|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
277-1456 |
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: 668.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 277 ERMKTPSLFITIHKIFWrqilgmgvSSFMVSVC--------QFLSPIALNRLLKHLESPSSSSVNPLVWIVLLLTGPFLT 348
Cdd:TIGR00957 300 HKPRKPSLFKVLYKTFG--------PYFLMSFCfkaihdlmMFIGPQILSLLIRFVNDPMAPDWQGYFYTGLLFVCACLQ 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 349 SLFTQFYLFMSTRYLARSYTTLVQQIYNKVIRSRFVQNKSgdSKVGRSNNLISTDVDDIGEIREFIHIIVRAPVEIAGSI 428
Cdd:TIGR00957 372 TLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKS--STVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILAL 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 429 YLLQKLLGWSAYVGLALTVLTCSVPIVLGPLVAKLTLRANRATDSRIELMSELLQSIRITKFFGWELPMLDRVKQRRQVE 508
Cdd:TIGR00957 450 YFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEE 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 509 LNRTWKLLLMEICIQVLVESLPVFSMFATFVVFTTIMGQTITPS-IAFTSISLFSFIRTQFSWIAYLMRQIVQIFVSIGR 587
Cdd:TIGR00957 530 LKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENNILDAeKAFVSLALFNILRFPLNILPMVISSIVQASVSLKR 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 588 VSDFLN----DPDEVDPVNTIEDTSQEIGFFNASLTWVSNPSPgdfCLRDLNIVFPRNKLSIVIGPTGSGKSSLISALLG 663
Cdd:TIGR00957 610 LRIFLSheelEPDSIERRTIKPGEGNSITVHNATFTWARDLPP---TLNGITFSIPEGALVAVVGQVGCGKSSLLSALLA 686
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 664 ELSLNKGSYNLPRSkgVSYVSQVPWLRNATIRDNILFDYPYIEERYKKVIQACGLLTDLQSFVASDLTEIGEKGVTLSGG 743
Cdd:TIGR00957 687 EMDKVEGHVHMKGS--VAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGG 764
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 744 QKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKHCF-QSSLMENRTVILVTHNVHlFMDSAAFIVTVKNGSafpVT 822
Cdd:TIGR00957 765 QKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIgPEGVLKNKTRILVTHGIS-YLPQVDVIIVMSGGK---IS 840
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 823 DKSS--PLL--------FLAEQAAS----------ASEAAAPDLAAIPIPN----------------------------- 853
Cdd:TIGR00957 841 EMGSyqELLqrdgafaeFLRTYAPDeqqghledswTALVSGEGKEAKLIENgmlvtdvvgkqlqrqlsasssdsgdqsrh 920
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 854 -----EVDDAEAADEkDGKLVEEEQRVTGDVVFSEIFSYMKHFGSgFYVAAVLLFFVTTQATSILIDLWVAFWTNSSVNS 928
Cdd:TIGR00957 921 hgssaELQKAEAKEE-TWKLMEADKAQTGQVELSVYWDYMKAIGL-FITFLSIFLFVCNHVSALASNYWLSLWTDDPMVN 998
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 929 PDVNNNKF-LFVYGTMLLAYSLLDFLRTVSYDRGAWWASRKLHDSMLESVFGTFASWFDKTPTGRIVNRFAKDIRSIDMN 1007
Cdd:TIGR00957 999 GTQNNTSLrLSVYGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSM 1078
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1008 LSGWLFFSINCFLSVAGGILSVSSAMPIFMIpaVIVCLAGYYFGL--LYTRAQVGVKRLISIYTSPIFSLLGESIVGVSV 1085
Cdd:TIGR00957 1079 IPPVIKMFMGSLFNVIGALIVILLATPIAAV--IIPPLGLLYFFVqrFYVASSRQLKRLESVSRSPVYSHFNETLLGVSV 1156
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1086 IRAFNRQTIFKQMFSERLDNLVRLQSTSYNLNRWVAVRTDGISGLVGAIAGLIALLQK-DLSPGVVGFSLNQAVIFSSSV 1164
Cdd:TIGR00957 1157 IRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRhSLSAGLVGLSVSYSLQVTFYL 1236
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1165 LLFVRSCNSLQAEMNSYERVLEYSKLPQEPAPTIAGQVP-ATWPKEGDIVFNHVSVSYSAAGPTILKDVNLHINPSEKVA 1243
Cdd:TIGR00957 1237 NWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPpSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVG 1316
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1244 VVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRISFIPQDPILFSGTVRSNLDPFDELEDNFLNEALK 1323
Cdd:TIGR00957 1317 IVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALE 1396
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1324 TSGASSMIMAHTDDqkpihitLDTHVASEGSNFSQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFG 1403
Cdd:TIGR00957 1397 LAHLKTFVSALPDK-------LDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFE 1469
|
1210 1220 1230 1240 1250
....*....|....*....|....*....|....*....|....*....|...
gi 19115470 1404 DATMLCIAHRLKTIVDYDKVMVLDKGVLVEYGPPAVLYHNNGHFRRMCDGSGI 1456
Cdd:TIGR00957 1470 DCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSMAKDAGL 1522
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
205-1455 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 637.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 205 FIPLFTPRVWYPLF---PEDNYQ----PSAEQVC-----SMFNfACSYGYLNPLVLTAKRRVVEVDDTPVIPDYDKNKAW 272
Cdd:PLN03232 194 YIPELDPYPGYHILnneSLDNVEydalRGGENICperyaSIFS-RIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 273 TYRFERMKT-------PSLFITIHKIFWRQILGMGVSSFMVSVCQFLSPIALNRLLKHLESPSSSSVNpLVWIVLLLTGP 345
Cdd:PLN03232 273 IKRFQRCWTeesrrpkPWLLRALNNSLGGRFWLGGIFKIGHDLSQFVGPVILSHLLQSMQEGDPAWVG-YVYAFLIFFGV 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 346 FLTSLFTQFYLFMSTRYLARSYTTLVQQIYNKVIRSRFVQNKSGDSkvGRSNNLISTDVDDIGEIREFIHIIVRAPVEIA 425
Cdd:PLN03232 352 TFGVLCESQYFQNVGRVGFRLRSTLVAAIFHKSLRLTHEARKNFAS--GKVTNMITTDANALQQIAEQLHGLWSAPFRII 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 426 GSIYLLQKLLGWSAYVGLALTVLTCSVPIVLGPLVAKLTLRANRATDSRIELMSELLQSIRITKFFGWELPMLDRVKQRR 505
Cdd:PLN03232 430 VSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIR 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 506 QVELNRTWKLLLMEICIQVLVESLPVFSMFATFVVFTtIMGQTITPSIAFTSISLFSFIRTQFSWIAYLMRQIVQIFVSI 585
Cdd:PLN03232 510 NEELSWFRKAQLLSAFNSFILNSIPVVVTLVSFGVFV-LLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSL 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 586 GRVSD-FLNDPDEVDPVNTIEDTSQEIGFFNASLTW---VSNPSpgdfcLRDLNIVFPRNKLSIVIGPTGSGKSSLISAL 661
Cdd:PLN03232 589 QRIEElLLSEERILAQNPPLQPGAPAISIKNGYFSWdskTSKPT-----LSDINLEIPVGSLVAIVGGTGEGKTSLISAM 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 662 LGELSLNKGSYNLPRSKgVSYVSQVPWLRNATIRDNILFDYPYIEERYKKVIQACGLLTDLQSFVASDLTEIGEKGVTLS 741
Cdd:PLN03232 664 LGELSHAETSSVVIRGS-VAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNIS 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 742 GGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKHCFQSSLmENRTVILVTHNVHlFMDSAAFIVTVKNG----- 816
Cdd:PLN03232 743 GGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDEL-KGKTRVLVTNQLH-FLPLMDRIILVSEGmikee 820
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 817 SAFPVTDKSSPLL--------FLAEQAASASEAAAPDLAAIPIPNEVDDAEAADEKDGK-----LVEEEQRVTGDVVFSE 883
Cdd:PLN03232 821 GTFAELSKSGSLFkklmenagKMDATQEVNTNDENILKLGPTVTIDVSERNLGSTKQGKrgrsvLVKQEERETGIISWNV 900
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 884 IFSYMKHFGSGFYVAAVLLFFVTTQATSILIDLWVAFWTNSSvNSPDVNNNKFLFVYGtmLLAYSLLdflrTVSYDRGAW 963
Cdd:PLN03232 901 LMRYNKAVGGLWVVMILLVCYLTTEVLRVSSSTWLSIWTDQS-TPKSYSPGFYIVVYA--LLGFGQV----AVTFTNSFW 973
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 964 W------ASRKLHDSMLESVFGTFASWFDKTPTGRIVNRFAKDIRSIDMNLSGwlffSINCFLSVAGGILS-------VS 1030
Cdd:PLN03232 974 LissslhAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVAN----LMNMFMNQLWQLLStfaligtVS 1049
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1031 SAMPIFMIPAVIVCLAGYyfgLLYTRAQVGVKRLISIYTSPIFSLLGESIVGVSVIRAFNRQTIFKQMFSERLDNLVRLQ 1110
Cdd:PLN03232 1050 TISLWAIMPLLILFYAAY---LYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFT 1126
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1111 STSYNLNRWVAVRTDGISGLVGAIAGLIALLQKDLSPGVVGFSLNQAVIFS---------SSVLlfvRSCNSLQAEMNSY 1181
Cdd:PLN03232 1127 LANTSSNRWLTIRLETLGGVMIWLTATFAVLRNGNAENQAGFASTMGLLLSytlnittllSGVL---RQASKAENSLNSV 1203
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1182 ERVLEYSKLPQEPAPTIAGQVP-ATWPKEGDIVFNHVSVSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLL 1260
Cdd:PLN03232 1204 ERVGNYIDLPSEATAIIENNRPvSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALF 1283
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1261 RFTHRISGEIYINGRETQSVNLNALRQRISFIPQDPILFSGTVRSNLDPFDELEDNFLNEALKTSGASSMImahtdDQKP 1340
Cdd:PLN03232 1284 RIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVI-----DRNP 1358
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1341 ihITLDTHVASEGSNFSQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAHRLKTIVDY 1420
Cdd:PLN03232 1359 --FGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDC 1436
|
1290 1300 1310
....*....|....*....|....*....|....*.
gi 19115470 1421 DKVMVLDKGVLVEYGPPAVLYHNNGH-FRRMCDGSG 1455
Cdd:PLN03232 1437 DKILVLSSGQVLEYDSPQELLSRDTSaFFRMVHSTG 1472
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
189-1455 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 630.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 189 YSPFLWFYFfitivgnfiPLFTPRVWY-PLFPED----NYQ--PSAEQVC-----SMFNFACsYGYLNPLVLTAKRRVVE 256
Cdd:PLN03130 187 FGILLLVYF---------PNLDPYPGYtPIGSESvddyEYEelPGGEQICperhaNIFSRIF-FGWMTPLMQLGYKRPLT 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 257 VDDTPVIPDYDK--------NKAWTYRFERMKtPSLFITIHKIFWRQILGMGVSSFMVSVCQFLSPIALNRLLKHLESPS 328
Cdd:PLN03130 257 EKDVWKLDTWDQtetlyrsfQKCWDEELKKPK-PWLLRALNNSLGGRFWLGGFFKIGNDLSQFVGPLLLNLLLESMQNGE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 329 SssvnplVWI-----VLLLTGPFLTSLFTQFYL--FMSTRYLARSytTLVQQIYNKVIRSRFVQNKSGDSkvGRSNNLIS 401
Cdd:PLN03130 336 P------AWIgyiyaFSIFVGVVLGVLCEAQYFqnVMRVGFRLRS--TLVAAVFRKSLRLTHEGRKKFTS--GKITNLMT 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 402 TDVDDIGEIREFIHIIVRAPVEIAGSIYLLQKLLGWSAYVGLALTVLTCSVPIVLGPLVAKLTLRANRATDSRIELMSEL 481
Cdd:PLN03130 406 TDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEV 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 482 LQSIRITKFFGWELPMLDRVKQRRQVELNRTWKLLLMEICIQVLVESLPVFSMFATFVVFTtIMGQTITPSIAFTSISLF 561
Cdd:PLN03130 486 LAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSFILNSIPVLVTVVSFGVFT-LLGGDLTPARAFTSLSLF 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 562 SFIRTQFSWIAYLMRQIVQIFVSIGRVSD-FLNDPDEVDPVNTIEDTSQEIGFFNASLTWVS-NPSPgdfCLRDLNIVFP 639
Cdd:PLN03130 565 AVLRFPLFMLPNLITQAVNANVSLKRLEElLLAEERVLLPNPPLEPGLPAISIKNGYFSWDSkAERP---TLSNINLDVP 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 640 RNKLSIVIGPTGSGKSSLISALLGELSLNKGSYNLPRSKgVSYVSQVPWLRNATIRDNILFDYPYIEERYKKVIQACGLL 719
Cdd:PLN03130 642 VGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGT-VAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQ 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 720 TDLQSFVASDLTEIGEKGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKHCFQSSLmENRTVILVTHN 799
Cdd:PLN03130 721 HDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDEL-RGKTRVLVTNQ 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 800 VHlFMDSAAFIV-----TVKNGSAFPVTDKSSPLL--------FLAEQAASASEAAAPDLAAIPIPNEV------DDAEA 860
Cdd:PLN03130 800 LH-FLSQVDRIIlvhegMIKEEGTYEELSNNGPLFqklmenagKMEEYVEENGEEEDDQTSSKPVANGNannlkkDSSSK 878
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 861 ADEKDGK--LVEEEQRVTGDVVFSEIFSYMKHFGSGFYVAAVLLFFVTTQATSILIDLWVAFWTNSSVNSPdvnnnkflf 938
Cdd:PLN03130 879 KKSKEGKsvLIKQEERETGVVSWKVLERYKNALGGAWVVMILFLCYVLTEVFRVSSSTWLSEWTDQGTPKT--------- 949
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 939 vYGTM--LLAYSLLDFLRTVSYDRGAWW-------ASRKLHDSMLESVFGTFASWFDKTPTGRIVNRFAKDIRSIDMNLS 1009
Cdd:PLN03130 950 -HGPLfyNLIYALLSFGQVLVTLLNSYWlimsslyAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVA 1028
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1010 GWlffsINCFLSVAGGILS------VSSAMPIFmipAVIVCLAGYYFGLLYTRAQV-GVKRLISIYTSPIFSLLGESIVG 1082
Cdd:PLN03130 1029 VF----VNMFLGQIFQLLStfvligIVSTISLW---AIMPLLVLFYGAYLYYQSTArEVKRLDSITRSPVYAQFGEALNG 1101
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1083 VSVIRAFNRQTIFKQMFSERLDNLVRLQSTSYNLNRWVAVRTDGISGLVGAIAGLIALLQKDLSPGVVGF---------- 1152
Cdd:PLN03130 1102 LSTIRAYKAYDRMAEINGRSMDNNIRFTLVNMSSNRWLAIRLETLGGLMIWLTASFAVMQNGRAENQAAFastmglllsy 1181
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1153 SLNQAVIFSSSVLLFVRSCNSLqaemNSYERVLEYSKLPQEPAPTIAG-QVPATWPKEGDIVFNHVSVSYSAAGPTILKD 1231
Cdd:PLN03130 1182 ALNITSLLTAVLRLASLAENSL----NAVERVGTYIDLPSEAPLVIENnRPPPGWPSSGSIKFEDVVLRYRPELPPVLHG 1257
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1232 VNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRISFIPQDPILFSGTVRSNLDPFD 1311
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFN 1337
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1312 ELEDNFLNEALKTsgassmimAHTDDQ-KPIHITLDTHVASEGSNFSQGQKQVLALARAIVRRSKIIILDECTASVDDAM 1390
Cdd:PLN03130 1338 EHNDADLWESLER--------AHLKDViRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRT 1409
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115470 1391 DQKIQKTLREAFGDATMLCIAHRLKTIVDYDKVMVLDKGVLVEYGPPAVLYHN-NGHFRRMCDGSG 1455
Cdd:PLN03130 1410 DALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNeGSAFSKMVQSTG 1475
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
208-1455 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 628.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 208 LFTPRvwyplfpEDNYQPSAEQVCSMfnfacsygylnpLVLTAKRRVVEVDDTPVIPdydknkawtyRFERMKTpsLFIT 287
Cdd:PTZ00243 193 LFTPE-------QSNMSTLEEPTDVR------------LYLSSTGSVVRPGPPPTPK----------RLSLLRT--LFAA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 288 IHKIFWRQILGMGVSSfmvsVCQFLSPIALNRLLKHLESPSSSsvnpLVWIVLLLTGPFLTSLF----TQFYLFMSTRYL 363
Cdd:PTZ00243 242 LPYYVWWQIPFKLLSD----VCTLTLPVLLKYFVKFLDADNAT----WGRGLGLVLTLFLTQLIqsvcLHRFYYISIRCG 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 364 ARSYTTLVQQIYNKV--IRSRFVQNKsgDSKVGRSNNLISTDVDDIGEIREFIHIIVRAPVEIAGSIYLLQKLLGWSAYV 441
Cdd:PTZ00243 314 LQYRSALNALIFEKCftISSKSLAQP--DMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWCALM 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 442 GLALTVLTcsvpIVLGPLVAKLTLRANR----ATDSRIELMSELLQSIRITKFFGWELPMLDRVKQRRQVELNRTWKLLL 517
Cdd:PTZ00243 392 AVAVLLVT----LPLNGAIMKHQMAARRkiakAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQL 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 518 MEICIQVLVESLPVFSMFATFVVFTtIMGQTITPSIAFTSISLFSFIRTQFSWIAYLMRQIVQIFVSIGRVSDFLNDPDE 597
Cdd:PTZ00243 468 ARVATSFVNNATPTLMIAVVFTVYY-LLGHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTFLECDNA 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 598 VdpVNTIEDTSQEIG--------------FFNASLT-----------------------WV---------SNPSP----- 626
Cdd:PTZ00243 547 T--CSTVQDMEEYWReqrehstacqlaavLENVDVTafvpvklprapkvktsllsralrMLcceqcrptkRHPSPsvvve 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 627 ----------------------------------------GDF-------CLRDLNIVFPRNKLSIVIGPTGSGKSSLIS 659
Cdd:PTZ00243 625 dtdygspssasrhiveggtgggheatptsersaktpkmktDDFfelepkvLLRDVSVSVPRGKLTVVLGATGSGKSTLLQ 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 660 ALLGELSLNKGSYNLPRSkgVSYVSQVPWLRNATIRDNILFDYPYIEERYKKVIQACGLLTDLQSFVASDLTEIGEKGVT 739
Cdd:PTZ00243 705 SLLSQFEISEGRVWAERS--IAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVN 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 740 LSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKHCFQSSLmENRTVILVTHNVHLfMDSAAFIVTVKNG--- 816
Cdd:PTZ00243 783 LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGAL-AGKTRVLATHQVHV-VPRADYVVALGDGrve 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 817 -----SAFPVTD----------KSSPLLFLAEQAASASEAAAPDLAAIPIPNEV--------DDAEAADEKDGKLVEEEQ 873
Cdd:PTZ00243 861 fsgssADFMRTSlyatlaaelkENKDSKEGDADAEVAEVDAAPGGAVDHEPPVAkqegnaegGDGAALDAAAGRLMTREE 940
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 874 RVTGDVVFSEIFSYMKHFGSGFYVAAVLLFFVTTQATSILIDLWVAFWtnsSVNSPDVNNNKFLFVYGTMLLAYSLLDFL 953
Cdd:PTZ00243 941 KASGSVPWSTYVAYLRFCGGLHAAGFVLATFAVTELVTVSSGVWLSMW---STRSFKLSAATYLYVYLGIVLLGTFSVPL 1017
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 954 R-TVSYD---RGawwaSRKLHDSMLESVFGTFASWFDKTPTGRIVNRFAKDIRSIDMNLSGWLFFSINCFLSVAGGILSV 1029
Cdd:PTZ00243 1018 RfFLSYEamrRG----SRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVT 1093
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1030 SSAMPiFMIPAVIVCLAGYY-FGLLYTRAQVGVKRLISIYTSPIFSLLGESIVGVSVIRAFNRQTIFKQMFSERLDnLVR 1108
Cdd:PTZ00243 1094 SASQP-FVLVALVPCGYLYYrLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQEALRRLD-VVY 1171
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1109 LQSTSYNL-NRWVAVRTDGISGLVGAIAGLIALLQKDL-----SPGVVGFSLNQAVIFSSSVLLFVRSCNSLQAEMNSYE 1182
Cdd:PTZ00243 1172 SCSYLENVaNRWLGVRVEFLSNIVVTVIALIGVIGTMLratsqEIGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVE 1251
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1183 RVLEYS-KLPQEPAPT-----------------IAGQV---PATWP-------KEGDIVFNHVSVSYSAAGPTILKDVNL 1234
Cdd:PTZ00243 1252 RLLYYTdEVPHEDMPEldeevdalerrtgmaadVTGTVviePASPTsaaphpvQAGSLVFEGVQMRYREGLPLVLRGVSF 1331
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1235 HINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRISFIPQDPILFSGTVRSNLDPFDELE 1314
Cdd:PTZ00243 1332 RIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEAS 1411
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1315 DNFLNEALKTSGASSMIMAHTDDqkpihitLDTHVASEGSNFSQGQKQVLALARAIVRR-SKIIILDECTASVDDAMDQK 1393
Cdd:PTZ00243 1412 SAEVWAALELVGLRERVASESEG-------IDSRVLEGGSNYSVGQRQLMCMARALLKKgSGFILMDEATANIDPALDRQ 1484
|
1370 1380 1390 1400 1410 1420
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19115470 1394 IQKTLREAFGDATMLCIAHRLKTIVDYDKVMVLDKGVLVEYGPPAVLYHN-NGHFRRMCDGSG 1455
Cdd:PTZ00243 1485 IQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNrQSIFHSMVEALG 1547
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
240-1449 |
7.25e-108 |
|
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: 376.17 E-value: 7.25e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 240 YGYLNPLVLTAKRRVVEVDDTPVIPDYDKNKAWTYRFER---------MKTPSLFITIHKIFWRQILGMGVSSFMVSVCQ 310
Cdd:TIGR01271 17 FWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLERewdrelasaKKNPKLLNALRRCFFWRFVFYGILLYFGEATK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 311 FLSPIALNRLLKHLESPSSSSVNPLVWIVLLLTGPFLT-SLFTQFYLFMSTRYLARSYTTLVQQIYNKVIR--SRFVQNK 387
Cdd:TIGR01271 97 AVQPLLLGRIIASYDPFNAPEREIAYYLALGLCLLFIVrTLLLHPAIFGLHHLGMQMRIALFSLIYKKTLKlsSRVLDKI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 388 SgdskVGRSNNLISTDVDDIGEIREFIHIIVRAPVEIAGSIYLLQKLLGWSAYVGLALTVLTCSVPIVLGPLVAKLtlRA 467
Cdd:TIGR01271 177 S----TGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQACLGQKMMPY--RD 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 468 NRA--TDSRIELMSELLQSIRITKFFGWELPMLDRVKQRRQVELNRTWKLLLmeicIQVLVESLPVFSMFatFVVFTTIM 545
Cdd:TIGR01271 251 KRAgkISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAY----LRYFYSSAFFFSGF--FVVFLSVV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 546 GQTITPSIA----FTSISLFSFIRT----QFSWIaylMRQIVQIFVSIGRVSDFLNDpdevDPVNTIED--TSQEIGFFN 615
Cdd:TIGR01271 325 PYALIKGIIlrriFTTISYCIVLRMtvtrQFPGA---IQTWYDSLGAITKIQDFLCK----EEYKTLEYnlTTTEVEMVN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 616 ASLTW-------------------VSNPSPGDF----------CLRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELS 666
Cdd:TIGR01271 398 VTASWdegigelfekikqnnkarkQPNGDDGLFfsnfslyvtpVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 667 LNKGsyNLPRSKGVSYVSQVPWLRNATIRDNILFDYPYIEERYKKVIQACGLLTDLQSFVASDLTEIGEKGVTLSGGQKQ 746
Cdd:TIGR01271 478 PSEG--KIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRA 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 747 RIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKHCFqSSLMENRTVILVT---------------HNVH---------- 801
Cdd:TIGR01271 556 RISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCL-CKLMSNKTRILVTsklehlkkadkilllHEGVcyfygtfsel 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 802 ---------LFMDSAAF----------IVT-------------------------------------------------- 812
Cdd:TIGR01271 635 qakrpdfssLLLGLEAFdnfsaerrnsILTetlrrvsidgdstvfsgpetikqsfkqpppefaekrkqsiilnpiasark 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 813 ----------------------------------------------VKNGSAFPVTDKSSPLLFL--------------- 831
Cdd:TIGR01271 715 fsfvqmgpqkaqattiedavrepserkfslvpedeqgeeslprgnqYHHGLQHQAQRRQSVLQLMthsnrgenrreqlqt 794
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 832 -----AEQAASASEAAAPDLAAIPIPNE--VDDAEAADEKDGK--LVEEEQRVTGDVVFSEIFSYMKHFGSGFYVAAVLL 902
Cdd:TIGR01271 795 sfrkkSSITQQNELASELDIYSRRLSKDsvYEISEEINEEDLKecFADERENVFETTTWNTYLRYITTNRNLVFVLIFCL 874
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 903 FFVTTQATSILIDLWV----AFWTNSSVN------SPDVNNNKFL---------FVYGTMLLAYSLLDFLRTVSYDRGAW 963
Cdd:TIGR01271 875 VIFLAEVAASLLGLWLitdnPSAPNYVDQqhanasSPDVQKPVIItptsayyifYIYVGTADSVLALGFFRGLPLVHTLL 954
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 964 WASRKLHDSMLESVFGTFASWFDKTPTGRIVNRFAKDIRSIDMNLSGWLFFSINCFLSVAGGILSVSSAMPIFMIPAVIV 1043
Cdd:TIGR01271 955 TVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPV 1034
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1044 CLAGYYFGLLYTRAQVGVKRLISIYTSPIFSLLGESIVGVSVIRAFNRQTIFKQMFSERLDNLVRLQSTSYNLNRWVAVR 1123
Cdd:TIGR01271 1035 AVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMR 1114
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1124 TDGISGLVGAIAGLIALLQKDLSPGVVGFSLNQAVIFSSSVLLFVRSCNSLQAEMNSYERVLEYSKLPQE-PAPTIAG-- 1200
Cdd:TIGR01271 1115 IDIIFVFFFIAVTFIAIGTNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEePRPSGGGgk 1194
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1201 ------------QVPATWPKEGDIVFNHVSVSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHrISG 1268
Cdd:TIGR01271 1195 yqlstvlvienpHAQKCWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEG 1273
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1269 EIYINGRETQSVNLNALRQRISFIPQDPILFSGTVRSNLDPFDELEDNFLNEALKTSGASSMIMAHTDdqkpihiTLDTH 1348
Cdd:TIGR01271 1274 EIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPD-------KLDFV 1346
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1349 VASEGSNFSQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAHRLKTIVDYDKVMVLDK 1428
Cdd:TIGR01271 1347 LVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEG 1426
|
1450 1460
....*....|....*....|.
gi 19115470 1429 GVLVEYGPPAVLYHNNGHFRR 1449
Cdd:TIGR01271 1427 SSVKQYDSIQKLLNETSLFKQ 1447
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1210-1437 |
1.53e-106 |
|
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: 337.16 E-value: 1.53e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1210 GDIVFNHVSVSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRI 1289
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1290 SFIPQDPILFSGTVRSNLDPFDELEDNFLNEALKTSGASSMIMAHTDdqkpihiTLDTHVASEGSNFSQGQKQVLALARA 1369
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPG-------GLDTVVEEGGENLSVGQRQLLCLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19115470 1370 IVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAHRLKTIVDYDKVMVLDKGVLVEYGPP 1437
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
611-817 |
2.54e-106 |
|
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: 335.98 E-value: 2.54e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 611 IGFFNASLTWVSNPSPGDFCLRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYNLPRSkgVSYVSQVPWLR 690
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--IAYVSQEPWIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 691 NATIRDNILFDYPYIEERYKKVIQACGLLTDLQSFVASDLTEIGEKGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSAL 770
Cdd:cd03250 79 NGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 19115470 771 DIHTSNWIYKHCFQSSLMENRTVILVTHNVHLFMDsAAFIVTVKNGS 817
Cdd:cd03250 159 DAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
897-1188 |
1.70e-100 |
|
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: 323.65 E-value: 1.70e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 897 VAAVLLFFVTTQATSILIDLWVAFWTNSS-----VNSPDVNNNKFLFVYGTMLLAYSLLDFLRTVSYDRGAWWASRKLHD 971
Cdd:cd18604 1 WALLLLLFVLSQLLSVGQSWWLGIWASAYetssaLPPSEVSVLYYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 972 SMLESVFGTFASWFDKTPTGRIVNRFAKDIRSIDMNLSGWLFFSINCFLSVAGGILSVSSAMPIFMIPAVIVCLAGYYFG 1051
Cdd:cd18604 81 RLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1052 LLYTRAQVGVKRLISIYTSPIFSLLGESIVGVSVIRAFNRQTIFKQMFSERLDNLVRLQSTSYNLNRWVAVRTDGISGLV 1131
Cdd:cd18604 161 RLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 19115470 1132 GAIAGLIALLQKDLSPGVVGFSLNQAVIFSSSVLLFVRSCNSLQAEMNSYERVLEYS 1188
Cdd:cd18604 241 SFATAALLVYGPGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
880-1450 |
1.02e-98 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 329.05 E-value: 1.02e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 880 VFSEIFSYMKHFGSGFYVAAVLLFFVTtqATSILIDLWVAFWTNSSVNSPDVNN-NKFLFVYGTMLLAYSLLDFLRTVSY 958
Cdd:COG1132 8 LLRRLLRYLRPYRGLLILALLLLLLSA--LLELLLPLLLGRIIDALLAGGDLSAlLLLLLLLLGLALLRALLSYLQRYLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 959 DRGAWWASRKLHDSMLESVFGTFASWFDKTPTGRIVNRFAKDIRSIDMNLSGWLFFSINCFLSVAGGILSVSSAMPIFMI 1038
Cdd:COG1132 86 ARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1039 PAVIVCLAGYYFGLLYTRAQVGVKRLISIYTSPIFSLLGESIVGVSVIRAFNRQTIFKQMFSERLDNLVRLQSTSYNLNR 1118
Cdd:COG1132 166 IVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1119 WVAVRTDGISGLVGAI---AGLIALLQKDLSPGVVGFSLNQAVIFSSSVLLFVRSCNSLQAEMNSYERVLEYSKLPQEPA 1195
Cdd:COG1132 246 LFFPLMELLGNLGLALvllVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1196 PTiAGQVPATwPKEGDIVFNHVSVSYsAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGR 1275
Cdd:COG1132 326 DP-PGAVPLP-PVRGEIEFENVSFSY-PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1276 ETQSVNLNALRQRISFIPQDPILFSGTVRSNL---DP---FDELEdnflnEALKTSGASSMIMAHTDDqkpihitLDTHV 1349
Cdd:COG1132 403 DIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRPdatDEEVE-----EAAKAAQAHEFIEALPDG-------YDTVV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1350 ASEGSNFSQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAHRLKTIVDYDKVMVLDKG 1429
Cdd:COG1132 471 GERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDG 550
|
570 580
....*....|....*....|.
gi 19115470 1430 VLVEYGPPAVLYHNNGHFRRM 1450
Cdd:COG1132 551 RIVEQGTHEELLARGGLYARL 571
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
299-588 |
3.53e-93 |
|
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: 303.65 E-value: 3.53e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 299 MGVSSFMVSVCQFLSPIALNRLLKHLESPSSSS-VNPLVWIVLLLTGPFLTSLFTQFYLFMSTRYLARSYTTLVQQIYNK 377
Cdd:cd18596 2 QALLAVLSSVLSFAPPFFLNRLLRYLEDPGEDAtVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 378 VIRSRFV-----------------QNKSGDSKVGRSNNLISTDVDDIGEIREFIHIIVRAPVEIAGSIYLLQKLLGWSAY 440
Cdd:cd18596 82 ALRRRDKsgssksseskkkdkeedEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 441 VGLALTVLTCSVPIVLGPLVAKLTLRANRATDSRIELMSELLQSIRITKFFGWELPMLDRVKQRRQVELNRTWKLLLMEI 520
Cdd:cd18596 162 VGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLDL 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19115470 521 CIQVLVESLPVFSMFATFVVFTTIMGQTITPSIAFTSISLFSFIRTQFSWIAYLMRQIVQIFVSIGRV 588
Cdd:cd18596 242 LLSLLWFLIPILVTVVTFATYTLVMGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
943-1450 |
4.91e-83 |
|
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: 288.66 E-value: 4.91e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 943 MLLAYSLLDFLRTVSYDRgawwASRKLHDSMLESVFGTF----ASWFDKTPTGRIVNRFaKDIRSIDMNLSGWLF-FSIN 1017
Cdd:COG2274 205 ALLFEGLLRLLRSYLLLR----LGQRIDLRLSSRFFRHLlrlpLSFFESRSVGDLASRF-RDVESIREFLTGSLLtALLD 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1018 CFLSVAGGILSVSSAMPIFMIPAVIVCLAGYYFGLLYTRAQVGVKRLISIYTSpIFSLLGESIVGVSVIRAFNRQTIFKQ 1097
Cdd:COG2274 280 LLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAK-RQSLLVETLRGIETIKALGAESRFRR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1098 MFSERLDNLVRLQSTSYNLNRWVAVRTDGISGLVGA---IAGLIALLQKDLSPG-VVGFslnQAVI--FSSSVLLFVRSC 1171
Cdd:COG2274 359 RWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVallWLGAYLVIDGQLTLGqLIAF---NILSgrFLAPVAQLIGLL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1172 NSLQAEMNSYERVLEYSKLPQEPAPTIAGQVPAtwPKEGDIVFNHVSVSYSAAGPTILKDVNLHINPSEKVAVVGRTGSG 1251
Cdd:COG2274 436 QRFQDAKIALERLDDILDLPPEREEGRSKLSLP--RLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSG 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1252 KSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRISFIPQDPILFSGTVRSNL---DPFDELEDnfLNEALKTSGAS 1328
Cdd:COG2274 514 KSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItlgDPDATDEE--IIEAARLAGLH 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1329 SMIMAHTDDqkpihitLDTHVASEGSNFSQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDATML 1408
Cdd:COG2274 592 DFIEALPMG-------YDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVI 664
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 19115470 1409 CIAHRLKTIVDYDKVMVLDKGVLVEYGPPAVLYHNNGHFRRM 1450
Cdd:COG2274 665 IIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1206-1437 |
1.21e-80 |
|
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: 263.89 E-value: 1.21e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1206 WPKEGDIVFNHVSVSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNAL 1285
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1286 RQRISFIPQDPILFSGTVRSNLDPFDELEDNFLNEALKtsgassmimahtddqkpihitldthVASEGSNFSQGQKQVLA 1365
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR-------------------------VSEGGLNLSQGQRQLLC 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19115470 1366 LARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAHRLKTIVDYDKVMVLDKGVLVEYGPP 1437
Cdd:cd03369 136 LARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
897-1188 |
4.76e-72 |
|
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: 242.79 E-value: 4.76e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 897 VAAVLLFFVTTQATSILIDLWVAFWTNSSVNSPDVNNNKFLFVYGTMLLAYS-LLDFLRTVSYDRGAWWASRKLHDSMLE 975
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASvLLVLLRWLLFVLAGLRASRRLHDKLLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 976 SVFGTFASWFDKTPTGRIVNRFAKDIRSIDMNLSGWLFFSINCFLSVAGGILSVSSAMPIFMIPAVIVCLAGYYFGLLYT 1055
Cdd:cd18580 81 SVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1056 RAQVGVKRLISIYTSPIFSLLGESIVGVSVIRAFNRQTIFKQMFSERLDNLVRLQSTSYNLNRWVAVRTDGISGLVGAIA 1135
Cdd:cd18580 161 RTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALLALVV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 19115470 1136 GLIALLQKD-LSPGVVGFSLNQAVIFSSSVLLFVRSCNSLQAEMNSYERVLEYS 1188
Cdd:cd18580 241 ALLAVLLRSsISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
990-1452 |
1.17e-71 |
|
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: 251.22 E-value: 1.17e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 990 TGRIVNRFAKDIRSIDmNL----------SGWLFFSINCFLSVaggiLSVSSAMPIFMIPAVIVCLAGYYFGLLYTRAQV 1059
Cdd:COG4987 111 SGDLLNRLVADVDALD-NLylrvllpllvALLVILAAVAFLAF----FSPALALVLALGLLLAGLLLPLLAARLGRRAGR 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1060 GVKRLISIYTSpifsLLGESIVGVSVIRAFNRQTIFKQMFSERLDNLVRLQSTSYNLNRWvavrTDGISGLVGAIAGLIA 1139
Cdd:COG4987 186 RLAAARAALRA----RLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSAL----AQALLQLAAGLAVVAV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1140 LLQkdLSPGVVGFSLNQAVIfssSVLLFV------------RSCNSLQAEMNSYERVLEyskLPQEPAPTIAGQVPATWP 1207
Cdd:COG4987 258 LWL--AAPLVAAGALSGPLL---ALLVLAalalfealaplpAAAQHLGRVRAAARRLNE---LLDAPPAVTEPAEPAPAP 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1208 KEGDIVFNHVSVSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQ 1287
Cdd:COG4987 330 GGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRR 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1288 RISFIPQDPILFSGTVRSNL---DPfdELEDNFLNEALKTSGASSMIMAHTDDqkpihitLDTHVASEGSNFSQGQKQVL 1364
Cdd:COG4987 410 RIAVVPQRPHLFDTTLRENLrlaRP--DATDEELWAALERVGLGDWLAALPDG-------LDTWLGEGGRRLSGGERRRL 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1365 ALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAHRLKTIVDYDKVMVLDKGVLVEYGPPAVLYHNN 1444
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQN 560
|
....*...
gi 19115470 1445 GHFRRMCD 1452
Cdd:COG4987 561 GRYRQLYQ 568
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1210-1445 |
3.42e-68 |
|
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: 229.42 E-value: 3.42e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1210 GDIVFNHVSVSYSAAGPTiLKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRI 1289
Cdd:cd03254 1 GEIEFENVNFSYDEKKPV-LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1290 SFIPQDPILFSGTVRSNLDPFDEL-EDNFLNEALKTSGASSMIMAHTDDqkpihitLDTHVASEGSNFSQGQKQVLALAR 1368
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNaTDEEVIEAAKEAGAHDFIMKLPNG-------YDTVLGENGGNLSQGERQLLAIAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19115470 1369 AIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAHRLKTIVDYDKVMVLDKGVLVEYGPPAVLYHNNG 1445
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1178-1445 |
2.49e-65 |
|
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: 232.73 E-value: 2.49e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1178 MNSYERVLEYskLPQEPAPTIAGQVPATWPKEGDIVFNHVSVSYsAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGL 1257
Cdd:COG4988 305 IAAAEKIFAL--LDAPEPAAPAGTAPLPAAGPPSIELEDVSFSY-PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLN 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1258 TLLRFTHRISGEIYINGRETQSVNLNALRQRISFIPQDPILFSGTVRSNL-----DPFDELednfLNEALKTSGASSMIM 1332
Cdd:COG4988 382 LLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLrlgrpDASDEE----LEAALEAAGLDEFVA 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1333 AHTDDqkpihitLDTHVASEGSNFSQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAH 1412
Cdd:COG4988 458 ALPDG-------LDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITH 530
|
250 260 270
....*....|....*....|....*....|...
gi 19115470 1413 RLKTIVDYDKVMVLDKGVLVEYGPPAVLYHNNG 1445
Cdd:COG4988 531 RLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
300-588 |
2.25e-64 |
|
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: 220.82 E-value: 2.25e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 300 GVSSFMVSVCQFLSPIALNRLLKHLESPSSSSVNP-LVWIVLLLTGPFLTSLFTQFYLFMSTRYLARSYTTLVQQIYNKV 378
Cdd:cd18579 3 GLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPLSEgYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 379 IRSRfvQNKSGDSKVGRSNNLISTDVDDIGEIREFIHIIVRAPVEIAGSIYLLQKLLGWSAYVGLALTVLTCSVPIVLGP 458
Cdd:cd18579 83 LRLS--SSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 459 LVAKLTLRANRATDSRIELMSELLQSIRITKFFGWELPMLDRVKQRRQVELNRTWKLLLMEICIQVLVESLPVFSMFATF 538
Cdd:cd18579 161 LISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 19115470 539 VVFtTIMGQTITPSIAFTSISLFSFIRTQFSWIAYLMRQIVQIFVSIGRV 588
Cdd:cd18579 241 ATY-VLLGNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1212-1429 |
3.19e-60 |
|
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: 204.15 E-value: 3.19e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRISF 1291
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1292 IPQDPILFSGTVRSNLdpfdelednflnealktsgassmimahtddqkpihitldthvasegsnFSQGQKQVLALARAIV 1371
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------------LSGGQRQRIAIARALL 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 19115470 1372 RRSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAHRLKTIVDYDKVMVLDKG 1429
Cdd:cd03228 113 RDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
900-1188 |
1.99e-59 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350047 [Multi-domain] Cd Length: 296 Bit Score: 206.56 E-value: 1.99e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 900 VLLFFVTTQATSILIDLWVAFWTNSSVNSPDVNNNK---FLFVYGTMLLAYSLLDFLRTVSYDRGAWWASRKLHDSMLES 976
Cdd:cd18603 4 ILLLYLLSQAFSVGSNIWLSEWSDDPALNGTQDTEQrdyRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHNKLLHN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 977 VFGTFASWFDKTPTGRIVNRFAKDIRSIDMNLSGWLFFSINCFLSVAGGILSVSSAMPIFMipAVIVCLAGYYFGL--LY 1054
Cdd:cd18603 84 ILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFL--VVIIPLAILYFFIqrFY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1055 TRAQVGVKRLISIYTSPIFSLLGESIVGVSVIRAFNRQTIFKQMFSERLDNLVRLQSTSYNLNRWVAVRTDGISGLVGAI 1134
Cdd:cd18603 162 VATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLIVLF 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 19115470 1135 AGLIALLQKD-LSPGVVGFSLNQAVIFSSSVLLFVRSCNSLQAEMNSYERVLEYS 1188
Cdd:cd18603 242 AALFAVLSRDsLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEYS 296
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1210-1447 |
1.80e-58 |
|
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: 202.45 E-value: 1.80e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1210 GDIVFNHVSVSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRI 1289
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1290 SFIPQDPILFSGTVRSNLDPFDELEDNFLNEALKTSGASSMImahtddqKPIHITLDTHVASEGSNFSQGQKQVLALARA 1369
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMV-------KSLPGGLDAVVTEGGENFSVGQRQLFCLARA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19115470 1370 IVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAHRLKTIVDYDKVMVLDKGVLVEY-GPPAVLYHNNGHF 1447
Cdd:cd03288 171 FVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECdTPENLLAQEDGVF 249
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
897-1187 |
9.43e-57 |
|
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: 199.29 E-value: 9.43e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 897 VAAVLLFFVTTQATSILIDLWVAFWTNSSVNSPDVNNN----KFLFVYGTMLLAYSLLDFLRTVSYDRGAWWASRKLHDS 972
Cdd:cd18605 1 LILILLSLILMQASRNLIDFWLSYWVSHSNNSFFNFINdsfnFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 973 MLESVFGTFASWFDKTPTGRIVNRFAKDIRSIDMNLSgwlfFSINCFL----SVAGGILSVSSAMPIFMIPAVIVCLAGY 1048
Cdd:cd18605 81 LLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLP----FILNILLaqlfGLLGYLVVICYQLPWLLLLLLPLAFIYY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1049 YFGLLYTRAQVGVKRLISIYTSPIFSLLGESIVGVSVIRAFNRQTIFKQMFSERLDNLVRLQSTSYNLNRWVAVRTDGIS 1128
Cdd:cd18605 157 RIQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLG 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19115470 1129 GLVGAIAGLIALLQ----KDLSPGVVGFSLNQAVIFSSSVLLFVRSCNSLQAEMNSYERVLEY 1187
Cdd:cd18605 237 VLIVTFVALTAVVQhffgLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQY 299
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1212-1450 |
5.71e-56 |
|
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: 194.68 E-value: 5.71e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSY-SAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRIS 1290
Cdd:cd03249 1 IEFKNVSFRYpSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1291 FIPQDPILFSGTVRSNL-----DPFDELEDnflnEALKTSGASSMIMAHTDdqkpihiTLDTHVASEGSNFSQGQKQVLA 1365
Cdd:cd03249 81 LVSQEPVLFDGTIAENIrygkpDATDEEVE----EAAKKANIHDFIMSLPD-------GYDTLVGERGSQLSGGQKQRIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1366 LARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAHRLKTIVDYDKVMVLDKGVLVEYGPPAVLYHNNG 1445
Cdd:cd03249 150 IARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKG 229
|
....*
gi 19115470 1446 HFRRM 1450
Cdd:cd03249 230 VYAKL 234
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
881-1450 |
2.79e-55 |
|
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: 203.41 E-value: 2.79e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 881 FSEIFSYMKHFGSGFYVAAVLLFFVTtqATSILIDLWVAFWTNSSVNSPDVNNNKF--LFVYGTMLLAySLLDFLRTVSY 958
Cdd:TIGR02203 2 FRRLWSYVRPYKAGLVLAGVAMILVA--ATESTLAALLKPLLDDGFGGRDRSVLWWvpLVVIGLAVLR-GICSFVSTYLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 959 DRGAWWASRKLHDSMLESVFGTFASWFDKTPTGRIVNRFAKDIRSIDMNLSGWLFFSINCFLSVAGGI-----LSVSSAM 1033
Cdd:TIGR02203 79 SWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFivllyYSWQLTL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1034 PIFMIPAVIVCLAGYYfgllyTRAQVGVKRLISIYTSPIFSLLGESIVGVSVIRAFNRQTIFKQMFsERLDNLVRLQSTS 1113
Cdd:TIGR02203 159 IVVVMLPVLSILMRRV-----SKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRF-DAVSNRNRRLAMK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1114 ynlnrwvAVRTDGISG----LVGAIAgLIALLQKDLSPGVVG-FSLNQAVIFSSSVLLFVRSCNSL-------QAEMNSY 1181
Cdd:TIGR02203 233 -------MTSAGSISSpitqLIASLA-LAVVLFIALFQAQAGsLTAGDFTAFITAMIALIRPLKSLtnvnapmQRGLAAA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1182 ERVLEYSKLPQEPAptiAGQVPATwPKEGDIVFNHVSVSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLR 1261
Cdd:TIGR02203 305 ESLFTLLDSPPEKD---TGTRAIE-RARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1262 FTHRISGEIYINGRETQSVNLNALRQRISFIPQDPILFSGTVRSNL---DPfDELEDNFLNEALKTSGASSMImahtdDQ 1338
Cdd:TIGR02203 381 FYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRT-EQADRAEIERALAAAYAQDFV-----DK 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1339 KPIhiTLDTHVASEGSNFSQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAHRLKTIV 1418
Cdd:TIGR02203 455 LPL--GLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIE 532
|
570 580 590
....*....|....*....|....*....|..
