL-----LSGFEEkn 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 13591916 1117 -ASYSSVCSHLAETFQGSQVVRAFQAQGPFTAQHDALMDENQRISFPRLV 1165
Cdd:cd18578 186 kKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRAL 235
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
750-834 |
1.99e-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: 45.95 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 750 NLSGGQKQRLSLARAVYRRAAVYLMDDPLAALD---AHVSQEVFKQVIGPSGLlqgtTRILVTHTLHVLPQ-ADQILVLA 825
Cdd:TIGR03269 168 DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpqtAKLVHNALEEAVKASGI----SMVLTSHWPEVIEDlSDKAIWLE 243
|
....*....
gi 13591916 826 NGTIAEMGS 834
Cdd:TIGR03269 244 NGEIKEEGT 252
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
745-832 |
2.15e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.50 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 745 GEQGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKQVigPSGLLQGTTRILVTHTL-------HVLPQ 817
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEV--RSMVRDGATVLLTTQYMeeaeqlaHELTV 216
|
90
....*....|....*
gi 13591916 818 ADQILVLANGTIAEM 832
Cdd:NF000106 217 IDRGRVIADGKVDEL 231
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
644-783 |
2.18e-04 |
|
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: 45.59 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGEL--LKVEGSVSIEGS--------------VAYVPQE-AWVQNTSVV 706
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSplkasnirdteragIVIIHQElTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 707 ENVCFRQELDLP-----WLQEVLEACALGSDVASFPAGVHTPVGEQGmnlsGGQKQRLSLARAVYRRAAVYLMDDPLAAL 781
Cdd:TIGR02633 97 ENIFLGNEITLPggrmaYNAMYLRAKNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
..
gi 13591916 782 DA 783
Cdd:TIGR02633 173 TE 174
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
647-826 |
2.35e-04 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 43.30 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 647 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSI--EGSVAYVPQEAWVQNTSvvenvcFRQELDLPWlqevl 724
Cdd:cd03223 20 LSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpeGEDLLFLPQRPYLPLGT------LREQLIYPW----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 725 eacalgsdvasfpagvhtpvgeqGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKQVigpsgLLQGTT 804
Cdd:cd03223 89 -----------------------DDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL-----KELGIT 140
|
170 180
....*....|....*....|..
gi 13591916 805 RILVTHTLHVLPQADQILVLAN 826
Cdd:cd03223 141 VISVGHRPSLWKFHDRVLDLDG 162
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
627-841 |
2.53e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 44.74 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 627 ISIHNGTFAWSQESP---PCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGSVayvpqeawVQNT 703
Cdd:PRK13649 3 INLQNVSYTYQAGTPfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTL--------ITST 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 704 SVVENVCF-RQELDL----PWLQeVLEACALgSDVASFPA--GVHTPVGEQ---------GMN----------LSGGQKQ 757
Cdd:PRK13649 75 SKNKDIKQiRKKVGLvfqfPESQ-LFEETVL-KDVAFGPQnfGVSQEEAEAlareklalvGISeslfeknpfeLSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 758 RLSLARAVYRRAAVYLMDDPLAALDAHVSQE---VFKQVigpsgLLQGTTRILVTHTL-HVLPQADQILVLANGTIAEMG 833
Cdd:PRK13649 153 RVAIAGILAMEPKILVLDEPTAGLDPKGRKElmtLFKKL-----HQSGMTIVLVTHLMdDVANYADFVYVLEKGKLVLSG 227
|
....*...
gi 13591916 834 SYQDLLHR 841
Cdd:PRK13649 228 KPKDIFQD 235
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1281-1478 |
3.02e-04 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 45.06 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1281 VQGVSLKIHAGEKVGIVGRTGAGKSSltwgLLRL----QEATEGGIwidgvpitDMGlHTLrsRITIIPQDPVLFPGSLR 1356
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKST----LLKLlageLEPDSGTV--------KLG-ETV--KIGYFDQHQEELDPDKT 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1357 MnLDLLQENTDEGiwaalETVQLKAFVTSL--PGQLQYE-CSgqgdDLSVGQKQLLCLARALLRKTQILILDEATASVDP 1433
Cdd:COG0488 396 V-LDELRDGAPGG-----TEQEVRGYLGRFlfSGDDAFKpVG----VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDI 465
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 13591916 1434 GTEIQMQAALERWfaQCTVLLIAH-R--LRSVmnCARVLVMDEGQVAE 1478
Cdd:COG0488 466 ETLEALEEALDDF--PGTVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1282-1307 |
3.29e-04 |
|
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: 42.44 E-value: 3.29e-04
10 20
....*....|....*....|....*.