gi 19115470 1419 DYDKVMVLDKGVLVEYGPPAVLYHNNGHFRRM 1450
Cdd:TIGR02203 533 KADRIVVMDDGRIVERGTHNELLARNGLYAQL 564
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1212-1450 |
5.06e-55 |
|
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: 191.67 E-value: 5.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAAGPtILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRISF 1291
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1292 IPQDPILFSGTVRSN-----LDPFDELednfLNEALKTSGASSMIMAHTDdqkpihiTLDTHVASEGSNFSQGQKQVLAL 1366
Cdd:cd03253 80 VPQDTVLFNDTIGYNirygrPDATDEE----VIEAAKAAQIHDKIMRFPD-------GYDTIVGERGLKLSGGEKQRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1367 ARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAHRLKTIVDYDKVMVLDKGVLVEYGPPAVLYHNNGH 1446
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGL 228
|
....
gi 19115470 1447 FRRM 1450
Cdd:cd03253 229 YAEM 232
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1212-1451 |
5.60e-55 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 191.68 E-value: 5.60e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRISF 1291
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1292 IPQDPILFSGTVRSNL---DPFDELEDnfLNEALKTSGASSMIMaHTDDQkpihitLDTHVASEGSNFSQGQKQVLALAR 1368
Cdd:cd03251 81 VSQDVFLFNDTVAENIaygRPGATREE--VEEAARAANAHEFIM-ELPEG------YDTVIGERGVKLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1369 AIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAHRLKTIVDYDKVMVLDKGVLVEYGPPAVLYHNNGHFR 1448
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYA 231
|
...
gi 19115470 1449 RMC 1451
Cdd:cd03251 232 KLH 234
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
292-798 |
1.27e-53 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 198.47 E-value: 1.27e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 292 FWRQILGMGVSSFMVSVCQFLSPIALNRLL-KHLESPSSSSVNPLVWIVLLLTgpFLTSLFTQFYLFMSTRYLARSYTTL 370
Cdd:COG1132 19 YRGLLILALLLLLLSALLELLLPLLLGRIIdALLAGGDLSALLLLLLLLLGLA--LLRALLSYLQRYLLARLAQRVVADL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 371 VQQIYNKVIR---SRFVQNKSGDskvgrsnnLISTDVDDIGEIREFIH----IIVRAPVEIAGSIYLLQKLLGWSAYVGL 443
Cdd:COG1132 97 RRDLFEHLLRlplSFFDRRRTGD--------LLSRLTNDVDAVEQFLAhglpQLVRSVVTLIGALVVLFVIDWRLALIVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 444 ALTVLTCSVPIVLGPLVAKLTLRANRATDSRIELMSELLQSIRITKFFGWELPMLDRVKQRRQVELNRTWKLLLMEICIQ 523
Cdd:COG1132 169 LVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 524 VLVESLPVFSMFATFVVFTT-IMGQTITPSIAFTSISLFSFIRTQFSWIAYLMRQIVQIFVSIGRVSDFLNDPDEV-DPV 601
Cdd:COG1132 249 PLMELLGNLGLALVLLVGGLlVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIpDPP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 602 NTIE--DTSQEIGFFNASLTWvsnpSPGDFCLRDLNIVFPRN-KLSIViGPTGSGKSSLISALLGELSLNKGS------- 671
Cdd:COG1132 329 GAVPlpPVRGEIEFENVSFSY----PGDRPVLKDISLTIPPGeTVALV-GPSGSGKSTLVNLLLRFYDPTSGRilidgvd 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 672 ---YNLP--RSKgVSYVSQVPWLRNATIRDNILFDYPYIEEryKKVIQACGLlTDLQSFVAS-----DlTEIGEKGVTLS 741
Cdd:COG1132 404 irdLTLEslRRQ-IGVVPQDTFLFSGTIRENIRYGRPDATD--EEVEEAAKA-AQAHEFIEAlpdgyD-TVVGERGVNLS 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 19115470 742 GGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKHCfqSSLMENRTVILVTH 798
Cdd:COG1132 479 GGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEAL--ERLMKGRTTIVIAH 533
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
983-1450 |
8.75e-53 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 196.48 E-value: 8.75e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 983 SWFDKTPTGRIVNRFAKD---IRSIDMNLSGWLFFS---INCFLsVAGGILSVSSAMPIFMI-PAVIVCLagyyfgLLYT 1055
Cdd:PRK10790 114 SAFDTQPVGQLISRVTNDtevIRDLYVTVVATVLRSaalIGAML-VAMFSLDWRMALVAIMIfPAVLVVM------VIYQ 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1056 RAQVGVKRLISIYTSPIFSLLGESIVGVSVIRAFNRQtifkQMFSERLdnlvRLQSTSYNLNRWVAVRTDGI-------- 1127
Cdd:PRK10790 187 RYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQ----ARFGERM----GEASRSHYMARMQTLRLDGFllrpllsl 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1128 -SGLVgaIAGLiaLLQKDLSP-GVVGFSLNQAVIFS----SSVLLFVRSCNS-LQAEMNSYERVLEYSKLPQEpaptiaG 1200
Cdd:PRK10790 259 fSALI--LCGL--LMLFGFSAsGTIEVGVLYAFISYlgrlNEPLIELTTQQSmLQQAVVAGERVFELMDGPRQ------Q 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1201 QVPATWP-KEGDIVFNHVSVSYSAAGPtILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQS 1279
Cdd:PRK10790 329 YGNDDRPlQSGRIDIDNVSFAYRDDNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSS 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1280 VNLNALRQRISFIPQDPILFSGTVRSNLDPFDELEDNFLNEALKTSGASSMIMAHTDDqkpihitLDTHVASEGSNFSQG 1359
Cdd:PRK10790 408 LSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDG-------LYTPLGEQGNNLSVG 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1360 QKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAHRLKTIVDYDKVMVLDKGVLVEYGPPAV 1439
Cdd:PRK10790 481 QKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQ 560
|
490
....*....|.
gi 19115470 1440 LYHNNGHFRRM 1450
Cdd:PRK10790 561 LLAAQGRYWQM 571
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
897-1188 |
2.55e-52 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 186.14 E-value: 2.55e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 897 VAAVLLFFVTTQATSILIDLWVAFWTNssvNSPDVNNNKFLFVYGTMLLAYSLLDFLRTVSYDRGAWWASRKLHDSMLES 976
Cdd:cd18606 1 LPLLLLLLILSQFAQVFTNLWLSFWTE---DFFGLSQGFYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 977 VFGTFASWFDKTPTGRIVNRFAKDIRSIDMNLSGWLFFSINCFLSVAGGILSVSSAMPIFMIPAVIVCLAGYYFGLLYTR 1056
Cdd:cd18606 78 VLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1057 AQVGVKRLISIYTSPIFSLLGESIVGVSVIRAFNRQTIFKQMFSERLDNLVRLQSTSYNLNRWVAVRTDGISGLVGAIAG 1136
Cdd:cd18606 158 SSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLLVLIVA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 19115470 1137 LIALLQK-DLSPGVVGFSLNQAVIFSSSVLLFVRSCNSLQAEMNSYERVLEYS 1188
Cdd:cd18606 238 LLCVTRRfSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHYA 290
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
612-817 |
4.36e-50 |
|
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: 176.75 E-value: 4.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 612 GFFnaslTWVSNPSpgdfCLRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKG----SYNLPRSKG-------- 679
Cdd:cd03290 6 GYF----SWGSGLA----TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGkvhwSNKNESEPSfeatrsrn 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 680 ---VSYVSQVPWLRNATIRDNILFDYPYIEERYKKVIQACGLLTDLQSFVASDLTEIGEKGVTLSGGQKQRIALARAVYS 756
Cdd:cd03290 78 rysVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115470 757 PTSIVLMDDVFSALDIHTSNwiykHCFQSSLME-----NRTVILVTHNVHlFMDSAAFIVTVKNGS 817
Cdd:cd03290 158 NTNIVFLDDPFSALDIHLSD----HLMQEGILKflqddKRTLVLVTHKLQ-YLPHADWIIAMKDGS 218
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
894-1188 |
7.26e-48 |
|
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: 173.90 E-value: 7.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 894 GFYVA-AVLLFFVTTQATSILIDLWVAFW------------TNSSVNSPDVNNN----KFLFVYGTMLLAYSLLDFLRTV 956
Cdd:cd18599 1 GYVVFlFVLLLFILSVGSTVFSDWWLSYWlkqgsgnttnnvDNSTVDSGNISDNpdlnFYQLVYGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 957 SYDRGAWWASRKLHDSMLESVFGTFASWFDKTPTGRIVNRFAKDIRSIDMNLSgwlfFSINCFL----SVAGGILSVSSA 1032
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLP----FTLENFLqnvlLVVFSLIIIAIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1033 MPIFMIPAVIVCLAGYYFGLLYTRAQVGVKRLISIYTSPIFSLLGESIVGVSVIRAFNRQTIFKQMFSERLDNLVRLQST 1112
Cdd:cd18599 157 FPWFLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19115470 1113 SYNLNRWVAVRTDGIS-GLVGAIAGLIALLQKDLSPGVVGFSLNQAVIFSSSVLLFVRSCNSLQAEMNSYERVLEYS 1188
Cdd:cd18599 237 FNCAMRWLAVRLDILAvLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1210-1432 |
1.47e-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: 169.69 E-value: 1.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1210 GDIVFNHVSVSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRI 1289
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1290 SFIPQDPILFSGTVRSNLDPFD-ELEDNFLNEALKTSGASSMIMAHTDDqkpihitLDTHVASEGSNFSQGQKQVLALAR 1368
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGApLADDERILRAAELAGVTDFVNKHPNG-------LDLQIGERGRGLSGGQRQAVALAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115470 1369 AIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAHRLKTIVDYDKVMVLDKGVLV 1432
Cdd:cd03245 154 ALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1190-1450 |
9.78e-47 |
|
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: 178.48 E-value: 9.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1190 LPQEPAPTIAGQVPATWPKEGDIVFNHVSVSYSAAGPtILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGE 1269
Cdd:COG5265 336 LDQPPEVADAPDAPPLVVGGGEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1270 IYINGRETQSVNLNALRQRISFIPQDPILFSGTVRSNL---DP---FDELEdnflnEALKtsgassmiMAHTDDqkpiHI 1343
Cdd:COG5265 415 ILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIaygRPdasEEEVE-----AAAR--------AAQIHD----FI 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1344 T-----LDTHVASEGSNFSQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAHRLKTIV 1418
Cdd:COG5265 478 EslpdgYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIV 557
|
250 260 270
....*....|....*....|....*....|..
gi 19115470 1419 DYDKVMVLDKGVLVEYGPPAVLYHNNGHFRRM 1450
Cdd:COG5265 558 DADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
304-587 |
5.73e-46 |
|
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: 167.65 E-value: 5.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 304 FMVSVCQFLSPIALNRLLKHLESPSSSSVNPLVWIVLLLTGPFLTSLFTQFYLFMSTRYLARSYTTLVQQIYNKVIR-SR 382
Cdd:cd18595 7 LLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRKALRlSN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 383 FVQNKSGdskVGRSNNLISTDVDDIGEIREFIHIIVRAPVEIAGSIYLLQKLLGWSAYVGLALTVLTCSVPIVLGPLVAK 462
Cdd:cd18595 87 SARKKST---VGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARKIKK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 463 LTLRANRATDSRIELMSELLQSIRITKFFGWELPMLDRVKQRRQVELNRTWKLLLMEICIQVLVESLPVFSMFATFVVFT 542
Cdd:cd18595 164 LQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFATYV 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 19115470 543 TIMG-QTITPSIAFTSISLFSFIRTQFSWIAYLMRQIVQIFVSIGR 587
Cdd:cd18595 244 LSDPdNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKR 289
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1212-1450 |
6.64e-46 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 165.74 E-value: 6.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRISF 1291
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1292 IPQDPILFSGTVRSNL---DPFDELEDnfLNEALKTSGASSMIMahtddQKPihITLDTHVASEGSNFSQGQKQVLALAR 1368
Cdd:cd03252 81 VLQENVLFNRSIRDNIalaDPGMSMER--VIEAAKLAGAHDFIS-----ELP--EGYDTIVGEQGAGLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1369 AIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAHRLKTIVDYDKVMVLDKGVLVEYGPPAVLYHNNGHFR 1448
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYA 231
|
..
gi 19115470 1449 RM 1450
Cdd:cd03252 232 YL 233
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
300-588 |
1.04e-44 |
|
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: 164.16 E-value: 1.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 300 GVSSFMVSVCQFLSPIALNRLLKHLESPSSSSVNPLVW--------IVLLLtgpFLTSLFTQFYLFMSTRYLARSYTTLV 371
Cdd:cd18597 3 GLLKLLADVLQVLSPLLLKYLINFVEDAYLGGPPPSIGygigyaigLFLLQ---LLSSLLLNHFFYRSMLTGAQVRAALT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 372 QQIYNKVIRsrfvqnKSGDSKVGRSN----NLISTDVDDIGEIREFIHIIVRAPVEIAGSIYLLQKLLGWSAYVGLALTV 447
Cdd:cd18597 80 KAIYRKSLR------LSGKSRHEFPNgkitNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 448 LTCSVPIVLGPLVAKLTLRANRATDSRIELMSELLQSIRITKFFGWELPMLDRVKQRRQVELNRTWKLLLMEICIQVLVE 527
Cdd:cd18597 154 LSIPLQGFLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAF 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19115470 528 SLPVFSMFATFVVFTTImGQTITPSIAFTSISLFSFIRTQFSWIAYLMRQIVQIFVSIGRV 588
Cdd:cd18597 234 SLPVLASMLSFITYYAT-GHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
867-1450 |
1.04e-44 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 174.14 E-value: 1.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 867 KLVEEEQRVTGDVVFsEIFSYMKHFGSGFYVAAVLLFFVTTQATSI------LIDlwvafWTNSSVNSPDVNNNkfLFVY 940
Cdd:TIGR00958 136 KEAEQGQSETADLLF-RLLGLSGRDWPWLISAFVFLTLSSLGEMFIpfytgrVID-----TLGGDKGPPALASA--IFFM 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 941 GTMLLAYSLLDFLRTVSYDRGAWWASRKLHDSMLESVFGTFASWFDKTPTGRIVNRFAKDIRsidmNLSGWLFFSINCFL 1020
Cdd:TIGR00958 208 CLLSIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQ----TMSRSLSLNVNVLL 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1021 ----SVAGGI-----LSVSSAM-------PIFMIPAVIvclaGYYFGLLYTRAQVGVKRLISIYTspifsllgESIVGVS 1084
Cdd:TIGR00958 284 rnlvMLLGLLgfmlwLSPRLTMvtlinlpLVFLAEKVF----GKRYQLLSEELQEAVAKANQVAE--------EALSGMR 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1085 VIRAFNRQTIFKQMFSERLD---NLVRLQSTSYNLNRWV-AVRTDGISGLVGAIAGLIALLQKDLSPGVVGFSLNQaVIF 1160
Cdd:TIGR00958 352 TVRSFAAEEGEASRFKEALEetlQLNKRKALAYAGYLWTtSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQ-EQL 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1161 SSSVLLFVRSCNSLQAEMNSYERVLEY-SKLPQEPAPtiAGQVPAtwPKEGDIVFNHVSVSYsaagPT-----ILKDVNL 1234
Cdd:TIGR00958 431 GEAVRVLSYVYSGMMQAVGASEKVFEYlDRKPNIPLT--GTLAPL--NLEGLIEFQDVSFSY----PNrpdvpVLKGLTF 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1235 HINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRISFIPQDPILFSGTVRSNLD-PFDEL 1313
Cdd:TIGR00958 503 TLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAyGLTDT 582
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1314 EDNFLNEALKTSGASSMIMAHTDdqkpihiTLDTHVASEGSNFSQGQKQVLALARAIVRRSKIIILDECTAsvddAMDQK 1393
Cdd:TIGR00958 583 PDEEIMAAAKAANAHDFIMEFPN-------GYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATS----ALDAE 651
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 19115470 1394 IQKTLRE--AFGDATMLCIAHRLKTIVDYDKVMVLDKGVLVEYGPPAVLYHNNGHFRRM 1450
Cdd:TIGR00958 652 CEQLLQEsrSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
897-1188 |
1.99e-44 |
|
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: 163.93 E-value: 1.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 897 VAAVLLFFVTTQATSILIDLWVAFWTNS------------SVNSPDVNNNKFLFVYGTMLLAYSLLDFLRTVSYDRGAWW 964
Cdd:cd18602 1 VALVLALALLKQGLRVATDFWLADWTEAnhdvasvvfnitSSSLEDDEVSYYISVYAGLSLGAVILSLVTNLAGELAGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 965 ASRKLHDSMLESVFGTFASWFDKTPTGRIVNRFAKDIRSIDMNLSGWLFFSINCFLSVAGGILSVSSAMPIFMIPAVIVC 1044
Cdd:cd18602 81 AARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPII 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1045 LAGYYFGLLYTRAQVGVKRLISIYTSPIFSLLGESIVGVSVIRAFNRQTIFKQMFSERLDN----LVRLQSTsynlNRWV 1120
Cdd:cd18602 161 IVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRnntaFLFLNTA----NRWL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19115470 1121 AVRTDGISGLVGAIAGLIAL---LQKDLSPGVVGFSLNQAVIFSSSVLLFVRSCNSLQAEMNSYERVLEYS 1188
Cdd:cd18602 237 GIRLDYLGAVIVFLAALSSLtaaLAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEYT 307
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
893-1188 |
2.17e-44 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 164.03 E-value: 2.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 893 SGFYVAAVLLFFVTTQATSILIDLWVAFW-----------------TNSSVNSPDVNNNKFLFVYGTMLLAYSLLDFLRT 955
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWanleeklndttdrvqgeNSTNVDIEDLDRDFNLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 956 VSYDRGAWWASRKLHDSMLESVFGTFASWFDKTPTGRIVNRFAKDIRSIDMNLsGWLFFS-INCFLSVAGGILSVSSAMP 1034
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLL-PLTFLDfLQLLLQVVGVVLLAVVVNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1035 ---IFMIPAVI--VCLAGYYfgLLYTRAqvgVKRLISIYTSPIFSLLGESIVGVSVIRAFNRQTIFKQMFSERLDnlvrL 1109
Cdd:cd18601 160 wvlIPVIPLVIlfLFLRRYY--LKTSRE---VKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQD----L 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1110 QSTSYNL----NRWVAVRTDGISGLVGAIAGLIAL-LQKDLSPGVVGFSLNQAVIFSSSVLLFVRSCNSLQAEMNSYERV 1184
Cdd:cd18601 231 HSEAWFLflatSRWLAVRLDALCALFVTVVAFGSLfLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERV 310
|
....
gi 19115470 1185 LEYS 1188
Cdd:cd18601 311 LEYS 314
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
269-798 |
1.15e-43 |
|
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: 171.17 E-value: 1.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 269 NKAWTYRFERMKTPSLFITIHKIFWRQILGMGVSSFMVSVCQFLSPIA----LNRLLKHLespSSSSVNPLVWIVLLLTg 344
Cdd:COG2274 131 TPEFDKRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFtqvvIDRVLPNQ---DLSTLWVLAIGLLLAL- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 345 pFLTSLFT--QFYLFMSTRylARSYTTLVQQIYNKVIR---SRFVQNKSGDskvgrsnnlISTDVDDIGEIREFI-HIIV 418
Cdd:COG2274 207 -LFEGLLRllRSYLLLRLG--QRIDLRLSSRFFRHLLRlplSFFESRSVGD---------LASRFRDVESIREFLtGSLL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 419 RAPVEIAGS-IYLLqkLL----GWSAYVGLALTVLTCSVPIVLGPLVAKLTLRANRATDSRIELMSELLQSIRITKFFGW 493
Cdd:COG2274 275 TALLDLLFVlIFLI--VLffysPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGA 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 494 ELPMLDRVKQRRQVELNRTWKLLLMEICIQVLVESLPVFSMFATFVV-FTTIMGQTITPS--IAFTSISlfSFIRTQFSW 570
Cdd:COG2274 353 ESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLgAYLVIDGQLTLGqlIAFNILS--GRFLAPVAQ 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 571 IAYLMRQIVQIFVSIGRVSDFLNDPDEVDPVNTIEDTSQ---EIGFFNASLTWvsnPSPGDFCLRDLNIVFPRNKLSIVI 647
Cdd:COG2274 431 LIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRlkgDIELENVSFRY---PGDSPPVLDNISLTIKPGERVAIV 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 648 GPTGSGKSSLISALLGELSLNKGS-----YNL----PRS--KGVSYVSQVPWLRNATIRDNILFDYPYI-EERYKKVIQA 715
Cdd:COG2274 508 GRSGSGKSTLLKLLLGLYEPTSGRilidgIDLrqidPASlrRQIGVVLQDVFLFSGTIRENITLGDPDAtDEEIIEAARL 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 716 CGLLTDLQSFVASDLTEIGEKGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTsnwiyKHCFQSSLME---NRT 792
Cdd:COG2274 588 AGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAET-----EAIILENLRRllkGRT 662
|
....*.
gi 19115470 793 VILVTH 798
Cdd:COG2274 663 VIIIAH 668
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
900-1451 |
1.27e-43 |
|
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: 171.08 E-value: 1.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 900 VLLFFVTTQATSILIDLWVAFWTNSSVNS--PDVNNNKFLFVYGTMLLAY---SLLDFLRTVSYDRGAWWASRKLHDSML 974
Cdd:TIGR01193 157 LIVNIVIAAIIVTLISIAGSYYLQKIIDTyiPHKMMGTLGIISIGLIIAYiiqQILSYIQIFLLNVLGQRLSIDIILSYI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 975 ESVFGTFASWFDKTPTGRIVNRFAKDIRSIDMNLSGWLFFSINCFLSVAGGILSVSSAMPIFM-----IPAVIVCLagYY 1049
Cdd:TIGR01193 237 KHLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLlsllsIPVYAVII--IL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1050 FGLLYTRAQVGVKRLISIYTSPIFsllgESIVGVSVIRAFN-RQTIFKQM---FSERLDNLVRLQSTSYNLNRWVAVrTD 1125
Cdd:TIGR01193 315 FKRTFNKLNHDAMQANAVLNSSII----EDLNGIETIKSLTsEAERYSKIdseFGDYLNKSFKYQKADQGQQAIKAV-TK 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1126 GISGLVGAIAGLIALLQKDLSPGvvgfslnQAVIFSSSVLLFVRSCNS-------LQAEMNSYERVLEYSKLPQEPAPti 1198
Cdd:TIGR01193 390 LILNVVILWTGAYLVMRGKLTLG-------QLITFNALLSYFLTPLENiinlqpkLQAARVANNRLNEVYLVDSEFIN-- 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1199 AGQVPATWPKEGDIVFNHVSVSYsAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQ 1278
Cdd:TIGR01193 461 KKKRTELNNLNGDIVINDVSYSY-GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLK 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1279 SVNLNALRQRISFIPQDPILFSGTVRSNL--DPFDELEDNFLNEALKtsgassmIMAHTDDQKPIHITLDTHVASEGSNF 1356
Cdd:TIGR01193 540 DIDRHTLRQFINYLPQEPYIFSGSILENLllGAKENVSQDEIWAACE-------IAEIKDDIENMPLGYQTELSEEGSSI 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1357 SQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREaFGDATMLCIAHRLKTIVDYDKVMVLDKGVLVEYGP 1436
Cdd:TIGR01193 613 SGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGS 691
|
570
....*....|....*
gi 19115470 1437 PAVLYHNNGHFRRMC 1451
Cdd:TIGR01193 692 HDELLDRNGFYASLI 706
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
983-1457 |
2.15e-43 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 168.22 E-value: 2.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 983 SWFDKTPTGRIVNRFakdIRSIDMNLSGWL-FFSINCFLSVAggiLSVSSAMPIFM---IPAVIVCLAGYYFGL--LYTR 1056
Cdd:PRK13657 105 AWHSQRGSGRALHTL---LRGTDALFGLWLeFMREHLATLVA---LVVLLPLALFMnwrLSLVLVVLGIVYTLIttLVMR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1057 AQVGVKRLISIYTSPIFSLLGESIVGVSVIRAFNRQTIFKQMFSERLDNLVRLQSTSynLNRW----VAVRTDG-ISGLV 1131
Cdd:PRK13657 179 KTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQALRDIADNLLAAQMPV--LSWWalasVLNRAAStITMLA 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1132 GAIAGlIALLQKD-LSPG----VVGFS------LNQAVIFSSSVLlfvrscnSLQAEMNSYERVLEYSKLPQEPAPTI-A 1199
Cdd:PRK13657 257 ILVLG-AALVQKGqLRVGevvaFVGFAtlligrLDQVVAFINQVF-------MAAPKLEEFFEVEDAVPDVRDPPGAIdL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1200 GQVpatwpkEGDIVFNHVSVSYSAAGPTIlKDVNLHINPSEKVAVVGRTGSGKSTLgLTLLrftHRI----SGEIYINGR 1275
Cdd:PRK13657 329 GRV------KGAVEFDDVSFSYDNSRQGV-EDVSFEAKPGQTVAIVGPTGAGKSTL-INLL---QRVfdpqSGRILIDGT 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1276 ETQSVNLNALRQRISFIPQDPILFSGTVRSNL-----DPFDElEdnfLNEALKTSGASSMIMAHTDDqkpihitLDTHVA 1350
Cdd:PRK13657 398 DIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIrvgrpDATDE-E---MRAAAERAQAHDFIERKPDG-------YDTVVG 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1351 SEGSNFSQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAHRLKTIVDYDKVMVLDKGV 1430
Cdd:PRK13657 467 ERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGR 546
|
490 500
....*....|....*....|....*..
gi 19115470 1431 LVEYGPPAVLYHNNGHFRRMCDGSGIT 1457
Cdd:PRK13657 547 VVESGSFDELVARGGRFAALLRAQGML 573
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
608-819 |
2.73e-42 |
|
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: 156.94 E-value: 2.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 608 SQEIGFFNASLTWVSNPspgdfCLRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSynLPRSKGVSYVSQVP 687
Cdd:cd03291 35 SDDNNLFFSNLCLVGAP-----VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGK--IKHSGRISFSSQFS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 688 WLRNATIRDNILFDYPYIEERYKKVIQACGLLTDLQSFVASDLTEIGEKGVTLSGGQKQRIALARAVYSPTSIVLMDDVF 767
Cdd:cd03291 108 WIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPF 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 19115470 768 SALDIHTSNWIYKHCFqSSLMENRTVILVTHNV-HLfmDSAAFIVTVKNGSAF 819
Cdd:cd03291 188 GYLDVFTEKEIFESCV-CKLMANKTRILVTSKMeHL--KKADKILILHEGSSY 237
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1180-1451 |
1.72e-40 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 159.22 E-value: 1.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1180 SYERVLEYskLPQEPAPTIAGQVPATwPKEGDIVFNHVSVSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLgLTL 1259
Cdd:PRK11160 310 SARRINEI--TEQKPEVTFPTTSTAA-ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTL-LQL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1260 L-RFTHRISGEIYINGRETQSVNLNALRQRISFIPQDPILFSGTVRSNL---DPfdELEDNFLNEALKTSGASSmimaHT 1335
Cdd:PRK11160 386 LtRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGLEK----LL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1336 DDQKPihitLDTHVASEGSNFSQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAHRLK 1415
Cdd:PRK11160 460 EDDKG----LNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLT 535
|
250 260 270
....*....|....*....|....*....|....*.
gi 19115470 1416 TIVDYDKVMVLDKGVLVEYGPPAVLYHNNGHFRRMC 1451
Cdd:PRK11160 536 GLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLK 571
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
944-1426 |
3.38e-40 |
|
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: 157.45 E-value: 3.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 944 LLAYSLLDFLRTVSYDRGAWWASRKLHDSMLESVFGTFASWFDKTPTGRIVNRFAKDIRSIDMNLSGWLFFSINC----- 1018
Cdd:TIGR02857 54 LLLRALLGWLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAvivpl 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1019 -FLSV-------AGGILSVSSAM-PIFMIpavivcLAGYYFGLLYTRAQVGVKRLisiytSPIFSllgESIVGVSVIRAF 1089
Cdd:TIGR02857 134 aILAAvfpqdwiSGLILLLTAPLiPIFMI------LIGWAAQAAARKQWAALSRL-----SGHFL---DRLRGLPTLKLF 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1090 NRQTifKQmfserldnLVRLQSTSYNLnRWVAVRTDGISGLVGAIAGLIALLQKDLSPGVVGFSL-NQAVIFSSS--VLL 1166
Cdd:TIGR02857 200 GRAK--AQ--------AAAIRRSSEEY-RERTMRVLRIAFLSSAVLELFATLSVALVAVYIGFRLlAGDLDLATGlfVLL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1167 FV-------RSCNSL-------QAEMNSYERVLEysklpQEPAPTiAGQVPATWPKEGDIVFNHVSVSYSAAGPtILKDV 1232
Cdd:TIGR02857 269 LApefylplRQLGAQyharadgVAAAEALFAVLD-----AAPRPL-AGKAPVTAAPASSLEFSGVSVAYPGRRP-ALRPV 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1233 NLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRISFIPQDPILFSGTVRSNL---DP 1309
Cdd:TIGR02857 342 SFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIrlaRP 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1310 fdELEDNFLNEALKTSGASSMIMAhtddqkpIHITLDTHVASEGSNFSQGQKQVLALARAIVRRSKIIILDECTASVDDA 1389
Cdd:TIGR02857 422 --DASDAEIREALERAGLDEFVAA-------LPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAE 492
|
490 500 510
....*....|....*....|....*....|....*..
gi 19115470 1390 MDQKIQKTLREAFGDATMLCIAHRLKTIVDYDKVMVL 1426
Cdd:TIGR02857 493 TEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1210-1468 |
3.41e-40 |
|
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: 150.39 E-value: 3.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1210 GDIVFNHVSVSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHrISGEIYINGRETQSVNLNALRQRI 1289
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1290 SFIPQDPILFSGTVRSNLDPFDELEDNFLNEALKTSGASSMImahtdDQKPIHitLDTHVASEGSNFSQGQKQVLALARA 1369
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVI-----EQFPGQ--LDFVLVDGGCVLSHGHKQLMCLARS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1370 IVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAHRLKTIVDYDKVMVLDKGVLVEYGPPAVLYHNNGHFRR 1449
Cdd:cd03289 153 VLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQ 232
|
250
....*....|....*....
gi 19115470 1450 MCDGSGITFLPPETRGSKS 1468
Cdd:cd03289 233 AISPSDRLKLFPRRNSSKS 251
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1082-1445 |
2.26e-39 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 155.95 E-value: 2.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1082 GVSVIRAFNRQTIFKQMFsERLDNLVRLQSTSYnlnrwvaVRTDGIS-GLVGAIAGL----------IALLQKDLSPGVV 1150
Cdd:PRK11176 213 GHKEVLIFGGQEVETKRF-DKVSNRMRQQGMKM-------VSASSISdPIIQLIASLalafvlyaasFPSVMDTLTAGTI 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1151 gfslnqAVIFSSSVLLfVRSCNSL-------QAEMNSYERVLEYSKLPQEPAptiAGQVPATWPKeGDIVFNHVSVSYSA 1223
Cdd:PRK11176 285 ------TVVFSSMIAL-MRPLKSLtnvnaqfQRGMAACQTLFAILDLEQEKD---EGKRVIERAK-GDIEFRNVTFTYPG 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1224 AGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRISFIPQDPILFSGTV 1303
Cdd:PRK11176 354 KEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTI 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1304 RSNL-----DPF--DELEdnflnEALKTSGASSMI--MAHtddqkpihiTLDTHVASEGSNFSQGQKQVLALARAIVRRS 1374
Cdd:PRK11176 434 ANNIayartEQYsrEQIE-----EAARMAYAMDFInkMDN---------GLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19115470 1375 KIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAHRLKTIVDYDKVMVLDKGVLVEYGPPAVLYHNNG 1445
Cdd:PRK11176 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNG 570
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1190-1450 |
9.90e-39 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 154.23 E-value: 9.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1190 LPQEPAPTIAGQVPATWPKEGDIVFNHVSVsYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRF-THRisG 1268
Cdd:PRK11174 328 LETPLAHPQQGEKELASNDPVTIEAEDLEI-LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFlPYQ--G 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1269 EIYINGRETQSVNLNALRQRISFIPQDPILFSGTVRSNL---DPfdELEDNFLNEALKTSGASSMIMAHTDDqkpihitL 1345
Cdd:PRK11174 405 SLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVllgNP--DASDEQLQQALENAWVSEFLPLLPQG-------L 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1346 DTHVASEGSNFSQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAHRLKTIVDYDKVMV 1425
Cdd:PRK11174 476 DTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWV 555
|
250 260
....*....|....*....|....*
gi 19115470 1426 LDKGVLVEYGPPAVLYHNNGHFRRM 1450
Cdd:PRK11174 556 MQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1212-1443 |
2.75e-38 |
|
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: 143.24 E-value: 2.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAaGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLT---LLRFThriSGEIYINGRETQSVNLNALRQR 1288
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLlngLLKPT---SGEVLVDGKDITKKNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1289 ISFIPQDPI--LFSGTVRS-------NLD-PFDELEDNfLNEALKTSGASSMImahtddQKPIHiTLdthvasegsnfSQ 1358
Cdd:COG1122 77 VGLVFQNPDdqLFAPTVEEdvafgpeNLGlPREEIRER-VEEALELVGLEHLA------DRPPH-EL-----------SG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1359 GQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLRE-AFGDATMLCIAHRLKTIVDY-DKVMVLDKGVLVEYGP 1436
Cdd:COG1122 138 GQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAELaDRVIVLDDGRIVADGT 217
|
....*..
gi 19115470 1437 PAVLYHN 1443
Cdd:COG1122 218 PREVFSD 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1019-1414 |
2.86e-38 |
|
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: 151.74 E-value: 2.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1019 FLSVAGGILSVSSAMPIFMIPAVivclagyyFGLLYTRAQVGVKRLISIYTSPIFSLLgesiVGVSVIRAFNRQTIFKQM 1098
Cdd:TIGR02868 151 LSVPAALILAAGLLLAGFVAPLV--------SLRAARAAEQALARLRGELAAQLTDAL----DGAAELVASGALPAALAQ 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1099 FSERLDNLVRLQSTSYNLNRWvavrTDGISGLVGAIAGLIALLQKdlSPGVVGFSLNqAVIFSSSVLL----------FV 1168
Cdd:TIGR02868 219 VEEADRELTRAERRAAAATAL----GAALTLLAAGLAVLGALWAG--GPAVADGRLA-PVTLAVLVLLplaafeafaaLP 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1169 RSCNSLQAEMNSYERVLEyskLPQEPAPTIAGQVPA---TWPKEGDIVFNHVSVSYsAAGPTILKDVNLHINPSEKVAVV 1245
Cdd:TIGR02868 292 AAAQQLTRVRAAAERIVE---VLDAAGPVAEGSAPAagaVGLGKPTLELRDLSAGY-PGAPPVLDGVSLDLPPGERVAIL 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1246 GRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRISFIPQDPILFSGTVRSNL---DPfdELEDNFLNEAL 1322
Cdd:TIGR02868 368 GPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLrlaRP--DATDEELWAAL 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1323 KTSGASSMIMAHTDDqkpihitLDTHVASEGSNFSQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAF 1402
Cdd:TIGR02868 446 ERVGLADWLRALPDG-------LDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAAL 518
|
410
....*....|..
gi 19115470 1403 GDATMLCIAHRL 1414
Cdd:TIGR02868 519 SGRTVVLITHHL 530
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1209-1431 |
6.89e-38 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 142.22 E-value: 6.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1209 EGDIVFNHVSVSYSAAGPT-ILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQ 1287
Cdd:cd03248 9 KGIVKFQNVTFAYPTRPDTlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1288 RISFIPQDPILFSGTVRSNLD------PFDELEdnflnEALKTSGASSMIMAHTDDqkpihitLDTHVASEGSNFSQGQK 1361
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAyglqscSFECVK-----EAAQKAHAHSFISELASG-------YDTEVGEKGSQLSGGQK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1362 QVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAHRLKTIVDYDKVMVLDKGVL 1431
Cdd:cd03248 157 QRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
300-588 |
1.19e-37 |
|
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: 143.46 E-value: 1.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 300 GVSSFMVSVCQFLSPIALNRLLKHLESPSSSSVNPLVWIVLLLTGPFLTSLFTQFYLFMSTRYLARSYTTLVQQIYNKVI 379
Cdd:cd18598 3 GLLKLLADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTAVYRKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 380 RSRFVQNKSGDSkvGRSNNLISTDVDDIGEIREFIHIIVRAPVEIAGSIYLLQKLLGWSAYVGLALTVLTCSVPIVLGPL 459
Cdd:cd18598 83 RVRSSSLSKFST--GEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 460 VAKLTLRANRATDSRIELMSELLQSIRITKFFGWELPMLDRVKQRRQVELNR-TWKLLLMEICIqVLVESLPVFSMFATF 538
Cdd:cd18598 161 IGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKAlKGRKYLDALCV-YFWATTPVLISILTF 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 19115470 539 VVFtTIMGQTITPSIAFTSISLF---SFIRTQFSWIaylMRQIVQIFVSIGRV 588
Cdd:cd18598 240 ATY-VLMGNTLTAAKVFTSLALFnmlIGPLNAFPWV---LNGLVEAWVSLKRL 288
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
587-816 |
1.95e-37 |
|
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: 149.91 E-value: 1.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 587 RVSDFLNDPDEVDPVNTIEDTSQ---EIGFFNASLTWvsnpSPGDFCLRDLNIVFPRNKLSIVIGPTGSGKSSLISALLG 663
Cdd:COG4988 310 KIFALLDAPEPAAPAGTAPLPAAgppSIELEDVSFSY----PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 664 ELSLNKGS--------YNLPRS---KGVSYVSQVPWLRNATIRDNILFDYPYI-EERYKKVIQACGLLtdlqSFVAS--- 728
Cdd:COG4988 386 FLPPYSGSilingvdlSDLDPAswrRQIAWVPQNPYLFAGTIRENLRLGRPDAsDEELEAALEAAGLD----EFVAAlpd 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 729 --DlTEIGEKGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIykhcFQS--SLMENRTVILVTHNVHLfM 804
Cdd:COG4988 462 glD-TPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEI----LQAlrRLAKGRTVILITHRLAL-L 535
|
250
....*....|..
gi 19115470 805 DSAAFIVTVKNG 816
Cdd:COG4988 536 AQADRILVLDDG 547
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1134-1446 |
3.75e-37 |
|
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: 148.13 E-value: 3.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1134 IAGLIALLQKDLSPGVVGFSLNQAVIFSSSVLLFVRSCNSLQAEMNSYERVLEYSKLPQEPAPTIAGQVPATWPKEGDIV 1213
Cdd:COG1123 181 ILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAAVPRLGAARGRAAPAAAAAEPL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1214 --FNHVSVSYSAAGP---TILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVN---LNAL 1285
Cdd:COG1123 261 leVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1286 RQRISFIPQDPilfsgtvRSNLDP----FDELEDNFLN--------------EALKTSGassmimahtddqkpihitLDT 1347
Cdd:COG1123 341 RRRVQMVFQDP-------YSSLNPrmtvGDIIAEPLRLhgllsraerrervaELLERVG------------------LPP 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1348 HVAS----EgsnFSQGQKQVLALARAIVRRSKIIILDECTAsvddAMDQKIQ-------KTLREAFGdATMLCIAHRLkT 1416
Cdd:COG1123 396 DLADryphE---LSGGQRQRVAIARALALEPKLLILDEPTS----ALDVSVQaqilnllRDLQRELG-LTYLFISHDL-A 466
|
330 340 350
....*....|....*....|....*....|..
gi 19115470 1417 IVDY--DKVMVLDKGVLVEYGPPAVLYHNNGH 1446
Cdd:COG1123 467 VVRYiaDRVAVMYDGRIVEDGPTEEVFANPQH 498
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1212-1435 |
9.98e-37 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 137.06 E-value: 9.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNlNALRQRISF 1291
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1292 IPQDPILFSGTVRSNLdpfdelednflnealktsgassmimahtddqkpihitldthvaseGSNFSQGQKQVLALARAIV 1371
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------------GRRFSGGERQRLALARILL 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115470 1372 RRSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAHRLKTIVDYDKVMVLDKGVLVEYG 1435
Cdd:cd03247 115 QDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
943-1469 |
1.16e-36 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 147.73 E-value: 1.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 943 MLLAYSLLDFLRTVSYDRGAWWASRKLHD---SMLESVFGTFAS----WFDKTPTGRIVNRFakdIRSIDMNLSGWLFFS 1015
Cdd:TIGR01192 58 TLALWAGFGVFNTIAYVLVAREADRLAHGrraTLLTEAFGRIISmplsWHQQRGTSNALHTL---LRATETLFGLWLEFM 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1016 INCFLSVAGGILSVSSAMPI-FMIPAVIVCLAGYYF---GLLYTRAQVGvKRLISIYTSPIFSLLGESIVGVSVIRAFNR 1091
Cdd:TIGR01192 135 RQHLATFVALFLLIPTAFAMdWRLSIVLMVLGILYIliaKLVMQRTKNG-QAAVEHHYHNVFKHVSDSISNVSVVHSYNR 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1092 QTIFKQMFSERLDNLVRLQSTSYN-------LNRWVAVrtdgISGLVGAIAGLIALLQKDLSPG----VVGFSlNQAVIF 1160
Cdd:TIGR01192 214 IEAETSALKQFTNNLLSAQYPVLDwwalasgLNRMAST----ISMMCILVIGTVLVIKGELSVGeviaFIGFA-NLLIGR 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1161 SSSVLLFVRSCNSLQAEMNSYERVLEYSKLPQEPAPtiAGQVPATwpkEGDIVFNHVSVSY--SAAGptiLKDVNLHINP 1238
Cdd:TIGR01192 289 LDQMSGFITQIFEARAKLEDFFDLEDSVFQREEPAD--APELPNV---KGAVEFRHITFEFanSSQG---VFDVSFEAKA 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1239 SEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRISFIPQDPILFSGTVRSNLDPFDE-LEDNF 1317
Cdd:TIGR01192 361 GQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREgATDEE 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1318 LNEALKTSGASSMIMAHTDDqkpihitLDTHVASEGSNFSQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKT 1397
Cdd:TIGR01192 441 VYEAAKAAAAHDFILKRSNG-------YDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNA 513
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19115470 1398 LREAFGDATMLCIAHRLKTIVDYDKVMVLDKGVLVEYGPPAVLYHNNGHFRRMCDGSGITFLPPETRGSKSA 1469
Cdd:TIGR01192 514 IDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRRSGLLTNQPATKPLRKA 585
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1103-1436 |
1.51e-36 |
|
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: 147.20 E-value: 1.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1103 LDNLVRLQSTSYNLNRWVAVRTDGISGLVGAIA------------GLIALL--QKDLSPGVvgfslnqavIFSSSVLL-- 1166
Cdd:COG4618 213 LPALRRRWQRANARALALQARASDRAGGFSALSkflrlllqsavlGLGAYLviQGEITPGA---------MIAASILMgr 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1167 -------FVRSCNSLQAEMNSYERVLEY-SKLPQEPAPTiagQVPAtwPKeGDIVFNHVSVSYSAAGPTILKDVNLHINP 1238
Cdd:COG4618 284 alapieqAIGGWKQFVSARQAYRRLNELlAAVPAEPERM---PLPR--PK-GRLSVENLTVVPPGSKRPILRGVSFSLEP 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1239 SEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRISFIPQDPILFSGTVRSNLDPFDELEDNFL 1318
Cdd:COG4618 358 GEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIARFGDADPEKV 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1319 NEALKTSGASSMIMahtddqkpihiTL----DTHVASEGSNFSQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKI 1394
Cdd:COG4618 438 VAAAKLAGVHEMIL-----------RLpdgyDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAAL 506
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 19115470 1395 QKTLRE--AFGdATMLCIAHRLKTIVDYDKVMVLDKGVLVEYGP 1436
Cdd:COG4618 507 AAAIRAlkARG-ATVVVITHRPSLLAAVDKLLVLRDGRVQAFGP 549
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
398-798 |
2.94e-36 |
|
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: 146.45 E-value: 2.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 398 NLISTDVDDIGEIreFIHIIVraPVEIAGSIYLLQKLLGWSAYVGLALTVLTC-SVPIVLGP-LVAKLTLRANRA-TDSR 474
Cdd:COG4987 116 NRLVADVDALDNL--YLRVLL--PLLVALLVILAAVAFLAFFSPALALVLALGlLLAGLLLPlLAARLGRRAGRRlAAAR 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 475 IELMS---ELLQSIRitkffgwELPMLDRVKQRRQV--ELNRTW-KLLLMEICIQVLVESLPVFSMFATfVVFTTIMG-- 546
Cdd:COG4987 192 AALRArltDLLQGAA-------ELAAYGALDRALARldAAEARLaAAQRRLARLSALAQALLQLAAGLA-VVAVLWLAap 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 547 ----QTITPS----IAFTSISLFSFIRTqfswIAYLMRQIVQIFVSIGRVSDFLNDPDEV-DPVNTIEDTSQ-EIGFFNA 616
Cdd:COG4987 264 lvaaGALSGPllalLVLAALALFEALAP----LPAAAQHLGRVRAAARRLNELLDAPPAVtEPAEPAPAPGGpSLELEDV 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 617 SLTWVSNPSPgdfCLRDLNIVFPRN-KLSIViGPTGSGKSSLISALLGELSLNKGSY--------NLPRS---KGVSYVS 684
Cdd:COG4987 340 SFRYPGAGRP---VLDGLSLTLPPGeRVAIV-GPSGSGKSTLLALLLRFLDPQSGSItlggvdlrDLDEDdlrRRIAVVP 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 685 QVPWLRNATIRDNILFDYPYI-EERYKKVIQACGLLTDLQSFVASDLTEIGEKGVTLSGGQKQRIALARAVYSPTSIVLM 763
Cdd:COG4987 416 QRPHLFDTTLRENLRLARPDAtDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLL 495
|
410 420 430
....*....|....*....|....*....|....*
gi 19115470 764 DDVFSALDIHTSNWIYKHCFQssLMENRTVILVTH 798
Cdd:COG4987 496 DEPTEGLDAATEQALLADLLE--ALAGRTVLLITH 528
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1214-1435 |
3.16e-36 |
|
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: 137.25 E-value: 3.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1214 FNHVSVSYSAAG--PTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVN---LNALRQR 1288
Cdd:cd03257 4 VKNLSVSFPTGGgsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1289 ISFIPQDPIlfsgtvrSNLDPFDELEDNfLNEALKTSGASS--MIMAHTDDQKPIHITLDTHVASEGSN-FSQGQKQVLA 1365
Cdd:cd03257 84 IQMVFQDPM-------SSLNPRMTIGEQ-IAEPLRIHGKLSkkEARKEAVLLLLVGVGLPEEVLNRYPHeLSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19115470 1366 LARAIVRRSKIIILDECTAsvddAMDQKIQ-------KTLREAFGdATMLCIAHRLKtIVDY--DKVMVLDKGVLVEYG 1435
Cdd:cd03257 156 IARALALNPKLLIADEPTS----ALDVSVQaqildllKKLQEELG-LTLLFITHDLG-VVAKiaDRVAVMYAGKIVEEG 228
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1213-1429 |
2.16e-35 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 134.52 E-value: 2.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1213 VFNHVSVSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRISFI 1292
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1293 PQDP--ILFSGTVrsnldpFDELEDNFLN-------------EALKTSGassmiMAHTDDQKPIHitldthvasegsnFS 1357
Cdd:cd03225 81 FQNPddQFFGPTV------EEEVAFGLENlglpeeeieerveEALELVG-----LEGLRDRSPFT-------------LS 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115470 1358 QGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLRE--AFGdATMLCIAHRLKTIVDY-DKVMVLDKG 1429
Cdd:cd03225 137 GGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKlkAEG-KTIIIVTHDLDLLLELaDRVIVLEDG 210
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1217-1431 |
2.73e-35 |
|
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: 132.73 E-value: 2.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1217 VSVSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLG---LTLLRFTHrisGEIYINGRETQSVNLNALRQRISFIP 1293
Cdd:cd03246 6 VSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLArliLGLLRPTS---GRVRLDGADISQWDPNELGDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1294 QDPILFSGTVRSNLdpfdelednflnealktsgassmimahtddqkpihitldthvasegsnFSQGQKQVLALARAIVRR 1373
Cdd:cd03246 83 QDDELFSGSIAENI------------------------------------------------LSGGQRQRLGLARALYGN 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 19115470 1374 SKIIILDECTASVDDAMDQKIQKTLREA-FGDATMLCIAHRLKTIVDYDKVMVLDKGVL 1431
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1212-1443 |
2.78e-35 |
|
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: 142.35 E-value: 2.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLT---LLRFTHRISGEIYINGRETQSVNLNALRQR 1288
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALAlmgLLPHGGRISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1289 ISFIPQDPilfsgtvRSNLDPFDELEDnfLNEALKTSGASSMIMAHTDDQKPIHITLDTHVASEGSNFSQGQKQVLALAR 1368
Cdd:COG1123 85 IGMVFQDP-------MTQLNPVTVGDQ--IAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19115470 1369 AIVRRSKIIILDECTASVDDAMDQKIQKTLRE--AFGDATMLCIAHRLKTIVDY-DKVMVLDKGVLVEYGPPAVLYHN 1443
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1229-1384 |
3.92e-35 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 131.23 E-value: 3.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1229 LKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRISFIPQDPILFSG-TVRSNL 1307
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19115470 1308 DPFDELEDNFlnealktSGASSMIMAHTDDQKPIHITLDTHVASEGSNFSQGQKQVLALARAIVRRSKIIILDECTA 1384
Cdd:pfam00005 81 RLGLLLKGLS-------KREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1219-1412 |
2.62e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 131.09 E-value: 2.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1219 VSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRISFIPQDPIL 1298
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1299 FSGTVRSNLD-PFDELEDNF----LNEALKTSGASSMIMahtddQKPIHitldthvasegsNFSQGQKQVLALARAIVRR 1373
Cdd:COG4619 86 WGGTVRDNLPfPFQLRERKFdrerALELLERLGLPPDIL-----DKPVE------------RLSGGERQRLALIRALLLQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 19115470 1374 SKIIILDECTASVDDAMDQKIQKTLREAF--GDATMLCIAH 1412
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSH 189
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
631-816 |
2.23e-33 |
|
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: 127.11 E-value: 2.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGS--------YNLPRS---KGVSYVSQVPWLRNATIRDNIL 699
Cdd:cd03228 18 LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEilidgvdlRDLDLEslrKNIAYVPQDPFLFSGTIRENIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 700 fdypyieerykkviqacglltdlqsfvasdlteigekgvtlSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIY 779
Cdd:cd03228 98 -----------------------------------------SGGQRQRIAIARALLRDPPILILDEATSALDPETEALIL 136
|
170 180 190
....*....|....*....|....*....|....*..
gi 19115470 780 KHCFQssLMENRTVILVTHNVHLfMDSAAFIVTVKNG 816
Cdd:cd03228 137 EALRA--LAKGKTVIVIAHRLST-IRDADRIIVLDDG 170
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
300-587 |
6.90e-33 |
|
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: 130.43 E-value: 6.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 300 GVSSFMVSVCQFLSPIALNRLLKHLESPSSSSVNPL------------------VWIVLLLTGPFLTSLFTQFYLFMSTR 361
Cdd:cd18591 3 GILKLLGDLLGFVGPLCISGIVDYVEENTYSSSNSTdklsvsyvtveeffsngyVLAVILFLALLLQATFSQASYHIVIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 362 YLARSYTTLVQQIYNKVIRSRFVQNKSGDSKVGRSNNLISTDVDDIGEIREFIHIIVRAPVEIAGSIYLLQKLLGWSAYV 441
Cdd:cd18591 83 EGIRLKTALQAMIYEKALRLSSWNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSALI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 442 GLALTVLTCSVPIVLGPLVAKLTLRANRATDSRIELMSELLQSIRITKFFGWELPMLDRVKQRRQVELNRTWKLLLMEIC 521
Cdd:cd18591 163 GAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYWSL 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115470 522 IQVLVESLPVFSMFATFVVFTTIMGQTITPSIAFTSISLFSFIRTQFSWIAYLMRQIVQIFVSIGR 587
Cdd:cd18591 243 MTFLTQASPILVTLVTFGLYPYLEGEPLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRR 308
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1212-1429 |
7.43e-33 |
|
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: 126.82 E-value: 7.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSY---SAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGretqsvnlnalrqR 1288
Cdd:cd03250 1 ISVEDASFTWdsgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1289 ISFIPQDPILFSGTVRSNL---DPFDEledNFLNEALKtsgASSM-----IMAHTDdqkpihitlDTHVASEGSNFSQGQ 1360
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENIlfgKPFDE---ERYEKVIK---ACALepdleILPDGD---------LTEIGEKGINLSGGQ 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115470 1361 KQVLALARAIVRRSKIIILDECTASVDDA-----MDQKIQKTLREafgDATMLCIAHRLKTIVDYDKVMVLDKG 1429
Cdd:cd03250 133 KQRISLARAVYSDADIYLLDDPLSAVDAHvgrhiFENCILGLLLN---NKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
308-588 |
1.56e-32 |
|
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: 128.83 E-value: 1.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 308 VCQFLSPIALNR-LLKHLESPSSSSVNPLVWIVLLLTGPFLTSLFTQFYLFMSTRYLARSYTTLVQQIYNKVIRSRFVQN 386
Cdd:cd18592 11 IFGFIGPTILIRkLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYKKILRLRSLGD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 387 KSgdskVGRSNNLISTDVDDIGEIREFIHIIVRAPVE-IAGSIYLLQkLLGWSAYVGLALTVLTCSVPIVLGPLVAKLTL 465
Cdd:cd18592 91 KS----VGELINIFSNDGQRLFDAAVFGPLVIGGPVVlILGIVYSTY-LLGPWALLGMLVFLLFYPLQAFIAKLTGKFRR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 466 RANRATDSRIELMSELLQSIRITKFFGWELPMLDRVKQRRQVELnrtwKLLLMEICIQVLVESL-PVFSMFATFVVFT-- 542
Cdd:cd18592 166 KAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEER----KILEKAGYLQSISISLaPIVPVIASVVTFLah 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 19115470 543 TIMGQTITPSIAFTSISLFSFIRTQFSWIAYLMRQIVQIFVSIGRV 588
Cdd:cd18592 242 VALGNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
631-802 |
3.47e-31 |
|
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: 130.10 E-value: 3.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYNL-----------PRSKGVSYVSQVPWLRNATIRDNIL 699
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVngvpladadadSWRDQIAWVPQHPFLFAGTIAENIR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 700 FDYPYI-EERYKKVIQACGLLTDLQSFVASDLTEIGEKGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWI 778
Cdd:TIGR02857 418 LARPDAsDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEV 497
|
170 180
....*....|....*....|....
gi 19115470 779 YKHCFQssLMENRTVILVTHNVHL 802
Cdd:TIGR02857 498 LEALRA--LAQGRTVLLVTHRLAL 519
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1214-1429 |
2.49e-30 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 117.73 E-value: 2.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1214 FNHVSVSYsaAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRISFIP 1293
Cdd:cd00267 2 IENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1294 QdpilfsgtvrsnldpfdelednflnealktsgassmimahtddqkpihitldthvasegsnFSQGQKQVLALARAIVRR 1373
Cdd:cd00267 80 Q-------------------------------------------------------------LSGGQRQRVALARALLLN 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 19115470 1374 SKIIILDECTASVDDAMDQKIQKTLREAF-GDATMLCIAHRLKTIVDY-DKVMVLDKG 1429
Cdd:cd00267 99 PDLLLLDEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1212-1440 |
1.16e-29 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 118.81 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSaaGPTILKDVNLHINPSEKVAVVGRTGSGKSTLgL----TLLRFThriSGEIYINGRETQSVNlNALRQ 1287
Cdd:COG4555 2 IEVENLSKKYG--KVPALKDVSFTAKDGEITGLLGPNGAGKTTL-LrmlaGLLKPD---SGSILIDGEDVRKEP-REARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1288 RISFIPQDPILFSG-TVRSNLDPFDELEDNFLNEALKtsgASSMIMAHTDDQKPIHITLdthvasegSNFSQGQKQVLAL 1366
Cdd:COG4555 75 QIGVLPDERGLYDRlTVRENIRYFAELYGLFDEELKK---RIEELIELLGLEEFLDRRV--------GELSTGMKKKVAL 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19115470 1367 ARAIVRRSKIIILDECTASVdDAMDQK-IQKTLREAFG-DATMLCIAHRLKTIVDY-DKVMVLDKGVLVEYGPPAVL 1440
Cdd:COG4555 144 ARALVHDPKVLLLDEPTNGL-DVMARRlLREILRALKKeGKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1212-1440 |
8.90e-29 |
|
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: 116.51 E-value: 8.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAaGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSV---NLNALRQR 1288
Cdd:cd03256 1 IEVENLSKTYPN-GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgkALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1289 ISFIPQDPIL----------------FSGTVRSNLDPFDELEDNFLNEALKTSGassmimahtddqkpihitLDTHVASE 1352
Cdd:cd03256 80 IGMIFQQFNLierlsvlenvlsgrlgRRSTWRSLFGLFPKEEKQRALAALERVG------------------LLDKAYQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1353 GSNFSQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREA---FGDaTMLCIAHRLKTIVDY-DKVMVLDK 1428
Cdd:cd03256 142 ADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInreEGI-TVIVSLHQVDLAREYaDRIVGLKD 220
|
250
....*....|..
gi 19115470 1429 GVLVEYGPPAVL 1440
Cdd:cd03256 221 GRIVFDGPPAEL 232
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1212-1438 |
9.49e-29 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 116.44 E-value: 9.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAA--GPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRI 1289
Cdd:COG1124 2 LEVRNLSVSYGQGgrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1290 SFIPQDPilfsgtvRSNLDPFDELEDnFLNEALKtsgassmIMAHTDDQKPIH-----ITLDTHVASE-GSNFSQGQKQV 1363
Cdd:COG1124 82 QMVFQDP-------YASLHPRHTVDR-ILAEPLR-------IHGLPDREERIAelleqVGLPPSFLDRyPHQLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1364 LALARAIVRRSKIIILDECTAsvddAMDQKIQ-------KTLREAFGdATMLCIAHRLKtIVDY--DKVMVLDKGVLVEY 1434
Cdd:COG1124 147 VAIARALILEPELLLLDEPTS----ALDVSVQaeilnllKDLREERG-LTYLFVSHDLA-VVAHlcDRVAVMQNGRIVEE 220
|
....
gi 19115470 1435 GPPA 1438
Cdd:COG1124 221 LTVA 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1212-1437 |
1.01e-28 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 115.74 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYsaAGPTILKDVNLHINPSEKVAVVGRTGSGKSTL-----GLTLLRFTHRISGEIYINGRE--TQSVNLNA 1284
Cdd:cd03260 1 IELRDLNVYY--GDKHALKDISLDIPKGEITALIGPSGCGKSTLlrllnRLNDLIPGAPDEGEVLLDGKDiyDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1285 LRQRISFIPQDPILFSGTVRSNLDPFDELEDNFLNEALKTSGASSMIMAHTDDqkpihitlDTHVASEGSNFSQGQKQVL 1364
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWD--------EVKDRLHALGLSGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115470 1365 ALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAHRL---KTIVDYdkVMVLDKGVLVEYGPP 1437
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMqqaARVADR--TAFLLNGRLVEFGPT 224
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
631-798 |
1.22e-28 |
|
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: 115.40 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSY--------NLPRS---KGVSYVSQVPWLRNATIRDNIL 699
Cdd:cd03254 19 LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlidgidirDISRKslrSMIGVVLQDTFLFSGTIMENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 700 FDYPYIEEryKKVIQACGL--LTDLQSFVASDL-TEIGEKGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSN 776
Cdd:cd03254 99 LGRPNATD--EEVIEAAKEagAHDFIMKLPNGYdTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEK 176
|
170 180
....*....|....*....|....*
gi 19115470 777 WIykhcfQSS---LMENRTVILVTH 798
Cdd:cd03254 177 LI-----QEAlekLMKGRTSIIIAH 196
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1212-1438 |
1.28e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 115.96 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSaaGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRetqsvNLNALRQRISF 1291
Cdd:COG1121 7 IELENLTVSYG--GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK-----PPRRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1292 IPQD-------PIlfsgTVR----SNLDP-------FDELEDNFLNEALKTSGASSmiMAHtddqKPIhitldthvaseg 1353
Cdd:COG1121 80 VPQRaevdwdfPI----TVRdvvlMGRYGrrglfrrPSRADREAVDEALERVGLED--LAD----RPI------------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1354 SNFSQGQKQ-VLaLARAIVRRSKIIILDECTASVDDAMDQKIQKTLRE--AFGdATMLCIAHRLKTIVDY-DKVMVLDKG 1429
Cdd:COG1121 138 GELSGGQQQrVL-LARALAQDPDLLLLDEPFAGVDAATEEALYELLRElrREG-KTILVVTHDLGAVREYfDRVLLLNRG 215
|
....*....
gi 19115470 1430 VlVEYGPPA 1438
Cdd:COG1121 216 L-VAHGPPE 223
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1212-1438 |
8.19e-28 |
|
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: 114.45 E-value: 8.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTL-----GLTLLRfthriSGEIYINGRETQSV-NLNAL 1285
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLakllnGLLLPT-----SGKVTVDGLDTLDEeNLWEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1286 RQRISFIPQDP--ILFSGTVRS-------NLD-PFDELEDNfLNEALKTSGassmiMAHTDDQKPihitldthvasegSN 1355
Cdd:TIGR04520 76 RKKVGMVFQNPdnQFVGATVEDdvafgleNLGvPREEMRKR-VDEALKLVG-----MEDFRDREP-------------HL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1356 FSQGQKQVLALARAIVRRSKIIILDECTASVD-----DAMdqKIQKTLREAFGdATMLCIAHRLKTIVDYDKVMVLDKGV 1430
Cdd:TIGR04520 137 LSGGQKQRVAIAGVLAMRPDIIILDEATSMLDpkgrkEVL--ETIRKLNKEEG-ITVISITHDMEEAVLADRVIVMNKGK 213
|
....*...
gi 19115470 1431 LVEYGPPA 1438
Cdd:TIGR04520 214 IVAEGTPR 221
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
631-817 |
1.08e-27 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 113.02 E-value: 1.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALL-------GELSLNkG----SYNLP--RSKgVSYVSQVPWLRNATIRDN 697
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLErfydptsGEILLD-GvdirDLNLRwlRSQ-IGLVSQEPVLFDGTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 698 ILFDYPYIEEryKKVIQACGLlTDLQSFVASDL----TEIGEKGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIH 773
Cdd:cd03249 97 IRYGKPDATD--EEVEEAAKK-ANIHDFIMSLPdgydTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 19115470 774 TSNWIykhcfQSSL---MENRTVILVTHNVHLFMDsAAFIVTVKNGS 817
Cdd:cd03249 174 SEKLV-----QEALdraMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQ 214
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1214-1431 |
5.10e-27 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 110.32 E-value: 5.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1214 FNHVSVSYSaaGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRetqsvNLNALRQRISFIP 1293
Cdd:cd03235 2 VEDLTVSYG--GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1294 Q----D---PILFSGTVRSNLDPFDELEDNF-------LNEALKTSGASSMImahtddQKPIhitldthvasegSNFSQG 1359
Cdd:cd03235 75 QrrsiDrdfPISVRDVVLMGLYGHKGLFRRLskadkakVDEALERVGLSELA------DRQI------------GELSGG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115470 1360 QKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGD-ATMLCIAHRLKTIVDY-DKVMVLDKGVL 1431
Cdd:cd03235 137 QQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEYfDRVLLLNRTVV 210
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1212-1429 |
3.08e-26 |
|
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: 106.89 E-value: 3.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYsaAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLN--ALRQRI 1289
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1290 SFIPQDPILFSG-TVRSNLdpfdelednflneALKTSGassmimahtddqkpihitldthvasegsnfsqGQKQVLALAR 1368
Cdd:cd03229 79 GMVFQDFALFPHlTVLENI-------------ALGLSG--------------------------------GQQQRVALAR 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115470 1369 AIVRRSKIIILDECTASVDDAMDQKIQ---KTLREAFGdATMLCIAHRLKTIVDY-DKVMVLDKG 1429
Cdd:cd03229 114 ALAMDPDVLLLDEPTSALDPITRREVRallKSLQAQLG-ITVVLVTHDLDEAARLaDRVVVLRDG 177
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1212-1438 |
4.34e-26 |
|
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: 108.98 E-value: 4.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYsaAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRISF 1291
Cdd:COG1120 2 LEAENLSVGY--GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1292 IPQDPIL-FSGTVR-----------SNLDPFDELEDNFLNEALKTSGASSmiMAHtddqKPIHiTLdthvasegsnfSQG 1359
Cdd:COG1120 80 VPQEPPApFGLTVRelvalgryphlGLFGRPSAEDREAVEEALERTGLEH--LAD----RPVD-EL-----------SGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1360 QKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLRE--AFGDATMLCIAHRLKTIVDY-DKVMVLDKGVLVEYGP 1436
Cdd:COG1120 142 ERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNLAARYaDRLVLLKDGRIVAQGP 221
|
..
gi 19115470 1437 PA 1438
Cdd:COG1120 222 PE 223
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1212-1439 |
4.94e-26 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 107.83 E-value: 4.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAaGPTILKDVNLHINPSEKVAVVGRTGSGKStlglTLLRFTHRI----SGEIYINGRETQSVN---LNA 1284
Cdd:COG2884 2 IRFENVSKRYPG-GREALSDVSLEIEKGEFVFLTGPSGAGKS----TLLKLLYGEerptSGQVLVNGQDLSRLKrreIPY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1285 LRQRISFIPQD-PILFSGTVRSNL---------DPfDELEDNfLNEALKTSGassmiMAHTDDQKPIHItldthvasegs 1354
Cdd:COG2884 77 LRRRIGVVFQDfRLLPDRTVYENValplrvtgkSR-KEIRRR-VREVLDLVG-----LSDKAKALPHEL----------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1355 nfSQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLRE--AFGdATMLcIA-HRLKTIVDYDK-VMVLDKGV 1430
Cdd:COG2884 139 --SGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEinRRG-TTVL-IAtHDLELVDRMPKrVLELEDGR 214
|
....*....
gi 19115470 1431 LVEYGPPAV 1439
Cdd:COG2884 215 LVRDEARGV 223
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1212-1444 |
5.72e-26 |
|
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: 108.14 E-value: 5.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYsaAGPTILKDVNLHINPSEKVAVVGRTGSGKSTL-----GltLLRFThriSGEIYINGRETQSVN---LN 1283
Cdd:COG1127 6 IEVRNLTKSF--GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLlkliiG--LLRPD---SGEILVDGQDITGLSekeLY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1284 ALRQRISFIPQDPILFSG-TVRSNLD-PFDELEDnfLNEALKTSGASSMI----MAHTDDQKPihitldthvaSEgsnFS 1357
Cdd:COG1127 79 ELRRRIGMLFQGGALFDSlTVFENVAfPLREHTD--LSEAEIRELVLEKLelvgLPGAADKMP----------SE---LS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1358 QG-QKQVlALARAIVRRSKIIILDECTASVD----DAMDQKIqKTLREAFGdATMLCIAHRLKTIVDY-DKVMVLDKGVL 1431
Cdd:COG1127 144 GGmRKRV-ALARALALDPEILLYDEPTAGLDpitsAVIDELI-RELRDELG-LTSVVVTHDLDSAFAIaDRVAVLADGKI 220
|
250
....*....|...
gi 19115470 1432 VEYGPPAVLYHNN 1444
Cdd:COG1127 221 IAEGTPEELLASD 233
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1220-1450 |
9.13e-26 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 114.04 E-value: 9.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1220 SYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRISFIPQDPILF 1299
Cdd:PRK10789 322 TYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLF 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1300 SGTVRSNLdpfdelednflneALKTSGASSMIMAHTDDQKPIHITL-------DTHVASEGSNFSQGQKQVLALARAIVR 1372
Cdd:PRK10789 402 SDTVANNI-------------ALGRPDATQQEIEHVARLASVHDDIlrlpqgyDTEVGERGVMLSGGQKQRISIARALLL 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19115470 1373 RSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAHRLKTIVDYDKVMVLDKGVLVEYGPPAVLYHNNGHFRRM 1450
Cdd:PRK10789 469 NAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDM 546
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1212-1437 |
9.66e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 108.54 E-value: 9.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRISF 1291
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1292 IPQDP------------ILFsGTVRSNLDPfDELEDNFLNEALKTSgassmimahtddqkpihitLDTHVASEGSNFSQG 1359
Cdd:PRK13632 88 IFQNPdnqfigatveddIAF-GLENKKVPP-KKMKDIIDDLAKKVG-------------------MEDYLDKEPQNLSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1360 QKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLRE--AFGDATMLCIAHRLKTIVDYDKVMVLDKGVLVEYGPP 1437
Cdd:PRK13632 147 QKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKP 226
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
626-817 |
1.66e-25 |
|
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: 106.55 E-value: 1.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 626 PGDFCLRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGS----------YNLP--RSKgVSYVSQVPWLRNAT 693
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSilidgqdireVTLDslRRA-IGVVPQDTVLFNDT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 694 IRDNILFDYPYI-EERYKKVIQACGLLTDLQSFVASDLTEIGEKGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDI 772
Cdd:cd03253 91 IGYNIRYGRPDAtDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 19115470 773 HTSNWIYKHCfqSSLMENRTVILVTHNVHLFMDSAAFIVtVKNGS 817
Cdd:cd03253 171 HTEREIQAAL--RDVSKGRTTIVIAHRLSTIVNADKIIV-LKDGR 212
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
631-816 |
2.25e-25 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 105.28 E-value: 2.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGS----------YNLP--RSKgVSYVSQVPWLRNATIRDNI 698
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEiyldgkplsaMPPPewRRQ-VAYVPQEPALWGGTVRDNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 699 LFDYPYIEERYKKViQACGLLTDLQsFVASDLteigEKGVT-LSGGQKQRIALARA-VYSPtSIVLMDDVFSALDIHTS- 775
Cdd:COG4619 95 PFPFQLRERKFDRE-RALELLERLG-LPPDIL----DKPVErLSGGERQRLALIRAlLLQP-DVLLLDEPTSALDPENTr 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 19115470 776 ---NWIYKHCFQsslmENRTVILVTHNVHLFMDSAAFIVTVKNG 816
Cdd:COG4619 168 rveELLREYLAE----EGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
380-799 |
4.23e-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: 111.68 E-value: 4.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 380 RSRFvqnKSGDSkVGRsnnlISTDVDDIGeirefiHIIVRA--PVEIAGSIYLLQKLLGWSAYVGLALTVLTC-SVPIVL 456
Cdd:TIGR02868 104 RRRL---RRGDL-LGR----LGADVDALQ------DLYVRVivPAGVALVVGAAAVAAIAVLSVPAALILAAGlLLAGFV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 457 GPLVAkltLRANRATDSRIE-LMSELLQSIRIT-------KFFGWELPMLDRVkQRRQVEL----NRTWKLLLMEICIQV 524
Cdd:TIGR02868 170 APLVS---LRAARAAEQALArLRGELAAQLTDAldgaaelVASGALPAALAQV-EEADRELtraeRRAAAATALGAALTL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 525 LVESLPVFSMFATFVvfTTIMGQTITPS----IAFTSISLFSfirtQFSWIAYLMRQIVQIFVSIGRVSDFLNDPDEVDP 600
Cdd:TIGR02868 246 LAAGLAVLGALWAGG--PAVADGRLAPVtlavLVLLPLAAFE----AFAALPAAAQQLTRVRAAAERIVEVLDAAGPVAE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 601 VNTIEDTSQEIGFFNASLTWVSNPSPGD-FCLRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYNL----- 674
Cdd:TIGR02868 320 GSAPAAGAVGLGKPTLELRDLSAGYPGApPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLdgvpv 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 675 ------PRSKGVSYVSQVPWLRNATIRDNILFDYPYI-EERYKKVIQACGLLTDLQSFVASDLTEIGEKGVTLSGGQKQR 747
Cdd:TIGR02868 400 ssldqdEVRRRVSVCAQDAHLFDTTVRENLRLARPDAtDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQR 479
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 19115470 748 IALARAVYSPTSIVLMDDVFSALDIHTSNWIYKHCFQSslMENRTVILVTHN 799
Cdd:TIGR02868 480 LALARALLADAPILLLDEPTEHLDAETADELLEDLLAA--LSGRTVVLITHH 529
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
314-566 |
5.89e-25 |
|
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: 106.56 E-value: 5.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 314 PIALNRLLKHL-ESPSSSSVNPLVWIVLLLTGPFLTSLFTQFYLFMSTRYLARSYTTLVQQIYNKVIR--SRFVQNKSgd 390
Cdd:cd18594 17 PLLLGRLVAYFvPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKKTLKlsSSALSKIT-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 391 skVGRSNNLISTDVDDIGEIREFIHIIVRAPVEIAGSIYLLQKLLGWSAYVGLALTVLTCSVPIVLGPLVAKLTLRANRA 470
Cdd:cd18594 95 --TGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFAKYRRKTAGL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 471 TDSRIELMSELLQSIRITKFFGWELPMLDRVKQRRQVELNRTWKLLLMEICIQVLVESLPVFSMFATFVVFTTiMGQTIT 550
Cdd:cd18594 173 TDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPYVL-TGNTLT 251
|
250
....*....|....*.
gi 19115470 551 PSIAFTSISLFSFIRT 566
Cdd:cd18594 252 ARKVFTVISLLNALRM 267
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1215-1435 |
1.03e-24 |
|
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: 102.51 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1215 NHVSVSYSaaGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRISFIPQ 1294
Cdd:cd03214 3 ENLSVGYG--GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1295 dpilfsgtvrsnldpfdelednflneALKTSGASSMImahtddQKPIHiTLdthvasegsnfSQGQKQVLALARAIVRRS 1374
Cdd:cd03214 81 --------------------------ALELLGLAHLA------DRPFN-EL-----------SGGERQRVLLARALAQEP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115470 1375 KIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIA--HRLKTIVDY-DKVMVLDKGVLVEYG 1435
Cdd:cd03214 117 PILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMvlHDLNLAARYaDRVILLKDGRIVAQG 180
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1212-1436 |
1.07e-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: 104.20 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAAGPTI--LKDVNLHINPSEKVAVVGRTGSGKSTLgLTLLRFTHR-ISGEIYINGRETQSVN---LNAL 1285
Cdd:cd03258 2 IELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTL-IRCINGLERpTSGSVLVDGTDLTLLSgkeLRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1286 RQRISFIPQDPILFSG-TVRSNLD--------PFDELEDNfLNEALKTSGassmiMAHTDDQKPihitldthvasegSNF 1356
Cdd:cd03258 81 RRRIGMIFQHFNLLSSrTVFENVAlpleiagvPKAEIEER-VLELLELVG-----LEDKADAYP-------------AQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1357 SQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLRE---AFGdATMLCIAHRLKTIVDY-DKVMVLDKGVLV 1432
Cdd:cd03258 142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDinrELG-LTIVLITHEMEVVKRIcDRVAVMEKGEVV 220
|
....
gi 19115470 1433 EYGP 1436
Cdd:cd03258 221 EEGT 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
646-798 |
1.13e-24 |
|
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: 103.82 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 646 VIGPTGSGKSSLISALLGELSLNKGSYNL---------PR--SKGVSYVSQVPWLRNATIRDNILFDYPYIE-ERYKKVI 713
Cdd:cd03245 35 IIGRVGSGKSTLLKLLAGLYKPTSGSVLLdgtdirqldPAdlRRNIGYVPQDVTLFYGTLRDNITLGAPLADdERILRAA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 714 QACGLLTDLQSFVASDLTEIGEKGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIyKHCFQSSLmENRTV 793
Cdd:cd03245 115 ELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERL-KERLRQLL-GDKTL 192
|
....*
gi 19115470 794 ILVTH 798
Cdd:cd03245 193 IIITH 197
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1212-1419 |
1.18e-24 |
|
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: 103.72 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAAGPT--ILKDVNLHINPSEKVAVVGRTGSGKSTLgL----TLLRFThriSGEIYINGRETQSVNLNAL 1285
Cdd:cd03255 1 IELKNLSKTYGGGGEKvqALKGVSLSIEKGEFVAIVGPSGSGKSTL-LnilgGLDRPT---SGEVRVDGTDISKLSEKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1286 ----RQRISFIPQD----PILfsgTVRSNL--------DPFDELEDNFLnEALKTSGassmiMAHTDDQKPihitldthv 1349
Cdd:cd03255 77 aafrRRHIGFVFQSfnllPDL---TALENVelplllagVPKKERRERAE-ELLERVG-----LGDRLNHYP--------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1350 asegSNFSQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLRE---AFG--------DATMLCIAHRLKTIV 1418
Cdd:cd03255 139 ----SELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnkEAGttivvvthDPELAEYADRIIELR 214
|
.
gi 19115470 1419 D 1419
Cdd:cd03255 215 D 215
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
626-816 |
1.81e-24 |
|
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: 101.17 E-value: 1.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 626 PGDFCLRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSynlprskgvsyvsqvpwlrnATIRDNILFDYPYI 705
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGE--------------------ILIDGKDIAKLPLE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 706 EERYKkviqaCGLLtdLQsfvasdlteigekgvtLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKhCFQS 785
Cdd:cd00267 70 ELRRR-----IGYV--PQ----------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLE-LLRE 125
|
170 180 190
....*....|....*....|....*....|.
gi 19115470 786 SLMENRTVILVTHNVHLFMDSAAFIVTVKNG 816
Cdd:cd00267 126 LAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
631-811 |
3.70e-24 |
|
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: 102.19 E-value: 3.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVF-PRNKLSIViGPTGSGKSSLISALLGELSLNKGSY--------NLP----RSKgVSYVSQVPWLRNATIRDN 697
Cdd:cd03244 20 LKNISFSIkPGEKVGIV-GRTGSGKSSLLLALFRLVELSSGSIlidgvdisKIGlhdlRSR-ISIIPQDPVLFSGTIRSN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 698 I-LFDYpYIEERYKKVIQACGLLTDLQSFVASDLTEIGEKGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSN 776
Cdd:cd03244 98 LdPFGE-YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDA 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 19115470 777 WIykhcfQSSLME---NRTVILVTHNVHLFMDSAAFIV 811
Cdd:cd03244 177 LI-----QKTIREafkDCTVLTIAHRLDTIIDSDRILV 209
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1212-1435 |
4.14e-24 |
|
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: 101.47 E-value: 4.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVS----YSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTL--GLTLLRFTHRISGEIYINGRetqSVNLNAL 1285
Cdd:cd03213 4 LSFRNLTVTvkssPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLlnALAGRRTGLGVSGEVLINGR---PLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1286 RQRISFIPQDPILFSG-TVRSNLDpfdelednflnealktsgassmimahtddqkpihitldthVASEGSNFSQGQKQVL 1364
Cdd:cd03213 81 RKIIGYVPQDDILHPTlTVRETLM----------------------------------------FAAKLRGLSGGERKRV 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115470 1365 ALARAIVRRSKIIILDECTASVDDAMDQKIQKTLRE-AFGDATMLCIAHRLKTIV--DYDKVMVLDKGVLVEYG 1435
Cdd:cd03213 121 SIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSEIfeLFDKLLLLSQGRVIYFG 194
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
299-588 |
5.34e-24 |
|
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: 103.84 E-value: 5.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 299 MGVSSFMVSVCQFLSPIALNRLLKHLESPSSSSVNPLVWI----VLLLTgpFLTSLFTQFYLFMSTRYLARSYTTLVQQI 374
Cdd:cd18593 2 LGIFLFLEEAIRVVQPIFLGKLIRYFEGNGSSISLTEAYLyaggVSLCS--FLFIITHHPYFFGMQRIGMRLRVACSSLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 375 YNKVIRsrfVQNKS-GDSKVGRSNNLISTDVD--DIGEIreFIHIIVRAPVEIAGSIYLLQKLLGWSAYVGLAltVLTCS 451
Cdd:cd18593 80 YRKALR---LSQAAlGKTTVGQIVNLLSNDVNrfDQAVL--FLHYLWVAPLQLIAVIYILWFEIGWSCLAGLA--VLLIL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 452 VPI--VLGPLVAKLTLRANRATDSRIELMSELLQSIRITKFFGWELPMLDRVKQRRQVELNRTWK---LLLMEICIQVLV 526
Cdd:cd18593 153 IPLqsFFGKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRtsfLRALNMGLFFVS 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115470 527 ESLPVFSMFATFVvfttIMGQTITPSIAFTSISLFSFIRTQFSWiaYLMRQIVQIF---VSIGRV 588
Cdd:cd18593 233 SKLILFLTFLAYI----LLGNILTAERVFVTMALYNAVRLTMTL--FFPFAIQFGSelsVSIRRI 291
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1212-1433 |
5.42e-24 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 102.04 E-value: 5.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYS--AAGPTILKDVNLHINPSEKVAVVGRTGSGKSTL----GLtLLRFThriSGEIYINGRETQSVNLNAL 1285
Cdd:COG1136 5 LELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLlnilGG-LDRPT---SGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1286 ----RQRISFIPQDPILFSG-TVRSN------LDPFDELEDNF-LNEALKTSGassmiMAHTDDQKPihitldthvaseg 1353
Cdd:COG1136 81 arlrRRHIGFVFQFFNLLPElTALENvalpllLAGVSRKERRErARELLERVG-----LGDRLDHRP------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1354 SNFSQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLRE---AFGdATMLCIAHRLKtIVDY-DKVMVLDKG 1429
Cdd:COG1136 143 SQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnrELG-TTIVMVTHDPE-LAARaDRVIRLRDG 220
|
....
gi 19115470 1430 VLVE 1433
Cdd:COG1136 221 RIVS 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1212-1431 |
1.04e-23 |
|
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: 99.39 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYsaAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSvNLNALRQRISF 1291
Cdd:cd03230 1 IEVRNLSKRY--GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1292 IPQDPILFSG-TVRSNLDpfdelednflnealktsgassmimahtddqkpihitldthvasegsnFSQGQKQVLALARAI 1370
Cdd:cd03230 78 LPEEPSLYENlTVRENLK-----------------------------------------------LSGGMKQRLALAQAL 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19115470 1371 VRRSKIIILDECTASVDDAMDQKIQKTLRE-AFGDATMLCIAHRLKTIVDY-DKVMVLDKGVL 1431
Cdd:cd03230 111 LHDPELLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1212-1438 |
1.72e-23 |
|
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: 101.31 E-value: 1.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSaaGPTILKDVNLHINPSEKVAVVGRTGSGKSTLgLTLL-RFTHRISG-EIYINGRETQSVNLNALRQRI 1289
Cdd:COG1119 4 LELRNVTVRRG--GKTILDDISWTVKPGEHWAILGPNGAGKSTL-LSLItGDLPPTYGnDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1290 SFI-P--QDPILFSGTVR--------SNLDPFDELEDNFLNEA---LKTSGASSMImahtddQKPIHiTLdthvasegsn 1355
Cdd:COG1119 81 GLVsPalQLRFPRDETVLdvvlsgffDSIGLYREPTDEQRERArelLELLGLAHLA------DRPFG-TL---------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1356 fSQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLRE--AFGDATMLCIAHRLKTIVD-YDKVMVLDKGVLV 1432
Cdd:COG1119 144 -SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEEIPPgITHVLLLKDGRVV 222
|
....*.
gi 19115470 1433 EYGPPA 1438
Cdd:COG1119 223 AAGPKE 228
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1212-1440 |
1.79e-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: 100.65 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSaaGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVN---LNALRQR 1288
Cdd:cd03261 1 IELRGLTKSFG--GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1289 ISFIPQDPILFSG-TVRSNL--------DPFDELEDNFLNEALKTSGassmiMAHTDDQKPihitldthvasegSNFSQG 1359
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVafplrehtRLSEEEIREIVLEKLEAVG-----LRGAEDLYP-------------AELSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1360 QKQVLALARAIVRRSKIIILDECTASVD----DAMDQKIQkTLREAFGdATMLCIAHRLKTIVDY-DKVMVLDKGVLVEY 1434
Cdd:cd03261 141 MKKRVALARALALDPELLLYDEPTAGLDpiasGVIDDLIR-SLKKELG-LTSIMVTHDLDTAFAIaDRIAVLYDGKIVAE 218
|
....*.
gi 19115470 1435 GPPAVL 1440
Cdd:cd03261 219 GTPEEL 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
631-805 |
2.53e-23 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 99.53 E-value: 2.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYNLP------RSKGVSYVSQ---VPWLRNATIRDNIL-- 699
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFgkplekERKRIGYVPQrrsIDRDFPISVRDVVLmg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 700 ------FDYPYIEERYKKVIQAcglltdLQSFVASDLTE--IGEkgvtLSGGQKQRIALARAVYSPTSIVLMDDVFSALD 771
Cdd:cd03235 95 lyghkgLFRRLSKADKAKVDEA------LERVGLSELADrqIGE----LSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
|
170 180 190
....*....|....*....|....*....|....
gi 19115470 772 IHTSNWIYKHcFQSSLMENRTVILVTHNVHLFMD 805
Cdd:cd03235 165 PKTQEDIYEL-LRELRREGMTILVVTHDLGLVLE 197
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1212-1426 |
3.63e-23 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 107.81 E-value: 3.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAAGPT-ILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYIN-GRETQSVNLNALRQRI 1289
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVeIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKWWRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1290 SFIPQDPILFSGTVRSN----LDPFDELE--DNFLNE---------------ALKTSGASSMIMAHTDDQKPIHI----- 1343
Cdd:PTZ00265 463 GVVSQDPLLFSNSIKNNikysLYSLKDLEalSNYYNEdgndsqenknkrnscRAKCAGDLNDMSNTTDSNELIEMrknyq 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1344 -------------------------TLDTHVASEGSNFSQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTL 1398
Cdd:PTZ00265 543 tikdsevvdvskkvlihdfvsalpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
|
250 260 270
....*....|....*....|....*....|
gi 19115470 1399 REAFGDAT--MLCIAHRLKTIVDYDKVMVL 1426
Cdd:PTZ00265 623 NNLKGNENriTIIIAHRLSTIRYANTIFVL 652
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
336-802 |
3.74e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 106.73 E-value: 3.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 336 VWIVLLLTgpfLTSLFTQFYLFMSTRYLarsYTTLVQQIYNKVIRSR-------FVQNKSGD--SKVGRSNNLISTDVDD 406
Cdd:TIGR00958 204 IFFMCLLS---IASSVSAGLRGGSFNYT---MARINLRIREDLFRSLlrqdlgfFDENKTGEltSRLSSDTQTMSRSLSL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 407 igeireFIHIIVRAPVEIAGSIYLLQKLLGWSAYVGLALTVLTCSVPIVLGPLVAKLTLRANRATDSRIELMSELLQSIR 486
Cdd:TIGR00958 278 ------NVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 487 ITKFFGWELPMLDRVKQRRQVELNRTWKLLLMEIciqVLVESLPVFSMFatfvVFTTIM---GQTITPSiAFTSISLFSF 563
Cdd:TIGR00958 352 TVRSFAAEEGEASRFKEALEETLQLNKRKALAYA---GYLWTTSVLGML----IQVLVLyygGQLVLTG-KVSSGNLVSF 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 564 IRTQFSWIAYLmRQIVQIFVSI-------GRVSDFLNDPDEVDPVNTIEDTSQE--IGFFNASLTWVSNPS-PgdfCLRD 633
Cdd:TIGR00958 424 LLYQEQLGEAV-RVLSYVYSGMmqavgasEKVFEYLDRKPNIPLTGTLAPLNLEglIEFQDVSFSYPNRPDvP---VLKG 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 634 LNIVFPRNKLSIVIGPTGSGKSSLISALL-------GELSLNkgsyNLPRS--------KGVSYVSQVPWLRNATIRDNI 698
Cdd:TIGR00958 500 LTFTLHPGEVVALVGPSGSGKSTVAALLQnlyqptgGQVLLD----GVPLVqydhhylhRQVALVGQEPVLFSGSVRENI 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 699 LFDYPYIE-ERYKKVIQACGLLTDLQSFVASDLTEIGEKGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNW 777
Cdd:TIGR00958 576 AYGLTDTPdEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQL 655
|
490 500
....*....|....*....|....*
gi 19115470 778 IYkhcfQSSLMENRTVILVTHNVHL 802
Cdd:TIGR00958 656 LQ----ESRSRASRTVLLIAHRLST 676
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1212-1450 |
5.44e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 100.47 E-value: 5.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLT---LLRFThriSGEIYINGRETQSVNLNALRQR 1288
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLlngLLLPE---AGTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1289 ISFIPQDPI-LFSG-TVRSNLD--------PFDELEDNfLNEALKTSGassmiMAHTDDQKPIHItldthvasegsnfSQ 1358
Cdd:PRK13635 83 VGMVFQNPDnQFVGaTVQDDVAfglenigvPREEMVER-VDQALRQVG-----MEDFLNREPHRL-------------SG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1359 GQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLRE--AFGDATMLCIAHRLKTIVDYDKVMVLDKGVLVEYGP 1436
Cdd:PRK13635 144 GQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGT 223
|
250
....*....|....
gi 19115470 1437 PAVLYHNNGHFRRM 1450
Cdd:PRK13635 224 PEEIFKSGHMLQEI 237
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
624-798 |
1.31e-22 |
|
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: 98.07 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 624 PSPGDFCLRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGS----------YNLP--RSKgVSYVSQVPWLRN 691
Cdd:cd03251 11 PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRilidghdvrdYTLAslRRQ-IGLVSQDVFLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 692 ATIRDNILFDYPYIEEryKKVIQACGLlTDLQSFVAS-----DlTEIGEKGVTLSGGQKQRIALARAVYSPTSIVLMDDV 766
Cdd:cd03251 90 DTVAENIAYGRPGATR--EEVEEAARA-ANAHEFIMElpegyD-TVIGERGVKLSGGQRQRIAIARALLKDPPILILDEA 165
|
170 180 190
....*....|....*....|....*....|....*
gi 19115470 767 FSALDIHTSNWIykhcfQSS---LMENRTVILVTH 798
Cdd:cd03251 166 TSALDTESERLV-----QAAlerLMKNRTTFVIAH 195
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
631-804 |
1.54e-22 |
|
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: 97.54 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYNL------PRSKGVSYVSQ----VPWLrnaTIRDNILF 700
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepvtGPGPDRGYVFQqdalLPWL---TVLDNVAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 701 -------DYPYIEERYKKVIQACGLLTDLQSFVAsdlteigekgvTLSGGQKQRIALARA-VYSPtSIVLMDDVFSALDI 772
Cdd:cd03293 97 glelqgvPKAEARERAEELLELVGLSGFENAYPH-----------QLSGGMRQRVALARAlAVDP-DVLLLDEPFSALDA 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 19115470 773 HT----SNWIYKHCFQsslmENRTVILVTHNVH--LFM 804
Cdd:cd03293 165 LTreqlQEELLDIWRE----TGKTVLLVTHDIDeaVFL 198
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1212-1435 |
2.08e-22 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 97.20 E-value: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYsaAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQsvNLNALRQRISF 1291
Cdd:cd03259 1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT--GVPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1292 IPQDPILFSG-TVRSNL--------DPFDELEDNfLNEALKtsgasSMIMAHTDDQKPihitldthvasegSNFSQGQKQ 1362
Cdd:cd03259 77 VFQDYALFPHlTVAENIafglklrgVPKAEIRAR-VRELLE-----LVGLEGLLNRYP-------------HELSGGQQQ 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115470 1363 VLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAF--GDATMLCIAHRLKTIVDY-DKVMVLDKGVLVEYG 1435
Cdd:cd03259 138 RVALARALAREPSLLLLDEPLSALDAKLREELREELKELQreLGITTIYVTHDQEEALALaDRIAVMNEGRIVQVG 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1210-1443 |
2.18e-22 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 100.53 E-value: 2.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1210 GDIVFNHVSVSYSAAgpTILKDVNLHINPSEKVAVVGRTGSGKSTL-----GLtllrftHRIS-GEIYINGREtqsVNLN 1283
Cdd:COG3839 2 ASLELENVSKSYGGV--EALKDIDLDIEDGEFLVLLGPSGCGKSTLlrmiaGL------EDPTsGEILIGGRD---VTDL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1284 ALRQR-ISFIPQDPILF-SGTVRSNL--------DPFDELEDNfLNEALKTSGassmiMAHTDDQKPihitldthvaseg 1353
Cdd:COG3839 71 PPKDRnIAMVFQSYALYpHMTVYENIafplklrkVPKAEIDRR-VREAAELLG-----LEDLLDRKP------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1354 SNFSQGQKQVLALARAIVRRSKIIILDECTASVD----DAMDQKIQKTLREaFGdATMLCIAHrlktivDY-------DK 1422
Cdd:COG3839 132 KQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRR-LG-TTTIYVTH------DQveamtlaDR 203
|
250 260
....*....|....*....|.