gi 13591916 1282 QGVSLKIHAGEKVGIVGRTGAGKSSL 1307
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKSTL 42
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1280-1457 |
3.40e-04 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 44.08 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPIT----DMGL----HTLRSRITIIpqDPVLF 1351
Cdd:COG4525 22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTgpgaDRGVvfqkDALLPWLNVL--DNVAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1352 PGSLR-MNLDLLQENTDEgiwaALETVQLKAFVTSLPGQLqyecSGqgddlsvGQKQLLCLARALLRKTQILILDEATAS 1430
Cdd:COG4525 100 GLRLRgVPKAERRARAEE----LLALVGLADFARRRIWQL----SG-------GMRQRVGIARALAADPRFLLMDEPFGA 164
|
170 180
....*....|....*....|....*....
gi 13591916 1431 VDPGTEIQMQAALERWFAQC--TVLLIAH 1457
Cdd:COG4525 165 LDALTREQMQELLLDVWQRTgkGVFLITH 193
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
644-777 |
3.74e-04 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 45.06 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKssllsallGELLKV--------EGSVSIEG--SVAYVPQEA-WVQNTSVVENVC-- 710
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGK--------STLLKIlagelepdSGEVSIPKglRIGYLPQEPpLDDDLTVLDTVLdg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 711 ------FRQELD---------------LPWLQEVLEAC---ALGSDVAS------FPAGVH-TPVGEqgmnLSGGQKQRL 759
Cdd:COG0488 86 daelraLEAELEeleaklaepdedlerLAELQEEFEALggwEAEARAEEilsglgFPEEDLdRPVSE----LSGGWRRRV 161
|
170
....*....|....*...
gi 13591916 760 SLARAVYRRAAVYLMDDP 777
Cdd:COG0488 162 ALARALLSEPDLLLLDEP 179
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
623-829 |
4.33e-04 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 43.71 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 623 SKDRISIHNGTFAwsqesppCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEG------------- 689
Cdd:PRK11614 7 SFDKVSAHYGKIQ-------ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGkditdwqtakimr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 690 -SVAYVPQEAWV-QNTSVVENVCF------RQEldlpWLQEVLEACALgsdvasFPAgVHTPVGEQGMNLSGGQKQRLSL 761
Cdd:PRK11614 80 eAVAIVPEGRRVfSRMTVEENLAMggffaeRDQ----FQERIKWVYEL------FPR-LHERRIQRAGTMSGGEQQMLAI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13591916 762 ARAVYRRAAVYLMDDPLAALDAHVSQEVFKQVigPSGLLQGTTRILVTHTLH-VLPQADQILVLANGTI 829
Cdd:PRK11614 149 GRALMSQPRLLLLDEPSLGLAPIIIQQIFDTI--EQLREQGMTIFLVEQNANqALKLADRGYVLENGHV 215
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
751-839 |
4.44e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 43.93 E-value: 4.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 751 LSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKQVigpSGLLQGTTRILVTHTLHVLPQ-ADQILVLANGTI 829
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFI---RSLADRLTVIIVTHNLAQAARiSDRAALFFDGRL 240
|
90
....*....|
gi 13591916 830 AEMGSYQDLL 839
Cdd:PRK14271 241 VEEGPTEQLF 250
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
644-830 |
4.52e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 44.62 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGS--------------VAYVP----QEAWVQNTSV 705
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprdairagIAYVPedrkGEGLVLDLSI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 706 VENVC---FRQELDLPWLQEVLEACALGSDVASF---PAGVHTPVGeqgmNLSGGQKQRLSLARAVYRRAAVYLMDDPLA 779
Cdd:COG1129 348 RENITlasLDRLSRGGLLDRRRERALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTR 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 13591916 780 ALDAHVSQEVFKqvigpsgLL-----QGTTRILVTHTLH-VLPQADQILVLANGTIA 830
Cdd:COG1129 424 GIDVGAKAEIYR-------LIrelaaEGKAVIVISSELPeLLGLSDRILVMREGRIV 473
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
635-782 |
5.88e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 42.91 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 635 AWSQESPPCLHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGS----------VAYVPQ-EAWVQNT 703
Cdd:PRK13543 18 AFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatrgdrsrfMAYLGHlPGLKADL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 704 SVVENVCFrqeldlpwlqevleACAL-GSDVASFPAGVHTPVGEQGM------NLSGGQKQRLSLARAVYRRAAVYLMDD 776
Cdd:PRK13543 98 STLENLHF--------------LCGLhGRRAKQMPGSALAIVGLAGYedtlvrQLSAGQKKRLALARLWLSPAPLWLLDE 163
|
....*.