gi 19115470 1423 VMVLDKGVLVEYGPPAVLYHN 1443
Cdd:COG3839 204 IAVMNDGRIQQVGTPEELYDR 224
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
897-1164 |
3.38e-22 |
|
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: 98.10 E-value: 3.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 897 VAAVLLFFVTTQATSILIDLWVAFWTNSSVNSPDVNNNKFLFVYGTMLLAY---SLLDFLRTVSYDRGAWWASRKLHDSM 973
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGlaqFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 974 LESVFGTFASWFDKTPTGRIVNRFAKDIRSIDMNLSGWLFFSINCFLSVAGGILSVSSAMPIFMIPAVIVCLAGYYFGLL 1053
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1054 YTRAQVGVKRLISIYTSPIFSLLGESIVGVSVIRAFNRQTIFKQMFSERLDNLVRLQSTSYNLNRWVAVRTDGISGLVGA 1133
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....
gi 19115470 1134 IA---GLIALLQKDLSPGVVGFSLNQAVIFSSSV 1164
Cdd:pfam00664 241 LAlwfGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
631-816 |
1.05e-21 |
|
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: 95.23 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALL-------GELSLNKGSYNLPRSK----GVSYVSQVPWLRNATIRDNIL 699
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLEnfyqpqgGQVLLDGKPISQYEHKylhsKVSLVGQEPVLFARSLQDNIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 700 FDYPYIE-ERYKKVIQACGLLTDLQSFVASDLTEIGEKGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWI 778
Cdd:cd03248 110 YGLQSCSfECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQV 189
|
170 180 190
....*....|....*....|....*....|....*...
gi 19115470 779 ykHCFQSSLMENRTVILVTHNVHLfMDSAAFIVTVKNG 816
Cdd:cd03248 190 --QQALYDWPERRTVLVIAHRLST-VERADQILVLDGG 224
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1180-1429 |
2.00e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 100.27 E-value: 2.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1180 SYERVLEYSKLPQEPAPTIAGqvpatwPKEGDIVFNHVSVsYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLgltl 1259
Cdd:COG4178 337 GFEEALEAADALPEAASRIET------SEDGALALEDLTL-RTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTL---- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1260 LRfthRISGeI--YINGRetqsVNLNALrQRISFIPQDPILFSGTVRSNL---DPFDELEDNFLNEALKTSGassmiMAH 1334
Cdd:COG4178 406 LR---AIAG-LwpYGSGR----IARPAG-ARVLFLPQRPYLPLGTLREALlypATAEAFSDAELREALEAVG-----LGH 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1335 TDDQkpihitLDThVASEGSNFSQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAHRL 1414
Cdd:COG4178 472 LAER------LDE-EADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRS 544
|
250
....*....|....*
gi 19115470 1415 KTIVDYDKVMVLDKG 1429
Cdd:COG4178 545 TLAAFHDRVLELTGD 559
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1216-1443 |
2.32e-21 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 94.42 E-value: 2.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1216 HVSVSYSAAgpTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNA-LRQRISFIPQ 1294
Cdd:cd03224 5 NLNAGYGKS--QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1295 DPILFSG-TVRSNL-------------DPFDELEDNFlnealktsgassmimahtddqkPIhitLDTHVASEGSNFSQGQ 1360
Cdd:cd03224 83 GRRIFPElTVEENLllgayarrrakrkARLERVYELF----------------------PR---LKERRKQLAGTLSGGE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1361 KQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLRE-AFGDATMLCI---AHRLKTIVDYdkVMVLDKGVLVEYGP 1436
Cdd:cd03224 138 QQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRElRDEGVTILLVeqnARFALEIADR--AYVLERGRVVLEGT 215
|
....*..
gi 19115470 1437 PAVLYHN 1443
Cdd:cd03224 216 AAELLAD 222
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
631-800 |
2.75e-21 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 95.16 E-value: 2.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSL---ISALL----GELSLNkGSYNLPRSKGVSYVSQ----VPWLrnaTIRDNIL 699
Cdd:COG1116 27 LDDVSLTVAAGEFVALVGPSGCGKSTLlrlIAGLEkptsGEVLVD-GKPVTGPGPDRGVVFQepalLPWL---TVLDNVA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 700 F-------DYPYIEERYKKVIQACGLLTDLQSFVAsdlteigekgvTLSGGQKQRIALARA-VYSPtSIVLMDDVFSALD 771
Cdd:COG1116 103 LglelrgvPKAERRERARELLELVGLAGFEDAYPH-----------QLSGGMRQRVAIARAlANDP-EVLLMDEPFGALD 170
|
170 180 190
....*....|....*....|....*....|....
gi 19115470 772 IHTsnwiyKHCFQSSLME-----NRTVILVTHNV 800
Cdd:COG1116 171 ALT-----RERLQDELLRlwqetGKTVLFVTHDV 199
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1229-1443 |
3.36e-21 |
|
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: 99.37 E-value: 3.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1229 LKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFtHRISGEIYINGRETQSVN---LNALRQRISFIPQDPilFSG---- 1301
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--FGSlspr 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1302 -TV-----------RSNLDPfDELEDNFLnEALKTSGASSMIMahtddQKPIHitldthvasEgsnFSQGQKQVLALARA 1369
Cdd:COG4172 379 mTVgqiiaeglrvhGPGLSA-AERRARVA-EALEEVGLDPAAR-----HRYPH---------E---FSGGQRQRIAIARA 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1370 IVRRSKIIILDECTAsvddAMDQKIQK-------TLREAFGdATMLCIAHRLKtIVDY--DKVMVLDKGVLVEYGPPAVL 1440
Cdd:COG4172 440 LILEPKLLVLDEPTS----ALDVSVQAqildllrDLQREHG-LAYLFISHDLA-VVRAlaHRVMVMKDGKVVEQGPTEQV 513
|
...
gi 19115470 1441 YHN 1443
Cdd:COG4172 514 FDA 516
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1215-1443 |
3.68e-21 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 96.28 E-value: 3.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1215 NHVSVSYSAAGPTI--LKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRF---THRISGEIYINGRETQSVNLNALRQ-- 1287
Cdd:COG0444 5 RNLKVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlppPGITSGEILFDGEDLLKLSEKELRKir 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1288 --RISFIPQDPIlfsgtvrSNLDPF----DELEDnflnealktsgassMIMAHTDDQKP------------IHITLDTHV 1349
Cdd:COG0444 85 grEIQMIFQDPM-------TSLNPVmtvgDQIAE--------------PLRIHGGLSKAeareraiellerVGLPDPERR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1350 AS----EgsnFSQGQKQVLALARAIVRRSKIIILDECTAsvddAMDQKIQ-------KTLREAFGdATMLCIAHRLkTIV 1418
Cdd:COG0444 144 LDryphE---LSGGMRQRVMIARALALEPKLLIADEPTT----ALDVTIQaqilnllKDLQRELG-LAILFITHDL-GVV 214
|
250 260
....*....|....*....|....*..
gi 19115470 1419 DY--DKVMVLDKGVLVEYGPPAVLYHN 1443
Cdd:COG0444 215 AEiaDRVAVMYAGRIVEEGPVEELFEN 241
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
626-798 |
6.25e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 99.15 E-value: 6.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 626 PGDFCLRdlnivfPRNKLSIViGPTGSGKSSLISALLG-------------ELS-LNKGSYNlprsKGVSYVSQVPWLRN 691
Cdd:PRK11174 368 PLNFTLP------AGQRIALV-GPSGAGKTSLLNALLGflpyqgslkingiELReLDPESWR----KHLSWVGQNPQLPH 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 692 ATIRDNILFDYPYI-EERYKKVIQacglLTDLQSFVASDL----TEIGEKGVTLSGGQKQRIALARAVYSPTSIVLMDDV 766
Cdd:PRK11174 437 GTLRDNVLLGNPDAsDEQLQQALE----NAWVSEFLPLLPqgldTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEP 512
|
170 180 190
....*....|....*....|....*....|....*
gi 19115470 767 FSALDIHTSNWIykhcfQSSL---MENRTVILVTH 798
Cdd:PRK11174 513 TASLDAHSEQLV-----MQALnaaSRRQTTLMVTH 542
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
631-798 |
6.88e-21 |
|
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: 91.73 E-value: 6.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGS--------YNLP---RSKGVSYVSQVpwlrnatirdnil 699
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEilldgkdlASLSpkeLARKIAYVPQA------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 700 fdypyIEerykkviqacglLTDLQSFVASDLTEigekgvtLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIY 779
Cdd:cd03214 82 -----LE------------LLGLAHLADRPFNE-------LSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELL 137
|
170
....*....|....*....
gi 19115470 780 KHCFQSSLMENRTVILVTH 798
Cdd:cd03214 138 ELLRRLARERGKTVVMVLH 156
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1216-1429 |
9.07e-21 |
|
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: 91.93 E-value: 9.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1216 HVSVSYSAaGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRetqSVNLNALRQRISFIPQD 1295
Cdd:cd03226 4 NISFSYKK-GTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK---PIKAKERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1296 P--ILFSGTVRSNLDPFDELEDNFLNEA---LKTSGassmimahtddqkpIHITLDTHVASegsnFSQGQKQVLALARAI 1370
Cdd:cd03226 80 VdyQLFTDSVREELLLGLKELDAGNEQAetvLKDLD--------------LYALKERHPLS----LSGGQKQRLAIAAAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19115470 1371 VRRSKIIILDECTASVD-DAMDQ--KIQKTLREAfgDATMLCIAHRLKTIVDY-DKVMVLDKG 1429
Cdd:cd03226 142 LSGKDLLIFDEPTSGLDyKNMERvgELIRELAAQ--GKAVIVITHDYEFLAKVcDRVLLLANG 202
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1212-1431 |
9.54e-21 |
|
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: 92.21 E-value: 9.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSaaGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRE--TQSVNLNALRQRI 1289
Cdd:cd03262 1 IEIKNLHKSFG--DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKltDDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1290 SFIPQDPILFSG-TVRSNLD---------PFDELEDNFLnEALKTSGassmiMAHTDDQKPIHItldthvasegsnfSQG 1359
Cdd:cd03262 79 GMVFQQFNLFPHlTVLENITlapikvkgmSKAEAEERAL-ELLEKVG-----LADKADAYPAQL-------------SGG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115470 1360 QKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLRE-AFGDATMLCIAHRLKTIVDY-DKVMVLDKGVL 1431
Cdd:cd03262 140 QQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDlAEEGMTMVVVTHEMGFAREVaDRVIFMDDGRI 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
631-802 |
2.09e-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: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGS---YNLPRSKG---VSYVSQ---VPWLRNATIRDNIL-- 699
Cdd:COG1121 22 LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTvrlFGKPPRRArrrIGYVPQraeVDWDFPITVRDVVLmg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 700 ------FDYPYIEERYKKVIQAcgL-LTDLQSFvASDLteIGEkgvtLSGGQKQRIALARAVYSPTSIVLMDDVFSALDI 772
Cdd:COG1121 102 rygrrgLFRRPSRADREAVDEA--LeRVGLEDL-ADRP--IGE----LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDA 172
|
170 180 190
....*....|....*....|....*....|....*
gi 19115470 773 HTSNWIYKhcfqssLM-----ENRTVILVTHNVHL 802
Cdd:COG1121 173 ATEEALYE------LLrelrrEGKTILVVTHDLGA 201
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1209-1427 |
3.21e-20 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 98.18 E-value: 3.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1209 EGDIVFNHVSVSY-SAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRF-----THRI---------------- 1266
Cdd:PTZ00265 1163 KGKIEIMDVNFRYiSRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlknDHHIvfknehtndmtneqdy 1242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1267 ---------------------------------SGEIYINGRETQSVNLNALRQRISFIPQDPILFSGTVRSNLDPFDE- 1312
Cdd:PTZ00265 1243 qgdeeqnvgmknvnefsltkeggsgedstvfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEd 1322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1313 --LEDnfLNEALKTSGASSMIMAHTDDqkpihitLDTHVASEGSNFSQGQKQVLALARAIVRRSKIIILDECTASVDDAM 1390
Cdd:PTZ00265 1323 atRED--VKRACKFAAIDEFIESLPNK-------YDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS 1393
|
250 260 270
....*....|....*....|....*....|....*....
gi 19115470 1391 DQKIQKTLREA--FGDATMLCIAHRLKTIVDYDKVMVLD 1427
Cdd:PTZ00265 1394 EKLIEKTIVDIkdKADKTIITIAHRIASIKRSDKIVVFN 1432
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
631-798 |
5.18e-20 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 90.27 E-value: 5.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSL---ISALL----GELSLN-KGSYNLP-RSKGVSYVSQ----VPWLrnaTIRDN 697
Cdd:cd03259 16 LDDLSLTVEPGEFLALLGPSGCGKTTLlrlIAGLErpdsGEILIDgRDVTGVPpERRNIGMVFQdyalFPHL---TVAEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 698 ILF-------DYPYIEERYKKVIQACGLLTDLQSFVAsdlteigekgvTLSGGQKQRIALARAVYSPTSIVLMDDVFSAL 770
Cdd:cd03259 93 IAFglklrgvPKAEIRARVRELLELVGLEGLLNRYPH-----------ELSGGQQQRVALARALAREPSLLLLDEPLSAL 161
|
170 180
....*....|....*....|....*....
gi 19115470 771 DIHTSNWIYKHcFQSSLMENR-TVILVTH 798
Cdd:cd03259 162 DAKLREELREE-LKELQRELGiTTIYVTH 189
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1229-1446 |
6.33e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 91.44 E-value: 6.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1229 LKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRISFIPQDP------------ 1296
Cdd:COG4167 29 VKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMIFQDPntslnprlnigq 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1297 ILfSGTVRSNLDpFDELEDNFL-NEALKTSGassMIMAHTDDqkPIHItldthvasegsnFSQGQKQVLALARAIVRRSK 1375
Cdd:COG4167 109 IL-EEPLRLNTD-LTAEEREERiFATLRLVG---LLPEHANF--YPHM------------LSSGQKQRVALARALILQPK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1376 IIILDECTASVDDAMDQKI-------QKTLREAFgdatmLCIAHRL---KTIVdyDKVMVLDKGVLVEYGPPAVLYHNNG 1445
Cdd:COG4167 170 IIIADEALAALDMSVRSQIinlmlelQEKLGISY-----IYVSQHLgivKHIS--DKVLVMHQGEVVEYGKTAEVFANPQ 242
|
.
gi 19115470 1446 H 1446
Cdd:COG4167 243 H 243
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1212-1400 |
6.61e-20 |
|
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: 89.46 E-value: 6.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYsaAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLgltlLR----FTHRISGEIYINGRETQSvNLNALRQ 1287
Cdd:COG4133 3 LEAENLSCRR--GERLLFSGLSFTLAAGEALALTGPNGSGKTTL----LRilagLLPPSAGEVLWNGEPIRD-AREDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1288 RISFIPQDPILFSG-TVRSNLDpfdelednFLNEALKTSGASSMIMAHTDdqkpiHITLDTHVASEGSNFSQGQKQVLAL 1366
Cdd:COG4133 76 RLAYLGHADGLKPElTVRENLR--------FWAALYGLRADREAIDEALE-----AVGLAGLADLPVRQLSAGQKRRVAL 142
|
170 180 190
....*....|....*....|....*....|....
gi 19115470 1367 ARAIVRRSKIIILDECTASVDDAMDQKIQKTLRE 1400
Cdd:COG4133 143 ARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA 176
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
314-798 |
8.03e-20 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 95.54 E-value: 8.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 314 PIALNRLLKHLESPSSSS-VNPLVWIVLLLTGPFLTSLFTQFYLFmsTRYLARSYTTLVQQIYNKVIR---SRFVQNKSG 389
Cdd:TIGR02204 38 PYAVRLMIDHGFSKDSSGlLNRYFAFLLVVALVLALGTAARFYLV--TWLGERVVADIRRAVFAHLISlspSFFDKNRSG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 390 DskvgrsnnLISTDVDDIGEIREFI----HIIVRAPVEIAGSIYLLqkllgWSAYVGLALTVLTcSVPIVLGPLVA---K 462
Cdd:TIGR02204 116 E--------VVSRLTTDTTLLQSVIgsslSMALRNALMCIGGLIMM-----FITSPKLTSLVLL-AVPLVLLPILLfgrR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 463 LTLRANRATDSRIELMS---ELLQSIRITKFFGWElpmlDRVKQRRQVELNRTWKLLLMEICIQVLVESLPVFSMFATFV 539
Cdd:TIGR02204 182 VRKLSRESQDRIADAGSyagETLGAIRTVQAFGHE----DAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 540 VFTTIMGQ-TITPSIAFTSISLFSF----IRTQFSWIAYLMRQIVQIFVSIGRVSDFLNDPDEV----DPVNTIEDTSQE 610
Cdd:TIGR02204 258 GVLWVGAHdVIAGKMSAGTLGQFVFyavmVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIkapaHPKTLPVPLRGE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 611 IGFFNASLTWVSNPSpgDFCLRDLNI-VFPRNKLSIViGPTGSGKSSLISALLGELSLNKGSYNL---------PRS--K 678
Cdd:TIGR02204 338 IEFEQVNFAYPARPD--QPALDGLNLtVRPGETVALV-GPSGAGKSTLFQLLLRFYDPQSGRILLdgvdlrqldPAElrA 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 679 GVSYVSQVPWLRNATIRDNILFDYPYIE----ERYKKVIQACGLLTDLQSFVAsdlTEIGEKGVTLSGGQKQRIALARAV 754
Cdd:TIGR02204 415 RMALVPQDPVLFAASVMENIRYGRPDATdeevEAAARAAHAHEFISALPEGYD---TYLGERGVTLSGGQRQRIAIARAI 491
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 19115470 755 YSPTSIVLMDDVFSALDIHTsnwiyKHCFQSSL---MENRTVILVTH 798
Cdd:TIGR02204 492 LKDAPILLLDEATSALDAES-----EQLVQQALetlMKGRTTLIIAH 533
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
631-798 |
9.64e-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: 90.49 E-value: 9.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGS--------YNLP---RSKGVSYVSQ---VPWlrNATIRD 696
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEvlldgrdlASLSrreLARRIAYVPQeppAPF--GLTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 697 NILF-DYPYI-------EERYKKVIQAcgL-LTDLQSFVASDLTEigekgvtLSGGQKQRIALARAVYSPTSIVLMDDVF 767
Cdd:COG1120 95 LVALgRYPHLglfgrpsAEDREAVEEA--LeRTGLEHLADRPVDE-------LSGGERQRVLIARALAQEPPLLLLDEPT 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 19115470 768 SALDIHtsnwiykHcfQSSLME---------NRTVILVTH 798
Cdd:COG1120 166 SHLDLA-------H--QLEVLEllrrlarerGRTVVMVLH 196
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1212-1436 |
1.10e-19 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 92.06 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAAGPTI--LKDVNLHINPSEKVAVVGRTGSGKSTLG--LTLL-RFThriSGEIYINGRETQSVN---LN 1283
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIrcINLLeRPT---SGSVLVDGVDLTALSereLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1284 ALRQRISFIPQDPILFSG-TVRSNLdpfdELednflneALKTSGAS---------SMI----MAHTDDQKPihitldthv 1349
Cdd:COG1135 79 AARRKIGMIFQHFNLLSSrTVAENV----AL-------PLEIAGVPkaeirkrvaELLelvgLSDKADAYP--------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1350 asegSNFSQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREA---FGdATMLCIAHRL---KTIVdyDKV 1423
Cdd:COG1135 139 ----SQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDInreLG-LTIVLITHEMdvvRRIC--DRV 211
|
250
....*....|...
gi 19115470 1424 MVLDKGVLVEYGP 1436
Cdd:COG1135 212 AVLENGRIVEQGP 224
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1212-1432 |
1.25e-19 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 87.48 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAAgpTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLN-ALRQRIS 1290
Cdd:cd03216 1 LELRGITKRFGGV--KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRdARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1291 FIPQdpilfsgtvrsnldpfdelednflnealktsgassmimahtddqkpihitldthvasegsnFSQGQKQVLALARAI 1370
Cdd:cd03216 79 MVYQ-------------------------------------------------------------LSVGERQMVEIARAL 97
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115470 1371 VRRSKIIILDECTASVDDAMDQKIQKTLRE--AFGdATMLCIAHRLKTIVDY-DKVMVLDKGVLV 1432
Cdd:cd03216 98 ARNARLLILDEPTAALTPAEVERLFKVIRRlrAQG-VAVIFISHRLDEVFEIaDRVTVLRDGRVV 161
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1229-1437 |
1.59e-19 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 89.32 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1229 LKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETqsVNLNALRQRISFIPQDPILFsgtvrSNLD 1308
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI--TNLPPEKRDISYVPQNYALF-----PHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1309 PFDELEDNFLNEALKTSG--------ASSMIMAHTDDQKPihITLdthvasegsnfSQGQKQVLALARAIVRRSKIIILD 1380
Cdd:cd03299 88 VYKNIAYGLKKRKVDKKEierkvleiAEMLGIDHLLNRKP--ETL-----------SGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115470 1381 ECTAsvddAMDQKIQKTLREAFGDA------TMLCIAHRLKTI-VDYDKVMVLDKGVLVEYGPP 1437
Cdd:cd03299 155 EPFS----ALDVRTKEKLREELKKIrkefgvTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKP 214
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1212-1440 |
1.74e-19 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 88.72 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLgLTLLRFTHRI-SGEIYINGRETQSvNLNALRQRIS 1290
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTT-LKMLTGELRPtSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1291 FIPQDPILFSG-TVRSNLdpfdelednflnealktsgassMIMA------HTDDQKPIHITLD----THVA-SEGSNFSQ 1358
Cdd:cd03263 79 YCPQFDALFDElTVREHL----------------------RFYArlkglpKSEIKEEVELLLRvlglTDKAnKRARTLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1359 GQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAHRLKTIvDY--DKVMVLDKGVLVEYGP 1436
Cdd:cd03263 137 GMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEA-EAlcDRIAIMSDGKLRCIGS 215
|
....
gi 19115470 1437 PAVL 1440
Cdd:cd03263 216 PQEL 219
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
631-816 |
2.09e-19 |
|
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: 89.15 E-value: 2.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYnlpRSKGVSYVSQVPWLRNA--------------TIRD 696
Cdd:COG4555 17 LKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSI---LIDGEDVRKEPREARRQigvlpderglydrlTVRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 697 NILF---DYPYIEERYKKVIQAcgLLTDLqsfvasDLTEIGEKGV-TLSGGQKQRIALARAVYSPTSIVLMDDVFSALDI 772
Cdd:COG4555 94 NIRYfaeLYGLFDEELKKRIEE--LIELL------GLEEFLDRRVgELSTGMKKKVALARALVHDPKVLLLDEPTNGLDV 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 19115470 773 HTSNWIYKHcFQSSLMENRTVILVTHNVHLFMDSAAFIVTVKNG 816
Cdd:COG4555 166 MARRLLREI-LRALKKEGKTVLFSSHIMQEVEALCDRVVILHKG 208
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
559-798 |
2.63e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 93.72 E-value: 2.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 559 SLFSFIRTQFSWIAYLMRQIVQIFVSIGRVSDF---LNDPDEVDPVNTIEDTSQEIGFFNASLTwVSNPSpGDFCLRDLN 635
Cdd:COG4178 306 SAFGQVQGALSWFVDNYQSLAEWRATVDRLAGFeeaLEAADALPEAASRIETSEDGALALEDLT-LRTPD-GRPLLEDLS 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 636 IVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYNLPRSKGVSYVSQVPWLRNATIRDNILfdYPYIEERY-----K 710
Cdd:COG4178 384 LSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPYLPLGTLREALL--YPATAEAFsdaelR 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 711 KVIQACGLlTDLqsfvASDLTEIGEKGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKHcFQSSLmEN 790
Cdd:COG4178 462 EALEAVGL-GHL----AERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL-LREEL-PG 534
|
....*...
gi 19115470 791 RTVILVTH 798
Cdd:COG4178 535 TTVISVGH 542
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
586-811 |
2.79e-19 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 93.62 E-value: 2.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 586 GRVSDFLNDPDEVDpvNTIEDTSQEIGFFNASLTWVSNPSPGDFCLRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGEL 665
Cdd:PRK10789 288 SRIRAMLAEAPVVK--DGSEPVPEGRGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHF 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 666 SLNKGS---YNLP---------RSKgVSYVSQVPWLRNATIRDNILFDYP-YIEERYKKVIQACGLLTDLQSFVASDLTE 732
Cdd:PRK10789 366 DVSEGDirfHDIPltklqldswRSR-LAVVSQTPFLFSDTVANNIALGRPdATQQEIEHVARLASVHDDILRLPQGYDTE 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19115470 733 IGEKGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKHCFQSSlmENRTVILVTHNVHLFMDSAAFIV 811
Cdd:PRK10789 445 VGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWG--EGRTVIISAHRLSALTEASEILV 521
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
631-816 |
2.88e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 88.19 E-value: 2.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGS-----YNLPRSKGvsyvSQVPWLR--------------N 691
Cdd:COG2884 18 LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQvlvngQDLSRLKR----REIPYLRrrigvvfqdfrllpD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 692 ATIRDNILF-------DYPYIEERYKKVIQACGLLTDLQSFVAsdlteigekgvTLSGGQKQRIALARA-VYSPtSIVLM 763
Cdd:COG2884 94 RTVYENVALplrvtgkSRKEIRRRVREVLDLVGLSDKAKALPH-----------ELSGGEQQRVAIARAlVNRP-ELLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 19115470 764 DDVFSALDIHTSNWIYKHcfqssLME-NR---TVILVTHNVHLFMDSAAFIVTVKNG 816
Cdd:COG2884 162 DEPTGNLDPETSWEIMEL-----LEEiNRrgtTVLIATHDLELVDRMPKRVLELEDG 213
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1229-1443 |
3.13e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 89.72 E-value: 3.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1229 LKDVNLHINPSEKVAVVGRTGSGKSTL-----GltLLRFThriSGEIYINGRE--TQSVNLNALRQRISFIPQDP--ILF 1299
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLiqhlnG--LLKPT---SGKIIIDGVDitDKKVKLSDIRKKVGLVFQYPeyQLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1300 SGTVR-------SNLDPFDELEDNFLNEALKTSGASSMIMAhtdDQKPIHItldthvasegsnfSQGQKQVLALARAIVR 1372
Cdd:PRK13637 98 EETIEkdiafgpINLGLSEEEIENRVKRAMNIVGLDYEDYK---DKSPFEL-------------SGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115470 1373 RSKIIILDECTASVD----DAMDQKIqKTLREAFgDATMLCIAHRLKTIVDY-DKVMVLDKGVLVEYGPPAVLYHN 1443
Cdd:PRK13637 162 EPKILILDEPTAGLDpkgrDEILNKI-KELHKEY-NMTIILVSHSMEDVAKLaDRIIVMNKGKCELQGTPREVFKE 235
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1229-1438 |
4.81e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.39 E-value: 4.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1229 LKDVNLHINPSEKVAVVGRTGSGKSTL-----GLtllrftHRI-SGEIYINGRETQSVN-LNALRQRISFIPQDPILFSG 1301
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLmkilsGV------YQPdSGEILLDGEPVRFRSpRDAQAAGIAIIHQELNLVPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1302 -TVRSNLdpfdelednFLNEALKTSG---------ASSMIMAHTDdqkpIHITLDTHVasegSNFSQGQKQVLALARAIV 1371
Cdd:COG1129 94 lSVAENI---------FLGREPRRGGlidwramrrRARELLARLG----LDIDPDTPV----GDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19115470 1372 RRSKIIILDECTASVDDA-MDQ--KIQKTLREAfgDATMLCIAHRLKTIVDY-DKVMVLDKGVLVEYGPPA 1438
Cdd:COG1129 157 RDARVLILDEPTASLTEReVERlfRIIRRLKAQ--GVAIIYISHRLDEVFEIaDRVTVLRDGRLVGTGPVA 225
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
627-817 |
6.09e-19 |
|
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: 86.97 E-value: 6.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 627 GDFCLrDLNIVFPRNKLSIViGPTGSGKSSLISALLGELSLNKG--------------SYNLP-RSKGVSYVSQVPWL-R 690
Cdd:cd03297 11 PDFTL-KIDFDLNEEVTGIF-GASGAGKSTLLRCIAGLEKPDGGtivlngtvlfdsrkKINLPpQQRKIGLVFQQYALfP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 691 NATIRDNILFDYPYIEERYKKvIQACGLLTDLQsfvasdLTEIGEKGV-TLSGGQKQRIALARAVYSPTSIVLMDDVFSA 769
Cdd:cd03297 89 HLNVRENLAFGLKRKRNREDR-ISVDELLDLLG------LDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 19115470 770 LDIHTSNWIYKHCFQSSLMENRTVILVTHN-VHLFMdSAAFIVTVKNGS 817
Cdd:cd03297 162 LDRALRLQLLPELKQIKKNLNIPVIFVTHDlSEAEY-LADRIVVMEDGR 209
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
631-816 |
1.32e-18 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 85.98 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYNLP-----------RSKGVSYVSQVP--WLRNATIRDN 697
Cdd:cd03225 17 LDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDgkdltklslkeLRRKVGLVFQNPddQFFGPTVEEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 698 ILF-------DYPYIEERYKKVIQACGLLTDLQSFVAsdlteigekgvTLSGGQKQRIALARAVYSPTSIVLMDDVFSAL 770
Cdd:cd03225 97 VAFglenlglPEEEIEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGVLAMDPDILLLDEPTAGL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 19115470 771 DIHTSNWIYKHcFQSSLMENRTVILVTHNVHLFMDSAAFIVTVKNG 816
Cdd:cd03225 166 DPAGRRELLEL-LKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1214-1433 |
1.84e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 87.05 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1214 FNHVSVSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVN---LNALRQRIS 1290
Cdd:PRK10419 13 YAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1291 FIPQDPIlfsG------TVRSNLD-PFDELEDnfLNEALKTSGASSMIMAhtddqkpihITLDTHVASE-GSNFSQGQKQ 1362
Cdd:PRK10419 93 MVFQDSI---SavnprkTVREIIRePLRHLLS--LDKAERLARASEMLRA---------VDLDDSVLDKrPPQLSGGQLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115470 1363 VLALARAIVRRSKIIILDECTASVDDAMD-QKIQ--KTLREAFGDATMLcIAHRLKtIVDY--DKVMVLDKGVLVE 1433
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQaGVIRllKKLQQQFGTACLF-ITHDLR-LVERfcQRVMVMDNGQIVE 232
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
897-1187 |
1.93e-18 |
|
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: 88.32 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 897 VAAVLLFFVTTQATSILIDLWVAFWTNSSVNSPDVNNNKFLFVYGTMLLAYSLLDFLRTVSYDRGAWWASRKLHDSMLES 976
Cdd:cd18600 33 ASLVGLWLLRSQADRVNTTRPESSSNTYAVIVTFTSSYYVFYIYVGVADSLLAMGFFRGLPLVHTLITVSKTLHQKMLHA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 977 VFGTFASWFDKTPTGRIVNRFAKDIRSIDMNLSGWLFFSINCFLSVAGGILSVSSAMPIFMIPAVIVCLAGYYFGLLYTR 1056
Cdd:cd18600 113 VLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIGAITVVSILQPYIFLATVPVIIAFIVLRAYFLR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1057 AQVGVKRLISIYTSPIFSLLGESIVGVSVIRAFNRQTIFKQMFSERLDnlvrLQSTSYNLN----RWVAVRTDGISGLVG 1132
Cdd:cd18600 193 TSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKALN----LHTANWFLYlstlRWFQMRIEMIFVIFF 268
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 19115470 1133 AIAGLIALLQKDLSPGVVGFSLNQAVIFSSSVLLFVRSCNSLQAEMNSYERVLEY 1187
Cdd:cd18600 269 TAVTFISIGTTGDGEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSRIFKF 323
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1212-1437 |
2.12e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 86.73 E-value: 2.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRISF 1291
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1292 IPQDPI-LFSGTV---------RSNLDPFDELEDnFLNEALKTSGassmiMAHTDDQKPihitldthvasegSNFSQGQK 1361
Cdd:PRK13648 88 VFQNPDnQFVGSIvkydvafglENHAVPYDEMHR-RVSEALKQVD-----MLERADYEP-------------NALSGGQK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19115470 1362 QVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLRE--AFGDATMLCIAHRLKTIVDYDKVMVLDKGVLVEYGPP 1437
Cdd:PRK13648 149 QRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKvkSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTP 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
631-765 |
2.51e-18 |
|
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: 83.08 E-value: 2.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYNL-----------PRSKGVSYVSQVPWL-RNATIRDNI 698
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLdgqdltdderkSLRKEIGYVFQDPQLfPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19115470 699 LFdYPYIEERYKKVIQAcGLLTDLQSFVASDL--TEIGEKGVTLSGGQKQRIALARAVYSPTSIVLMDD 765
Cdd:pfam00005 81 RL-GLLLKGLSKREKDA-RAEEALEKLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDE 147
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
627-816 |
3.37e-18 |
|
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: 85.47 E-value: 3.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 627 GDFCLRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYNL---------PRSKGVSYVSQVPWL-RNATIRD 696
Cdd:cd03299 11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLngkditnlpPEKRDISYVPQNYALfPHMTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 697 NILF-----DYPYiEERYKKVIQACGLLtdlqsfvasdltEIGE----KGVTLSGGQKQRIALARAVYSPTSIVLMDDVF 767
Cdd:cd03299 91 NIAYglkkrKVDK-KEIERKVLEIAEML------------GIDHllnrKPETLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19115470 768 SALDIHTsnwiykhcfQSSLME---------NRTVILVTHNvhlFMDSAAF---IVTVKNG 816
Cdd:cd03299 158 SALDVRT---------KEKLREelkkirkefGVTVLHVTHD---FEEAWALadkVAIMLNG 206
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
646-817 |
4.21e-18 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 83.52 E-value: 4.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 646 VIGPTGSGKSSLISALLGELSLNKGSYNLPR----------SKGVSYVSQVPWLRNATIRDNIlfdypyieerykkviqa 715
Cdd:cd03247 33 LLGRSGSGKSTLLQLLTGDLKPQQGEITLDGvpvsdlekalSSLISVLNQRPYLFDTTLRNNL----------------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 716 cglltdlqsfvasdlteigekGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKHCFQssLMENRTVIL 795
Cdd:cd03247 96 ---------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFE--VLKDKTLIW 152
|
170 180
....*....|....*....|...
gi 19115470 796 VTHnvHLF-MDSAAFIVTVKNGS 817
Cdd:cd03247 153 ITH--HLTgIEHMDKILFLENGK 173
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
623-802 |
5.41e-18 |
|
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: 82.97 E-value: 5.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 623 NPSPGDFCLRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYNLPRSKGVSYVSQVPWLRNATIRDNILfdY 702
Cdd:cd03223 9 ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYLPLGTLREQLI--Y 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 703 PYIEErykkviqacglltdlqsfvasdlteigekgvtLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKHC 782
Cdd:cd03223 87 PWDDV--------------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL 134
|
170 180
....*....|....*....|
gi 19115470 783 fQSSLMenrTVILVTHNVHL 802
Cdd:cd03223 135 -KELGI---TVISVGHRPSL 150
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
587-805 |
5.90e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 89.50 E-value: 5.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 587 RVSDFLNDPDEV--DPVNTIEDTSQEIGFFNASLTWVSNPSPgdfCLRDLNIVFPRNKLSIVIGPTGSGKSSLISaLL-- 662
Cdd:PRK11160 313 RINEITEQKPEVtfPTTSTAAADQVSLTLNNVSFTYPDQPQP---VLKGLSLQIKAGEKVALLGRTGCGKSTLLQ-LLtr 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 663 ------GELSLNkgsyNLP---------RSkGVSYVSQVPWLRNATIRDNILFDYPYI-EERYKKVIQACGLLTDLQSFV 726
Cdd:PRK11160 389 awdpqqGEILLN----GQPiadyseaalRQ-AISVVSQRVHLFSATLRDNLLLAAPNAsDEALIEVLQQVGLEKLLEDDK 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 727 ASDLTeIGEKGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKHCFQssLMENRTVILVTHNVHLF--M 804
Cdd:PRK11160 464 GLNAW-LGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAE--HAQNKTVLMITHRLTGLeqF 540
|
.
gi 19115470 805 D 805
Cdd:PRK11160 541 D 541
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
625-801 |
1.07e-17 |
|
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: 83.77 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 625 SPGDFC-LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGS--------------------YNLPRSKGVsyV 683
Cdd:cd03260 9 YYGDKHaLKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGApdegevlldgkdiydldvdvLELRRRVGM--V 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 684 SQVPWLRNATIRDNILF--------DYPYIEERYKKVIQACGLLTDlqsfVASDLteigeKGVTLSGGQKQRIALARAVY 755
Cdd:cd03260 87 FQKPNPFPGSIYDNVAYglrlhgikLKEELDERVEEALRKAALWDE----VKDRL-----HALGLSGGQQQRLCLARALA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 19115470 756 SPTSIVLMDDVFSALDIHTSNWIykhcfQSSLME---NRTVILVTHNVH 801
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKI-----EELIAElkkEYTIVIVTHNMQ 201
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
631-816 |
1.08e-17 |
|
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: 83.92 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGS----------YNLP--RSKgVSYVSQVPW--LRNATIRD 696
Cdd:COG1122 17 LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEvlvdgkditkKNLRelRRK-VGLVFQNPDdqLFAPTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 697 NILF-------DYPYIEERYKKVIQACGLltdlqsfvasdlTEIGEKGV-TLSGGQKQRIALARA-VYSPtSIVLMDDVF 767
Cdd:COG1122 96 DVAFgpenlglPREEIRERVEEALELVGL------------EHLADRPPhELSGGQKQRVAIAGVlAMEP-EVLVLDEPT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 19115470 768 SALDIHTSNWIYKHcFQSSLMENRTVILVTHNVHLFMDSAAFIVTVKNG 816
Cdd:COG1122 163 AGLDPRGRRELLEL-LKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDG 210
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
627-798 |
1.29e-17 |
|
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: 88.64 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 627 GDFCLRDLNIVFPRNKLSIVIGPTGSGKSSLISALL-------GELSLNKGSY-NLPRS---KGVSYVSQVPWLRNATIR 695
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVgffqarsGEILLNGFSLkDIDRHtlrQFINYLPQEPYIFSGSIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 696 DNILF-DYPYIEEryKKVIQACGLL---TDLQSFVASDLTEIGEKGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALD 771
Cdd:TIGR01193 566 ENLLLgAKENVSQ--DEIWAACEIAeikDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
170 180
....*....|....*....|....*..
gi 19115470 772 IHTSNWIYKHCFQsslMENRTVILVTH 798
Cdd:TIGR01193 644 TITEKKIVNNLLN---LQDKTIIFVAH 667
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1215-1443 |
1.56e-17 |
|
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: 83.49 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1215 NHVSVSYSAAgpTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQR-ISFIP 1293
Cdd:COG0410 7 ENLHAGYGGI--HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1294 QDPILFSG-TVRSNLdpfdelednflnealktsgassMIMAHT-DDQKPIHITLDtHV-----------ASEGSNFSQGQ 1360
Cdd:COG0410 85 EGRRIFPSlTVEENL----------------------LLGAYArRDRAEVRADLE-RVyelfprlkerrRQRAGTLSGGE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1361 KQVLALARAIVRRSKIIILDECTAS-----VDDAMDqkIQKTLREAfgDATMLCI---AHRLKTIVDYdkVMVLDKGVLV 1432
Cdd:COG0410 142 QQMLAIGRALMSRPKLLLLDEPSLGlapliVEEIFE--IIRRLNRE--GVTILLVeqnARFALEIADR--AYVLERGRIV 215
|
250
....*....|.
gi 19115470 1433 EYGPPAVLYHN 1443
Cdd:COG0410 216 LEGTAAELLAD 226
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
296-568 |
1.94e-17 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 84.23 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 296 ILGMGVSSFMVSVCQFLSPIALNRLLKHLE---SPSSSSVNPLVWIVLLLTGPFLTSLFTQFYLFMSTryLARSYTTLVQ 372
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLpdgDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHT--GERLSRRLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 373 QIYNKVIR--SRFVQNKSgdskVGRSNNLISTDVDDIGEIREFIHIIVRAPVEIAGSIYLLQKLLGWS-AYVGLALTVLT 449
Cdd:pfam00664 79 KLFKKILRqpMSFFDTNS----VGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKlTLVLLAVLPLY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 450 CSVPIVLGPLVAKLTLRANRATDSRIELMSELLQSIRITKFFGWELPMLDRVKQRRQVELNRTWKLLLMEICIQVLVESL 529
Cdd:pfam00664 155 ILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFI 234
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 19115470 530 PVFSMF-ATFVVFTTIMGQTITPSIAFTSISLFSFIRTQF 568
Cdd:pfam00664 235 GYLSYAlALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
631-816 |
2.28e-17 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 82.78 E-value: 2.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSY--------NLP-------RSKGVSYVSQ----VPWLrn 691
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVlidgqdisSLSerelarlRRRHIGFVFQffnlLPEL-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 692 aTIRDNILF-------DYPYIEERYKKVIQACGLLTDLQSFVAsdlteigekgvTLSGGQKQRIALARAVYSPTSIVLMD 764
Cdd:COG1136 102 -TALENVALplllagvSRKERRERARELLERVGLGDRLDHRPS-----------QLSGGQQQRVAIARALVNRPKLILAD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 19115470 765 DVFSALDIHTSNWIYKHCFQSSLMENRTVILVTHNVHLfmdsAAF---IVTVKNG 816
Cdd:COG1136 170 EPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPEL----AARadrVIRLRDG 220
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
604-817 |
3.14e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 87.00 E-value: 3.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 604 IEDTSQEIGFFNASLTWVSNPSPGdfcLRDLNIVFPRNKLSIVIGPTGSGKSSlISALL--------GELSL---NKGSY 672
Cdd:PRK11176 335 IERAKGDIEFRNVTFTYPGKEVPA---LRNINFKIPAGKTVALVGRSGSGKST-IANLLtrfydideGEILLdghDLRDY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 673 NLP--RSKgVSYVSQVPWLRNATIRDNILFDYpyiEERY-KKVIQACGLLTDLQSFVAS-----DlTEIGEKGVTLSGGQ 744
Cdd:PRK11176 411 TLAslRNQ-VALVSQNVHLFNDTIANNIAYAR---TEQYsREQIEEAARMAYAMDFINKmdnglD-TVIGENGVLLSGGQ 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115470 745 KQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIykhcfQSSLME---NRTVILVTHNVHLfMDSAAFIVTVKNGS 817
Cdd:PRK11176 486 RQRIAIARALLRDSPILILDEATSALDTESERAI-----QAALDElqkNRTSLVIAHRLST-IEKADEILVVEDGE 555
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1212-1435 |
3.35e-17 |
|
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: 81.88 E-value: 3.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYsaAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQsvNLNALRQRISF 1291
Cdd:cd03268 1 LKTNDLTKTY--GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--KNIEALRRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1292 IPQDPILFSG-TVRSNLDPFDEL---EDNFLNEALKTSGassmiMAHTDDQKPihitldthvasegSNFSQGQKQVLALA 1367
Cdd:cd03268 77 LIEAPGFYPNlTARENLRLLARLlgiRKKRIDEVLDVVG-----LKDSAKKKV-------------KGFSLGMKQRLGIA 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19115470 1368 RAIVRRSKIIILDECTASVDDAMDQKIQKTLRE--AFGdATMLCIAHRL---KTIVdyDKVMVLDKGVLVEYG 1435
Cdd:cd03268 139 LALLGNPDLLILDEPTNGLDPDGIKELRELILSlrDQG-ITVLISSHLLseiQKVA--DRIGIINKGKLIEEG 208
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1227-1436 |
3.62e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 86.68 E-value: 3.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1227 TILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFThRISGEIYINGRETQSVNLNAL---RQRISFIPQDPilfsgtv 1303
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDP------- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1304 RSNLDPFDELEdNFLNEALKTSGASsmIMAHTDDQKPIHITLDTHVASEG-----SNFSQGQKQVLALARAIVRRSKIII 1378
Cdd:PRK15134 372 NSSLNPRLNVL-QIIEEGLRVHQPT--LSAAQREQQVIAVMEEVGLDPETrhrypAEFSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115470 1379 LDECTASVDD-------AMDQKIQKTLREAFgdatmLCIAHRLKTIVDY-DKVMVLDKGVLVEYGP 1436
Cdd:PRK15134 449 LDEPTSSLDKtvqaqilALLKSLQQKHQLAY-----LFISHDLHVVRALcHQVIVLRQGEVVEQGD 509
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1211-1443 |
4.04e-17 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 84.76 E-value: 4.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1211 DIVFNHVSVSYsaAGPTILKDVNLHINPSEKVAVVGRTGSGKStlglTLLR----FTHRISGEIYINGREtqsvnLNAL- 1285
Cdd:COG3842 5 ALELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKT----TLLRmiagFETPDSGRILLDGRD-----VTGLp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1286 -RQR-ISFIPQDPILFSG-TVRSN---------LDPfDELEDNfLNEALKTSGassmiMAHTDDQKPihitldthvaseg 1353
Cdd:COG3842 74 pEKRnVGMVFQDYALFPHlTVAENvafglrmrgVPK-AEIRAR-VAELLELVG-----LEGLADRYP------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1354 SNFSQGQKQVLALARAIVRRSKIIILDECTAsvddAMDQKIQKTLRE-------AFGdATMLCIAHrlktivDY------ 1420
Cdd:COG3842 134 HQLSGGQQQRVALARALAPEPRVLLLDEPLS----ALDAKLREEMREelrrlqrELG-ITFIYVTH------DQeealal 202
|
250 260
....*....|....*....|....