gi 13591916 777 PLAALD 782
Cdd:PRK13543 164 PYANLD 169
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
653-789 |
5.95e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.41 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 653 QGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGSVAYVPQEAWVQNTSVVENVCFRQELDL---PWLQEVLEacal 729
Cdd:PRK13409 364 EGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQYIKPDYDGTVEDLLRSITDDLgssYYKSEIIK---- 439
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13591916 730 gsdvasfPAGVHtPVGEQGMN-LSGGQKQRLSLARAVYRRAAVYLMDDPLAALDahVSQEV 789
Cdd:PRK13409 440 -------PLQLE-RLLDKNVKdLSGGELQRVAIAACLSRDADLYLLDEPSAHLD--VEQRL 490
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1280-1460 |
6.65e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 43.23 E-value: 6.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQE-----ATEGGIWIDG----VPITDMglHTLRSRITIIPQDPVL 1350
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGhniySPRTDT--VDLRKEIGMVFQQPNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1351 FPGS--------LRMN-------LDLLQENTDEG--IWaalETVQLKAFVTSLpgqlqyecsgqgdDLSVGQKQLLCLAR 1413
Cdd:PRK14239 98 FPMSiyenvvygLRLKgikdkqvLDEAVEKSLKGasIW---DEVKDRLHDSAL-------------GLSGGQQQRVCIAR 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 13591916 1414 ALLRKTQILILDEATASVDPGTEIQMQAALERWFAQCTVLLIAHRLR 1460
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQ 208
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
644-824 |
6.89e-04 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 43.18 E-value: 6.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGS--VAYVPQEAWVQNTSVVENVCF-------RQE 714
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlrIGYVPQKLYLDTTLPLTVNRFlrlrpgtKKE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 715 LDLPWLQEVLEACALgsdvasfpagvhtpvgEQGMN-LSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHvSQEVFKQV 793
Cdd:PRK09544 100 DILPALKRVQAGHLI----------------DAPMQkLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVN-GQVALYDL 162
|
170 180 190
....*....|....*....|....*....|..
gi 13591916 794 IGPSGLLQGTTRILVTHTLH-VLPQADQILVL 824
Cdd:PRK09544 163 IDQLRRELDCAVLMVSHDLHlVMAKTDEVLCL 194
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1280-1487 |
7.35e-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: 44.02 E-value: 7.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQ--EATEGGI-----------WID-----GVPITDMG-------- 1333
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgYVErpskvGEPCPVCGgtlepeev 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1334 ---------LHTLRSRITIIPQDPVLFPGSLRMnLDLLQENTDEGIWAALETVQLKAFVTSLPgQLQYECSGQGDDLSVG 1404
Cdd:TIGR03269 95 dfwnlsdklRRRIRKRIAIMLQRTFALYGDDTV-LDNVLEALEEIGYEGKEAVGRAVDLIEMV-QLSHRITHIARDLSGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1405 QKQLLCLARALLRKTQILILDEATASVDPGTEIQMQAALERWFAQ--CTVLLIAHRLRSVMNCA-RVLVMDEGQVAESGS 1481
Cdd:TIGR03269 173 EKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsgISMVLTSHWPEVIEDLSdKAIWLENGEIKEEGT 252
|
....*.
gi 13591916 1482 PAQLLA 1487
Cdd:TIGR03269 253 PDEVVA 258
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
752-860 |
7.78e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 43.56 E-value: 7.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 752 SGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKqvigpsgLLQ------GTTRILVTHTLHVLPQ-ADQILVL 824
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMT-------LLNelkrefNTAIIMITHDLGVVAGiCDKVLVM 235
|
90 100 110
....*....|....*....|....*....|....*...
gi 13591916 825 ANGTIAEMGSYQDLLHR--NGALVGLLDGARQPAGEGE 860
Cdd:PRK09473 236 YAGRTMEYGNARDVFYQpsHPYSIGLLNAVPRLDAEGE 273
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1282-1382 |
8.16e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 42.48 E-value: 8.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1282 QGVSLKIHAGEKVGIVGRTGAGKSSLtwglLR----LQEATEGGIWIDGVPItdmglHTLRSRitiiPQDPVLFPG---- 1353
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSL----LRilagLARPDAGEVLWQGEPI-----RRQRDE----YHQDLLYLGhqpg 84
|
90 100 110
....*....|....*....|....*....|....*...
gi 13591916 1354 ---------SLRMNLDLLQENTDEGIWAALETVQLKAF 1382
Cdd:PRK13538 85 ikteltaleNLRFYQRLHGPGDDEALWEALAQVGLAGF 122
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
971-1142 |
8.19e-04 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 43.27 E-value: 8.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 971 ADDPVVDGKQMHSALRgSIFGLLGCLQAIGLFASMAAVFLGG-------ARASCLLFRSLLwdvaRSPIGFFERTPVGNL 1043
Cdd:cd18573 26 ASKESGDIEIFGLSLK-TFALALLGVFVVGAAANFGRVYLLRiagerivARLRKRLFKSIL----RQDAAFFDKNKTGEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1044 LNRFSKETDIV----DVDIPDKMRTLLTYAFGlleVGLAVSMATPLAIV--AILPLMLLYAGFQSLYVatccqlRRL--- 1114
Cdd:cd18573 101 VSRLSSDTSVVgkslTQNLSDGLRSLVSGVGG---IGMMLYISPKLTLVmlLVVPPIAVGAVFYGRYV------RKLskq 171
|
170 180 190
....*....|....*....|....*....|
gi 13591916 1115 --ESASYSSVCShlAETFQGSQVVRAFQAQ 1142
Cdd:cd18573 172 vqDALADATKVA--EERLSNIRTVRAFAAE 199
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1283-1486 |
8.78e-04 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 43.88 E-value: 8.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1283 GVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEA---TEGGIWIDGVPItdmGLHTLRSRITIIPQDPVLFP------- 1352
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI---DAKEMRAISAYVQQDDLFIPtltvreh 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1353 ----GSLRMNLDLLQENTDEGIWAALETVQLKAFVTSLPGQlqyecSGQGDDLSVGQKQLLCLARALLRKTQILILDEAT 1428
Cdd:TIGR00955 120 lmfqAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGV-----PGRVKGLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13591916 1429 ASVDPGTEIQMQAALERwFAQC--TVLLIAHRLRSVMNCA--RVLVMDEGQVAESGSPAQLL 1486
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKG-LAQKgkTIICTIHQPSSELFELfdKIILMAEGRVAYLGSPDQAV 255
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1270-1490 |
9.52e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.96 E-value: 9.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1270 GLRHRPELPMAVQGVSLKIHAGEKVGIVGRTGAGKSSLTwGLL----RLQEateGGIWIDGvpiTDMGLHTLRS----RI 1341
Cdd:NF033858 6 GVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLL-SLIagarKIQQ---GRVEVLG---GDMADARHRRavcpRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1342 TIIPQD------PVLfpgSLRMNLD----LLQENTDEG---IWAALETVQLKAFVTSLPGQLqyecSGqgddlsvGQKQl 1408
Cdd:NF033858 79 AYMPQGlgknlyPTL---SVFENLDffgrLFGQDAAERrrrIDELLRATGLAPFADRPAGKL----SG-------GMKQ- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1409 lclarallrKT----------QILILDEATASVDPgteiqmqaaLER---WfaqctvLLIAhRLR------SV------M 1463
Cdd:NF033858 144 ---------KLglccalihdpDLLILDEPTTGVDP---------LSRrqfW------ELID-RIRaerpgmSVlvatayM 198
|
250 260 270
....*....|....*....|....*....|.
gi 13591916 1464 NCA----RVLVMDEGQVAESGSPAQLLAQKG 1490
Cdd:NF033858 199 EEAerfdWLVAMDAGRVLATGTPAELLARTG 229
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
978-1235 |
9.89e-04 |
|
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: 42.88 E-value: 9.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 978 GKQMHSALRGSIFGLLGCLQAIGLFASMAAVFLG---GARAS----CLLFRSLLwdvaRSPIGFFERTPVGNLLNRFSKE 1050
Cdd:cd18563 34 GPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLarlGERITadlrRDLYEHLQ----RLSLSFFDKRQTGSLMSRVTSD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1051 TD-----IVDVdIPDKMRTLLTYafglleVGLAV---SMATPLAIVAILPLMLLYAGFQSLYVatccQLRRL---ESASY 1119
Cdd:cd18563 110 TDrlqdfLSDG-LPDFLTNILMI------IGIGVvlfSLNWKLALLVLIPVPLVVWGSYFFWK----KIRRLfhrQWRRW 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1120 SSVCSHLAETFQGSQVVRAF----QAQGPFTAQHDALMDENQRISfpRLVADRWLAANLeLLGNGLVFV--AATCAVLSk 1193
Cdd:cd18563 179 SRLNSVLNDTLPGIRVVKAFgqekREIKRFDEANQELLDANIRAE--KLWATFFPLLTF-LTSLGTLIVwyFGGRQVLS- 254
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 13591916 1194 AHLSAG-LAGFsVSAALQVTQTLQWVVRSWTDLENSMVAVERV 1235
Cdd:cd18563 255 GTMTLGtLVAF-LSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
740-830 |
9.94e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 43.36 E-value: 9.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 740 VHTPVGEQG-MNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFkQVIgpSGLL-QGTTRILVTHTL-HVLP 816
Cdd:PRK11288 385 IKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIY-NVI--YELAaQGVAVLFVSSDLpEVLG 461
|
90
....*....|....
gi 13591916 817 QADQILVLANGTIA 830
Cdd:PRK11288 462 VADRIVVMREGRIA 475
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
751-840 |
1.09e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 43.54 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 751 LSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEV------FKQVIGpSGLLqgttriLVTHTLHVLPQ-ADQILV 823
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQIlqllreLQQELN-MGLL------FITHNLSIVRKlADRVAV 229
|
90
....*....|....*..