gi 19115470 1421 -DKVMVLDKGVLVEYGPPAVLYHN 1443
Cdd:COG3842 203 aDRIAVMNDGRIEQVGTPEEIYER 226
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
631-800 |
7.48e-17 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 81.65 E-value: 7.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGS-----YNLPRS-----KGVSYVSQVPWL-RNATIRDNIL 699
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEvrvlgEDVARDpaevrRRIGYVPQEPALyPDLTVRENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 700 F-------DYPYIEERYKKVIQACGLLTDLQSFVAsdlteigekgvTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDI 772
Cdd:COG1131 96 FfarlyglPRKEARERIDELLELFGLTDAADRKVG-----------TLSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180
....*....|....*....|....*...
gi 19115470 773 HTSNWIYKHcFQSSLMENRTVILVTHNV 800
Cdd:COG1131 165 EARRELWEL-LRELAAEGKTVLLSTHYL 191
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
631-816 |
8.62e-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: 79.36 E-value: 8.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGsynlprskgvsyvsqvpwlrnaTIRdniLFDYPYIEERyK 710
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSG----------------------EIK---VLGKDIKKEP-E 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 711 KVIQACGLLTDLQSFVaSDLTeiGEKGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKHcFQSSLMEN 790
Cdd:cd03230 70 EVKRRIGYLPEEPSLY-ENLT--VRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWEL-LRELKKEG 145
|
170 180
....*....|....*....|....*.
gi 19115470 791 RTVILVTHNVHLFMDSAAFIVTVKNG 816
Cdd:cd03230 146 KTILLSSHILEEAERLCDRVAILNNG 171
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1212-1436 |
9.40e-17 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 83.31 E-value: 9.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAAGPTI--LKDVNLHINPSEKVAVVGRTGSGKStlglTLLRFTHRI----SGEIYINGRETQSVN---L 1282
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKS----TLIRCINLLerptSGRVLVDGQDLTALSekeL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1283 NALRQRISFIPQD-PILFSGTVRSN------LD--PFDELEDNfLNEALKTSGassmiMAHTDDQKPihitldthvaseg 1353
Cdd:PRK11153 78 RKARRQIGMIFQHfNLLSSRTVFDNvalpleLAgtPKAEIKAR-VTELLELVG-----LSDKADRYP------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1354 SNFSQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLRE---AFGdATMLCIAHRL---KTIVdyDKVMVLD 1427
Cdd:PRK11153 139 AQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDinrELG-LTIVLITHEMdvvKRIC--DRVAVID 215
|
....*....
gi 19115470 1428 KGVLVEYGP 1436
Cdd:PRK11153 216 AGRLVEQGT 224
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1229-1438 |
1.16e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 81.76 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1229 LKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRISFIPQDPI----------- 1297
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPStslnprqrisq 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1298 LFSGTVRSNLDPFDELEDNFLNEALKTSGAssmimahtddqKPIHITLDTHVasegsnFSQGQKQVLALARAIVRRSKII 1377
Cdd:PRK15112 109 ILDFPLRLNTDLEPEQREKQIIETLRQVGL-----------LPDHASYYPHM------LAPGQKQRLGLARALILRPKVI 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115470 1378 ILDECTASVDDAMDQKI---QKTLREAFGDATMLCIAH--RLKTIVdyDKVMVLDKGVLVEYGPPA 1438
Cdd:PRK15112 172 IADEALASLDMSMRSQLinlMLELQEKQGISYIYVTQHlgMMKHIS--DQVLVMHQGEVVERGSTA 235
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1228-1446 |
1.40e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 81.11 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1228 ILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTH-----RISGEIYINGRETQSVNLNALRQRISFIPQ--DPIlfs 1300
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQipNPI--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1301 gtvrSNLDPFDELEDNF-LNEALKTSGASSMIMAHTDDQKPIHITLDTHVASEGSNFSQGQKQVLALARAIVRRSKIIIL 1379
Cdd:PRK14247 95 ----PNLSIFENVALGLkLNRLVKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1380 DECTASVDDAMDQKIQKTLREAFGDATMLCIAH---RLKTIVDYdkVMVLDKGVLVEYGPPAVLYHNNGH 1446
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqQAARISDY--VAFLYKGQIVEWGPTREVFTNPRH 238
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1212-1412 |
1.49e-16 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 80.21 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAAGP--TILKDVNLHINPSEKVAVVGRTGSGKSTL-----GltLLRFThriSGEIYINGREtqsvnLNA 1284
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLlriiaG--LERPT---SGEVLVDGEP-----VTG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1285 LRQRISFIPQDPILFS-GTVRSN----LD----PFDELEDNFLnEALKTSGassmiMAHTDDQKPihitldthvasegSN 1355
Cdd:cd03293 71 PGPDRGYVFQQDALLPwLTVLDNvalgLElqgvPKAEARERAE-ELLELVG-----LSGFENAYP-------------HQ 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19115470 1356 FSQGQKQVLALARAIVRRSKIIILDECTASVD----DAMDQKIQKTLREAfgDATMLCIAH 1412
Cdd:cd03293 132 LSGGMRQRVALARALAVDPDVLLLDEPFSALDaltrEQLQEELLDIWRET--GKTVLLVTH 190
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1207-1443 |
1.68e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 81.77 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1207 PKEGDIVFNHVSVSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTL-----GLTLLRFTHRISgeIYINGRETQSVN 1281
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTIsklinGLLLPDDNPNSK--ITVDGITLTAKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1282 LNALRQRISFIPQDPI-LFSGTVRSNLDPFdelednflneALKTSGASSMIMAHTDDQKPIHITLDTHVASEGSNFSQGQ 1360
Cdd:PRK13640 79 VWDIREKVGIVFQNPDnQFVGATVGDDVAF----------GLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1361 KQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDA--TMLCIAHRLKTIVDYDKVMVLDKGVLVEYGPPA 1438
Cdd:PRK13640 149 KQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPV 228
|
....*
gi 19115470 1439 VLYHN 1443
Cdd:PRK13640 229 EIFSK 233
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1216-1441 |
1.71e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 81.43 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1216 HVSVSYsAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGR--ETQSVNLNALRQRISFIP 1293
Cdd:PRK13636 10 ELNYNY-SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESVGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1294 QDP--ILFSGTVRSNLD--------PFDELEDNfLNEALKTSGassmiMAHTDDqKPIHItldthvasegsnFSQGQKQV 1363
Cdd:PRK13636 89 QDPdnQLFSASVYQDVSfgavnlklPEDEVRKR-VDNALKRTG-----IEHLKD-KPTHC------------LSFGQKKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1364 LALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFG--DATMLCIAHRLKTIVDY-DKVMVLDKGVLVEYGPPAVL 1440
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYcDNVFVMKEGRVILQGNPKEV 229
|
.
gi 19115470 1441 Y 1441
Cdd:PRK13636 230 F 230
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
575-798 |
4.19e-16 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 84.02 E-value: 4.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 575 MRQIVQIF----VSIGRVSDFLNDPDEVDPVN--TIEDTSQEIGFFNASLTWVSNPSPgdfCLRDLNIVFPRNKLSIVIG 648
Cdd:TIGR01846 414 LAQLWQDFqqtgIALERLGDILNSPTEPRSAGlaALPELRGAITFENIRFRYAPDSPE---VLSNLNLDIKPGEFIGIVG 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 649 PTGSGKSSLIS------------ALLGELSLNKGSYNLPRsKGVSYVSQVPWLRNATIRDNILFDYPYIEEryKKVIQAc 716
Cdd:TIGR01846 491 PSGSGKSTLTKllqrlytpqhgqVLVDGVDLAIADPAWLR-RQMGVVLQENVLFSRSIRDNIALCNPGAPF--EHVIHA- 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 717 GLLTDLQSFVaSDL-----TEIGEKGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKHcfQSSLMENR 791
Cdd:TIGR01846 567 AKLAGAHDFI-SELpqgynTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRN--MREICRGR 643
|
....*..
gi 19115470 792 TVILVTH 798
Cdd:TIGR01846 644 TVIIIAH 650
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1214-1381 |
4.42e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.19 E-value: 4.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1214 FNHVSVSYsaAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLgLTLLR-FTHRISGEIYINGREtqsvnlnalrqRISFI 1292
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTL-LKILAgELEPDSGEVSIPKGL-----------RIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1293 PQDPILFSG-TVrsnldpFDELEDNF--LNEALKTSGASSMIMAHTDDQKPIHITLDTHVASEG---------------- 1353
Cdd:COG0488 67 PQEPPLDDDlTV------LDTVLDGDaeLRALEAELEELEAKLAEPDEDLERLAELQEEFEALGgweaearaeeilsglg 140
|
170 180 190
....*....|....*....|....*....|....*...
gi 19115470 1354 ----------SNFSQGQKQVLALARAIVRRSKIIILDE 1381
Cdd:COG0488 141 fpeedldrpvSELSGGWRRRVALARALLSEPDLLLLDE 178
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1212-1433 |
5.27e-16 |
|
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: 79.01 E-value: 5.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSY-SAAGP-TILKDVNLHINPSEKVAVVGRTGSGKSTLgLTLL----RFThriSGEIYINGREtqsvnLNAL 1285
Cdd:COG4181 9 IELRGLTKTVgTGAGElTILKGISLEVEAGESVAIVGASGSGKSTL-LGLLagldRPT---SGTVRLAGQD-----LFAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1286 ---------RQRISFIPQD-PILFSGTVRSNL----------DPFDELEdnflnEALKTSGassmiMAHTDDQKPIHItl 1345
Cdd:COG4181 80 dedararlrARHVGFVFQSfQLLPTLTALENVmlplelagrrDARARAR-----ALLERVG-----LGHRLDHYPAQL-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1346 dthvasegsnfSQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQK---TLREAFGdATMLCIAHRLKTIVDYDK 1422
Cdd:COG4181 148 -----------SGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDllfELNRERG-TTLVLVTHDPALAARCDR 215
|
250
....*....|.
gi 19115470 1423 VMVLDKGVLVE 1433
Cdd:COG4181 216 VLRLRAGRLVE 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
631-799 |
5.33e-16 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 77.26 E-value: 5.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYNL---------PRSKG--VSYVSQVPWLRNATIRDNIL 699
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdgadisqwdPNELGdhVGYLPQDDELFSGSIAENIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 700 fdypyieerykkviqacglltdlqsfvasdlteigekgvtlSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIY 779
Cdd:cd03246 98 -----------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALN 136
|
170 180
....*....|....*....|
gi 19115470 780 kHCFQSSLMENRTVILVTHN 799
Cdd:cd03246 137 -QAIAALKAAGATRIVIAHR 155
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1225-1448 |
5.99e-16 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 79.41 E-value: 5.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1225 GPTILKDVNLHINPSEKVAVVGRTGSGKSTL--GLTLLRF----THRIsGEIYINGRET---QSVNLNALRQRISFIPQD 1295
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLlrCINLLEQpeagTIRV-GDITIDTARSlsqQKGLIRQLRQHVGFVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1296 PILFSG-TVRSNL---------DPFDELEdnflneALKTSGASSMIMAHTDDQKPihitldthvasegSNFSQGQKQVLA 1365
Cdd:PRK11264 94 FNLFPHrTVLENIiegpvivkgEPKEEAT------ARARELLAKVGLAGKETSYP-------------RRLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1366 LARAIVRRSKIIILDECTASVDDAMDQKIQKTLRE-AFGDATMLCIAHRLKTIVDY-DKVMVLDKGVLVEYGPPAVLYHN 1443
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGPAKALFAD 234
|
....*
gi 19115470 1444 NGHFR 1448
Cdd:PRK11264 235 PQQPR 239
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1212-1431 |
7.00e-16 |
|
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: 78.22 E-value: 7.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYsAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNA---LRQR 1288
Cdd:cd03292 1 IEFINVTKTY-PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1289 ISFIPQDPILFsgtvrSNLDPFDELEdnFlneALKTSGASsmimaHTDDQKPIHITLD----THVASE-GSNFSQGQKQV 1363
Cdd:cd03292 80 IGVVFQDFRLL-----PDRNVYENVA--F---ALEVTGVP-----PREIRKRVPAALElvglSHKHRAlPAELSGGEQQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1364 LALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAHRLKTIVDYDK--VMVLDKGVL 1431
Cdd:cd03292 145 VAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRhrVIALERGKL 214
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1216-1438 |
7.63e-16 |
|
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: 78.63 E-value: 7.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1216 HVSVSYsaAGPTILKDVNLHINPSEKVAVVGRTGSGKSTL-----GLtlLRFThriSGEIYINGRETQSVNLNALRQR-I 1289
Cdd:cd03219 5 GLTKRF--GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLfnlisGF--LRPT---SGSVLFDGEDITGLPPHEIARLgI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1290 --SFipQDPILFSG-TVRSNLDPfdelednflneALKTSGASSMIMAHTDDQKPIHI-----TLD----THVASE-GSNF 1356
Cdd:cd03219 78 grTF--QIPRLFPElTVLENVMV-----------AAQARTGSGLLLARARREEREAReraeeLLErvglADLADRpAGEL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1357 SQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLRE-AFGDATMLCIAHRLKTIVDY-DKVMVLDKG-VLVE 1433
Cdd:cd03219 145 SYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRElRERGITVLLVEHDMDVVMSLaDRVTVLDQGrVIAE 224
|
....*
gi 19115470 1434 yGPPA 1438
Cdd:cd03219 225 -GTPD 228
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
631-816 |
7.64e-16 |
|
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: 78.68 E-value: 7.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKG-----SYNLPRS------KGVSYVSQVPWLRNATIRDNIL 699
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGrvlvdGHDLALAdpawlrRQVGVVLQENVLFNRSIRDNIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 700 FDYPYIEERykKVIQACGLlTDLQSFVaSDLTE-----IGEKGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHT 774
Cdd:cd03252 98 LADPGMSME--RVIEAAKL-AGAHDFI-SELPEgydtiVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYES 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 19115470 775 SNWIYKHcfQSSLMENRTVILVTHNVHLFMdSAAFIVTVKNG 816
Cdd:cd03252 174 EHAIMRN--MHDICAGRTVIIIAHRLSTVK-NADRIIVMEKG 212
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1228-1429 |
7.69e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 79.39 E-value: 7.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1228 ILKDVNLHINPSEKVAVVGRTGSGKSTlgltllrfTHRI--------SGEIYINGRETQSVNLNALRQRISFIPQDPI-L 1298
Cdd:PRK13650 22 TLNDVSFHVKQGEWLSIIGHNGSGKST--------TVRLidglleaeSGQIIIDGDLLTEENVWDIRHKIGMVFQNPDnQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1299 FSG-TVRSNLD--------PFDELEDNfLNEALKTSGassmiMAHTDDQKPihitldthvasegSNFSQGQKQVLALARA 1369
Cdd:PRK13650 94 FVGaTVEDDVAfglenkgiPHEEMKER-VNEALELVG-----MQDFKEREP-------------ARLSGGQKQRVAIAGA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19115470 1370 IVRRSKIIILDECTASVDDAMDQKIQKTLREAFGD--ATMLCIAHRLKTIVDYDKVMVLDKG 1429
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyqMTVISITHDLDEVALSDRVLVMKNG 216
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1219-1440 |
8.90e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 79.05 E-value: 8.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1219 VSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLgLTLLR-FTHRISGEIYINGRETQSVNLNALRQRISFIPQDPI 1297
Cdd:PRK13548 8 LSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTL-LRALSgELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1298 L-FSGTVR-----------SNLDPFDELEDnflnEALKTSGASSmiMAHTDDQkpihiTLdthvasegsnfSQGQKQVLA 1365
Cdd:PRK13548 87 LsFPFTVEevvamgraphgLSRAEDDALVA----AALAQVDLAH--LAGRDYP-----QL-----------SGGEQQRVQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1366 LARAIVRRS------KIIILDECTASVDDAMDQKIQKTLREAFGD--ATMLCIAHRLKTIVDY-DKVMVLDKGVLVEYGP 1436
Cdd:PRK13548 145 LARVLAQLWepdgppRWLLLDEPTSALDLAHQHHVLRLARQLAHErgLAVIVVLHDLNLAARYaDRIVLLHQGRLVADGT 224
|
....*
gi 19115470 1437 PA-VL 1440
Cdd:PRK13548 225 PAeVL 229
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1212-1413 |
1.03e-15 |
|
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: 76.42 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVsYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLgltlLRFTHRI----SGEIYINGREtqsvnlnalrq 1287
Cdd:cd03223 1 IELENLSL-ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSL----FRALAGLwpwgSGRIGMPEGE----------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1288 RISFIPQDPILFSGTVRSNLD-PFDElednflnealktsgassmimahtddqkpihitldthvasegsNFSQGQKQVLAL 1366
Cdd:cd03223 65 DLLFLPQRPYLPLGTLREQLIyPWDD------------------------------------------VLSGGEQQRLAF 102
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 19115470 1367 ARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFgdATMLCIAHR 1413
Cdd:cd03223 103 ARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELG--ITVISVGHR 147
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
631-798 |
1.04e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 77.52 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLN---KGSYNL---------PRSKGVSYVSQVPWL-RNATIRDN 697
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLngrrltalpAEQRRIGILFQDDLLfPHLSVGEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 698 ILFDYP---YIEERYKKVIQAcglLTDLqsfvasDLTEIGEKGV-TLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIH 773
Cdd:COG4136 97 LAFALPptiGRAQRRARVEQA---LEEA------GLAGFADRDPaTLSGGQRARVALLRALLAEPRALLLDEPFSKLDAA 167
|
170 180
....*....|....*....|....*
gi 19115470 774 TSNWIYKHCFQSSLMENRTVILVTH 798
Cdd:COG4136 168 LRAQFREFVFEQIRQRGIPALLVTH 192
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1229-1446 |
1.40e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 82.21 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1229 LKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVN---LNALRQRISFIPQDPIlfsgtvrS 1305
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPY-------A 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1306 NLDPFDELEDNFLnEALKTSG-----ASSMIMAHTDDQ---KPIHITLDTHvasegsNFSQGQKQVLALARAIVRRSKII 1377
Cdd:PRK10261 413 SLDPRQTVGDSIM-EPLRVHGllpgkAAAARVAWLLERvglLPEHAWRYPH------EFSGGQRQRICIARALALNPKVI 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19115470 1378 ILDECTASVDDAMDQKIQK---TLREAFGDAtMLCIAHRLKTIVDYD-KVMVLDKGVLVEYGPPAVLYHNNGH 1446
Cdd:PRK10261 486 IADEAVSALDVSIRGQIINlllDLQRDFGIA-YLFISHDMAVVERIShRVAVMYLGQIVEIGPRRAVFENPQH 557
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1212-1441 |
1.53e-15 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 77.66 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYsaAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQsvNLNALRQRISF 1291
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT--NLPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1292 IPQDPILFSgtvrsNLDPFDELEdnFLNEALKTSGASsmIMAHTDDQkpIHIT-LDTHVASEGSNFSQGQKQVLALARAI 1370
Cdd:cd03300 77 VFQNYALFP-----HLTVFENIA--FGLRLKKLPKAE--IKERVAEA--LDLVqLEGYANRKPSQLSGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115470 1371 VRRSKIIILDECTASVDDAMDQKIQ---KTLREAFGdATMLCIAH-RLKTIVDYDKVMVLDKGVLVEYGPPAVLY 1441
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQlelKRLQKELG-ITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEIY 219
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1212-1437 |
1.53e-15 |
|
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: 77.73 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYsAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRISF 1291
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1292 IPQDPILFSG-TVRSNLDPFDELEdNFLNEALKTSGASSMIMAHTDDQkpihitldTHVASEGSNFSQGQKQVLALARAI 1370
Cdd:cd03295 80 VIQQIGLFPHmTVEENIALVPKLL-KWPKEKIRERADELLALVGLDPA--------EFADRYPHELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115470 1371 VRRSKIIILDECTASVD----DAMDQ---KIQKTLREafgdaTMLCIAHRL-KTIVDYDKVMVLDKGVLVEYGPP 1437
Cdd:cd03295 151 AADPPLLLMDEPFGALDpitrDQLQEefkRLQQELGK-----TIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTP 220
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
365-588 |
1.75e-15 |
|
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: 78.80 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 365 RSYTTLVQQIYNKVIRSRFVQNKSgdSKVGRSNNLISTDVDDIGEIREFIHIIVRAPVEIAGSIYLLQKLLGWSAYVGLA 444
Cdd:cd18559 68 FASRAVHLDLYHKALRSPISFFER--TPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 445 LTVLTCSVPIVLGPLVAKLTLRANRATDSRIELMSELLQSIRITKFFGWELPMLDRVKQRRQVELNRTWKLLLMEICIQV 524
Cdd:cd18559 146 LGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVR 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115470 525 LVESLPVFSMFATFVVFTTIMGQTI-TPSIAFTSISLFSFIRTQFSWIAYLMRQIVQIFVSIGRV 588
Cdd:cd18559 226 LWCVGPCIVLFASFFAYVSRHSLAGlVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1233-1449 |
1.84e-15 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 77.49 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1233 NLHINPSEKVAVVGRTGSGKSTLgLTLLR-FTHRISGEIYINGretqsVNLNALR--QR-ISFIPQDPILFSG-TVRSN- 1306
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTL-LNLIAgFLPPDSGRILWNG-----QDLTALPpaERpVSMLFQENNLFPHlTVAQNi 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1307 ---LDP---FDELEDNFLNEALKTSGASSMimahtDDQKPihitldthvasegSNFSQGQKQVLALARAIVRRSKIIILD 1380
Cdd:COG3840 93 glgLRPglkLTAEQRAQVEQALERVGLAGL-----LDRLP-------------GQLSGGQRQRVALARCLVRKRPILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115470 1381 ECTASVDDAMDQK----IQKTLREAfgDATMLCIAHRLKTIVDY-DKVMVLDKGVLVEYGPPAVL--YHNNGHFRR 1449
Cdd:COG3840 155 EPFSALDPALRQEmldlVDELCRER--GLTVLMVTHDPEDAARIaDRVLLVADGRIAADGPTAALldGEPPPALAA 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
631-816 |
1.92e-15 |
|
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: 75.69 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGS-------------YNLPRSKGVSYVSQ----VPWLrnaT 693
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSilidgedltdledELPPLRRRIGMVFQdfalFPHL---T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 694 IRDNILFdypyieerykkviqacglltdlqsfvasdlteigekgvTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIH 773
Cdd:cd03229 93 VLENIAL--------------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 19115470 774 TSNWIYKHCFQSSLMENRTVILVTHNVHLFMDSAAFIVTVKNG 816
Cdd:cd03229 135 TRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
631-816 |
1.97e-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: 76.76 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSL---ISALL----GELSLNKGS-YNLP-------RSKGVSYVSQVPWL-RNATI 694
Cdd:cd03255 20 LKGVSLSIEKGEFVAIVGPSGSGKSTLlniLGGLDrptsGEVRVDGTDiSKLSekelaafRRRHIGFVFQSFNLlPDLTA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 695 RDNILF-------DYPYIEERYKKVIQACGLLTDLQSFVAsdlteigekgvTLSGGQKQRIALARAVYSPTSIVLMDDVF 767
Cdd:cd03255 100 LENVELplllagvPKKERRERAEELLERVGLGDRLNHYPS-----------ELSGGQQQRVAIARALANDPKIILADEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 19115470 768 SALDIHTSNWIYKHCFQSSLMENRTVILVTHNvhlfMDSAAF---IVTVKNG 816
Cdd:cd03255 169 GNLDSETGKEVMELLRELNKEAGTTIVVVTHD----PELAEYadrIIELRDG 216
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1212-1437 |
2.61e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 78.21 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAAG----PTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSV-NLNALR 1286
Cdd:PRK13633 5 IKCKNVSYKYESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1287 QRISFIPQDP--ILFSGTVRS-------NLD-PFDELEDNfLNEALKTSGassmiMAHTDDQKPiHItldthvasegsnF 1356
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEdvafgpeNLGiPPEEIRER-VDESLKKVG-----MYEYRRHAP-HL------------L 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1357 SQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDA--TMLCIAHRLKTIVDYDKVMVLDKGVLVEY 1434
Cdd:PRK13633 146 SGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVME 225
|
...
gi 19115470 1435 GPP 1437
Cdd:PRK13633 226 GTP 228
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
576-817 |
2.91e-15 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 80.85 E-value: 2.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 576 RQIVQIFVSIGRVSDFLNDPDEVDPVNTIEDTSQEIGFFNASltwVSNPSPGDFCLRDLNIVFPRNKLSIVIGPTGSGKS 655
Cdd:TIGR01842 282 KQFSGARQAYKRLNELLANYPSRDPAMPLPEPEGHLSVENVT---IVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKS 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 656 SLISALLGELSLNKGSYNL---------PRSKG--VSYVSQVPWLRNATIRDNIL-FDYPYIEErykKVIQAC---GLLT 720
Cdd:TIGR01842 359 TLARLIVGIWPPTSGSVRLdgadlkqwdRETFGkhIGYLPQDVELFPGTVAENIArFGENADPE---KIIEAAklaGVHE 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 721 DLQSFVASDLTEIGEKGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKhCFQSSLMENRTVILVTHNV 800
Cdd:TIGR01842 436 LILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALAN-AIKALKARGITVVVITHRP 514
|
250
....*....|....*..
gi 19115470 801 HLfMDSAAFIVTVKNGS 817
Cdd:TIGR01842 515 SL-LGCVDKILVLQDGR 530
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
631-798 |
4.62e-15 |
|
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: 75.59 E-value: 4.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYNL----PRSKGVSYVSQVPWL--RNA-----TIRDNIL 699
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWngepIRDAREDYRRRLAYLghADGlkpelTVRENLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 700 F-----DYPYIEERYKKVIQACGLLTDLQSFVAsdlteigekgvTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHT 774
Cdd:COG4133 98 FwaalyGLRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAG 166
|
170 180
....*....|....*....|....
gi 19115470 775 SNWIYKHcFQSSLMENRTVILVTH 798
Cdd:COG4133 167 VALLAEL-IAAHLARGGAVLLTTH 189
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
627-808 |
4.64e-15 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 76.61 E-value: 4.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 627 GDFC-LRDLNIVFPRNKLSIVIGPTGSGKSSLISAL-----------------LGELSLNKGSYNLP--RSKgVSYVSQV 686
Cdd:COG1117 22 GDKQaLKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndlipgarvegeilLDGEDIYDPDVDVVelRRR-VGMVFQK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 687 PwlrN---ATIRDNILF--------DYPYIEERYKKVIQACGLLTDlqsfVASDLteiGEKGVTLSGGQKQRIALAR--A 753
Cdd:COG1117 101 P---NpfpKSIYDNVAYglrlhgikSKSELDEIVEESLRKAALWDE----VKDRL---KKSALGLSGGQQQRLCIARalA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 19115470 754 VySPtSIVLMDDVFSALD-IHTS---NWIYkhcfqsSLMENRTVILVTHNvhlfMDSAA 808
Cdd:COG1117 171 V-EP-EVLLMDEPTSALDpISTAkieELIL------ELKKDYTIVIVTHN----MQQAA 217
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1228-1446 |
5.02e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 76.80 E-value: 5.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1228 ILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTH-----RISGEIYINGRETQSVNLNAL--RQRISFIPQDPilfs 1300
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPIevRREVGMVFQYP---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1301 gtvrsnlDPFDELE--DNF-----LNEALKTSGASSMIMAHTDDQKPIHITLDTHVASEGSNFSQGQKQVLALARAIVRR 1373
Cdd:PRK14267 95 -------NPFPHLTiyDNVaigvkLNGLVKSKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMK 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115470 1374 SKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAH---RLKTIVDYdkVMVLDKGVLVEYGPPAVLYHNNGH 1446
Cdd:PRK14267 168 PKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHspaQAARVSDY--VAFLYLGKLIEVGPTRKVFENPEH 241
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1233-1414 |
5.18e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 76.16 E-value: 5.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1233 NLHINPSEKVAVVGRTGSGKSTLgLTLLR-FTHRISGEIYINGretQSVNLNALRQR-ISFIPQDPILFSG-TVRSN--- 1306
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTL-LNLIAgFLTPASGSLTLNG---QDHTTTPPSRRpVSMLFQENNLFSHlTVAQNigl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1307 -LDPfdelednflneALKTSGASSMIMAHTDDQkpihITLDTHVASEGSNFSQGQKQVLALARAIVRRSKIIILDECTAS 1385
Cdd:PRK10771 95 gLNP-----------GLKLNAAQREKLHAIARQ----MGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSA 159
|
170 180 190
....*....|....*....|....*....|.
gi 19115470 1386 VDDAMDQKIQKTLREAFGDA--TMLCIAHRL 1414
Cdd:PRK10771 160 LDPALRQEMLTLVSQVCQERqlTLLMVSHSL 190
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1229-1440 |
6.98e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 76.70 E-value: 6.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1229 LKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRISFIPQDP--ILFSGTVRSN 1306
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPddQVFSSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1307 ---------LDPfDELEdNFLNEALKTSGassmiMAHTDDQKPIHItldthvasegsnfSQGQKQVLALARAIVRRSKII 1377
Cdd:PRK13647 101 vafgpvnmgLDK-DEVE-RRVEEALKAVR-----MWDFRDKPPYHL-------------SYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115470 1378 ILDECTASVDDAMDQKIQKTLREAFGDATMLCIA-HRLKTIVDY-DKVMVLDKGVLVEYGPPAVL 1440
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEWaDQVIVLKEGRVLAEGDKSLL 225
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1212-1438 |
1.09e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 75.50 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSY--------------SAAGPT------ILKDVNLHINPSEKVAVVGRTGSGKStlglTLLRFTHRI----S 1267
Cdd:COG1134 5 IEVENVSKSYrlyhepsrslkellLRRRRTrreefwALKDVSFEVERGESVGIIGRNGAGKS----TLLKLIAGIleptS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1268 GEIYINGRETQSVNLNAlrqriSFIPQ----DPILFSGTV----RSNLDP-------FDELEDnFLNEALKTsgassmim 1332
Cdd:COG1134 81 GRVEVNGRVSALLELGA-----GFHPEltgrENIYLNGRLlglsRKEIDEkfdeiveFAELGD-FIDQPVKT-------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1333 ahtddqkpihitldthvasegsnFSQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDA-TMLCIA 1411
Cdd:COG1134 147 -----------------------YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGrTVIFVS 203
|
250 260
....*....|....*....|....*...
gi 19115470 1412 HRLKTIVDY-DKVMVLDKGVLVEYGPPA 1438
Cdd:COG1134 204 HSMGAVRRLcDRAIWLEKGRLVMDGDPE 231
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1229-1446 |
1.15e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 75.58 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1229 LKDVNLHINPSEKVAVVGRTGSGKSTLgltlLRFTHR---------ISGEIYINGRETQSVNLNA--LRQRISFIPQDPI 1297
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTL----LRSINRmndlnpevtITGSIVYNGHNIYSPRTDTvdLRKEIGMVFQQPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1298 LFSGTVRSN----LDPFDELEDNFLNEALKTSGASSMIMAHTDDqkpihitldtHVASEGSNFSQGQKQVLALARAIVRR 1373
Cdd:PRK14239 97 PFPMSIYENvvygLRLKGIKDKQVLDEAVEKSLKGASIWDEVKD----------RLHDSALGLSGGQQQRVCIARVLATS 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115470 1374 SKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAHRLKTIVDY-DKVMVLDKGVLVEYGPPAVLYHNNGH 1446
Cdd:PRK14239 167 PKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRIsDRTGFFLDGDLIEYNDTKQMFMNPKH 240
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1212-1443 |
1.19e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 75.46 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAAgpTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFT-----HRISGEIYINGRE--TQSVNLNA 1284
Cdd:COG1117 12 IEVRNLNVYYGDK--QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlipgARVEGEILLDGEDiyDPDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1285 LRQRISFIPQDPILFSGTV---------------RSNLDP-----------FDELEDNflneaLKTSGASsmimahtddq 1338
Cdd:COG1117 90 LRRRVGMVFQKPNPFPKSIydnvayglrlhgiksKSELDEiveeslrkaalWDEVKDR-----LKKSALG---------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1339 kpihitldthvasegsnFSQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAHRL---K 1415
Cdd:COG1117 155 -----------------LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMqqaA 217
|
250 260
....*....|....*....|....*...
gi 19115470 1416 TIVDYdkVMVLDKGVLVEYGPPAVLYHN 1443
Cdd:COG1117 218 RVSDY--TAFFYLGELVEFGPTEQIFTN 243
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
631-812 |
1.19e-14 |
|
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: 74.85 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGS-----YNLPRS-----KGVSYVSQ---VPWlrNATIRDN 697
Cdd:cd03263 18 VDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTayingYSIRTDrkaarQSLGYCPQfdaLFD--ELTVREH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 698 ILF--------DYPYIEERyKKVIQACGLLTDLQSFVasdlteigekgVTLSGGQKQRIALARAVYSPTSIVLMDDVFSA 769
Cdd:cd03263 96 LRFyarlkglpKSEIKEEV-ELLLRVLGLTDKANKRA-----------RTLSGGMKRKLSLAIALIGGPSVLLLDEPTSG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 19115470 770 LDIHTSNWIYKhcFQSSLMENRTVILVTHNvhlfMDSAAFIVT 812
Cdd:cd03263 164 LDPASRRAIWD--LILEVRKGRSIILTTHS----MDEAEALCD 200
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1212-1436 |
1.39e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 75.69 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAaGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQsvnlNALRQR-IS 1290
Cdd:PRK15056 7 IVVNDVTVTWRN-GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNlVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1291 FIPQD-------PILFSGTVRsnLDPFDELedNFLNEALKTSGAS-SMIMAHTDDQKPIHITLdthvasegSNFSQGQKQ 1362
Cdd:PRK15056 82 YVPQSeevdwsfPVLVEDVVM--MGRYGHM--GWLRRAKKRDRQIvTAALARVDMVEFRHRQI--------GELSGGQKK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115470 1363 VLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDA-TMLCIAHRLKTIVDYDKVMVLDKGVLVEYGP 1436
Cdd:PRK15056 150 RVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGkTMLVSTHNLGSVTEFCDYTVMVKGTVLASGP 224
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1229-1441 |
1.53e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 75.90 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1229 LKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRISFIPQDPI-LFSGTVrsnl 1307
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPDnQFVGAT---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1308 dpfdeLEDNfLNEALKTSGASSMIMAHTDDQKPIHITLDTHVASEGSNFSQGQKQVLALARAIVRRSKIIILDECTASVD 1387
Cdd:PRK13642 99 -----VEDD-VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 19115470 1388 DAMDQKIQKTLREAFGD--ATMLCIAHRLKTIVDYDKVMVLDKGVLVEYGPPAVLY 1441
Cdd:PRK13642 173 PTGRQEIMRVIHEIKEKyqLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
901-1188 |
1.67e-14 |
|
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: 75.71 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 901 LLFFVTTQATSILIDLWVAFWTNSSVNSPDVNNNKFLFVYGTMLLAYSLLDFLRTVSYDRGAWWASRKLHDSMLESVFGT 980
Cdd:cd18559 5 IKLVLCNHVFSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 981 FASWFDKTPTGRIVNRFAKDIRSIdMNLSGWL--FFSINCFLSVAGGILsVSSAMPIFmipAVIVCLAGYYFGL--LYTR 1056
Cdd:cd18559 85 PISFFERTPSGELVNLFSKDLDRV-DSMAPQVikMWMGPLQNVIGLYLL-ILLAGPMA---AVGIPLGLLYVPVnrVYAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1057 AQVGVKRLISIYTSPIFSLLGESIVGVSVIRAFNRQTIFK-QMFSERLDNLVRLQSTSYnlNRWVAVRTDGISGLVGAIA 1135
Cdd:cd18559 160 SSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIrQVDAKRDNELAYLPSIVY--LRALAVRLWCVGPCIVLFA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 19115470 1136 GLIALLQKDLSPGVVGFSLNQAVIFSSSVLLFVRSCNSLQAEMNSYERVLEYS 1188
Cdd:cd18559 238 SFFAYVSRHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1216-1440 |
2.07e-14 |
|
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: 73.33 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1216 HVSVsysaAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRF-THRI-SGEIYINGRetqsvNLNAL----RQR- 1288
Cdd:cd03217 7 HVSV----GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpKYEVtEGEILFKGE-----DITDLppeeRARl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1289 ---ISFipQDPILFSGtvrsnldpfdelednflnealktsgassmimahtddqkpihITLDTHVASEGSNFSQGQKQVLA 1365
Cdd:cd03217 78 gifLAF--QYPPEIPG-----------------------------------------VKNADFLRYVNEGFSGGEKKRNE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1366 LARAIVRRSKIIILDECTASVD-DAMDQ--KIQKTLREafGDATMLCIAHRLKtIVDY---DKVMVLDKGVLVEYGPPAV 1439
Cdd:cd03217 115 ILQLLLLEPDLAILDEPDSGLDiDALRLvaEVINKLRE--EGKSVLIITHYQR-LLDYikpDRVHVLYDGRIVKSGDKEL 191
|
.
gi 19115470 1440 L 1440
Cdd:cd03217 192 A 192
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1219-1438 |
2.10e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 77.19 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1219 VSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRISFIPQDPIL 1298
Cdd:PRK09536 9 LSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1299 -FSGTVR-----------SNLDPFDELEDNFLNEALKTSGASSMImahtddQKPIhitldthvasegSNFSQGQKQVLAL 1366
Cdd:PRK09536 89 sFEFDVRqvvemgrtphrSRFDTWTETDRAAVERAMERTGVAQFA------DRPV------------TSLSGGERQRVLL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19115470 1367 ARAIVRRSKIIILDECTASVDdaMDQKIQkTL----REAFGDATMLCIAHRLKTIVDY-DKVMVLDKGVLVEYGPPA 1438
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLD--INHQVR-TLelvrRLVDDGKTAVAAIHDLDLAARYcDELVLLADGRVRAAGPPA 224
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
626-817 |
2.16e-14 |
|
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: 73.45 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 626 PGDFCLRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYNL--------PRSKGVSYVSQVP--WLRNATIR 695
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLngkpikakERRKSIGYVMQDVdyQLFTDSVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 696 DNILFDypyIEERYKKVIQACGLLTDLqsfvasDLTEIGEKG-VTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDiht 774
Cdd:cd03226 91 EELLLG---LKELDAGNEQAETVLKDL------DLYALKERHpLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD--- 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 19115470 775 snwiYKHcfqsslMEN------------RTVILVTHNVHLFMDSAAFIVTVKNGS 817
Cdd:cd03226 159 ----YKN------MERvgelirelaaqgKAVIVITHDYEFLAKVCDRVLLLANGA 203
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
646-771 |
2.26e-14 |
|
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: 77.87 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 646 VIGPTGSGKSSLISALLGELSLNKGS--------YNLPRS---KGVSYVSQVPWLRNATIRDNI-LFDYPYIEerykKVI 713
Cdd:COG4618 363 VIGPSGSGKSTLARLLVGVWPPTAGSvrldgadlSQWDREelgRHIGYLPQDVELFDGTIAENIaRFGDADPE----KVV 438
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19115470 714 QACgLLTDLQSFVAS-----DlTEIGEKGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALD 771
Cdd:COG4618 439 AAA-KLAGVHEMILRlpdgyD-TRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLD 499
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1225-1437 |
2.55e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 75.11 E-value: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1225 GPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVN--LNALRQRISFIPQDP--ILFS 1300
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKksLLEVRKTVGIVFQNPddQLFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1301 GTVRS-------NLD-PFDELEdNFLNEALKTSGASSMimahtdDQKPIHitldthvasegsNFSQGQKQVLALARAIVR 1372
Cdd:PRK13639 94 PTVEEdvafgplNLGlSKEEVE-KRVKEALKAVGMEGF------ENKPPH------------HLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19115470 1373 RSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIA-HRLKTIVDY-DKVMVLDKGVLVEYGPP 1437
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVPVYaDKVYVMSDGKIIKEGTP 221
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
603-805 |
2.55e-14 |
|
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: 77.87 E-value: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 603 TIEDTSQEIGFFNASLTwvsNPSpGDFCLRDLNIVFPRNKLSIVIGPTGSGKSSLISaLLGEL-SLNKGSYNLPRSKGVS 681
Cdd:TIGR00954 444 IVEYQDNGIKFENIPLV---TPN-GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELwPVYGGRLTKPAKGKLF 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 682 YVSQVPWLRNATIRDNILfdYP-YIEERYKKVIQACGLLTDLQSFvasDLTEIGEKGV----------TLSGGQKQRIAL 750
Cdd:TIGR00954 519 YVPQRPYMTLGTLRDQII--YPdSSEDMKRRGLSDKDLEQILDNV---QLTHILEREGgwsavqdwmdVLSGGEKQRIAM 593
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 19115470 751 ARAVYSPTSIVLMDDVFSALDIHTSNWIYKHC--FQSSLME--NRTVILVTHNVHLFMD 805
Cdd:TIGR00954 594 ARLFYHKPQFAILDECTSAVSVDVEGYMYRLCreFGITLFSvsHRKSLWKYHEYLLYMD 652
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1212-1437 |
2.81e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 75.02 E-value: 2.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAAGPTiLKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVN-LNALRQRIS 1290
Cdd:PRK13644 2 IRLENVSYSYPDGTPA-LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1291 FIPQDP-ILFSG-TVRSNLDPFDEledNFLNEALKTSGASSMIMAHTDDQKPIHITLDThvasegsnFSQGQKQVLALAR 1368
Cdd:PRK13644 81 IVFQNPeTQFVGrTVEEDLAFGPE---NLCLPPIEIRKRVDRALAEIGLEKYRHRSPKT--------LSGGQGQCVALAG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19115470 1369 AIVRRSKIIILDECTASVD----DAMDQKIQKTLREAfgdATMLCIAHRLKTIVDYDKVMVLDKGVLVEYGPP 1437
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDpdsgIAVLERIKKLHEKG---KTIVYITHNLEELHDADRIIVMDRGKIVLEGEP 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1215-1446 |
3.09e-14 |
|
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: 77.42 E-value: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1215 NHVSVSYSAAGPT--ILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRF----THRISGEIYINGRETQSVNLNALRQ- 1287
Cdd:COG4172 10 EDLSVAFGQGGGTveAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILFDGQDLLGLSERELRRi 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1288 ---RISFIPQDPIlfsgtvrSNLDPFDELEDNfLNEALKT----SGASSMIMAH--------TDDQKPI----Hitldth 1348
Cdd:COG4172 90 rgnRIAMIFQEPM-------TSLNPLHTIGKQ-IAEVLRLhrglSGAAARARALellervgiPDPERRLdaypH------ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1349 vasegsNFSQGQKQVLALARAIVRRSKIIILDECTAsvddAMDQKIQ-------KTLREAFGDAtMLCIAHRLkTIV-DY 1420
Cdd:COG4172 156 ------QLSGGQRQRVMIAMALANEPDLLIADEPTT----ALDVTVQaqildllKDLQRELGMA-LLLITHDL-GVVrRF 223
|
250 260
....*....|....*....|....*..
gi 19115470 1421 -DKVMVLDKGVLVEYGPPAVLYHNNGH 1446
Cdd:COG4172 224 aDRVAVMRQGEIVEQGPTAELFAAPQH 250
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
627-772 |
3.53e-14 |
|
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: 75.92 E-value: 3.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 627 GDFCLrDLNIVFPRNKLSIVIGPTGSGKSSL---ISALL----GELSLN--------KGSYNLPRSKGVSYVSQ----VP 687
Cdd:TIGR02142 10 GDFSL-DADFTLPGQGVTAIFGRSGSGKTTLirlIAGLTrpdeGEIVLNgrtlfdsrKGIFLPPEKRRIGYVFQearlFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 688 WLrnaTIRDNILFDY-----PYIEERYKKVIQACGLLTDLQSFVAsdlteigekgvTLSGGQKQRIALARAVYSPTSIVL 762
Cdd:TIGR02142 89 HL---SVRGNLRYGMkrarpSERRISFERVIELLGIGHLLGRLPG-----------RLSGGEKQRVAIGRALLSSPRLLL 154
|
170
....*....|
gi 19115470 763 MDDVFSALDI 772
Cdd:TIGR02142 155 MDEPLAALDD 164
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
578-798 |
3.62e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 77.31 E-value: 3.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 578 IVQIFVSIGRVSDFLNDPDEV----DPVNTIE--DTSQEIGFFNASLTWvSNPSPGdfcLRDLNI-VFPRNKLSIViGPT 650
Cdd:PRK13657 296 INQVFMAAPKLEEFFEVEDAVpdvrDPPGAIDlgRVKGAVEFDDVSFSY-DNSRQG---VEDVSFeAKPGQTVAIV-GPT 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 651 GSGKSSLISAL-------LGEL--------SLNKGSynLPRSKGVsyVSQVPWLRNATIRDNILFDYPYI--EERYK--K 711
Cdd:PRK13657 371 GAGKSTLINLLqrvfdpqSGRIlidgtdirTVTRAS--LRRNIAV--VFQDAGLFNRSIEDNIRVGRPDAtdEEMRAaaE 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 712 VIQAcglltdlQSFVASDL----TEIGEKGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIykhcfQSSL 787
Cdd:PRK13657 447 RAQA-------HDFIERKPdgydTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKV-----KAAL 514
|
250
....*....|....