gi 13591916 824 LANGTIAEMGSYQDLLH 840
Cdd:PRK15134 230 MQNGRCVEQNRAATLFS 246
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
746-828 |
1.12e-03 |
|
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: 41.54 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 746 EQGMN-LSGGQKQRLSLARAVYRRA--AVYLMDDPLAALDAHVSQ---EVFKQVIGpsgllQGTTRILVTHTLHVLPQAD 819
Cdd:cd03238 82 GQKLStLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINqllEVIKGLID-----LGNTVILIEHNLDVLSSAD 156
|
....*....
gi 13591916 820 QILVLANGT 828
Cdd:cd03238 157 WIIDFGPGS 165
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
750-842 |
1.16e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 43.42 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 750 NLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEvFKQVIGPsgLLQ--GTTRILVTHTLHVLPQADQILVLANG 827
Cdd:PRK10522 449 KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRRE-FYQVLLP--LLQemGKTIFAISHDDHYFIHADRLLEMRNG 525
|
90
....*....|....*.
gi 13591916 828 TIAEM-GSYQDLLHRN 842
Cdd:PRK10522 526 QLSELtGEERDAASRD 541
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
1001-1139 |
1.18e-03 |
|
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: 42.53 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1001 LFASMAAVFLGGARASCL--------------LFRSLLwdvaRSPIGFFERTPVGNLLNRFSKETDIVDVDIPDKMRTLL 1066
Cdd:cd18572 43 LLLSVLSGLFSGLRGGCFsyagtrlvrrlrrdLFRSLL----RQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1067 TYAFGLleVGLAVSMAT---PLAIVA--ILPLMLL----YAGFQSlyvatccQLRRLESASYSSVCSHLAETFQGSQVVR 1137
Cdd:cd18572 119 RNLVQL--VGGLAFMFSlswRLTLLAfiTVPVIALitkvYGRYYR-------KLSKEIQDALAEANQVAEEALSNIRTVR 189
|
..
gi 13591916 1138 AF 1139
Cdd:cd18572 190 SF 191
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
644-844 |
1.26e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 42.79 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKssllsallgellkvEGSVSIEGS---------VAYVPQE-AWVQNTSVVENVCF-- 711
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKtttiriilgilapdSGEVLWDGEpldpedrrrIGYLPEErGLYPKMKVGEQLVYla 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 712 ------RQELDlPWLQEVLEACALGsDVAsfpagvHTPVGEqgmnLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAhV 785
Cdd:COG4152 97 rlkglsKAEAK-RRADEWLERLGLG-DRA------NKKVEE----LSKGNQQKVQLIAALLHDPELLILDEPFSGLDP-V 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13591916 786 SQEVFKQVIgpsglL----QGTTRILVTHTL-HV--LpqADQILVLANGTIAEMGSYQDLLHRNGA 844
Cdd:COG4152 164 NVELLKDVI-----RelaaKGTTVIFSSHQMeLVeeL--CDRIVIINKGRKVLSGSVDEIRRQFGR 222
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
644-839 |
1.27e-03 |
|
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: 42.38 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKssllsallgellkvegS--VSIEGsvAYVPQeawvqntsvvenvCFRQELDL---- 717
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGK----------------StlLSLIT--GDLPP-------------TYGNDVRLfger 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 718 -----------------PWLQEVLEACALGSDV------ASFpaGVHTPVGEQ------------GM---------NLSG 753
Cdd:COG1119 68 rggedvwelrkriglvsPALQLRFPRDETVLDVvlsgffDSI--GLYREPTDEqrerarellellGLahladrpfgTLSQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 754 GQKQRLSLARAVYRRAAVYLMDDPLAALDAHvSQEVFKQVIgpSGLLQ--GTTRILVTHTLHVLPQA-DQILVLANGTIA 830
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLG-ARELLLALL--DKLAAegAPTLVLVTHHVEEIPPGiTHVLLLKDGRVV 222
|
....*....
gi 13591916 831 EMGSYQDLL 839
Cdd:COG1119 223 AAGPKEEVL 231
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
1029-1191 |
1.51e-03 |
|
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: 42.48 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1029 RSPIGFFERTPVGNLLNRFSkeTDIvdvdipDKMRTLLTYafGLleVGLAVSMATPLAIVAIL-----PLMLL-YAGFQS 1102
Cdd:cd18546 84 RLSLDFHERETSGRIMTRMT--SDI------DALSELLQT--GL--VQLVVSLLTLVGIAVVLlvldpRLALVaLAALPP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1103 LYVATCcQLRRLESASY-------SSVCSHLAETFQGSQVVRAFQAQGPFTAQHDALMDENQ--RISFPRLVAdrWLAAN 1173
Cdd:cd18546 152 LALATR-WFRRRSSRAYrrareriAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRdaRLRAQRLVA--IYFPG 228
|
170
....*....|....*...
gi 13591916 1174 LELLGNglvfvAATCAVL 1191
Cdd:cd18546 229 VELLGN-----LATAAVL 241
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1280-1480 |
1.59e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 42.85 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGlHTLRSR--ITIIPQD-PVLFPGSLR 1356
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD-HKLAAQlgIGIIYQElSVIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1357 MNLDLLQENTDE--GI----WAALetvQLKAFVTSLPGQLQYECSGQGDDLSVGQKQLLCLARALLRKTQILILDEATAS 1430
Cdd:PRK09700 99 ENLYIGRHLTKKvcGVniidWREM---RVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 13591916 1431 VDPGTEIQMQAALERWFAQCT-VLLIAHRLRSVMN-CARVLVMDEGQVAESG 1480
Cdd:PRK09700 176 LTNKEVDYLFLIMNQLRKEGTaIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
739-782 |
1.75e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 41.02 E-value: 1.75e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 13591916 739 GVHTPVGEQGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALD 782
Cdd:cd03222 60 GITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLD 103
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
337-540 |
1.89e-03 |
|
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: 42.07 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 337 MGDLESSAWTG--WLLAVLMFLSACLQTLFEQQYMYRVKvlqmRLRTAITGLVYRKVLVLSSGSRKSSAAGDVVNLVSVD 414
Cdd:cd18589 27 MNKDAPEAFTAaiTVMSLLTIASAVSEFVCDLIYNITMS----RIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 415 VQRLVESilhLNGLWLLFLWIIVCFVYL-----WQLLGPSALTAVAvflslLPLNFFITKKR-SFHQEEQMRQKASRARL 488
Cdd:cd18589 103 TEDMSES---LSENLSLLMWYLARGLFLfifmlWLSPKLALLTALG-----LPLLLLVPKFVgKFQQSLAVQVQKSLARA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 489 ------TSSMLRTVRTIKSHGWECA-FLERLlhirgQELGAL-KTSAFLFSVSLVSFQVS 540
Cdd:cd18589 175 nqvaveTFSAMKTVRSFANEEGEAQrYRQRL-----QKTYRLnKKEAAAYAVSMWTSSFS 229
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
751-828 |
2.30e-03 |
|
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: 40.12 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 751 LSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHvSQEVFKQvigpsGLL--QGTTrILVTHTLHVLPQ-ADQILVLANG 827
Cdd:cd03221 71 LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE-SIEALEE-----ALKeyPGTV-ILVSHDRYFLDQvATKIIELEDG 143
|
.
gi 13591916 828 T 828
Cdd:cd03221 144 K 144
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
951-1142 |
2.52e-03 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); 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: 350034 [Multi-domain] Cd Length: 289 Bit Score: 41.56 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 951 FLFL-----CQQVASFCQGYWLSlwaddpVVDGKQMHSALRGSIFGLlgCLQAIGlfASMAAVFLGG----------ARA 1015
Cdd:cd18590 2 FLFLtlaviCETFIPYYTGRVID------ILGGEYQHNAFTSAIGLM--CLFSLG--SSLSAGLRGGlfmctlsrlnLRL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1016 SCLLFRSLLwdvaRSPIGFFERTPVGNLLNRFSKETDIVDVDIPDKMRTLL---TYAFGLLevGLAVSMATPLAIVAILP 1092
Cdd:cd18590 72 RHQLFSSLV----QQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLrslVKTLGML--GFMLSLSWQLTLLTLIE 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 13591916 1093 lMLLYAGFQSLYVATCCQLRRLESASYSSVCSHLAETFQGSQVVRAFQAQ 1142
Cdd:cd18590 146 -MPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAE 194
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
657-789 |
2.60e-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: 42.08 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 657 LAVVGPVGAGKSSLLSALLGELLKVEGSVSIEGSVAYVPQ------EAWVQntSVVENVCfRQELDLPWLQ-EVLEacal 729
Cdd:COG1245 369 LGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQyispdyDGTVE--EFLRSAN-TDDFGSSYYKtEIIK---- 441
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13591916 730 gsdvasfPAGVHtPVGEQGM-NLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDahVSQEV 789
Cdd:COG1245 442 -------PLGLE-KLLDKNVkDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD--VEQRL 492
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
590-837 |
2.62e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 590 LVQARV-SFDRLAAflcLEEV--DPNGMVLSPSrcsSKDR-----ISIHNGTFAWSQeSPPCLHGINLTVPQGCLLAVVG 661
Cdd:PLN03073 470 LVQSRIkALDRLGH---VDAVvnDPDYKFEFPT---PDDRpgppiISFSDASFGYPG-GPLLFKNLNFGIDLDSRIAMVG 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 662 PVGAGKSSLLSALLGELLKVEGSV--SIEGSVAYVPQEAwVQNTSVVENVCFRQELDLPWLQEVLEACALGSdvasfpAG 739
Cdd:PLN03073 543 PNGIGKSTILKLISGELQPSSGTVfrSAKVRMAVFSQHH-VDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGS------FG 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 740 VHTPVGEQGM-NLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKQVIgpsgLLQGTTrILVTHTLHVLP-Q 817
Cdd:PLN03073 616 VTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLV----LFQGGV-LMVSHDEHLISgS 690
|
250 260
....*....|....*....|.