gi 19115470 788 ---MENRTVILVTH 798
Cdd:PRK13657 515 delMKGRTTFIIAH 528
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
631-799 |
4.01e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 73.21 E-value: 4.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKS-------SLISALLGEL--------SLNKGSYNlprsKGVSYVSQVPWLRNATIR 695
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKStllkivaSLISPTSGTLlfegedisTLKPEIYR----QQVSYCAQTPTLFGDTVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 696 DNILFdyPYiEERYKKViQACGLLTDLQSFVASDltEIGEKGVT-LSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHT 774
Cdd:PRK10247 99 DNLIF--PW-QIRNQQP-DPAIFLDDLERFALPD--TILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDESN 172
|
170 180
....*....|....*....|....*...
gi 19115470 775 S---NWIYKHCFQSslmENRTVILVTHN 799
Cdd:PRK10247 173 KhnvNEIIHRYVRE---QNIAVLWVTHD 197
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1227-1435 |
5.03e-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: 72.95 E-value: 5.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1227 TILKDVNLHINPSEKVAVVGRTGSGKStlglTLLRFTHRI----SGEIYINGRETQSVNLNAlrqriSFIPQ----DPIL 1298
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKS----TLLRLLAGIyppdSGTVTVRGRVSSLLGLGG-----GFNPEltgrENIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1299 FSGTVrSNLDP------------FDELEDnFLNEALKTsgassmimahtddqkpihitldthvasegsnFSQGQKQVLAL 1366
Cdd:cd03220 107 LNGRL-LGLSRkeidekideiieFSELGD-FIDLPVKT-------------------------------YSSGMKARLAF 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19115470 1367 ARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIA-HRLKTIVDY-DKVMVLDKGVLVEYG 1435
Cdd:cd03220 154 AIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1212-1443 |
5.75e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 74.10 E-value: 5.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAAGPTI---LKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGR----ETQSVNLNA 1284
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEkkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhitpETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1285 LRQRISFIPQDP--ILFSGTVRSNLD--P--FDELEDNFLNEA---LKTSGASSMIMAHTddqkPIHItldthvasegsn 1355
Cdd:PRK13641 83 LRKKVSLVFQFPeaQLFENTVLKDVEfgPknFGFSEDEAKEKAlkwLKKVGLSEDLISKS----PFEL------------ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1356 fSQGQKQVLALARAIVRRSKIIILDECTAsvddAMDQKIQKTLREAFGD-----ATMLCIAHRLKTIVDY-DKVMVLDKG 1429
Cdd:PRK13641 147 -SGGQMRRVAIAGVMAYEPEILCLDEPAA----GLDPEGRKEMMQLFKDyqkagHTVILVTHNMDDVAEYaDDVLVLEHG 221
|
250
....*....|....
gi 19115470 1430 VLVEYGPPAVLYHN 1443
Cdd:PRK13641 222 KLIKHASPKEIFSD 235
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1208-1435 |
5.86e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 73.54 E-value: 5.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1208 KEGDIVFNHVSVSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTH------RISGEIYINGRETQSVN 1281
Cdd:PRK14246 5 KSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQID 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1282 LNALRQRISFIPQDPILFSgtvrsNLDPFDELEDNFLNEALKTSGASSMIMAHTDDQKPIHITLDTHVASEGSNFSQGQK 1361
Cdd:PRK14246 85 AIKLRKEVGMVFQQPNPFP-----HLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19115470 1362 QVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAH---RLKTIVDYdkVMVLDKGVLVEYG 1435
Cdd:PRK14246 160 QRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHnpqQVARVADY--VAFLYNGELVEWG 234
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1228-1432 |
1.17e-13 |
|
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: 71.92 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1228 ILKDVNLHINPSEKVAVVGRTGSGKSTLgLTL----LRFTHRISGEIYINGREtqsVNLNALRQRISFIPQDPILFSG-T 1302
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTL-LDAisgrVEGGGTTSGQILFNGQP---RKPDQFQKCVAYVRQDDILLPGlT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1303 VRSNLdPFDEledNFLNEALKTSGASSMImahtDDQKPIHITLDTHVASEG-SNFSQGQKQVLALARAIVRRSKIIILDE 1381
Cdd:cd03234 98 VRETL-TYTA---ILRLPRKSSDAIRKKR----VEDVLLRDLALTRIGGNLvKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 19115470 1382 CTASVDDAMDQKIQKTLRE-AFGDATMLCIAH-------RLktivdYDKVMVLDKGVLV 1432
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQlARRNRIVILTIHqprsdlfRL-----FDRILLLSSGEIV 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1212-1443 |
1.20e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 72.43 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAAgpTILKDVNLHINPSEKVAVVGRTGSGKStlglTLLRFTHRI----SGEIYINGretQSVNLNALRQ 1287
Cdd:PRK09493 2 IEFKNVSKHFGPT--QVLHNIDLNIDQGEVVVIIGPSGSGKS----TLLRCINKLeeitSGDLIVDG---LKVNDPKVDE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1288 RIsfIPQDpilfSGTVRSNLDPFDELE--DNFLNEALKTSGASSmimahTDDQKPIHITLDT--------HVASEgsnFS 1357
Cdd:PRK09493 73 RL--IRQE----AGMVFQQFYLFPHLTalENVMFGPLRVRGASK-----EEAEKQARELLAKvglaerahHYPSE---LS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1358 QGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLRE-AFGDATMLCIAHRLKTIVDY-DKVMVLDKGVLVEYG 1435
Cdd:PRK09493 139 GGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDlAEEGMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDG 218
|
....*...
gi 19115470 1436 PPAVLYHN 1443
Cdd:PRK09493 219 DPQVLIKN 226
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1224-1429 |
1.43e-13 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 71.59 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1224 AGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQR----ISFIPQDPILF 1299
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1300 SGTVRSNL---DPFDELEDNFLNEALKTSgASSMIMAHTDdqkpihitlDTHVASEGSNFSQGQKQVLALARAIVRRSKI 1376
Cdd:cd03290 92 NATVEENItfgSPFNKQRYKAVTDACSLQ-PDIDLLPFGD---------QTEIGERGINLSGGQRQRICVARALYQNTNI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 19115470 1377 IILDECTASV-----DDAMDQKIQKTLREafGDATMLCIAHRLKTIVDYDKVMVLDKG 1429
Cdd:cd03290 162 VFLDDPFSALdihlsDHLMQEGILKFLQD--DKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1229-1446 |
1.67e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 73.46 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1229 LKDVNLHINPSEKVAVVGRTGSGKSTLG--LTLLRftHRISGEIYINGRETQSVN---LNALRQRISFIPQDPilFSG-- 1301
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLArlLTMIE--TPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNP--YGSln 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1302 ---TVRSNLDpfDELEDNF-LNEALKTSGASSMiMAHTDdQKPIHITLDTHVasegsnFSQGQKQVLALARAIVRRSKII 1377
Cdd:PRK11308 107 prkKVGQILE--EPLLINTsLSAAERREKALAM-MAKVG-LRPEHYDRYPHM------FSGGQRQRIAIARALMLDPDVV 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19115470 1378 ILDECTAsvddAMDQKIQKT-------LREAFGDAtMLCIAHRLkTIVDY--DKVMVLDKGVLVEYGPPAVLYHNNGH 1446
Cdd:PRK11308 177 VADEPVS----ALDVSVQAQvlnlmmdLQQELGLS-YVFISHDL-SVVEHiaDEVMVMYLGRCVEKGTKEQIFNNPRH 248
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
627-798 |
1.98e-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: 73.59 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 627 GDFC-LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGS--------YNLPRSK-GVSYVSQvpwlRNA---- 692
Cdd:COG3842 16 GDVTaLDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRilldgrdvTGLPPEKrNVGMVFQ----DYAlfph 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 693 -TIRDNILF-----DYPyIEERYKKVIQACGLLtdlqsfvasDLTEIGEKGV-TLSGGQKQRIALARA-VYSPtSIVLMD 764
Cdd:COG3842 92 lTVAENVAFglrmrGVP-KAEIRARVAELLELV---------GLEGLADRYPhQLSGGQQQRVALARAlAPEP-RVLLLD 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 19115470 765 DVFSALD----IHTSNWIYKHcfQSSLmeNRTVILVTH 798
Cdd:COG3842 161 EPLSALDaklrEEMREELRRL--QREL--GITFIYVTH 194
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
631-816 |
2.04e-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: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSY-----NLPRSKGvsyvSQVPWLR--------------N 691
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIrvngqDVSDLRG----RAIPYLRrkigvvfqdfrllpD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 692 ATIRDNILF-----DYPY--IEERYKKVIQACGLLTDLQSFVASdlteigekgvtLSGGQKQRIALARAVYSPTSIVLMD 764
Cdd:cd03292 93 RNVYENVAFalevtGVPPreIRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIAD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 19115470 765 DVFSALDIHTSNWIYKhCFQSSLMENRTVILVTHNVHLFMDSAAFIVTVKNG 816
Cdd:cd03292 162 EPTGNLDPDTTWEIMN-LLKKINKAGTTVVVATHAKELVDTTRHRVIALERG 212
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
627-799 |
2.04e-13 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 73.26 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 627 GDFC-LRDLNIVFPRNKLSIVIGPTGSGKSSL---ISALL----GELSLNkG---SYNLP-RSKGVSYVSQVPWL-RNAT 693
Cdd:COG1118 13 GSFTlLDDVSLEIASGELVALLGPSGSGKTTLlriIAGLEtpdsGRIVLN-GrdlFTNLPpRERRVGFVFQHYALfPHMT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 694 IRDNILF-------DYPYIEERYKKviqacgLLTDLQsfvasdLTEIGEKGVT-LSGGQKQRIALARAVYSPTSIVLMDD 765
Cdd:COG1118 92 VAENIAFglrvrppSKAEIRARVEE------LLELVQ------LEGLADRYPSqLSGGQRQRVALARALAVEPEVLLLDE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 19115470 766 VFSALDIHTSN----WiykhcfqssLME-----NRTVILVTHN 799
Cdd:COG1118 160 PFGALDAKVRKelrrW---------LRRlhdelGGTTVFVTHD 193
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1212-1443 |
2.25e-13 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 73.26 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYsaAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLgLtllrfthRI--------SGEIYINGRETQSvNLN 1283
Cdd:COG1118 3 IEVRNISKRF--GSFTLLDDVSLEIASGELVALLGPSGSGKTTL-L-------RIiagletpdSGRIVLNGRDLFT-NLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1284 ALRQRISFIPQDPILFSG-TVRsnldpfdeleDN--FLNEALKTSGAS---------SMI-MAHTDDQKPihitldthva 1350
Cdd:COG1118 72 PRERRVGFVFQHYALFPHmTVA----------ENiaFGLRVRPPSKAEirarveellELVqLEGLADRYP---------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1351 segSNFSQGQKQVLALARAIVRRSKIIILDECTAsvddAMDQKIQKTLR-------EAFG-----------DATMLCiah 1412
Cdd:COG1118 132 ---SQLSGGQRQRVALARALAVEPEVLLLDEPFG----ALDAKVRKELRrwlrrlhDELGgttvfvthdqeEALELA--- 201
|
250 260 270
....*....|....*....|....*....|.
gi 19115470 1413 rlktivdyDKVMVLDKGVLVEYGPPAVLYHN 1443
Cdd:COG1118 202 --------DRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1229-1435 |
2.66e-13 |
|
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: 70.79 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1229 LKDVNLHIN---PSEKVAVVGRTGSGKSTL-----GLTllRFTHrisGEIYINGR----ETQSVNLNALRQRISFIPQDP 1296
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLlrciaGLE--KPDG---GTIVLNGTvlfdSRKKINLPPQQRKIGLVFQQY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1297 ILFSG-TVRSNLdpfdelednflneALKTSGASSMIMAHTDDQKPIHITLDTHVASEGSNFSQGQKQVLALARAIVRRSK 1375
Cdd:cd03297 85 ALFPHlNVRENL-------------AFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19115470 1376 IIILDECTASVDDAMDQKIQKTLREAFGD--ATMLCIAHRLKTIVDY-DKVMVLDKGVLVEYG 1435
Cdd:cd03297 152 LLLLDEPFSALDRALRLQLLPELKQIKKNlnIPVIFVTHDLSEAEYLaDRIVVMEDGRLQYIG 214
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
627-816 |
2.70e-13 |
|
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: 71.18 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 627 GDFCLRDLNIVFPRNKLSIVIGPTGSGKSS---LISALL----GELSLNKGSYN------LPRSKGvsYV-SQVPWLRNA 692
Cdd:cd03295 13 GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTtmkMINRLIeptsGEIFIDGEDIReqdpveLRRKIG--YViQQIGLFPHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 693 TIRDNI-----LFDYP--YIEERYKKVIQACGLltDLQSFVASDLTEigekgvtLSGGQKQRIALARAVYSPTSIVLMDD 765
Cdd:cd03295 91 TVEENIalvpkLLKWPkeKIRERADELLALVGL--DPAEFADRYPHE-------LSGGQQQRVGVARALAADPPLLLMDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 766 VFSALDIHTsnwiykhcfQSSLME---------NRTVILVTHNVHLFMDSAAFIVTVKNG 816
Cdd:cd03295 162 PFGALDPIT---------RDQLQEefkrlqqelGKTIVFVTHDIDEAFRLADRIAIMKNG 212
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
631-798 |
2.75e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 74.37 E-value: 2.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYNL---PRS--------KGVSYVSQVPWLRNATIRDNIL 699
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLdgrPLSslshsvlrQGVAMVQQDPVVLADTFLANVT 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 700 FDYPYIEERYKKVIQACGLLTDLQSFVASDLTEIGEKGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIy 779
Cdd:PRK10790 437 LGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAI- 515
|
170 180
....*....|....*....|..
gi 19115470 780 khcfQSSLM---ENRTVILVTH 798
Cdd:PRK10790 516 ----QQALAavrEHTTLVVIAH 533
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
621-816 |
3.39e-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: 74.17 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 621 VSNPSPGDFCLRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGEL---------------SLNKGSYNLpRSKGVSYVSQ 685
Cdd:COG1123 12 VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLphggrisgevlldgrDLLELSEAL-RGRRIGMVFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 686 VPW--LRNATIRDNILF-------DYPYIEERYKKVIQACGLLTDLQSFVAsdlteigekgvTLSGGQKQRIALARAVYS 756
Cdd:COG1123 91 DPMtqLNPVTVGDQIAEalenlglSRAEARARVLELLEAVGLERRLDRYPH-----------QLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 757 PTSIVLMDDVFSALDIHTSNWIYKHCFQSSLMENRTVILVTHNVHLFMDSAAFIVTVKNG 816
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDG 219
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1211-1437 |
3.52e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 71.97 E-value: 3.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1211 DIVFNHVSVSYSAAGP---TILKDVNLHINPSEKVAVVGRTGSGKSTL-----GltLLRFThriSGEIYINGR----ETQ 1278
Cdd:PRK13634 2 DITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLlqhlnG--LLQPT---SGTVTIGERvitaGKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1279 SVNLNALRQRISFIPQDP--ILFSGTVRSNLdPFDELedNF---LNEALKTsgASSMIMAhtddqkpihITLDTHVASEg 1353
Cdd:PRK13634 77 NKKLKPLRKKVGIVFQFPehQLFEETVEKDI-CFGPM--NFgvsEEDAKQK--AREMIEL---------VGLPEELLAR- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1354 SNF--SQGQKQVLALARAIVRRSKIIILDECTAsvddAMDQKIQKTLREAF------GDATMLCIAHRLKTIVDY-DKVM 1424
Cdd:PRK13634 142 SPFelSGGQMRRVAIAGVLAMEPEVLVLDEPTA----GLDPKGRKEMMEMFyklhkeKGLTTVLVTHSMEDAARYaDQIV 217
|
250
....*....|...
gi 19115470 1425 VLDKGVLVEYGPP 1437
Cdd:PRK13634 218 VMHKGTVFLQGTP 230
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
631-816 |
3.54e-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: 70.67 E-value: 3.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYNLprsKGVSyVSQVPWLRNATIRDNI--LF-DYPYIEE 707
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLI---DGTD-INKLKGKALRQLRRQIgmIFqQFNLIER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 708 RYkkVIQA--CGLLTD-------LQSFVASD-------LTEIGEKGV------TLSGGQKQRIALARAVYSPTSIVLMDD 765
Cdd:cd03256 93 LS--VLENvlSGRLGRrstwrslFGLFPKEEkqralaaLERVGLLDKayqradQLSGGQQQRVAIARALMQQPKLILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 19115470 766 VFSALDIHTSNWIYKHCFQSSLMENRTVILVTHNVHLFMDSAAFIVTVKNG 816
Cdd:cd03256 171 PVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDG 221
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
610-811 |
4.70e-13 |
|
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: 69.75 E-value: 4.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 610 EIGFFNASLTWVSNPSPgdfCLRDLNI-VFPRNKLSIViGPTGSGKSSLISALLGELSLNKGSYNLP------------R 676
Cdd:cd03369 6 EIEVENLSVRYAPDLPP---VLKNVSFkVKAGEKIGIV-GRTGAGKSTLILALFRFLEAEEGKIEIDgidistipledlR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 677 SKgVSYVSQVPWLRNATIRDNIlfDypyIEERYkkviqacgllTDLQSFVAsdlTEIGEKGVTLSGGQKQRIALARAVYS 756
Cdd:cd03369 82 SS-LTIIPQDPTLFSGTIRSNL--D---PFDEY----------SDEEIYGA---LRVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 19115470 757 PTSIVLMDDVFSALDIHTSNWIYKHCfqSSLMENRTVILVTHNVHLFMDSAAFIV 811
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTI--REEFTNSTILTIAHRLRTIIDYDKILV 195
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
627-816 |
5.35e-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: 70.45 E-value: 5.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 627 GDF-CLRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYNL---------PRSKGVSYVSQVPWL-RNATIR 695
Cdd:cd03296 13 GDFvALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFggedatdvpVQERNVGFVFQHYALfRHMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 696 DNILF--------DYPYIEERYKKVIQACGLLtDLQSFVASDLTEigekgvtLSGGQKQRIALARAVYSPTSIVLMDDVF 767
Cdd:cd03296 93 DNVAFglrvkprsERPPEAEIRAKVHELLKLV-QLDWLADRYPAQ-------LSGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 19115470 768 SALDIHT----SNWIYKhcFQSSLmeNRTVILVTHNVHLFMDSAAFIVTVKNG 816
Cdd:cd03296 165 GALDAKVrkelRRWLRR--LHDEL--HVTTVFVTHDQEEALEVADRVVVMNKG 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
631-801 |
6.84e-13 |
|
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: 69.84 E-value: 6.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGS----------------YNLPRSKGVsyVSQVPWLRNA-T 693
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEvlidgedisglseaelYRLRRRMGM--LFQSGALFDSlT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 694 IRDNILF--------DYPYIEERYKKVIQACGLLTDLQSFVASdlteigekgvtLSGGQKQRIALARAVYSPTSIVLMDD 765
Cdd:cd03261 94 VFENVAFplrehtrlSEEEIREIVLEKLEAVGLRGAEDLYPAE-----------LSGGMKKRVALARALALDPELLLYDE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 19115470 766 VFSALDIHTSNWIykhcfqSSLM------ENRTVILVTHNVH 801
Cdd:cd03261 163 PTAGLDPIASGVI------DDLIrslkkeLGLTSIMVTHDLD 198
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
627-814 |
7.95e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 70.30 E-value: 7.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 627 GDFCLRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYNL---PRSKG-----VSYVSQ---VPWLRNATIR 695
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISIlgqPTRQAlqknlVAYVPQseeVDWSFPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 696 DNILFD-YPYI------EERYKKVIQACGLLTDLQSFVASdltEIGEkgvtLSGGQKQRIALARAVYSPTSIVLMDDVFS 768
Cdd:PRK15056 99 DVVMMGrYGHMgwlrraKKRDRQIVTAALARVDMVEFRHR---QIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 19115470 769 ALDIHTSNWIYkhcfqsSLM-----ENRTVILVTHNVHLFMDSAAFIVTVK 814
Cdd:PRK15056 172 GVDVKTEARII------SLLrelrdEGKTMLVSTHNLGSVTEFCDYTVMVK 216
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1212-1443 |
8.05e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 70.45 E-value: 8.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAAgpTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHrISGEIYINGR--------ETQSVNLN 1283
Cdd:PRK14258 8 IKVNNLSFYYDTQ--KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRveffnqniYERRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1284 ALRQRISFIPQDPILFSGTVRSNL---------DPFDELeDNFLNEALKTSGASSMImahtddQKPIHitldthvaSEGS 1354
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVaygvkivgwRPKLEI-DDIVESALKDADLWDEI------KHKIH--------KSAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1355 NFSQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAF--GDATMLCIAHRLKTIVDYDKVMVLDKG--- 1429
Cdd:PRK14258 150 DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQVSRLSDFTAFFKGnen 229
|
250
....*....|....*..
gi 19115470 1430 ---VLVEYGPPAVLYHN 1443
Cdd:PRK14258 230 rigQLVEFGLTKKIFNS 246
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
631-798 |
9.38e-13 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 72.93 E-value: 9.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLN-IVFPRNKLSIViGPTGSGKSSlISALL--------GELSLN--------KGSynLPRSKGVsyVSQVPWLRNAT 693
Cdd:COG5265 374 LKGVSfEVPAGKTVAIV-GPSGAGKST-LARLLfrfydvtsGRILIDgqdirdvtQAS--LRAAIGI--VPQDTVLFNDT 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 694 IRDNILFDYPYIEERykKVIQACGLlTDLQSFVASdL-----TEIGEKGVTLSGGQKQRIALARAVYSPTSIVLMDDVFS 768
Cdd:COG5265 448 IAYNIAYGRPDASEE--EVEAAARA-AQIHDFIES-LpdgydTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATS 523
|
170 180 190
....*....|....*....|....*....|...
gi 19115470 769 ALDIHTSNWIykhcfQSSLME---NRTVILVTH 798
Cdd:COG5265 524 ALDSRTERAI-----QAALREvarGRTTLVIAH 551
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1227-1400 |
1.13e-12 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 69.11 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1227 TILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQR-ISFIPQDPILFSG-TVR 1304
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYLPQEASIFRKlTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1305 SNLDPFdeLEDNFLNEALKTSGASSMImahtddqKPIHITldtHVA-SEGSNFSQGQKQVLALARAIVRRSKIIILDECT 1383
Cdd:cd03218 94 ENILAV--LEIRGLSKKEREEKLEELL-------EEFHIT---HLRkSKASSLSGGERRRVEIARALATNPKFLLLDEPF 161
|
170
....*....|....*..
gi 19115470 1384 ASVDDAMDQKIQKTLRE 1400
Cdd:cd03218 162 AGVDPIAVQDIQKIIKI 178
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1212-1432 |
1.27e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 68.75 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYsAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLgLTLLRFTHRIS-GEIYINGRET---QSVNLNALRQ 1287
Cdd:PRK10908 2 IRFEHVSKAY-LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTL-LKLICGIERPSaGKIWFSGHDItrlKNREVPFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1288 RISFIPQDP-ILFSGTVRSNLdpfdelednflNEALKTSGASSmimahTDDQKPIHITLD-THVASEGSNF----SQGQK 1361
Cdd:PRK10908 80 QIGMIFQDHhLLMDRTVYDNV-----------AIPLIIAGASG-----DDIRRRVSAALDkVGLLDKAKNFpiqlSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115470 1362 QVLALARAIVRRSKIIILDECTASVDDAMDQKIQKtLREAFG--DATMLCIAHRLKTIVDYD-KVMVLDKGVLV 1432
Cdd:PRK10908 144 QRVGIARAVVNKPAVLLADEPTGNLDDALSEGILR-LFEEFNrvGVTVLMATHDIGLISRRSyRMLTLSDGHLH 216
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
633-816 |
1.94e-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: 67.90 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 633 DLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYNLprsKGVSYVSQVPWLRNATI--RDNILFDYPYIEERYk 710
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLI---NGVDVTAAPPADRPVSMlfQENNLFAHLTVEQNV- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 711 kviqACGLLTDL------QSFVASDLTEIGEKGV------TLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWI 778
Cdd:cd03298 92 ----GLGLSPGLkltaedRQAIEVALARVGLAGLekrlpgELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEM 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 19115470 779 YKHCFQSSLMENRTVILVTHNVHLFMDSAAFIVTVKNG 816
Cdd:cd03298 168 LDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNG 205
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
631-802 |
2.07e-12 |
|
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: 68.30 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNK----------LSI-------VIGPTGSGKSSLISALLG--------------ELSLNKGSYNLPRSKG 679
Cdd:cd03257 4 VKNLSVSFPTGGgsvkalddvsFSIkkgetlgLVGESGSGKSTLARAILGllkptsgsiifdgkDLLKLSRRLRKIRRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 680 VSYVSQVPwlRNA-----TIRDNI------LFDYPYIEERYKKVIQA-CGLLTD---LQSFVASdlteigekgvtLSGGQ 744
Cdd:cd03257 84 IQMVFQDP--MSSlnprmTIGEQIaeplriHGKLSKKEARKEAVLLLlVGVGLPeevLNRYPHE-----------LSGGQ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 745 KQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIYK--HCFQSSLmeNRTVILVTHNVHL 802
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDllKKLQEEL--GLTLLFITHDLGV 208
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1216-1438 |
2.18e-12 |
|
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: 68.91 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1216 HVSVSYsaAGPTILKDVNLHINPSEKVAVVGRTGSGKSTL-----GLtlLRFThriSGEIYINGREtqsvnLNALR-QRI 1289
Cdd:COG0411 9 GLTKRF--GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLfnlitGF--YRPT---SGRILFDGRD-----ITGLPpHRI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1290 -------SFipQDPILFSG-TVRSNLD--PFDELEDNFLNEALKTSGASSMIMAHTDDqkpIHITLD----THVASE-GS 1354
Cdd:COG0411 77 arlgiarTF--QNPRLFPElTVLENVLvaAHARLGRGLLAALLRLPRARREEREARER---AEELLErvglADRADEpAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1355 NFSQGQKQVLALARAIVRRSKIIILDECTASVD----DAMDQKIQKtLREAFGdATMLCIAHRLKTIVDY-DKVMVLDKG 1429
Cdd:COG0411 152 NLSYGQQRRLEIARALATEPKLLLLDEPAAGLNpeetEELAELIRR-LRDERG-ITILLIEHDMDLVMGLaDRIVVLDFG 229
|
250
....*....|
gi 19115470 1430 -VLVEyGPPA 1438
Cdd:COG0411 230 rVIAE-GTPA 238
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1219-1389 |
2.18e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.20 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1219 VSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRISFIPQDPIL 1298
Cdd:PRK10247 13 VGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1299 FSGTVRSNLD-PF----DELEDNFLNEALKTSGASSMIMahtddQKPIhitldthvasegSNFSQGQKQVLALARAIVRR 1373
Cdd:PRK10247 93 FGDTVYDNLIfPWqirnQQPDPAIFLDDLERFALPDTIL-----TKNI------------AELSGGEKQRISLIRNLQFM 155
|
170
....*....|....*.
gi 19115470 1374 SKIIILDECTASVDDA 1389
Cdd:PRK10247 156 PKVLLLDEITSALDES 171
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1212-1443 |
2.34e-12 |
|
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: 68.52 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAAgpTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNlnaLRQR-IS 1290
Cdd:cd03296 3 IEVRNVSKRFGDF--VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP---VQERnVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1291 FIPQDPILFSG-TVRSNLdPFdelednflneALKTSGASSMIMAHTDDQKpIH-----ITLDTHVASEGSNFSQGQKQVL 1364
Cdd:cd03296 78 FVFQHYALFRHmTVFDNV-AF----------GLRVKPRSERPPEAEIRAK-VHellklVQLDWLADRYPAQLSGGQRQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1365 ALARAIVRRSKIIILDECTAsvddAMDQKIQKTLR---EAFGD---ATMLCIAHRLKTIVDY-DKVMVLDKGVLVEYGPP 1437
Cdd:cd03296 146 ALARALAVEPKVLLLDEPFG----ALDAKVRKELRrwlRRLHDelhVTTVFVTHDQEEALEVaDRVVVMNKGRIEQVGTP 221
|
....*.
gi 19115470 1438 AVLYHN 1443
Cdd:cd03296 222 DEVYDH 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
631-808 |
2.45e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 71.25 E-value: 2.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVF-PRNKLSIViGPTGSGKSSLISALLGELSLNKGSYNLPRSKGVSYVSQ-VPWLRNATIRDNILFDYPY---I 705
Cdd:COG0488 14 LDDVSLSInPGDRIGLV-GRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQePPLDDDLTVLDTVLDGDAElraL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 706 EERYKKVIQACGLLTDLQSFVASDLTEIGEKGV--------------------------TLSGGQKQRIALARAVYSPTS 759
Cdd:COG0488 93 EAELEELEAKLAEPDEDLERLAELQEEFEALGGweaearaeeilsglgfpeedldrpvsELSGGWRRRVALARALLSEPD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 19115470 760 IVLMDdvfsaLDIHTSNWI------YKHcfqsslmenrTVILVTHNVHlFMDSAA 808
Cdd:COG0488 173 LLLLDeptnhLDLESIEWLeeflknYPG----------TVLVVSHDRY-FLDRVA 216
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1228-1441 |
2.97e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 68.88 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1228 ILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGR--ETQSVNLNALRQRISFIPQDP--------- 1296
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDPeqqifytdi 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1297 ---ILFSgtVRSNLDPFDELednflneALKTSGASSMIMAHTDDQKPIHItldthvasegsnFSQGQKQVLALARAIVRR 1373
Cdd:PRK13638 96 dsdIAFS--LRNLGVPEAEI-------TRRVDEALTLVDAQHFRHQPIQC------------LSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1374 SKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCI-AHRLKTIVDY-DKVMVLDKGVLVEYGPPAVLY 1441
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIYEIsDAVYVLRQGQILTHGAPGEVF 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
631-804 |
3.54e-12 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 68.35 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYNL-------PRS-KGVsyVSQ----VPWLrnaTIRDNI 698
Cdd:COG4525 23 LQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLdgvpvtgPGAdRGV--VFQkdalLPWL---NVLDNV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 699 LF-------DYPYIEERYKKVIQACGLLTDLQSFVASdlteigekgvtLSGGQKQRIALARAVYSPTSIVLMDDVFSALD 771
Cdd:COG4525 98 AFglrlrgvPKAERRARAEELLALVGLADFARRRIWQ-----------LSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 19115470 772 IHTSNWIykhcfQSSLME-----NRTVILVTHNVH--LFM 804
Cdd:COG4525 167 ALTREQM-----QELLLDvwqrtGKGVFLITHSVEeaLFL 201
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1212-1435 |
4.24e-12 |
|
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: 67.01 E-value: 4.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAAGPTI--LKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETqSVNLNALRQRI 1289
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-VKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1290 SFIPQDPILFSG-TVRSNLDPFDEL---EDNFLNEALKTSgASSMIMAHTDDQKpihitldthvaseGSNFSQGQKQVLA 1365
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYFAGLyglKGDELTARLEEL-ADRLGMEELLDRR-------------VGGFSTGMRQKVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19115470 1366 LARAIVRRSKIIILDECTASVDDAMDQKIQKTLRE--AFGDATMLCiAHRLKTIVDY-DKVMVLDKGVLVEYG 1435
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDVMATRALREFIRQlrALGKCILFS-THIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
631-798 |
4.51e-12 |
|
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: 68.05 E-value: 4.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISAL-------LGEL--------SLNKGSYNLPRSKGVSYVSQ-VPWLRNATI 694
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCInrlieptSGKVlidgqdiaAMSRKELRELRRKKISMVFQsFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 695 RDNILF-------DYPYIEERYKKVIQACGLLTDLQSFvasdlteIGEkgvtLSGGQKQRIALARAVYSPTSIVLMDDVF 767
Cdd:cd03294 120 LENVAFglevqgvPRAEREERAAEALELVGLEGWEHKY-------PDE----LSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190
....*....|....*....|....*....|....*...
gi 19115470 768 SALD--IHTSnwiykhcFQSSLME-----NRTVILVTH 798
Cdd:cd03294 189 SALDplIRRE-------MQDELLRlqaelQKTIVFITH 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1183-1434 |
4.81e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.48 E-value: 4.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1183 RVLEYSKLPQEPAPTIAGQVPATWPKE---GDIVF--NHVSVSYsaAGPTILKDVNLHINPSEKVAVVGRTGSGKStlgl 1257
Cdd:COG0488 282 RIKALEKLEREEPPRRDKTVEIRFPPPerlGKKVLelEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKS---- 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1258 TLLRFthrISGEI-YINGRETQSVNLnalrqRISFIPQDpilfsgtvRSNLDP----FDELEDnfLNEALKTSGASSMI- 1331
Cdd:COG0488 356 TLLKL---LAGELePDSGTVKLGETV-----KIGYFDQH--------QEELDPdktvLDELRD--GAPGGTEQEVRGYLg 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1332 --MAHTDDQ-KPIhitldthvasegSNFSQGQKQVLALARAIVRRSKIIILDECTASVDDAMdqkiqktlREAFGDA--- 1405
Cdd:COG0488 418 rfLFSGDDAfKPV------------GVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET--------LEALEEAldd 477
|
250 260 270
....*....|....*....|....*....|....*
gi 19115470 1406 ---TMLCIAH-R--LKTIVdyDKVMVLDKGVLVEY 1434
Cdd:COG0488 478 fpgTVLLVSHdRyfLDRVA--TRILEFEDGGVREY 510
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1218-1441 |
4.97e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 69.59 E-value: 4.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1218 SVSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLgltlLR----FTHRISGEIYINGRETQsvNLNALRQRISFIP 1293
Cdd:PRK09452 19 GISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTV----LRliagFETPDSGRIMLDGQDIT--HVPAENRHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1294 QDPILFSG-TVRSNLD--------PFDELEDNFLnEALKtsgassMI-MAHTDDQKPihitldthvasegSNFSQGQKQV 1363
Cdd:PRK09452 93 QSYALFPHmTVFENVAfglrmqktPAAEITPRVM-EALR------MVqLEEFAQRKP-------------HQLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1364 LALARAIVRRSKIIILDECTASVDDAMDQKIQ---KTLREAFGdATMLCIAH-RLKTIVDYDKVMVLDKGVLVEYGPPAV 1439
Cdd:PRK09452 153 VAIARAVVNKPKVLLLDESLSALDYKLRKQMQnelKALQRKLG-ITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
..
gi 19115470 1440 LY 1441
Cdd:PRK09452 232 IY 233
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
631-817 |
5.16e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 69.34 E-value: 5.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYNL---------PRSKGVSYVSQVPWL-RNATIRDNILF 700
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFhgtdvsrlhARDRKVGFVFQHYALfRHMTVFDNIAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 701 --------DYPYIEERYKKVIQacgLLTDLQsfvasdLTEIGEKGVT-LSGGQKQRIALARAVYSPTSIVLMDDVFSALD 771
Cdd:PRK10851 98 gltvlprrERPNAAAIKAKVTQ---LLEMVQ------LAHLADRYPAqLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 19115470 772 IHT----SNWIYKhcfqssLMENR--TVILVTHNVHLFMDSAAFIVTVKNGS 817
Cdd:PRK10851 169 AQVrkelRRWLRQ------LHEELkfTSVFVTHDQEEAMEVADRVVVMSQGN 214
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1217-1446 |
5.40e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 68.20 E-value: 5.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1217 VSVSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFT-----HRISGEIYINGRETQSV-NLNALRQRIS 1290
Cdd:PRK14271 25 VNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdkvsgYRYSGDVLLGGRSIFNYrDVLEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1291 FIPQDPILFSGTVRSNLDPFDELEDNFLNEALKTSGASSMIMAHTDDqkpihiTLDTHVASEGSNFSQGQKQVLALARAI 1370
Cdd:PRK14271 105 MLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWD------AVKDRLSDSPFRLSGGQQQLLCLARTL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19115470 1371 VRRSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAHRLKTIVDY-DKVMVLDKGVLVEYGPPAVLYHNNGH 1446
Cdd:PRK14271 179 AVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARIsDRAALFFDGRLVEEGPTEQLFSSPKH 255
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1219-1400 |
5.42e-12 |
|
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: 66.23 E-value: 5.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1219 VSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGREtqsvnLNALRQrisfIPQDPIL 1298
Cdd:TIGR01189 6 LACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTP-----LAEQRD----EPHENIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1299 FSG---------TVRSNLDPFDEL---EDNFLNEALKTSGASsmimAHTDdqKPIHitldthvasegsNFSQGQKQVLAL 1366
Cdd:TIGR01189 77 YLGhlpglkpelSALENLHFWAAIhggAQRTIEDALAAVGLT----GFED--LPAA------------QLSAGQQRRLAL 138
|
170 180 190
....*....|....*....|....*....|....
gi 19115470 1367 ARAIVRRSKIIILDECTASVDDAMDQKIQKTLRE 1400
Cdd:TIGR01189 139 ARLWLSRRPLWILDEPTTALDKAGVALLAGLLRA 172
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
631-771 |
6.32e-12 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 68.95 E-value: 6.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSL---ISALL----GELSLN-KGSYNLPRSK-GVSYVSQVPWL-RNATIRDNILF 700
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLlrmIAGLEdptsGEILIGgRDVTDLPPKDrNIAMVFQSYALyPHMTVYENIAF 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19115470 701 -----DYPyIEERYKKVIQACGLLtdlqsfvasDLTEIGEKGV-TLSGGQKQRIALARA-VYSPtSIVLMDDVFSALD 771
Cdd:COG3839 99 plklrKVP-KAEIDRRVREAAELL---------GLEDLLDRKPkQLSGGQRQRVALGRAlVREP-KVFLLDEPLSNLD 165
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
645-799 |
6.69e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.44 E-value: 6.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 645 IVIGPTGSGKSSL---ISALL----GELSLNKGSYNLPRskgvsYVSQVPWL--RNA-----TIRDNILF-------DYP 703
Cdd:PRK13539 32 VLTGPNGSGKTTLlrlIAGLLppaaGTIKLDGGDIDDPD-----VAEACHYLghRNAmkpalTVAENLEFwaaflggEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 704 YIEErykkVIQACGLltdlqsfvaSDLTEIgeKGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHT----SNWIY 779
Cdd:PRK13539 107 DIAA----ALEAVGL---------APLAHL--PFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAvalfAELIR 171
|
170 180
....*....|....*....|
gi 19115470 780 KHcfqssLMENRTVILVTHN 799
Cdd:PRK13539 172 AH-----LAQGGIVIAATHI 186
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
626-812 |
6.89e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 67.42 E-value: 6.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 626 PGDFCLRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYNL-------PRS-KGVSYVSQ--VPWlRNatIR 695
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdgkpvegPGAeRGVVFQNEglLPW-RN--VQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 696 DNILFDYpyieeRYKKVIQACGLLTDLQSFVASDLTEIGEKGV-TLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHT 774
Cdd:PRK11248 89 DNVAFGL-----QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 19115470 775 snwiyKHCFQSSLME-----NRTVILVTHNVhlfmDSAAFIVT 812
Cdd:PRK11248 164 -----REQMQTLLLKlwqetGKQVLLITHDI----EEAVFMAT 197
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
627-799 |
8.22e-12 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 66.70 E-value: 8.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 627 GDFCLR-DLNIvfPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYNLprsKGVSYVSQVPWLR---------N----A 692
Cdd:COG3840 12 GDFPLRfDLTI--AAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILW---NGQDLTALPPAERpvsmlfqenNlfphL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 693 TIRDNILF----DYPYIEERYKKVIQAcglltdLQSFvasDLTEIGE-KGVTLSGGQKQRIALARAVYSPTSIVLMDDVF 767
Cdd:COG3840 87 TVAQNIGLglrpGLKLTAEQRAQVEQA------LERV---GLAGLLDrLPGQLSGGQRQRVALARCLVRKRPILLLDEPF 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 19115470 768 SALD-------------IHTSnwiykhcfqsslmENRTVILVTHN 799
Cdd:COG3840 158 SALDpalrqemldlvdeLCRE-------------RGLTVLMVTHD 189
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
606-828 |
9.67e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 67.34 E-value: 9.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 606 DTSQEIGFFNASLTWvSNPSPGDF-CLRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGS-----YNLPRS-- 677
Cdd:PRK13645 2 DFSKDIILDNVSYTY-AKKTPFEFkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtivgdYAIPANlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 678 ---------KGVSYVSQVP--WLRNATIRDNILFDYPYI----EERYKKVIQACGLLTDLQSFVASDLTEigekgvtLSG 742
Cdd:PRK13645 81 kikevkrlrKEIGLVFQFPeyQLFQETIEKDIAFGPVNLgenkQEAYKKVPELLKLVQLPEDYVKRSPFE-------LSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 743 GQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKHCFQSSLMENRTVILVTHNVHLFMDSAAFIVTVKNGSafpVT 822
Cdd:PRK13645 154 GQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGK---VI 230
|
....*.
gi 19115470 823 DKSSPL 828
Cdd:PRK13645 231 SIGSPF 236
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1227-1435 |
9.81e-12 |
|
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: 66.12 E-value: 9.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1227 TILKDVNLHINPSEKVAVVGRTGSGKSTLgLTLLRFTHRI-SGEIYINGREtqsVN-LNALRQRISFIPQDPILFSG-TV 1303
Cdd:cd03301 14 TALDDLNLDIADGEFVVLLGPSGCGKTTT-LRMIAGLEEPtSGRIYIGGRD---VTdLPPKDRDIAMVFQNYALYPHmTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1304 RSNLD--------PFDELEDNfLNEALKTSGassmiMAHTDDQKPihitldthvasegSNFSQGQKQVLALARAIVRRSK 1375
Cdd:cd03301 90 YDNIAfglklrkvPKDEIDER-VREVAELLQ-----IEHLLDRKP-------------KQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19115470 1376 IIILDECTASVDD----AMDQKIQKTLREAfgDATMLCIAHrlktivDY-------DKVMVLDKGVLVEYG 1435
Cdd:cd03301 151 VFLMDEPLSNLDAklrvQMRAELKRLQQRL--GTTTIYVTH------DQveamtmaDRIAVMNDGQIQQIG 213
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
631-818 |
1.04e-11 |
|
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: 66.34 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGelslnkgsYNLPRSKGVSY------------------VSQVPWLrna 692
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISG--------LAQPTSGGVILegkqitepgpdrmvvfqnYSLLPWL--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 693 TIRDNI-------LFDYPYIEERykKVIQacglltdlQSFVASDLTEIGEKGVT-LSGGQKQRIALARAVYSPTSIVLMD 764
Cdd:TIGR01184 70 TVRENIalavdrvLPDLSKSERR--AIVE--------EHIALVGLTEAADKRPGqLSGGMKQRVAIARALSIRPKVLLLD 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19115470 765 DVFSALDIHTsnwiyKHCFQSSLM----ENR-TVILVTHNVhlfmDSAAF----IVTVKNGSA 818
Cdd:TIGR01184 140 EPFGALDALT-----RGNLQEELMqiweEHRvTVLMVTHDV----DEALLlsdrVVMLTNGPA 193
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1215-1446 |
1.06e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 69.35 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1215 NHVSVSYSAAGP--TILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHR-----ISGEIYINGretQSVnLNA--- 1284
Cdd:PRK15134 9 ENLSVAFRQQQTvrTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSppvvyPSGDIRFHG---ESL-LHAseq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1285 -LRQ----RISFIPQDPILfsgtvrsNLDPFDELEDNF-----LNEALKTSGASSMIMAHTdDQKPIHitldtHVASEGS 1354
Cdd:PRK15134 85 tLRGvrgnKIAMIFQEPMV-------SLNPLHTLEKQLyevlsLHRGMRREAARGEILNCL-DRVGIR-----QAAKRLT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1355 NF----SQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDATM--LCIAHRLKtIVDY--DKVMVL 1426
Cdd:PRK15134 152 DYphqlSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMglLFITHNLS-IVRKlaDRVAVM 230
|
250 260
....*....|....*....|
gi 19115470 1427 DKGVLVEYGPPAVLYHNNGH 1446
Cdd:PRK15134 231 QNGRCVEQNRAATLFSAPTH 250
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1212-1441 |
1.06e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 67.50 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAAGP---TILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYING----RETQSVNLNA 1284
Cdd:PRK13646 3 IRFDNVSYTYQKGTPyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1285 LRQRISFIPQDP--ILFSGTVRSNLD--------PFDELEDnFLNEALKTSGASSMIMAhtddQKPIHItldthvasegs 1354
Cdd:PRK13646 83 VRKRIGMVFQFPesQLFEDTVEREIIfgpknfkmNLDEVKN-YAHRLLMDLGFSRDVMS----QSPFQM----------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1355 nfSQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGD--ATMLCIAHRLKTIVDY-DKVMVLDKGVL 1431
Cdd:PRK13646 147 --SGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVARYaDEVIVMKEGSI 224
|
250
....*....|
gi 19115470 1432 VEYGPPAVLY 1441
Cdd:PRK13646 225 VSQTSPKELF 234
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1227-1442 |
1.09e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 67.83 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1227 TILKDVNLHINPSEKVAVVGRTGSGKSTLG---LTLLRFTHRISGEIYINGRETQSVN---LNALR-QRISFIPQDPIlf 1299
Cdd:PRK09473 30 TAVNDLNFSLRAGETLGIVGESGSGKSQTAfalMGLLAANGRIGGSATFNGREILNLPekeLNKLRaEQISMIFQDPM-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1300 sgtvrSNLDPFDELEDNFL---------------NEALKTSGASSMIMAHTddqkpiHITLDTHvasegsNFSQGQKQVL 1364
Cdd:PRK09473 108 -----TSLNPYMRVGEQLMevlmlhkgmskaeafEESVRMLDAVKMPEARK------RMKMYPH------EFSGGMRQRV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1365 ALARAIVRRSKIIILDECTASVDDAMDQKIQKTLRE---AFGDATMLcIAHRLKTIVDY-DKVMVLDKGVLVEYGPPA-V 1439
Cdd:PRK09473 171 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElkrEFNTAIIM-ITHDLGVVAGIcDKVLVMYAGRTMEYGNARdV 249
|
...