gi 13591916 818 ADQILVLANGTIAEM-GSYQD 837
Cdd:PLN03073 691 VDELWVVSEGKVTPFhGTFHD 711
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
1014-1235 |
3.56e-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: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1014 RASCLLFRSLLwdvaRSPIGFFERTPVGNLLNRFSKETDIVDVDIPDKMRTLLTYAFGLLEVGLAVSMATPLAIVAILpL 1093
Cdd:cd18566 76 RLSNAAFEHLL----SLPLSFFEREPSGAHLERLNSLEQIREFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLV-L 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1094 MLLYAGFqSLYVATccQLRRLESASY---SSVCSHLAETFQGSQVVRAFQAQGPFTAQHDALMDENQRISFPrlVADRWL 1170
Cdd:cd18566 151 LGLFVLV-AILLGP--ILRRALKERSradERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFK--VAKINA 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13591916 1171 AANlellGNGLVF-VAATCAVLS-------KAHLSAG-LAGFSVSAAlQVTQTLQWVVRSWTDLENSMVAVERV 1235
Cdd:cd18566 226 VAQ----TLGQLFsQVSMVAVVAfgallviNGDLTVGaLIACTMLSG-RVLQPLQRAFGLWTRFQQVRVAVRRL 294
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
647-829 |
4.47e-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: 41.35 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 647 INLTVPQGCLLAVVGPVGAGKSSLLSALLGELL-KVEGSV--------------SIEGSVAYVPQE----------AWVQ 701
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVfingkpvdirnpaqAIRAGIAMVPEDrkrhgivpilGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 702 NT--SVVENVCFRQELDlpwlqEVLEACALGSDVASFPAGVHTPVGEQGmNLSGGQKQRLSLARAVYRRAAVYLMDDPLA 779
Cdd:TIGR02633 359 NItlSVLKSFCFKMRID-----AAAELQIIGSAIQRLKVKTASPFLPIG-RLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 13591916 780 ALDAHVSQEVFKQVigpsGLL--QGTTRILVTHTL-HVLPQADQILVLANGTI 829
Cdd:TIGR02633 433 GVDVGAKYEIYKLI----NQLaqEGVAIIVVSSELaEVLGLSDRVLVIGEGKL 481
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
644-834 |
5.75e-03 |
|
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: 39.82 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 644 LHGINLTVPQGCLLAVVGPVGAGKssllsallGELLKV----EGSVSIEGSVAYVPQEawVQNTSVVEN------VCFRQ 713
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGK--------STLAKTimghPKYEVTEGEILFKGED--ITDLPPEERarlgifLAFQY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 714 ELDLPwlqevleacalGSDVASFPAGVhtpvgeqGMNLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAhVSQEVFKQV 793
Cdd:cd03217 86 PPEIP-----------GVKNADFLRYV-------NEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI-DALRLVAEV 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 13591916 794 IgpSGLL-QGTTRILVTHTLHVL--PQADQILVLANGTIAEMGS 834
Cdd:cd03217 147 I--NKLReEGKSVLIITHYQRLLdyIKPDRVHVLYDGRIVKSGD 188
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1280-1485 |
6.09e-03 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 40.38 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1280 AVQGVSLKIHAGEKVGIVGRTGAGKSSLTW---GLLRLQEATEGGIWIDGVPITDMG----------LHT--------LR 1338
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsGLITGDKSAGSHIELLGRTVQREGrlardirksrANTgyifqqfnLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1339 SRITIIPQDPVLFPGSL---RMNLDLLQENTDEGIWAALETVQLKAF----VTSLPGqlqyecsgqgddlsvGQKQLLCL 1411
Cdd:PRK09984 99 NRLSVLENVLIGALGSTpfwRTCFSWFTREQKQRALQALTRVGMVHFahqrVSTLSG---------------GQQQRVAI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13591916 1412 ARALLRKTQILILDEATASVDP-GTEIQMQAAleRWFAQ---CTVLLIAHRLRSVMN-CARVLVMDEGQVAESGSPAQL 1485
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPeSARIVMDTL--RDINQndgITVVVTLHQVDYALRyCERIVALRQGHVFYDGSSQQF 240
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
1019-1235 |
6.38e-03 |
|
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: 40.45 E-value: 6.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1019 LFRSLLwdvaRSPIGFFERTPVGNLLNRfsketdIV-DVdipDKMRTLLTYAF------GLLEVGLAVSMAT---PLAIV 1088
Cdd:cd18544 80 LFSHIQ----RLPLSFFDRTPVGRLVTR------VTnDT---EALNELFTSGLvtligdLLLLIGILIAMFLlnwRLALI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1089 --AILPLMLLyagFQSLYvatccqlRRLESASY-------SSVCSHLAETFQGSQVVRAFQAQGPFTAQHDALMDENQRI 1159
Cdd:cd18544 147 slLVLPLLLL---ATYLF-------RKKSRKAYrevreklSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1160 SFPRLVADRWLAANLELLGN---GLVFVAATCAVLSKAhLSAG-LAGFsVSAALQVTQTLQWVVRSWTDLENSMVAVERV 1235
Cdd:cd18544 217 NLKSIKLFALFRPLVELLSSlalALVLWYGGGQVLSGA-VTLGvLYAF-IQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
990-1148 |
6.80e-03 |
|
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: 40.14 E-value: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 990 FGLLGCLQA-IGLFASMAAVFLG---GARASCLLFRSLLwdvaRSPIGFFERTPVGNLLNRFSKETDIvdvdipdkmRTL 1065
Cdd:cd18567 48 FGLLLLLQAlLSALRSWLVLYLStslNLQWTSNLFRHLL----RLPLSYFEKRHLGDIVSRFGSLDEI---------QQT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1066 LTYAF------GLLEVGLAVSM---ATPLAIVAILpLMLLYAGFQSLYVAtccQLRRL--ESASYSSVC-SHLAETFQGS 1133
Cdd:cd18567 115 LTTGFvealldGLMAILTLVMMflySPKLALIVLA-AVALYALLRLALYP---PLRRAteEQIVASAKEqSHFLETIRGI 190
|
170
....*....|....*
gi 13591916 1134 QVVRAFQAQGPFTAQ 1148
Cdd:cd18567 191 QTIKLFGREAEREAR 205
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
751-857 |
7.19e-03 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 40.06 E-value: 7.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 751 LSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKQVigpSGLLQ--GTTRILVTHTLHVLPQ-ADQILVLANG 827
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLL---KKLQQqfGTACLFITHDLRLVERfCQRVMVMDNG 228
|
90 100 110
....*....|....*....|....*....|
gi 13591916 828 TIAEMgsyqdllhrngALVGLLDGARQPAG 857
Cdd:PRK10419 229 QIVET-----------QPVGDKLTFSSPAG 247
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
750-847 |
7.57e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 40.78 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 750 NLSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKqvigpsgLL-----QGTTRILVTHTLH-VLPQADQILV 823
Cdd:COG3845 141 DLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFE-------ILrrlaaEGKSIIFITHKLReVMAIADRVTV 213
|
90 100
....*....|....*....|....
gi 13591916 824 LangtiaemgsyqdllhRNGALVG 847
Cdd:COG3845 214 L----------------RRGKVVG 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
751-841 |
7.72e-03 |
|
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: 40.82 E-value: 7.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 751 LSGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKqvigpsgLLQ------GTTRILVTHTLHVLPQ-ADQILV 823
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILD-------LLKdlqrelGMALLLITHDLGVVRRfADRVAV 229
|
90
....*....|....*...
gi 13591916 824 LANGTIAEMGSYQDLLHR 841
Cdd:COG4172 230 MRQGEIVEQGPTAELFAA 247
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
752-833 |
8.97e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 39.91 E-value: 8.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 752 SGGQKQRLSLARAVYRRAAVYLMDDPLAALDAHVSQEVFKqvigpsgLLQGTTR------ILVTHTLHV---LpqADQIL 822
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLD-------LLRGLVRelglavVIVTHDLAVarlL--AHRLL 223
|
90
....*....|.
gi 13591916 823 VLANGTIAEMG 833
Cdd:PRK11701 224 VMKQGRVVESG 234
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1281-1487 |
9.08e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 40.37 E-value: 9.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1281 VQGVSLKIHAGEKVGIVGRTGAGKSSLTWGLLRLQEATEGGIWIDGVPITDMGLHT-LRSRITIIPQDP-----VLfpG- 1353
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGIVYISEDRkrdglVL--Gm 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13591916 1354 SLRMNLDL--LQENTDEGIW----AALETVQ--LKAFVTSLPGQLQyecsgQGDDLSVGQKQLLCLARALLRKTQILILD 1425
Cdd:PRK10762 346 SVKENMSLtaLRYFSRAGGSlkhaDEQQAVSdfIRLFNIKTPSMEQ-----AIGLLSGGNQQKVAIARGLMTRPKVLILD 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13591916 1426 EATASVDPGTEIQMQAALERWFAQ-CTVLLIAHRLRSVMNCA-RVLVMDEGQV-----AESGSPAQLLA 1487
Cdd:PRK10762 421 EPTRGVDVGAKKEIYQLINQFKAEgLSIILVSSEMPEVLGMSdRILVMHEGRIsgeftREQATQEKLMA 489
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