gi 19115470 1440 LYH 1442
Cdd:PRK09473 250 FYQ 252
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
651-800 |
1.13e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.06 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 651 GSGKSSLISALLGELSL---NKGSYNLPRSKGV-SYVSQVPWLRNATIRDNILFDYP-YIEERYKKVIQACGLLTDLQSF 725
Cdd:PTZ00265 1265 GSGEDSTVFKNSGKILLdgvDICDYNLKDLRNLfSIVSQEPMLFNMSIYENIKFGKEdATREDVKRACKFAAIDEFIESL 1344
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115470 726 VASDLTEIGEKGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKHCFQSSLMENRTVILVTHNV 800
Cdd:PTZ00265 1345 PNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI 1419
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
627-771 |
1.16e-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: 68.20 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 627 GDFCLrDLNIVFPRNKLSIVIGPTGSGKSSLISAL--L-----GELSLN-------KGSYNLPRSK-GVSYVSQ----VP 687
Cdd:COG4148 12 GGFTL-DVDFTLPGRGVTALFGPSGSGKTTLLRAIagLerpdsGRIRLGgevlqdsARGIFLPPHRrRIGYVFQearlFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 688 WLrnaTIRDNILF---------DYPYIEErykkVIQACGLLTDLQSFVAsdlteigekgvTLSGGQKQRIALARAVYSPT 758
Cdd:COG4148 91 HL---SVRGNLLYgrkrapraeRRISFDE----VVELLGIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSP 152
|
170
....*....|...
gi 19115470 759 SIVLMDDVFSALD 771
Cdd:COG4148 153 RLLLMDEPLAALD 165
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
635-815 |
1.25e-11 |
|
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: 66.80 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 635 NIVF---PRNKLSIvIGPTGSGKSSLISALL------GELSLNKGSYN-LPRS---KGVSYVSQVPWLRNATIRDNILFD 701
Cdd:cd03289 22 NISFsisPGQRVGL-LGRTGSGKSTLLSAFLrllnteGDIQIDGVSWNsVPLQkwrKAFGVIPQKVFIFSGTFRKNLDPY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 702 YPYIEERYKKVIQACGLLTDLQSFVASDLTEIGEKGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKH 781
Cdd:cd03289 101 GKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKT 180
|
170 180 190
....*....|....*....|....*....|....
gi 19115470 782 CFQSslMENRTVILVTHNVHLFMDSAAFIVTVKN 815
Cdd:cd03289 181 LKQA--FADCTVILSEHRIEAMLECQRFLVIEEN 212
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
631-808 |
1.26e-11 |
|
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: 63.62 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLN-IVFPRNKLSIViGPTGSGKSSLISALLGELSLNKGSYNLPRSKGVSYVSQvpwlrnatirdnilfdypyieery 709
Cdd:cd03221 16 LKDISlTINPGDRIGLV-GRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ------------------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 710 kkviqacglltdlqsfvasdlteigekgvtLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKHcfqssLME 789
Cdd:cd03221 71 ------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEA-----LKE 115
|
170 180
....*....|....*....|
gi 19115470 790 -NRTVILVTHNvHLFMDSAA 808
Cdd:cd03221 116 yPGTVILVSHD-RYFLDQVA 134
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
631-802 |
1.86e-11 |
|
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: 65.98 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALL-------GELSLNKGSYNLPRSKG----VSYVSQVPwlRNA-----TI 694
Cdd:COG1124 21 LKDVSLEVAPGESFGLVGESGSGKSTLLRALAglerpwsGEVTFDGRPVTRRRRKAfrrrVQMVFQDP--YASlhprhTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 695 RDNI-----LFDYPYIEERYKKVIQACGLLTD-LQSFVASdlteigekgvtLSGGQKQRIALARAVYSPTSIVLMDDVFS 768
Cdd:COG1124 99 DRILaeplrIHGLPDREERIAELLEQVGLPPSfLDRYPHQ-----------LSGGQRQRVAIARALILEPELLLLDEPTS 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 19115470 769 ALDIHTsnwiykhcfQSSLM---------ENRTVILVTHNVHL 802
Cdd:COG1124 168 ALDVSV---------QAEILnllkdlreeRGLTYLFVSHDLAV 201
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
631-800 |
1.88e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 65.95 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISAL--LGEL--------SLNKGSYNL--PRS------KGVSYVSQVPWLRNA 692
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLnpevtitgSIVYNGHNIysPRTdtvdlrKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 693 TIRDNILFDYPYIEERYKKVIQAcGLLTDLQSfvASDLTEIGEK----GVTLSGGQKQRIALARAVYSPTSIVLMDDVFS 768
Cdd:PRK14239 101 SIYENVVYGLRLKGIKDKQVLDE-AVEKSLKG--ASIWDEVKDRlhdsALGLSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
170 180 190
....*....|....*....|....*....|..
gi 19115470 769 ALDIHTSNWIYKHCFqsSLMENRTVILVTHNV 800
Cdd:PRK14239 178 ALDPISAGKIEETLL--GLKDDYTMLLVTRSM 207
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1224-1426 |
1.89e-11 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 64.56 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1224 AGPTILKDVNLHINPSEKVAVVGRTGSGKSTLgLTLLRFTHR-ISGEIyingRETQSVNLNALRQRISFIPQDPILFSGT 1302
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTL-LKVLAGVLRpTSGTV----RRAGGARVAYVPQRSEVPDSLPLTVRDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1303 V-------RSNLDPFDELEDNFLNEALKTSGASSMimahtdDQKPIHiTLdthvasegsnfSQGQKQVLALARAIVRRSK 1375
Cdd:NF040873 78 VamgrwarRGLWRRLTRDDRAAVDDALERVGLADL------AGRQLG-EL-----------SGGQRQRALLAQGLAQEAD 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 19115470 1376 IIILDECTASVDDAMDQKIQKTLREAFGD-ATMLCIAHRLKTIVDYDKVMVL 1426
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLAEEHARgATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1226-1446 |
2.03e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 67.04 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1226 PTILK---DVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRE---TQSVNLNALRQRISFIPQDPIlf 1299
Cdd:PRK15079 31 PKTLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDllgMKDDEWRAVRSDIQMIFQDPL-- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1300 sgtvrSNLDPFDELEDnFLNEALKT-----------SGASSMIMahtddqK----PIHITLDTHvasegsNFSQGQKQVL 1364
Cdd:PRK15079 109 -----ASLNPRMTIGE-IIAEPLRTyhpklsrqevkDRVKAMML------KvgllPNLINRYPH------EFSGGQCQRI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1365 ALARAIVRRSKIIILDECTAsvddAMDQKIQ-------KTLREAFGdATMLCIAHRLkTIVDY--DKVMVLDKGVLVEYG 1435
Cdd:PRK15079 171 GIARALILEPKLIICDEPVS----ALDVSIQaqvvnllQQLQREMG-LSLIFIAHDL-AVVKHisDRVLVMYLGHAVELG 244
|
250
....*....|.
gi 19115470 1436 PPAVLYHNNGH 1446
Cdd:PRK15079 245 TYDEVYHNPLH 255
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1199-1387 |
2.27e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 68.07 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1199 AGQVPATWPKegdIVFNHVSVSYSAAGPTiLKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQ 1278
Cdd:PRK10522 313 RPQAFPDWQT---LELRNVTFAYQDNGFS-VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1279 SVNLNALRQRISFIPQDPILFSGTVRS-NLDPFDELEDNFLnEALKtsgassmiMAHTddqkpihITLDTHVASEgSNFS 1357
Cdd:PRK10522 389 AEQPEDYRKLFSAVFTDFHLFDQLLGPeGKPANPALVEKWL-ERLK--------MAHK-------LELEDGRISN-LKLS 451
|
170 180 190
....*....|....*....|....*....|
gi 19115470 1358 QGQKQVLALARAIVRRSKIIILDECTASVD 1387
Cdd:PRK10522 452 KGQKKRLALLLALAEERDILLLDEWAADQD 481
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
631-816 |
3.93e-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: 64.20 E-value: 3.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKG---------SYNLPRSKGVSYVSQ----VPwlrNATIRDN 697
Cdd:cd03301 16 LDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGriyiggrdvTDLPPKDRDIAMVFQnyalYP---HMTVYDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 698 ILF-------DYPYIEERYKKVIQACGLLTDLQSFVAsdlteigekgvTLSGGQKQRIALARAVYSPTSIVLMDDVFSAL 770
Cdd:cd03301 93 IAFglklrkvPKDEIDERVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRAIVREPKVFLMDEPLSNL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 19115470 771 D----IHTSNWIYKhcFQSSLmeNRTVILVTHNVHLFMDSAAFIVTVKNG 816
Cdd:cd03301 162 DaklrVQMRAELKR--LQQRL--GTTTIYVTHDQVEAMTMADRIAVMNDG 207
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1225-1455 |
3.95e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 64.91 E-value: 3.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1225 GPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQR-ISFIPQDPILFSG-T 1302
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGYLPQEASIFRRlS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1303 VRSNLDPFDELEDNFLNEALKTSGASSMimahtddqKPIHItldTHVA-SEGSNFSQGQKQVLALARAIVRRSKIIILDE 1381
Cdd:PRK10895 95 VYDNLMAVLQIRDDLSAEQREDRANELM--------EEFHI---EHLRdSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19115470 1382 CTASVD--DAMD-QKIQKTLREAfgDATMLCIAHRLKTIVDY-DKVMVLDKGVLVEYGPPAVLYhNNGHFRRMCDGSG 1455
Cdd:PRK10895 164 PFAGVDpiSVIDiKRIIEHLRDS--GLGVLITDHNVRETLAVcERAYIVSQGHLIAHGTPTEIL-QDEHVKRVYLGED 238
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1231-1435 |
3.96e-11 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 64.05 E-value: 3.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1231 DVNLHINPSEKVAVVGRTGSGKSTLgLTLLR-FTHRISGEIYINGretqsVNLNAL---RQRISFIPQDPILFSG-TVRS 1305
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTL-LNLIAgFETPQSGRVLING-----VDVTAAppaDRPVSMLFQENNLFAHlTVEQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1306 NLDpfdelednflnealktSGASSMIMAHTDDQKPIH-----ITLDTHVASEGSNFSQGQKQVLALARAIVRRSKIIILD 1380
Cdd:cd03298 90 NVG----------------LGLSPGLKLTAEDRQAIEvalarVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 19115470 1381 ECTASVDDAMDQKIQKTLREAFGDA--TMLCIAHRLKTIVD-YDKVMVLDKGVLVEYG 1435
Cdd:cd03298 154 EPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1218-1442 |
3.97e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 66.59 E-value: 3.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1218 SVSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLgLTLLRFTHRI-SGEIYINGretQSVNLNALRQR-ISFIPQD 1295
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTL-LRMIAGLEDItSGDLFIGE---KRMNDVPPAERgVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1296 PILFsgtvrsnldPFDELEDNfLNEALKTSGASS-------------MIMAHTDDQKPihitldthvasegSNFSQGQKQ 1362
Cdd:PRK11000 84 YALY---------PHLSVAEN-MSFGLKLAGAKKeeinqrvnqvaevLQLAHLLDRKP-------------KALSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1363 VLALARAIVRRSKIIILDECTASVDDAMD-------QKIQKTLReafgdATMLCIAH-RLKTIVDYDKVMVLDKGVLVEY 1434
Cdd:PRK11000 141 RVAIGRTLVAEPSVFLLDEPLSNLDAALRvqmrieiSRLHKRLG-----RTMIYVTHdQVEAMTLADKIVVLDAGRVAQV 215
|
....*...
gi 19115470 1435 GPPAVLYH 1442
Cdd:PRK11000 216 GKPLELYH 223
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
631-802 |
5.04e-11 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 64.75 E-value: 5.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKG--SYN------------------LPRSKGVSY---VSQV- 686
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGevRLNgrplaawspwelarrravLPQHSSLAFpftVEEVv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 687 -----PWLRNATIRDNIlfdypyieerykkvIQACGLLTDLQSFVASDLTeigekgvTLSGGQKQRIALARA-------V 754
Cdd:COG4559 97 algraPHGSSAAQDRQI--------------VREALALVGLAHLAGRSYQ-------TLSGGEQQRVQLARVlaqlwepV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 19115470 755 YSPTSIVLMDDVFSALDIHtsnwiykHcfQSSLM--------ENRTVILVTHNVHL 802
Cdd:COG4559 156 DGGPRWLFLDEPTSALDLA-------H--QHAVLrlarqlarRGGGVVAVLHDLNL 202
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
631-817 |
5.07e-11 |
|
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: 63.11 E-value: 5.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALL---GELSLNKGSYNLPRSKGVSyVSQvpwlrnatirdnilfdypyiee 707
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLyasGKARLISFLPKFSRNKLIF-IDQ---------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 708 rykkviqacglltdLQSFVASDLT--EIGEKGVTLSGGQKQRIALARAVYSPT--SIVLMDDVFSALDIHTSNWIYKhCF 783
Cdd:cd03238 68 --------------LQFLIDVGLGylTLGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLE-VI 132
|
170 180 190
....*....|....*....|....*....|....
gi 19115470 784 QSSLMENRTVILVTHNVHlFMDSAAFIVTVKNGS 817
Cdd:cd03238 133 KGLIDLGNTVILIEHNLD-VLSSADWIIDFGPGS 165
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1214-1435 |
5.09e-11 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 63.84 E-value: 5.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1214 FNHVSVSYSAAgpTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSvnlnALRQRISFIP 1293
Cdd:cd03269 3 VENVTKRFGRV--TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI----AARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1294 QDPILFSG-TVRSNLDPFDELEDNFLNEALKTSgassmimahTDDQKPIHITldTHVASEGSNFSQGQKQVLALARAIVR 1372
Cdd:cd03269 77 EERGLYPKmKVIDQLVYLAQLKGLKKEEARRRI---------DEWLERLELS--EYANKRVEELSKGNQQKVQFIAAVIH 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19115470 1373 RSKIIILDECTASVD----DAMDQKIQkTLREAfgDATMLCIAHRLKTIVDY-DKVMVLDKGVLVEYG 1435
Cdd:cd03269 146 DPELLILDEPFSGLDpvnvELLKDVIR-ELARA--GKTVILSTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
631-799 |
7.20e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 64.26 E-value: 7.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISAL-------LGELSLNKGSYNL--PR--SKGVSYVSQVPWL-RNATIRDni 698
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFarlltpqSGTVFLGDKPISMlsSRqlARRLALLPQHHLTpEGITVRE-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 699 LFDY---PYI-------EERYKKVIQAcglLTDLQsfvasdLTEIGEKGVT-LSGGQKQRIALARAVYSPTSIVLMDDVF 767
Cdd:PRK11231 96 LVAYgrsPWLslwgrlsAEDNARVNQA---MEQTR------INHLADRRLTdLSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 19115470 768 SALDIHtsnwiykHcfQSSLM--------ENRTVILVTHN 799
Cdd:PRK11231 167 TYLDIN-------H--QVELMrlmrelntQGKTVVTVLHD 197
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
631-816 |
7.24e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 64.30 E-value: 7.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISAL-------------------LGELSLNKGSYNLPRSKGVSYVSQVPWlRN 691
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLnrlieiydskikvdgkvlyFGKDIFQIDAIKLRKEVGMVFQQPNPF-PH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 692 ATIRDNILfdYPY----IEER--YKKVIQAC----GLLTDLQSFVASDLTEigekgvtLSGGQKQRIALARAVYSPTSIV 761
Cdd:PRK14246 105 LSIYDNIA--YPLkshgIKEKreIKKIVEEClrkvGLWKEVYDRLNSPASQ-------LSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 19115470 762 LMDDVFSALDIHTSNWIYKhcFQSSLMENRTVILVTHNVHLFMDSAAFIVTVKNG 816
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEK--LITELKNEIAIVIVSHNPQQVARVADYVAFLYNG 228
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
640-801 |
7.28e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 64.29 E-value: 7.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 640 RNKLSIVIGPTGSGKSSLISAL--LGELS-----------LNKGSY----NLPR-SKGVSYVSQVPWLRNATIRDNILFD 701
Cdd:PRK14258 32 QSKVTAIIGPSGCGKSTFLKCLnrMNELEsevrvegrvefFNQNIYerrvNLNRlRRQVSMVHPKPNLFPMSVYDNVAYG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 702 YPYIEERYK----KVIQACGLLTDLQSFVASdltEIGEKGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNW 777
Cdd:PRK14258 112 VKIVGWRPKleidDIVESALKDADLWDEIKH---KIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMK 188
|
170 180
....*....|....*....|....*
gi 19115470 778 IyKHCFQSSLMENR-TVILVTHNVH 801
Cdd:PRK14258 189 V-ESLIQSLRLRSElTMVIVSHNLH 212
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
627-808 |
1.08e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 64.03 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 627 GDF-CLRDLNIVFPRNKLSIVIGPTGSGKSS----------LISALLGELSLNKGSYNLPRS--------KGVSYVSQVP 687
Cdd:PRK14243 21 GSFlAVKNVWLDIPKNQITAFIGPSGCGKSTilrcfnrlndLIPGFRVEGKVTFHGKNLYAPdvdpvevrRRIGMVFQKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 688 WLRNATIRDNILFDyPYIEerykkviqacGLLTDLQSFVASDLT------EIGEK----GVTLSGGQKQRIALARAVYSP 757
Cdd:PRK14243 101 NPFPKSIYDNIAYG-ARIN----------GYKGDMDELVERSLRqaalwdEVKDKlkqsGLSLSGGQQQRLCIARAIAVQ 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 19115470 758 TSIVLMDDVFSALDIHTSNWIYKhcFQSSLMENRTVILVTHNvhlfMDSAA 808
Cdd:PRK14243 170 PEVILMDEPCSALDPISTLRIEE--LMHELKEQYTIIIVTHN----MQQAA 214
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1221-1435 |
1.37e-10 |
|
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: 64.11 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1221 YSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGretqsvnlnalrqRISFIPQDPILFS 1300
Cdd:cd03291 45 LCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1301 GTVRSNLD---PFDELEdnfLNEALKTSGASSMIMAHTDDQKpihitldTHVASEGSNFSQGQKQVLALARAIVRRSKII 1377
Cdd:cd03291 112 GTIKENIIfgvSYDEYR---YKSVVKACQLEEDITKFPEKDN-------TVLGEGGITLSGGQRARISLARAVYKDADLY 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 19115470 1378 ILDECTASVDDAMDQKI-QKTLREAFGDATMLCIAHRLKTIVDYDKVMVLDKGVLVEYG 1435
Cdd:cd03291 182 LLDSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYG 240
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1130-1456 |
1.56e-10 |
|
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: 66.19 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1130 LVGAIAGLIALLQKDLSPGVVGFSLNQAVIFSSSVLLFVRSCNSLQAE-MNSYERVLEYSKLPQEPAPT----IAGQVPA 1204
Cdd:TIGR01257 845 LDAALYGLLAWYLDQVFPGDYGTPLPWYFLLQESYWLGGEGCSTREERaLEKTEPLTEEMEDPEHPEGIndsfFERELPG 924
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1205 TWPkeGDIVFNHVSVsYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSvNLNA 1284
Cdd:TIGR01257 925 LVP--GVCVKNLVKI-FEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDA 1000
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1285 LRQRISFIPQDPILFSG-TVRSNLDPFDELEDNFLNEAlktsgasSMIMAHTDDQKPIHITLDthvaSEGSNFSQGQKQV 1363
Cdd:TIGR01257 1001 VRQSLGMCPQHNILFHHlTVAEHILFYAQLKGRSWEEA-------QLEMEAMLEDTGLHHKRN----EEAQDLSGGMQRK 1069
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1364 LALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAHRL-KTIVDYDKVMVLDKGVLVEYGPPAvlyh 1442
Cdd:TIGR01257 1070 LSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMdEADLLGDRIAIISQGRLYCSGTPL---- 1145
|
330
....*....|....
gi 19115470 1443 nnghFRRMCDGSGI 1456
Cdd:TIGR01257 1146 ----FLKNCFGTGF 1155
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
631-798 |
1.67e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.67 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSlnkgsyNLPrSKGVSYVSQVPWLRNATIRDNILFDYPYIEEryK 710
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK------GTP-VAGCVDVPDNQFGREASLIDAIGRKGDFKDA--V 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 711 KVIQACGlLTDLQSFVAsdlteigeKGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNwIYKHCFQSSLMEN 790
Cdd:COG2401 117 ELLNAVG-LSDAVLWLR--------RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK-RVARNLQKLARRA 186
|
....*....
gi 19115470 791 R-TVILVTH 798
Cdd:COG2401 187 GiTLVVATH 195
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
983-1184 |
1.72e-10 |
|
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: 63.72 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 983 SWFDKTPTGRIVNRFAKDIRSIDMNLSGWLFFSINCFLSVAGGI-----LSVSSAMpIFMIPAVIVCLAGYYFGLLYTRA 1057
Cdd:cd07346 88 SFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALvilfyLNWKLTL-VALLLLPLYVLILRYFRRRIRKA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1058 QVGVKRLISIytspIFSLLGESIVGVSVIRAFNRQTIFKQMFSERLDNLVRLQSTSYNLNRWVAVRTDGISGLVGAI--- 1134
Cdd:cd07346 167 SREVRESLAE----LSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALvll 242
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 19115470 1135 AGLIALLQKDLSPGVVGFSLNQAVIFSSSVLLFVRSCNSLQAEMNSYERV 1184
Cdd:cd07346 243 YGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1228-1443 |
1.79e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 63.06 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1228 ILKDVNLHINPSEKVAVVGRTGSGKSTLgLTLLRFTHRIS-GEIYINGRETQSV-------------NLNALRQRISFIP 1293
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTF-LRCINFLEKPSeGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1294 QdpilfsgtvRSNLDPFDELEDNFLNEALKTSGASSM--------------IMAHTDDQKPIHItldthvasegsnfSQG 1359
Cdd:PRK10619 99 Q---------HFNLWSHMTVLENVMEAPIQVLGLSKQeareravkylakvgIDERAQGKYPVHL-------------SGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1360 QKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLRE-AFGDATMLCIAHRLKTIVDYDK-VMVLDKGVLVEYGPP 1437
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHVSShVIFLHQGKIEEEGAP 236
|
....*.
gi 19115470 1438 AVLYHN 1443
Cdd:PRK10619 237 EQLFGN 242
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
631-807 |
2.00e-10 |
|
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: 62.69 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGS----------------YNLPRSKGVSYvsQvpwlRNA-- 692
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEilvdgqditglsekelYELRRRIGMLF--Q----GGAlf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 693 ---TIRDNILF------DYPY--IEERYKKVIQACGLLTDLQSFVASdlteigekgvtLSGGQKQRIALARA-VYSPtSI 760
Cdd:COG1127 95 dslTVFENVAFplrehtDLSEaeIRELVLEKLELVGLPGAADKMPSE-----------LSGGMRKRVALARAlALDP-EI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 19115470 761 VLMDDVFSALDIHTSNWIYKhcfqssLMENR------TVILVTHNvhlfMDSA 807
Cdd:COG1127 163 LLYDEPTAGLDPITSAVIDE------LIRELrdelglTSVVVTHD----LDSA 205
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1129-1381 |
2.13e-10 |
|
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: 65.20 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1129 GLVGAIAGLIALLQkDLSPGVV-GFSLnqavifsssVLLFVRS-----CNSL----QAEMnSYERVLEYSKLPQEPAPTI 1198
Cdd:COG4615 245 ALIGLILFLLPALG-WADPAVLsGFVL---------VLLFLRGplsqlVGALptlsRANV-ALRKIEELELALAAAEPAA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1199 AGQVPATWPKE-GDIVFNHVSVSYSAA--------GPtilkdVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGE 1269
Cdd:COG4615 314 ADAAAPPAPADfQTLELRGVTYRYPGEdgdegftlGP-----IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1270 IYINGRETQSVNLNALRQRISFIPQDPILFsgtvRSNLDPFDELEDNFLNEALKTsgassMIMAHtddqkpihitldtHV 1349
Cdd:COG4615 389 ILLDGQPVTADNREAYRQLFSAVFSDFHLF----DRLLGLDGEADPARARELLER-----LELDH-------------KV 446
|
250 260 270
....*....|....*....|....*....|....*..
gi 19115470 1350 ASEGSNF-----SQGQKQVLALARAIVRRSKIIILDE 1381
Cdd:COG4615 447 SVEDGRFsttdlSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
631-802 |
2.55e-10 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 62.16 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKlSI-VIGPTGSGKSSLISALLGELSLNKGSynlprskgVSYVSQVPWL--------RNATIRDNILF- 700
Cdd:cd03220 38 LKDVSFEVPRGE-RIgLIGRNGAGKSTLLRLLAGIYPPDSGT--------VTVRGRVSSLlglgggfnPELTGRENIYLn 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 701 ------DYPYIEERYKKVIqacglltdlqsfvasDLTEIGEKG----VTLSGGQKQRIALARAVYSPTSIVLMDDVFSAL 770
Cdd:cd03220 109 grllglSRKEIDEKIDEII---------------EFSELGDFIdlpvKTYSSGMKARLAFAIATALEPDILLIDEVLAVG 173
|
170 180 190
....*....|....*....|....*....|..
gi 19115470 771 DIHTSNWIYKHcFQSSLMENRTVILVTHNVHL 802
Cdd:cd03220 174 DAAFQEKCQRR-LRELLKQGKTVILVSHDPSS 204
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1212-1399 |
2.72e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 63.95 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYsaaGPT-ILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQsvNLNALRQRIS 1290
Cdd:PRK10851 3 IEIANIKKSF---GRTqVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS--RLHARDRKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1291 FIPQDPILFSG-TVRSNLD------PFDELEDnflNEALKTSGAS--SMI-MAHTDDQKPihitldthvasegSNFSQGQ 1360
Cdd:PRK10851 78 FVFQHYALFRHmTVFDNIAfgltvlPRRERPN---AAAIKAKVTQllEMVqLAHLADRYP-------------AQLSGGQ 141
|
170 180 190
....*....|....*....|....*....|....*....
gi 19115470 1361 KQVLALARAIVRRSKIIILDECTAsvddAMDQKIQKTLR 1399
Cdd:PRK10851 142 KQRVALARALAVEPQILLLDEPFG----ALDAQVRKELR 176
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1227-1437 |
2.92e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 64.68 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1227 TILKDVNLHINPSEKVAVVGRTGSGKSTLgLTLLRFTHR----ISGEIYINGRetqSVNLNALRQRISFIPQDPILF-SG 1301
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTL-MNALAFRSPkgvkGSGSVLLNGM---PIDAKEMRAISAYVQQDDLFIpTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1302 TVRSNLdpfdelednflnealktsgassMIMAH-------TDDQKPIHIT-----------LDTHVASEG--SNFSQGQK 1361
Cdd:TIGR00955 115 TVREHL----------------------MFQAHlrmprrvTKKEKRERVDevlqalglrkcANTRIGVPGrvKGLSGGER 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19115470 1362 QVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLRE-AFGDATMLCIAHRLKTIV--DYDKVMVLDKGVLVEYGPP 1437
Cdd:TIGR00955 173 KRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGlAQKGKTIICTIHQPSSELfeLFDKIILMAEGRVAYLGSP 251
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
610-811 |
3.88e-10 |
|
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: 62.23 E-value: 3.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 610 EIGFFNASLTWVSNPSPgdfCLRDLN-IVFPRNKLSIViGPTGSGKSSLISALLGELSLNKGSY--------NLP----R 676
Cdd:cd03288 19 EIKIHDLCVRYENNLKP---VLKHVKaYIKPGQKVGIC-GRTGSGKSSLSLAFFRMVDIFDGKIvidgidisKLPlhtlR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 677 SKgVSYVSQVPWLRNATIRDNILFDYPYIEERYKKVIQACGLLTDLQSFVASDLTEIGEKGVTLSGGQKQRIALARAVYS 756
Cdd:cd03288 95 SR-LSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVR 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 19115470 757 PTSIVLMDDVFSALDIHTSNWIYKHCFQSslMENRTVILVTHNVHLFMDSAAFIV 811
Cdd:cd03288 174 KSSILIMDEATASIDMATENILQKVVMTA--FADRTVVTIAHRVSTILDADLVLV 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1229-1401 |
3.94e-10 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 60.52 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1229 LKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRE-TQSVNLNALRQRISFIPQDPI---LFSG-TV 1303
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPvTRRSPRDAIRAGIAYVPEDRKregLVLDlSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1304 RSNLdpfdelednFLNEALktSGassmimahtddqkpihitldthvasegsnfsqGQKQVLALARAIVRRSKIIILDECT 1383
Cdd:cd03215 96 AENI---------ALSSLL--SG--------------------------------GNQQKVVLARWLARDPRVLILDEPT 132
|
170
....*....|....*...
gi 19115470 1384 ASVDDAMDQKIQKTLREA 1401
Cdd:cd03215 133 RGVDVGAKAEIYRLIREL 150
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1219-1432 |
4.08e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.04 E-value: 4.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1219 VSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLN-ALRQRISFIPQDpi 1297
Cdd:PRK09700 11 IGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAAQLGIGIIYQE-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1298 lfsgtvRSNLDPFDELEDNFLNEAL--KTSGA-----------SSMIMAHTDdqkpIHITLDTHVAsegsNFSQGQKQVL 1364
Cdd:PRK09700 89 ------LSVIDELTVLENLYIGRHLtkKVCGVniidwremrvrAAMMLLRVG----LKVDLDEKVA----NLSISHKQML 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1365 ALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDAT-MLCIAHRLKTIVDY-DKVMVLDKGVLV 1432
Cdd:PRK09700 155 EIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTaIVYISHKLAEIRRIcDRYTVMKDGSSV 224
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1225-1447 |
4.12e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 63.32 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1225 GPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVnlnALRQR-ISFIPQDPILFSG-T 1302
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV---PPYQRpINMMFQSYALFPHmT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1303 VRSNLdPFDELEDNFLNEALKTSGASSMIMAHTDD---QKPihitldthvasegSNFSQGQKQVLALARAIVRRSKIIIL 1379
Cdd:PRK11607 108 VEQNI-AFGLKQDKLPKAEIASRVNEMLGLVHMQEfakRKP-------------HQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19115470 1380 DECTASVDDAMDQKIQKTLREAFGDATMLCIahrlktIVDYD---------KVMVLDKGVLVEYGPPAVLY-HNNGHF 1447
Cdd:PRK11607 174 DEPMGALDKKLRDRMQLEVVDILERVGVTCV------MVTHDqeeamtmagRIAIMNRGKFVQIGEPEEIYeHPTTRY 245
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1211-1437 |
4.30e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 61.95 E-value: 4.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1211 DIVFNHVSVSYSAAgpTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRIS 1290
Cdd:PRK11231 2 TLRTENLTVGYGTK--RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1291 FIPQDPILFSG-TVRsnldpfdEL----EDNFLNEALKTSGASSMIMahtddQKPIHITLDTHVASEG-SNFSQGQKQVL 1364
Cdd:PRK11231 80 LLPQHHLTPEGiTVR-------ELvaygRSPWLSLWGRLSAEDNARV-----NQAMEQTRINHLADRRlTDLSGGQRQRA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115470 1365 ALARAIVRRSKIIILDECTASVDDAMDQKIQKTLRE--AFGDaTMLCIAHRLKTIVDY-DKVMVLDKGVLVEYGPP 1437
Cdd:PRK11231 148 FLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRElnTQGK-TVVTVLHDLNQASRYcDHLVVLANGHVMAQGTP 222
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
631-816 |
4.96e-10 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 61.64 E-value: 4.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKS---SLISALL----GELSLNKgsYNLPRSKGVSYVSQVPWLRNA-------TIRD 696
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKStllSMISRLLppdsGEVLVDG--LDVATTPSRELAKRLAILRQEnhinsrlTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 697 NILFD-YPY-----IEERYKKVIQACGLLtdlqsfvasDLTEIGEKGV-TLSGGQKQRIALARAVYSPTSIVLMDDVFSA 769
Cdd:COG4604 95 LVAFGrFPYskgrlTAEDREIIDEAIAYL---------DLEDLADRYLdELSGGQRQRAFIAMVLAQDTDYVLLDEPLNN 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 770 LDIhtsnwiyKHCFQssLME---------NRTVILVTHNVHLfmdsAAF----IVTVKNG 816
Cdd:COG4604 166 LDM-------KHSVQ--MMKllrrladelGKTVVIVLHDINF----ASCyadhIVAMKDG 212
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
631-801 |
5.40e-10 |
|
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: 61.44 E-value: 5.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLG--------------ELSLNKGSYNLPRSKGVSYVSQ-VPWLRNATIR 695
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGlerptsgsvlvdgtDLTLLSGKELRKARRRIGMIFQhFNLLSSRTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 696 DNIlfDYP---------YIEERYKKVIQACGlLTDLQSFVASdlteigekgvTLSGGQKQRIALARAVYSPTSIVLMDDV 766
Cdd:cd03258 101 ENV--ALPleiagvpkaEIEERVLELLELVG-LEDKADAYPA----------QLSGGQKQRVGIARALANNPKVLLCDEA 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 19115470 767 FSALDIHTSNWIYK--HCFQSSLmeNRTVILVTHNVH 801
Cdd:cd03258 168 TSALDPETTQSILAllRDINREL--GLTIVLITHEME 202
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1212-1435 |
5.64e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 61.62 E-value: 5.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYsaAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLgLTLLRFTHRISGEIYINGretqSVNLNALRQRISF 1291
Cdd:PRK11247 13 LLLNAVSKRY--GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTL-LRLLAGLETPSAGELLAG----TAPLAEAREDTRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1292 IPQDpilfsgtvrSNLDPFDELEDNFlneALKTSGassmimahtDDQKPIHITLDTHVASEGSN-----FSQGQKQVLAL 1366
Cdd:PRK11247 86 MFQD---------ARLLPWKKVIDNV---GLGLKG---------QWRDAALQALAAVGLADRANewpaaLSGGQKQRVAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115470 1367 ARAIVRRSKIIILDECTASVDD----AMDQKIQKTLRE-AFgdaTMLCIAHRLKtivdyDKVMVLDKGVLVEYG 1435
Cdd:PRK11247 145 ARALIHRPGLLLLDEPLGALDAltriEMQDLIESLWQQhGF---TVLLVTHDVS-----EAVAMADRVLLIEEG 210
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
631-800 |
7.93e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 61.23 E-value: 7.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGelsLNKGSynlprsKGVSYVSQVPWlrnATIRDNI--LFDypyiEER 708
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAG---LETPS------AGELLAGTAPL---AEAREDTrlMFQ----DAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 709 ---YKKVIQACGL-LTD------LQSFVASDLTE-IGEKGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHT--- 774
Cdd:PRK11247 92 llpWKKVIDNVGLgLKGqwrdaaLQALAAVGLADrANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTrie 171
|
170 180 190
....*....|....*....|....*....|..
gi 19115470 775 ------SNWiYKHCFqsslmenrTVILVTHNV 800
Cdd:PRK11247 172 mqdlieSLW-QQHGF--------TVLLVTHDV 194
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1221-1437 |
8.17e-10 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 61.51 E-value: 8.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1221 YSAAGPTI-LKDVNLHINPSEKVAVVGRTGSGKStlglTLLRFTHRI----SGEIYINGRETQSVNLNALRQ----RISF 1291
Cdd:cd03294 31 LKKTGQTVgVNDVSLDVREGEIFVIMGLSGSGKS----TLLRCINRLieptSGKVLIDGQDIAAMSRKELRElrrkKISM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1292 IPQDPILFSG-TVRSNLD--------PFDELEDNFLnEALKTSGASSMImahtdDQKPihitldthvasegSNFSQGQKQ 1362
Cdd:cd03294 107 VFQSFALLPHrTVLENVAfglevqgvPRAEREERAA-EALELVGLEGWE-----HKYP-------------DELSGGMQQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1363 VLALARAIVRRSKIIILDECTASVD-----DAMDQ--KIQKTLREafgdaTMLCIAHRLKTIVDY-DKVMVLDKGVLVEY 1434
Cdd:cd03294 168 RVGLARALAVDPDILLMDEAFSALDplirrEMQDEllRLQAELQK-----TIVFITHDLDEALRLgDRIAIMKDGRLVQV 242
|
...
gi 19115470 1435 GPP 1437
Cdd:cd03294 243 GTP 245
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1212-1438 |
1.11e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 61.30 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAAGP---TILKDVNLHINPSEKVAVVGRTGSGKSTLgLTLLRFTH-RISGEIYINGRE--TQSVN--LN 1283
Cdd:PRK13649 3 INLQNVSYTYQAGTPfegRALFDVNLTIEDGSYTAFIGHTGSGKSTI-MQLLNGLHvPTQGSVRVDDTLitSTSKNkdIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1284 ALRQRISFIPQDP--ILFSGTV-------RSNLDPFDELEDNFLNEALKTSGASSMIMahtdDQKPIHItldthvasegs 1354
Cdd:PRK13649 82 QIRKKVGLVFQFPesQLFEETVlkdvafgPQNFGVSQEEAEALAREKLALVGISESLF----EKNPFEL----------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1355 nfSQGQKQVLALARAIVRRSKIIILDECTAsvddAMDQKIQKTLREAF-----GDATMLCIAHRLKTIVDY-DKVMVLDK 1428
Cdd:PRK13649 147 --SGGQMRRVAIAGILAMEPKILVLDEPTA----GLDPKGRKELMTLFkklhqSGMTIVLVTHLMDDVANYaDFVYVLEK 220
|
250
....*....|
gi 19115470 1429 GVLVEYGPPA 1438
Cdd:PRK13649 221 GKLVLSGKPK 230
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1212-1429 |
1.61e-09 |
|
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: 57.84 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSaaGPTILKDVNLHINPSEKVAVVGRTGSGKSTLgltllrfthrisgeiyingretqsvnLNALRQRIsf 1291
Cdd:cd03221 1 IELENLSKTYG--GKLLLKDISLTINPGDRIGLVGRNGAGKSTL--------------------------LKLIAGEL-- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1292 ipqdpILFSGTVRsnldpfdelednflnealktsgassmimaHTDDQKPIHItldthvasegSNFSQGQKQVLALARAIV 1371
Cdd:cd03221 51 -----EPDEGIVT-----------------------------WGSTVKIGYF----------EQLSGGEKMRLALAKLLL 86
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19115470 1372 RRSKIIILDECTASVDDAMDQKIQKTLREAFGdaTMLCIAH-R--LKTIVdyDKVMVLDKG 1429
Cdd:cd03221 87 ENPNLLLLDEPTNHLDLESIEALEEALKEYPG--TVILVSHdRyfLDQVA--TKIIELEDG 143
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1211-1440 |
1.73e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 61.39 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1211 DIVFNHVSVSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSvNLNALRQRIS 1290
Cdd:PRK13536 39 TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1291 FIPQ-DPILFSGTVRSNLDPFDELednFlneALKTSGASSMIMAHTDDQKpihitLDTHVASEGSNFSQGQKQVLALARA 1369
Cdd:PRK13536 118 VVPQfDNLDLEFTVRENLLVFGRY---F---GMSTREIEAVIPSLLEFAR-----LESKADARVSDLSGGMKRRLTLARA 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19115470 1370 IVRRSKIIILDECTASVDDAMDQKIQKTLRE--AFGDATMLCI-----AHRLktivdYDKVMVLDKGVLVEYGPPAVL 1440
Cdd:PRK13536 187 LINDPQLLILDEPTTGLDPHARHLIWERLRSllARGKTILLTThfmeeAERL-----CDRLCVLEAGRKIAEGRPHAL 259
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1228-1387 |
2.10e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 59.44 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1228 ILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNA---LRQR-ISFIPQDPILfsgtv 1303
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQFHHL----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1304 rsnLDPFDELEDNFL-------NEALKTSGASSMIMAhtddqkpihITLDTHVASEGSNFSQGQKQVLALARAIVRRSKI 1376
Cdd:PRK11629 99 ---LPDFTALENVAMplligkkKPAEINSRALEMLAA---------VGLEHRANHRPSELSGGERQRVAIARALVNNPRL 166
|
170
....*....|.
gi 19115470 1377 IILDECTASVD 1387
Cdd:PRK11629 167 VLADEPTGNLD 177
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1216-1436 |
2.38e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.61 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1216 HVSVSYSaaGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQR-ISFIPQ 1294
Cdd:PRK15439 16 SISKQYS--GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgIYLVPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1295 DPILFSG-TVRSNLdpfdelednfLNEALKTSGASSMiMAHTDDQKPIHITLDTHVASegsnFSQGQKQVLALARAIVRR 1373
Cdd:PRK15439 94 EPLLFPNlSVKENI----------LFGLPKRQASMQK-MKQLLAALGCQLDLDSSAGS----LEVADRQIVEILRGLMRD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19115470 1374 SKIIILDECTASVD----DAMDQKIQKTLREAFGdatMLCIAHRLKTIVDY-DKVMVLDKGVLVEYGP 1436
Cdd:PRK15439 159 SRILILDEPTASLTpaetERLFSRIRELLAQGVG---IVFISHKLPEIRQLaDRISVMRDGTIALSGK 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1225-1437 |
3.01e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 61.36 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1225 GPTILKDVNLHINPSEKVAVVGRTGSGKSTLgLTLLRFTHR---ISGEI-----------YIN-----GRETQSVNLNAL 1285
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMDQyepTSGRIiyhvalcekcgYVErpskvGEPCPVCGGTLE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1286 RQRISFIPQDPILFSGTVRSNLDPF---------DELEDNFLN--EALKTSGASSMIMAhTDDQKPIHITLD-THVASEg 1353
Cdd:TIGR03269 91 PEEVDFWNLSDKLRRRIRKRIAIMLqrtfalygdDTVLDNVLEalEEIGYEGKEAVGRA-VDLIEMVQLSHRiTHIARD- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1354 snFSQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDA--TMLCIAHRLKTIVDY-DKVMVLDKGV 1430
Cdd:TIGR03269 169 --LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEVIEDLsDKAIWLENGE 246
|
....*..
gi 19115470 1431 LVEYGPP 1437
Cdd:TIGR03269 247 IKEEGTP 253
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1212-1447 |
3.18e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 60.50 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAAgpTILKDVNLHINPSEKVAVVGRTGSGKSTLgltlLRFTHRI----SGEIYINGREtqsVNLNALRQ 1287
Cdd:PRK11432 7 VVLKNITKRFGSN--TVIDNLNLTIKQGTMVTLLGPSGCGKTTV----LRLVAGLekptEGQIFIDGED---VTHRSIQQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1288 R-ISFIPQDPILFsgtvrsnldPFDELEDNfLNEALKTSGASSMIMAHTDDQKPIHITL----DTHVasegSNFSQGQKQ 1362
Cdd:PRK11432 78 RdICMVFQSYALF---------PHMSLGEN-VGYGLKMLGVPKEERKQRVKEALELVDLagfeDRYV----DQISGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1363 VLALARAIVRRSKIIILDECTASVD----DAMDQKIQKtLREAFGdATMLCIAH-RLKTIVDYDKVMVLDKGVLVEYGPP 1437
Cdd:PRK11432 144 RVALARALILKPKVLLFDEPLSNLDanlrRSMREKIRE-LQQQFN-ITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSP 221
|
250
....*....|.
gi 19115470 1438 AVLY-HNNGHF 1447
Cdd:PRK11432 222 QELYrQPASRF 232
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1229-1443 |
3.32e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 59.41 E-value: 3.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1229 LKDVNLHINPSEKVAVVGRTGSGKSTL-----GLTLLRFTHRISGEIYINGRE--TQSVNLNALRQRISFIPQDPILFSG 1301
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTIlrcfnRLNDLIPGFRVEGKVTFHGKNlyAPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1302 TVRSNL----------DPFDELEDNFLNEAlktsgassmimAHTDDQKpihitldTHVASEGSNFSQGQKQVLALARAIV 1371
Cdd:PRK14243 106 SIYDNIaygaringykGDMDELVERSLRQA-----------ALWDEVK-------DKLKQSGLSLSGGQQQRLCIARAIA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1372 RRSKIIILDECTASVDDAMDQKIQKTLREAFGDATMLCIAH------RLKTIVDYDKVMVLDKGV----LVEYGPPAVLY 1441
Cdd:PRK14243 168 VQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHnmqqaaRVSDMTAFFNVELTEGGGrygyLVEFDRTEKIF 247
|
..
gi 19115470 1442 HN 1443
Cdd:PRK14243 248 NS 249
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
646-810 |
3.44e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 58.83 E-value: 3.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 646 VIGPTGSGKSSLISALLGELSLNKGSYNLprsKGVSYVSQVPWLRNATI--RDNILFDYPYIEerykkviQACGL----- 718
Cdd:PRK10771 30 ILGPSGAGKSTLLNLIAGFLTPASGSLTL---NGQDHTTTPPSRRPVSMlfQENNLFSHLTVA-------QNIGLglnpg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 719 --LTDLQSfvaSDLTEIGEK-GVT---------LSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKHCFQSS 786
Cdd:PRK10771 100 lkLNAAQR---EKLHAIARQmGIEdllarlpgqLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVC 176
|
170 180
....*....|....*....|....
gi 19115470 787 LMENRTVILVTHNVhlfmDSAAFI 810
Cdd:PRK10771 177 QERQLTLLMVSHSL----EDAARI 196
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1229-1440 |
4.31e-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: 58.54 E-value: 4.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1229 LKDVNLHINPSEKVAVVGRTGSGKST---LGLTLLRFThriSGEIYING----RETQSVnlnalRQRISFIPQDPILFSG 1301
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTtikMLTTLLKPT---SGRATVAGhdvvREPREV-----RRRIGIVFQDLSVDDE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1302 -TVRSNLDPFDELednflnealktSGASSMIMAHTDDQKPIHITL----DTHVasegSNFSQGQKQVLALARAIVRRSKI 1376
Cdd:cd03265 88 lTGWENLYIHARL-----------YGVPGAERRERIDELLDFVGLleaaDRLV----KTYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19115470 1377 IILDECTASVD-DAMDQ--KIQKTLREAFG-----------DATMLCiahrlktivdyDKVMVLDKGVLVEYGPPAVL 1440
Cdd:cd03265 153 LFLDEPTIGLDpQTRAHvwEYIEKLKEEFGmtilltthymeEAEQLC-----------DRVAIIDHGRIIAEGTPEEL 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
643-802 |
4.46e-09 |
|
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: 60.69 E-value: 4.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 643 LSIViGPTGSGKSSLISALLGELSLNKGSYNL--------------PRSKGVSYVSQ------VPWLrnaTIRDNI---- 698
Cdd:COG1123 294 LGLV-GESGSGKSTLARLLLGLLRPTSGSILFdgkdltklsrrslrELRRRVQMVFQdpysslNPRM---TVGDIIaepl 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 699 ----LFDYPYIEERYKKVIQACGLLTD-LQSFVASdlteigekgvtLSGGQKQRIALARA-VYSPtSIVLMDDVFSALDI 772
Cdd:COG1123 370 rlhgLLSRAERRERVAELLERVGLPPDlADRYPHE-----------LSGGQRQRVAIARAlALEP-KLLILDEPTSALDV 437
|
170 180 190
....*....|....*....|....*....|....*....
gi 19115470 773 HTsnwiykhcfQSSLME---------NRTVILVTHNVHL 802
Cdd:COG1123 438 SV---------QAQILNllrdlqrelGLTYLFISHDLAV 467
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1229-1441 |
4.51e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 59.43 E-value: 4.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1229 LKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRISFIPQDP--ILFSGTVRS- 1305
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQd 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1306 ------NLDPFDELEDNFLNEALKTSGassmiMAHTDDQKPIHItldthvasegsnfSQGQKQVLALARAIVRRSKIIIL 1379
Cdd:PRK13652 100 iafgpiNLGLDEETVAHRVSSALHMLG-----LEELRDRVPHHL-------------SGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115470 1380 DECTASVD-DAMDQKIQ--KTLREAFGdATMLCIAHRLKTIVDY-DKVMVLDKGVLVEYGPPAVLY 1441
Cdd:PRK13652 162 DEPTAGLDpQGVKELIDflNDLPETYG-MTVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGTVEEIF 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
631-816 |
5.12e-09 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 58.63 E-value: 5.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYNLprsKGVSYVSQVPWLRnATIR------DNILFDYPy 704
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRL---NGRPLADWSPAEL-ARRRavlpqhSSLSFPFT- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 705 IEE-----RY---------KKVIQACGLLTDLQSFVASDLTeigekgvTLSGGQKQRIALARA------VYSPTSIVLMD 764
Cdd:PRK13548 93 VEEvvamgRAphglsraedDALVAAALAQVDLAHLAGRDYP-------QLSGGEQQRVQLARVlaqlwePDGPPRWLLLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115470 765 DVFSALDIHtsnwiykHcfQSSLME---------NRTVILVTHNVHLfmdSAAF---IVTVKNG 816
Cdd:PRK13548 166 EPTSALDLA-------H--QHHVLRlarqlaherGLAVIVVLHDLNL---AARYadrIVLLHQG 217
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1210-1443 |
5.89e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 59.25 E-value: 5.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1210 GDIVFNHVSVSYSAAGP---TILKDVNLHINPSEKVAVVGRTGSGKSTL-----GLTLLRFTHRISGEIYINGRETQSVN 1281
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMiqltnGLIISETGQTIVGDYAIPANLKKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1282 LNALRQRISFIPQDP--ILFSGTVRSNL--DPFDELEDNflNEALKTSGASSMIMAHTDDqkpihitldtHVASEGSNFS 1357
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIafGPVNLGENK--QEAYKKVPELLKLVQLPED----------YVKRSPFELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1358 QGQKQVLALARAIVRRSKIIILDECTASVDDAMDQ---KIQKTLREAFGDATMLcIAHRLKTIVDY-DKVMVLDKGVLVE 1433
Cdd:PRK13645 153 GGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfiNLFERLNKEYKKRIIM-VTHNMDQVLRIaDEVIVMHEGKVIS 231
|
250
....*....|
gi 19115470 1434 YGPPAVLYHN 1443
Cdd:PRK13645 232 IGSPFEIFSN 241
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1229-1438 |
7.03e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 60.04 E-value: 7.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1229 LKDVNLHINPSEKVAVVGRTGSGKSTL-----GltLLRFThriSGEIYINGREtqsVNLN----ALRQRISFIPQDPILF 1299
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLmkilyG--LYQPD---SGEILIDGKP---VRIRsprdAIALGIGMVHQHFMLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1300 sgtvrsnlDPFDELEdNFL-------NEALKTSGASSMIMAhTDDQKPIHITLDTHVasegSNFSQGQKQVLALARAIVR 1372
Cdd:COG3845 93 --------PNLTVAE-NIVlgleptkGGRLDRKAARARIRE-LSERYGLDVDPDAKV----EDLSVGEQQRVEILKALYR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19115470 1373 RSKIIILDECTA-----SVDDAMdqKIQKTLREAfGdATMLCIAHRLKTIVDY-DKVMVLDKGVLVEYGPPA 1438
Cdd:COG3845 159 GARILILDEPTAvltpqEADELF--EILRRLAAE-G-KSIIFITHKLREVMAIaDRVTVLRRGKVVGTVDTA 226
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1244-1443 |
7.79e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 59.09 E-value: 7.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1244 VVGRTGSGKSTL-----GLTLLRFTHRISGEIYINGRETQSV-----------NLNALRQRISFIPQDP--ILFSGTVRS 1305
Cdd:PRK13631 57 IIGNSGSGKSTLvthfnGLIKSKYGTIQVGDIYIGDKKNNHElitnpyskkikNFKELRRRVSMVFQFPeyQLFKDTIEK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1306 NLdpfdeledNFLNEALKTSGASSMIMAHTDDQKpihITLDTHVAsEGSNF--SQGQKQVLALARAIVRRSKIIILDECT 1383
Cdd:PRK13631 137 DI--------MFGPVALGVKKSEAKKLAKFYLNK---MGLDDSYL-ERSPFglSGGQKRRVAIAGILAIQPEILIFDEPT 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19115470 1384 ASVDDAMDQKIQKTLREAFGDA-TMLCIAHRLKTIVDY-DKVMVLDKGVLVEYGPPAVLYHN 1443
Cdd:PRK13631 205 AGLDPKGEHEMMQLILDAKANNkTVFVITHTMEHVLEVaDEVIVMDKGKILKTGTPYEIFTD 266
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
646-807 |
1.02e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 58.69 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 646 VIGPTGSGKSSLISALLGELSLNKGSYNL-----PRS-----KGVSYVSQVPWL-RNATIRDNILFDYPYIEERYKKVIQ 714
Cdd:PRK13536 72 LLGPNGAGKSTIARMILGMTSPDAGKITVlgvpvPARarlarARIGVVPQFDNLdLEFTVRENLLVFGRYFGMSTREIEA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 715 ACGLLTDLQSFVASDLTEIGEkgvtLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKHcFQSSLMENRTVI 794
Cdd:PRK13536 152 VIPSLLEFARLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWER-LRSLLARGKTIL 226
|
170
....*....|...
gi 19115470 795 LVTHnvhlFMDSA 807
Cdd:PRK13536 227 LTTH----FMEEA 235
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
631-807 |
1.02e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 58.08 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSS---LISALL----GELS-----LNKGSYNLPRSKgVSYVSQVPwlRN----ATI 694
Cdd:PRK13632 25 LKNVSFEINEGEYVAILGHNGSGKSTiskILTGLLkpqsGEIKidgitISKENLKEIRKK-IGIIFQNP--DNqfigATV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 695 RDNILF---DYPYIEERYKKVIQACGLLTDLQSFVASDLTEigekgvtLSGGQKQRIALARAVYSPTSIVLMDDVFSALD 771
Cdd:PRK13632 102 EDDIAFgleNKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQN-------LSGGQKQRVAIASVLALNPEIIIFDESTSMLD 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 19115470 772 IHTSNWIYKhcFQSSLMENR--TVILVTHNvhlfMDSA 807
Cdd:PRK13632 175 PKGKREIKK--IMVDLRKTRkkTLISITHD----MDEA 206
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1225-1387 |
1.06e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 59.65 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1225 GPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGREtqsVNLN----ALRQRISFIPQD----P 1296
Cdd:COG1129 264 VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKP---VRIRsprdAIRAGIAYVPEDrkgeG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1297 ILFSGTVRSN--LDPFDELEDN-FLNEALKTSGASSMImahtddqKPIHI---TLDTHVasegSNFSQGQKQVLALARAI 1370
Cdd:COG1129 341 LVLDLSIRENitLASLDRLSRGgLLDRRRERALAEEYI-------KRLRIktpSPEQPV----GNLSGGNQQKVVLAKWL 409
|
170
....*....|....*..
gi 19115470 1371 VRRSKIIILDECTASVD 1387
Cdd:COG1129 410 ATDPKVLILDEPTRGID 426
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
631-805 |
1.26e-08 |
|
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: 56.77 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISAL------------LGELSLNKGSYNLP--RSKgVSYVSQ----VPwlrNA 692
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCInlleepdsgtiiIDGLKLTDDKKNINelRQK-VGMVFQqfnlFP---HL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 693 TIRDNILFdyPYIEERYKKVIQACGLLTDLqsfvasdLTEIG--EKG----VTLSGGQKQRIALARAVYSPTSIVLMDDV 766
Cdd:cd03262 92 TVLENITL--APIKVKGMSKAEAEERALEL-------LEKVGlaDKAdaypAQLSGGQQQRVAIARALAMNPKVMLFDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 19115470 767 FSALDIHTSNWIYKhcfqssLM-----ENRTVILVTHNVH---------LFMD 805
Cdd:cd03262 163 TSALDPELVGEVLD------VMkdlaeEGMTMVVVTHEMGfarevadrvIFMD 209
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1212-1413 |
1.36e-08 |
|
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: 59.38 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSySAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLgltllrftHRISGEIY--INGRETQSVnlnalRQRI 1289
Cdd:TIGR00954 452 IKFENIPLV-TPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSL--------FRILGELWpvYGGRLTKPA-----KGKL 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1290 SFIPQDPILFSGTVRSNLDPFDELEDnflnealktsgassMIMAHTDDQKPIHItLD----THVASEGSNF--------- 1356
Cdd:TIGR00954 518 FYVPQRPYMTLGTLRDQIIYPDSSED--------------MKRRGLSDKDLEQI-LDnvqlTHILEREGGWsavqdwmdv 582
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 19115470 1357 -SQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAfgDATMLCIAHR 1413
Cdd:TIGR00954 583 lSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHR 638
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
627-807 |
1.47e-08 |
|
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: 56.61 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 627 GDF-CLRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGS-----YNLPRS-----KGVSYVSQVPWLRNA-TI 694
Cdd:cd03265 11 GDFeAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvagHDVVREprevrRRIGIVFQDLSVDDElTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 695 RDNI-----LFDYPYiEERYKKVIQACGLLtdlqsfvasDLTEIGEKGV-TLSGGQKQRIALARAVYSPTSIVLMDDVFS 768
Cdd:cd03265 91 WENLyiharLYGVPG-AERRERIDELLDFV---------GLLEAADRLVkTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 19115470 769 ALDIHTSNWIYKHCFQSSLMENRTVILVTHnvhlFMDSA 807
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTH----YMEEA 195
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
646-772 |
1.52e-08 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 57.54 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 646 VIGPTGSGKSSL---ISALL----GELSLN-----KGSYNLpRSKGVSYVSQVPwlrNATI--RDNI--LFDYPYI---- 705
Cdd:COG4167 44 IIGENGSGKSTLakmLAGIIeptsGEILINghkleYGDYKY-RCKHIRMIFQDP---NTSLnpRLNIgqILEEPLRlntd 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19115470 706 ---EERYKKVIQA---CGLLTDLQSFVASdlteigekgvTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDI 772
Cdd:COG4167 120 ltaEEREERIFATlrlVGLLPEHANFYPH----------MLSSGQKQRVALARALILQPKIIIADEALAALDM 182
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
606-816 |
1.53e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 57.49 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 606 DTSQEIGFfnaSLTWVSNPSPGDFCLRDLNIVFPRNKLSIVIGPTGSGKSSLISAL-------LGELSLNKGSYNLPRSK 678
Cdd:PRK10575 5 TNHSDTTF---ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLgrhqppsEGEILLDAQPLESWSSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 679 G----VSYV-SQVPWLRNATIRDNILFD-YPY--------IEERyKKVIQACGLLtDLQSFvASDLTEigekgvTLSGGQ 744
Cdd:PRK10575 82 AfarkVAYLpQQLPAAEGMTVRELVAIGrYPWhgalgrfgAADR-EKVEEAISLV-GLKPL-AHRLVD------SLSGGE 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19115470 745 KQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKHCFQSSLMENRTVILVTHNVHLFMDSAAFIVTVKNG 816
Cdd:PRK10575 153 RQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGG 224
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
631-808 |
2.02e-08 |
|
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: 57.06 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSL---ISALL----------GELSLNKGSYNLPRSKgVSYVSQVP--WLRNATIR 695
Cdd:TIGR04520 18 LKNVSLSIEKGEFVAIIGHNGSGKSTLaklLNGLLlptsgkvtvdGLDTLDEENLWEIRKK-VGMVFQNPdnQFVGATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 696 DNILF-------DYPYIEERYKKVIQACGLlTDLQSFVASdlteigekgvTLSGGQKQRIALARAV-YSPTSIVLmDDVF 767
Cdd:TIGR04520 97 DDVAFglenlgvPREEMRKRVDEALKLVGM-EDFRDREPH----------LLSGGQKQRVAIAGVLaMRPDIIIL-DEAT 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 19115470 768 SALD-------IHTSNWIYKHcfqsslmENRTVILVTHnvhlFMDSAA 808
Cdd:TIGR04520 165 SMLDpkgrkevLETIRKLNKE-------EGITVISITH----DMEEAV 201
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
631-802 |
2.13e-08 |
|
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: 56.29 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYNL---------PR---SKGVSYVSQVPWL-RNATIRDN 697
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdgrditglpPHeraRAGIGYVPEGRRIfPELTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 698 ILF-DYPYIEERYKKVI-QACGLLTDLQSFVASdlteigeKGVTLSGGQKQRIALARAVYSPTSIVLMD----------- 764
Cdd:cd03224 96 LLLgAYARRRAKRKARLeRVYELFPRLKERRKQ-------LAGTLSGGEQQMLAIARALMSRPKLLLLDepseglapkiv 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 19115470 765 -DVFSAL-DIHTsnwiykhcfqsslmENRTVILVTHNVHL 802
Cdd:cd03224 169 eEIFEAIrELRD--------------EGVTILLVEQNARF 194
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
630-814 |
2.16e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 55.06 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 630 CLRDLNIV-FPRNKLSIVIGPTGSGKSSLISA----LLGELS-LNKGSYNLPRSkGVSYVSqvpwlrnatirdnilfdyp 703
Cdd:cd03227 9 SYFVPNDVtFGEGSLTIITGPNGSGKSTILDAiglaLGGAQSaTRRRSGVKAGC-IVAAVS------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 704 yieerykkviqACGLLTDLQsfvasdlteigekgvtLSGGQKQRIALARAV----YSPTSIVLMDDVFSALDIHT----S 775
Cdd:cd03227 69 -----------AELIFTRLQ----------------LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDgqalA 121
|
170 180 190
....*....|....*....|....*....|....*....
gi 19115470 776 NWIYKHcfqssLMENRTVILVTHNvHLFMDSAAFIVTVK 814
Cdd:cd03227 122 EAILEH-----LVKGAQVIVITHL-PELAELADKLIHIK 154
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1229-1385 |
2.22e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.40 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1229 LKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLR-FTH-RISGEIYINGRETQSVNL-NALRQRISFIPQDPILFSG-TVr 1304
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvYPHgTYEGEIIFEGEELQASNIrDTERAGIAIIHQELALVKElSV- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1305 snldpfdeLEDNFLNEALKTSGASSMIMAHTDDQKPI-HITLDTHVASEGSNFSQGQKQVLALARAIVRRSKIIILDECT 1383
Cdd:PRK13549 100 --------LENIFLGNEITPGGIMDYDAMYLRAQKLLaQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
..
gi 19115470 1384 AS 1385
Cdd:PRK13549 172 AS 173
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
631-808 |
2.25e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 58.54 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRN-KLSIvIGPTGSGKSSLISALLGELSLNKGSYNLPRSKGVSYVSQvpwLR-----NATIRDNILFDYPY 704
Cdd:COG0488 331 LDDLSLRIDRGdRIGL-IGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQ---HQeeldpDKTVLDELRDGAPG 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 705 IEERYkkVIQACG--LLT--DLQSFVASdlteigekgvtLSGGQKQRIALARAVYSPTSIVLMD----DvfsaLDIHTsn 776
Cdd:COG0488 407 GTEQE--VRGYLGrfLFSgdDAFKPVGV-----------LSGGEKARLALAKLLLSPPNVLLLDeptnH----LDIET-- 467
|
170 180 190
....*....|....*....|....*....|...
gi 19115470 777 wiyKHCFQSSLME-NRTVILVTHNVHlFMDSAA 808
Cdd:COG0488 468 ---LEALEEALDDfPGTVLLVSHDRY-FLDRVA 496
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
631-808 |
2.35e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 57.34 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYNL---------------PRSKGVSYVSQVP--WLRNAT 693
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitagkknkklkPLRKKVGIVFQFPehQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 694 IRDNILFDyPY--------IEERYKKVIQACGLLTDLQSFVASDlteigekgvtLSGGQKQRIALARAV-YSPTSIVLmD 764
Cdd:PRK13634 103 VEKDICFG-PMnfgvseedAKQKAREMIELVGLPEELLARSPFE----------LSGGQMRRVAIAGVLaMEPEVLVL-D 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 19115470 765 DVFSALDIHTSNWIYKHCFQSSLMENRTVILVTHNvhlfMDSAA 808
Cdd:PRK13634 171 EPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHS----MEDAA 210
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1232-1438 |
2.35e-08 |
|
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: 58.66 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1232 VNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYI----------------NGRETQSVNLnaLRQRISFIPQD 1295
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkpgpdgRGRAKRYIGI--LHQEYDLYPHR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1296 PILFSGTVRSNLDPFDELEDNFLNEALKTSGassmimahTDDQKPIHItLDTHVasegSNFSQGQKQVLALARAIVRRSK 1375
Cdd:TIGR03269 381 TVLDNLTEAIGLELPDELARMKAVITLKMVG--------FDEEKAEEI-LDKYP----DELSEGERHRVALAQVLIKEPR 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19115470 1376 IIILDECTASVDDAMDQKIQKTL---REAFGDaTMLCIAHRLKTIVDY-DKVMVLDKGVLVEYGPPA 1438
Cdd:TIGR03269 448 IVILDEPTGTMDPITKVDVTHSIlkaREEMEQ-TFIIVSHDMDFVLDVcDRAALMRDGKIVKIGDPE 513
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
631-827 |
2.57e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.10 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLI---SALL----GELSLN--------KGSYNLPRSKGVSYVSQVP--WLRNAT 693
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIqniNALLkpttGTVTVDditithktKDKYIRPVRKRIGMVFQFPesQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 694 IRDNILF-------DYPYIEERYKKVIQACGLLTDLQSfvasdlteigEKGVTLSGGQKQRIALARAVYSPTSIVLMDDV 766
Cdd:PRK13646 103 VEREIIFgpknfkmNLDEVKNYAHRLLMDLGFSRDVMS----------QSPFQMSGGQMRKIAIVSILAMNPDIIVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19115470 767 FSALDIHTSNWIYKHCFQSSLMENRTVILVTHNVHLFMDSAAFIVTVKNGSafpVTDKSSP 827
Cdd:PRK13646 173 TAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGS---IVSQTSP 230
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
631-807 |
2.85e-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: 56.29 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSY--------NLPRSK----GVSYVSQVPWL-RNATIRDN 697
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlfdgeditGLPPHEiarlGIGRTFQIPRLfPELTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 698 IL-----------------FDYPYIEERYKKVIQACGlLTDLQSFVASdlteigekgvTLSGGQKQRIALARAVYSPTSI 760
Cdd:cd03219 96 VMvaaqartgsglllararREEREARERAEELLERVG-LADLADRPAG----------ELSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 19115470 761 VLMDDVFSALDI----HTSNWIykhcfQSSLMENRTVILVTHNVHLFMDSA 807
Cdd:cd03219 165 LLLDEPAAGLNPeeteELAELI-----RELRERGITVLLVEHDMDVVMSLA 210
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
627-800 |
3.31e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 56.64 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 627 GDFCLRDLNIVFPRNKLSIVIGPTGSGKSSLI-----------------SALLGELSLNKGSYNLPRSKGVSYVSQVPWL 689
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLrtlnrmndkvsgyrysgDVLLGGRSIFNYRDVLEFRRRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 690 RNATIRDNILFDYpyieeRYKKVIQAcgllTDLQSFVASDLTEIG----------EKGVTLSGGQKQRIALARAVYSPTS 759
Cdd:PRK14271 113 FPMSIMDNVLAGV-----RAHKLVPR----KEFRGVAQARLTEVGlwdavkdrlsDSPFRLSGGQQQLLCLARTLAVNPE 183
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 19115470 760 IVLMDDVFSALDIHTSNWIYKhcFQSSLMENRTVILVTHNV 800
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEE--FIRSLADRLTVIIVTHNL 222
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
627-772 |
3.35e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 57.19 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 627 GDFCLrDLNIVFPRNKLSIVIGPTGSGKSSLISALLG-------ELSLN--------KGSYNLPRSKGVSYVSQvpwlrN 691
Cdd:PRK11144 11 GDLCL-TVNLTLPAQGITAIFGRSGAGKTSLINAISGltrpqkgRIVLNgrvlfdaeKGICLPPEKRRIGYVFQ-----D 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 692 A------TIRDNILFDY-PYIEERYKKVIQACGLLTDLQSFVAsdlteigekgvTLSGGQKQRIALARAVYSPTSIVLMD 764
Cdd:PRK11144 85 ArlfphyKVRGNLRYGMaKSMVAQFDKIVALLGIEPLLDRYPG-----------SLSGGEKQRVAIGRALLTAPELLLMD 153
|
....*...
gi 19115470 765 DVFSALDI 772
Cdd:PRK11144 154 EPLASLDL 161
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1227-1435 |
4.26e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 54.96 E-value: 4.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1227 TILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTH---RISGEIYINGRETQSVNLNALRQrISFIPQDPILFSG-T 1302
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEgnvSVEGDIHYNGIPYKEFAEKYPGE-IIYVSEEDVHFPTlT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1303 VRSNLDpFdelednflneALKTSGaSSMImahtddqkpihitldthvasegSNFSQGQKQVLALARAIVRRSKIIILDEC 1382
Cdd:cd03233 100 VRETLD-F----------ALRCKG-NEFV----------------------RGISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 19115470 1383 TASVDDAMDQKIQKTLRE---AFGDATMLCIAHRLKTIVD-YDKVMVLDKGVLVEYG 1435
Cdd:cd03233 146 TRGLDSSTALEILKCIRTmadVLKTTTFVSLYQASDEIYDlFDKVLVLYEGRQIYYG 202
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
631-799 |
4.54e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 56.00 E-value: 4.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLN-------------KGSYN-----LPRSKGVSYVSQVP-WLRN 691
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvegevrlfgRNIYSpdvdpIEVRREVGMVFQYPnPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 692 ATIRDNILFDYPY---------IEERYKKVIQACGLLTDLQSfvasdltEIGEKGVTLSGGQKQRIALARAVYSPTSIVL 762
Cdd:PRK14267 100 LTIYDNVAIGVKLnglvkskkeLDERVEWALKKAALWDEVKD-------RLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 19115470 763 MDDVFSALDIHTSNWIYKHCFQssLMENRTVILVTHN 799
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFE--LKKEYTIVLVTHS 207
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
627-798 |
4.59e-08 |
|
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: 55.71 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 627 GDFCLRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGS--------YNLPRSK-GVSYVSQ----VPWLrnaT 693
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEilldgkdiTNLPPHKrPVNTVFQnyalFPHL---T 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 694 IRDNILF-------DYPYIEERYKKVIQacglLTDLQSFVASDLTEigekgvtLSGGQKQRIALARAVYSPTSIVLMDDV 766
Cdd:cd03300 89 VFENIAFglrlkklPKAEIKERVAEALD----LVQLEGYANRKPSQ-------LSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 19115470 767 FSALDIHTSNWIykhcfQSSLME-----NRTVILVTH 798
Cdd:cd03300 158 LGALDLKLRKDM-----QLELKRlqkelGITFVFVTH 189
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1212-1442 |
4.67e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 56.28 E-value: 4.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAAGP---TILKDVNLHINPSEKVAVVGRTGSGKSTL------GLTLLRFTHRIsGEIYINGRETQSvNL 1282
Cdd:PRK13643 2 IKFEKVNYTYQPNSPfasRALFDIDLEVKKGSYTALIGHTGSGKSTLlqhlngLLQPTEGKVTV-GDIVVSSTSKQK-EI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1283 NALRQRISFIPQDP--ILFSGTV-------RSNLDPFDELEDNFLNEALKTSGASSMIMahtdDQKPIHItldthvaseg 1353
Cdd:PRK13643 80 KPVRKKVGVVFQFPesQLFEETVlkdvafgPQNFGIPKEKAEKIAAEKLEMVGLADEFW----EKSPFEL---------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1354 snfSQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREAFGDA-TMLCIAHRLKTIVDY-DKVMVLDKGVL 1431
Cdd:PRK13643 146 ---SGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGqTVVLVTHLMDDVADYaDYVYLLEKGHI 222
|
250
....*....|.
gi 19115470 1432 VEYGPPAVLYH 1442
Cdd:PRK13643 223 ISCGTPSDVFQ 233
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1229-1457 |
6.02e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 56.97 E-value: 6.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1229 LKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYING-----------RETQSVNLNALRQRISFIPQDPI 1297
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1298 LFSGTVRSNLD--PFDELEDNFLnEALKTSGASSMIMAHTDDqkpihitldthvasegsnFSQGQKQVLALARAIVRRSK 1375
Cdd:PRK10070 124 LDNTAFGMELAgiNAEERREKAL-DALRQVGLENYAHSYPDE------------------LSGGMRQRVGLARALAINPD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1376 IIILDECTASVDDAMDQKIQKTL--REAFGDATMLCIAHRLKTIVDY-DKVMVLDKGVLVEYGPPAVLYHN--NGHFRRM 1450
Cdd:PRK10070 185 ILLMDEAFSALDPLIRTEMQDELvkLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNNpaNDYVRTF 264
|
....*..
gi 19115470 1451 CDGSGIT 1457
Cdd:PRK10070 265 FRGVDIS 271
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
626-820 |
6.58e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 57.25 E-value: 6.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 626 PGDFCLRDLNIVF-PRNKLSiVIGPTGSGKSSL--ISA-----LLGELSLNKGsYNlprskgVSYVSQVPWL-RNATIRD 696
Cdd:TIGR03719 16 PKKEILKDISLSFfPGAKIG-VLGLNGAGKSTLlrIMAgvdkdFNGEARPQPG-IK------VGYLPQEPQLdPTKTVRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 697 NIL------------FDYPY-------------IEE--RYKKVIQACGLLT-DLQSFVASDLTEI--GEKGVT-LSGGQK 745
Cdd:TIGR03719 88 NVEegvaeikdaldrFNEISakyaepdadfdklAAEqaELQEIIDAADAWDlDSQLEIAMDALRCppWDADVTkLSGGER 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19115470 746 QRIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKHcfqssLMENR-TVILVTHNVHlFMDSAA-FIVTVKNGSAFP 820
Cdd:TIGR03719 168 RRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERH-----LQEYPgTVVAVTHDRY-FLDNVAgWILELDRGRGIP 238
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
611-800 |
6.81e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 55.58 E-value: 6.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 611 IGFFNASLTWVSNPSPgdfCLRDLNIVFPRNKLSIVIGPTGSGKSSlISALLGELSLnkgSYNLPRSK----GVSYVSQV 686
Cdd:PRK13640 6 VEFKHVSFTYPDSKKP---ALNDISFSIPRGSWTALIGHNGSGKST-ISKLINGLLL---PDDNPNSKitvdGITLTAKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 687 PW---------LRN-------ATIRDNILFDypyIEERykKVIQacgllTDLQSFVASDLTEIG------EKGVTLSGGQ 744
Cdd:PRK13640 79 VWdirekvgivFQNpdnqfvgATVGDDVAFG---LENR--AVPR-----PEMIKIVRDVLADVGmldyidSEPANLSGGQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 19115470 745 KQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKHCFQSSLMENRTVILVTHNV 800
Cdd:PRK13640 149 KQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDI 204
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
646-798 |
7.70e-08 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 56.27 E-value: 7.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 646 VIGPTGSGKSSLISALLGelsLNK---GS--------YNLP-------RSKGVSYVSQ----VPWLrnaTIRDNILF--- 700
Cdd:COG4175 58 IMGLSGSGKSTLVRCLNR---LIEptaGEvlidgediTKLSkkelrelRRKKMSMVFQhfalLPHR---TVLENVAFgle 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 701 ----DypyIEERYKKVIQA---CGLLTDLQSFVASdlteigekgvtLSGGQKQRIALARAVYSPTSIVLMDDVFSALD-- 771
Cdd:COG4175 132 iqgvP---KAERRERAREAlelVGLAGWEDSYPDE-----------LSGGMQQRVGLARALATDPDILLMDEAFSALDpl 197
|
170 180 190
....*....|....*....|....*....|..
gi 19115470 772 IHTSnwiykhcFQSSLME-----NRTVILVTH 798
Cdd:COG4175 198 IRRE-------MQDELLElqaklKKTIVFITH 222
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
631-808 |
7.98e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 55.61 E-value: 7.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLI---SALL----GE-------LSLNKGSYNLPR-SKGVSYVSQVP---WLRNA 692
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMqhfNALLkpssGTitiagyhITPETGNKNLKKlRKKVSLVFQFPeaqLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 693 TIRD------NILFDYPYIEERYKKVIQACGLLTDLqsfvasdlteIGEKGVTLSGGQKQRIALARAVYSPTSIVLMDDV 766
Cdd:PRK13641 103 VLKDvefgpkNFGFSEDEAKEKALKWLKKVGLSEDL----------ISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 19115470 767 FSALDIHTSNWIYKhCFQSSLMENRTVILVTHNvhlfMDSAA 808
Cdd:PRK13641 173 AAGLDPEGRKEMMQ-LFKDYQKAGHTVILVTHN----MDDVA 209
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
934-1163 |
9.42e-08 |
|
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: 55.26 E-value: 9.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 934 NKFLFVYGTMLLAYSLLDFLRTVSYDRGAWWASRKLHDSMLESVFGTFASWFDKTPTGRIVNRFAKDI----RSIDMNLS 1009
Cdd:cd18557 36 NELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTsvlqSAVTDNLS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1010 GWLFfsinCFLSVAGGI-----------LSVSSAMPIFMIPAVIVclaGYYFGLLYTRAQVGVKRLISIytspifslLGE 1078
Cdd:cd18557 116 QLLR----NILQVIGGLiilfilswkltLVLLLVIPLLLIASKIY---GRYIRKLSKEVQDALAKAGQV--------AEE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1079 SIVGVSVIRAFNRQTIFKQMFSERLDnlvrlqsTSYNLNRWVAvRTDGISGLVGAIAGLIALL-----------QKDLSP 1147
Cdd:cd18557 181 SLSNIRTVRSFSAEEKEIRRYSEALD-------RSYRLARKKA-LANALFQGITSLLIYLSLLlvlwyggylvlSGQLTV 252
|
250
....*....|....*..
gi 19115470 1148 G-VVGFSLNQAVIFSSS 1163
Cdd:cd18557 253 GeLTSFILYTIMVASSV 269
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
631-821 |
9.89e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 56.20 E-value: 9.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYNLP---------------RSKGVSYVSQ-VPWLRNATI 694
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvdiakisdaelrevRRKKIAMVFQsFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 695 RDNILFDYPYI----EERYKKVIQACGLLtDLQSFVASDLTEigekgvtLSGGQKQRIALARAVYSPTSIVLMDDVFSAL 770
Cdd:PRK10070 124 LDNTAFGMELAginaEERREKALDALRQV-GLENYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 19115470 771 DIHTSNWIYKHCFQSSLMENRTVILVTHNVHLFMDSAAFIVTVKNGSAFPV 821
Cdd:PRK10070 196 DPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQV 246
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
935-1101 |
1.17e-07 |
|
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: 55.09 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 935 KFLFVYGTMLLAYSLLDFLRTVSYDRGAWWASRKLHDSMLESVFGTFASWFDKTPTGRIVNRFAKDIRSIDMnlsgwlFF 1014
Cdd:cd18544 42 LLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNE------LF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1015 SiNCFLSVAGGILSVSSAMpIFM--------------IPAVIvcLAGYYFGLLYTRAQVGVKRLISIytspIFSLLGESI 1080
Cdd:cd18544 116 T-SGLVTLIGDLLLLIGIL-IAMfllnwrlalisllvLPLLL--LATYLFRKKSRKAYREVREKLSR----LNAFLQESI 187
|
170 180
....*....|....*....|.
gi 19115470 1081 VGVSVIRAFNRQTIFKQMFSE 1101
Cdd:cd18544 188 SGMSVIQLFNREKREFEEFDE 208
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
631-798 |
1.23e-07 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 55.10 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSS-------LISALLGELSLNkG----SYN---LPRSKGvsYVSQ----VPwlrNA 692
Cdd:COG1125 18 VDDLSLTIPAGEFTVLVGPSGCGKTTtlrminrLIEPTSGRILID-GedirDLDpveLRRRIG--YVIQqiglFP---HM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 693 TIRDNI-----LFDYPyiEERYKKviQACGLLtDLqsfVASDLTEIGEK-GVTLSGGQKQRIALARAVYSPTSIVLMDDV 766
Cdd:COG1125 92 TVAENIatvprLLGWD--KERIRA--RVDELL-EL---VGLDPEEYRDRyPHELSGGQQQRVGVARALAADPPILLMDEP 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 19115470 767 FSALDIhtsnwIYKHCFQSSLME-----NRTVILVTH 798
Cdd:COG1125 164 FGALDP-----ITREQLQDELLRlqrelGKTIVFVTH 195
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
631-826 |
1.28e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 54.25 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISAL-------LGELSLNKGSYNLPRSKGVSYVSQvpwLR------------- 690
Cdd:PRK11124 18 LFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNIAGNHFDFSKTPSDKAIRE---LRrnvgmvfqqynlw 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 691 -NATIRDNiLFDYP-----YIEERYKKviQACGLLTDLQsfvasdLTEIGEK-GVTLSGGQKQRIALARAVYSPTSIVLM 763
Cdd:PRK11124 95 pHLTVQQN-LIEAPcrvlgLSKDQALA--RAEKLLERLR------LKPYADRfPLHLSGGQQQRVAIARALMMEPQVLLF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115470 764 DDVFSALDIHTSNWIYKhcFQSSLMENR-TVILVTHNVHLFMDSAAFIVTVKNGSAFPVTDKSS 826
Cdd:PRK11124 166 DEPTAALDPEITAQIVS--IIRELAETGiTQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC 227
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1215-1387 |
1.36e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 56.27 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1215 NHVSVSYSAAGPTI--LKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNAL----RQR 1288
Cdd:PRK10535 8 KDIRRSYPSGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1289 ISFIPQdpilfsgtvRSNLDPFDELEDNFLNEAL--KTSGASSMIMAHTDDQKpihITLDTHVASEGSNFSQGQKQVLAL 1366
Cdd:PRK10535 88 FGFIFQ---------RYHLLSHLTAAQNVEVPAVyaGLERKQRLLRAQELLQR---LGLEDRVEYQPSQLSGGQQQRVSI 155
|
170 180
....*....|....*....|.
gi 19115470 1367 ARAIVRRSKIIILDECTASVD 1387
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALD 176
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1227-1438 |
1.38e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.83 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1227 TILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLL-RFTH-------RISGEIYINGRETQSVNLNALRQRISFIPQ--DP 1296
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGggaprgaRVTGDVTLNGEPLAAIDAPRLARLRAVLPQaaQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1297 ILfsgtvrsnldPFDELEDNFLNE--ALKTSGASSMIMAHTDDQKPIHITLDTHVASEGSNFSQGQKQVLALARAI---- 1370
Cdd:PRK13547 95 AF----------AFSAREIVLLGRypHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlw 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115470 1371 -----VRRSKIIILDECTASVDDAMDQKIQKTLREAFGDATM--LCIAHRLKTIVDY-DKVMVLDKGVLVEYGPPA 1438
Cdd:PRK13547 165 pphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgvLAIVHDPNLAARHaDRIAMLADGAIVAHGAPA 240
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1219-1387 |
1.49e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 53.70 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1219 VSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGREtqsvNLNALRQR-ISFIPQDPI 1297
Cdd:PRK13543 17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT----ATRGDRSRfMAYLGHLPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1298 LfsgtvRSNLDPFDELedNFLN-----EALKTSGASSMIMAHTDDQkpihitlDTHVasegSNFSQGQKQVLALARAIVR 1372
Cdd:PRK13543 93 L-----KADLSTLENL--HFLCglhgrRAKQMPGSALAIVGLAGYE-------DTLV----RQLSAGQKKRLALARLWLS 154
|
170
....*....|....*
gi 19115470 1373 RSKIIILDECTASVD 1387
Cdd:PRK13543 155 PAPLWLLDEPYANLD 169
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1214-1400 |
1.55e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 54.11 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1214 FNHVSVSYSAAgpTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRE-TQSVNLNALRQRISFI 1292
Cdd:PRK11614 8 FDKVSAHYGKI--QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDiTDWQTAKIMREAVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1293 PQDPILFSG-TVRSNL--DPFDELEDNFLNEALKTSGassmimahtddqkpIHITLDTHVASEGSNFSQGQKQVLALARA 1369
Cdd:PRK11614 86 PEGRRVFSRmTVEENLamGGFFAERDQFQERIKWVYE--------------LFPRLHERRIQRAGTMSGGEQQMLAIGRA 151
|
170 180 190
....*....|....*....|....*....|.
gi 19115470 1370 IVRRSKIIILDECTASVDDAMDQKIQKTLRE 1400
Cdd:PRK11614 152 LMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQ 182
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
618-798 |
1.72e-07 |
|
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: 52.94 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 618 LTWVSNPSPGDFC---LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLN--KGS--YN-LPRSKG-----VSYVS 684
Cdd:cd03213 9 LTVTVKSSPSKSGkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEvlINgRPLDKRsfrkiIGYVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 685 QvpwlrnatirDNILFDYPYIEERYKkvIQACglltdLQSfvasdlteigekgvtLSGGQKQRIALARAVYSPTSIVLMD 764
Cdd:cd03213 89 Q----------DDILHPTLTVRETLM--FAAK-----LRG---------------LSGGERKRVSIALELVSNPSLLFLD 136
|
170 180 190
....*....|....*....|....*....|....
gi 19115470 765 DVFSALDIHTSNWIYKhCFQSSLMENRTVILVTH 798
Cdd:cd03213 137 EPTSGLDSSSALQVMS-LLRRLADTGRTIICSIH 169
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1225-1429 |
1.98e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 55.60 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1225 GPTILKDVNLHINPSEKVAVVGRTGSGKSTLgLTLLRFTH---RISGEIYINGRETQSVNL-NALRQRISFIPQDPILfs 1300
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTL-MKILSGVYphgTWDGEIYWSGSPLKASNIrDTERAGIVIIHQELTL-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1301 gtvrsnLDPFDELEDNFLNEALKTSGA----SSMIMAHTDDQKPIHITlDTHVASEGSNFSQGQKQVLALARAIVRRSKI 1376
Cdd:TIGR02633 90 ------VPELSVAENIFLGNEITLPGGrmayNAMYLRAKNLLRELQLD-ADNVTRPVGDYGGGQQQLVEIAKALNKQARL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 19115470 1377 IILDECTASVDDAMDQKIQKTLRE--AFGDATMLcIAHRLKTIVDY-DKVMVLDKG 1429
Cdd:TIGR02633 163 LILDEPSSSLTEKETEILLDIIRDlkAHGVACVY-ISHKLNEVKAVcDTICVIRDG 217
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
631-801 |
1.98e-07 |
|
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: 53.88 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSlnkgsynlPRSKGVSYVSQVPW------LRNATI----RDNILF 700
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQ--------PTSGEVRVAGLVPWkrrkkfLRRIGVvfgqKTQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 701 DYPYIE-------------ERYKKVIQACGLLTDLQSFVASDLTEigekgvtLSGGQKQRIALARAVYSPTSIVLMDDVF 767
Cdd:cd03267 109 DLPVIDsfyllaaiydlppARFKKRLDELSELLDLEELLDTPVRQ-------LSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190
....*....|....*....|....*....|....*.
gi 19115470 768 SALDIHTSNWIYKhcFQSSLMENR--TVILVTHNVH 801
Cdd:cd03267 182 IGLDVVAQENIRN--FLKEYNRERgtTVLLTSHYMK 215
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
631-816 |
2.66e-07 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 52.97 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPrNKLSIVIGPTGSGKSSLISALLGELSLNKGS-----YNLPRSKG-----VSYVSQ-VPWLRNATIRD--- 696
Cdd:cd03264 16 LDGVSLTLG-PGMYGLLGPNGAGKTTLMRILATLTPPSSGTiridgQDVLKQPQklrrrIGYLPQeFGVYPNFTVREfld 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 697 --NILFDYPYIEERyKKVIQACGLLtdlqsfvasDLTEIGEKGV-TLSGGQKQRIALARAVYSPTSIVLMDDVFSALD-- 771
Cdd:cd03264 95 yiAWLKGIPSKEVK-ARVDEVLELV---------NLGDRAKKKIgSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDpe 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 19115470 772 --IHTSNWIykhcfqSSLMENRTVILVTHNVHLFMDSAAFIVTVKNG 816
Cdd:cd03264 165 erIRFRNLL------SELGEDRIVILSTHIVEDVESLCNQVAVLNKG 205
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1229-1412 |
2.74e-07 |
|
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: 53.21 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1229 LKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRfTHRI-SGEIYINgRETQSVNLN--------ALRQR-ISFIPQ---- 1294
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG-NYLPdSGSILVR-HDGGWVDLAqaspreilALRRRtIGYVSQflrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1295 -----------DPILFSGTVRSnldpfdelednflnEALKTSGAssmIMAHTD------DQKPihitldthvasegSNFS 1357
Cdd:COG4778 105 iprvsaldvvaEPLLERGVDRE--------------EARARARE---LLARLNlperlwDLPP-------------ATFS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 19115470 1358 QGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQKTLREA-FGDATMLCIAH 1412
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkARGTAIIGIFH 210
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
631-798 |
2.90e-07 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 54.31 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNK----------LSI-------VIGPTGSGKSSLIS--ALL-----GEL--------SLNKG-------- 670
Cdd:COG1135 4 LENLSKTFPTKGgpvtalddvsLTIekgeifgIIGYSGAGKSTLIRciNLLerptsGSVlvdgvdltALSERelraarrk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 671 ------SYNLPRSKgvsyvsqvpwlrnaTIRDNILFdyPYI------EERYKKVIQacgLLtdlqsfvasDLTEIGEKG- 737
Cdd:COG1135 84 igmifqHFNLLSSR--------------TVAENVAL--PLEiagvpkAEIRKRVAE---LL---------ELVGLSDKAd 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115470 738 ---VTLSGGQKQRIALARA-VYSPtSIVLMDDVFSALDIHTSNwiykhcfqsSLME-----NR----TVILVTH 798
Cdd:COG1135 136 aypSQLSGGQKQRVGIARAlANNP-KVLLCDEATSALDPETTR---------SILDllkdiNRelglTIVLITH 199
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
631-825 |
3.10e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 53.59 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLIsallgeLSLNkgSYNLPrSKGVSYV-------SQVPWLRN------------ 691
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLL------LHLN--GIYLP-QRGRVKVmgrevnaENEKWVRSkvglvfqdpddq 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 692 ---ATIRDNILF-------DYPYIEERYKKVIQACGLltdlqsfvasdlTEIGEKG-VTLSGGQKQRIALARAVYSPTSI 760
Cdd:PRK13647 92 vfsSTVWDDVAFgpvnmglDKDEVERRVEEALKAVRM------------WDFRDKPpYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19115470 761 VLMDDVFSALDIHTsnwiykhcfQSSLME--------NRTVILVTHNVHLFMDSAAFIVTVKNGSAFPVTDKS 825
Cdd:PRK13647 160 IVLDEPMAYLDPRG---------QETLMEildrlhnqGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1232-1443 |
3.21e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 53.46 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1232 VNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNAL-RQRISFIPQDPILF-SGTVRSNL-- 1307
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIaRMGVVRTFQHVRLFrEMTVIENLlv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1308 DPFDELEDNFLNEALKTSG-----ASSMIMAHTDDQKpihITLDTHVASEGSNFSQGQKQVLALARAIVRRSKIIILDEC 1382
Cdd:PRK11300 104 AQHQQLKTGLFSGLLKTPAfrraeSEALDRAATWLER---VGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115470 1383 TASVD----DAMDQKIQKtLREAFGdATMLCIAHRLKTIVDY-DKVMVLDKGVLVEYGPPAVLYHN 1443
Cdd:PRK11300 181 AAGLNpketKELDELIAE-LRNEHN-VTVLLIEHDMKLVMGIsDRIYVVNQGTPLANGTPEEIRNN 244
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
611-811 |
3.89e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 53.22 E-value: 3.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 611 IGFFNASLTWVSNPSpgdFCLRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSY---NLPRS--------KG 679
Cdd:PRK13648 8 IVFKNVSFQYQSDAS---FTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynNQAITddnfeklrKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 680 VSYVSQVPwlRNATIRDNILFDY---------PYiEERYKKVIQAcglLTDLQSFVASDlteigEKGVTLSGGQKQRIAL 750
Cdd:PRK13648 85 IGIVFQNP--DNQFVGSIVKYDVafglenhavPY-DEMHRRVSEA---LKQVDMLERAD-----YEPNALSGGQKQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 751 ARAVYSPTSIVLMDDVFSALDIHTsnwiykhcfQSSLME---------NRTVILVTHNVHLFMDSAAFIV 811
Cdd:PRK13648 154 AGVLALNPSVIILDEATSMLDPDA---------RQNLLDlvrkvksehNITIISITHDLSEAMEADHVIV 214
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
618-811 |
4.15e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 53.51 E-value: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 618 LTWVSNP-SPgdF---CLRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGS------------YNLPR-SKGV 680
Cdd:PRK13637 8 LTHIYMEgTP--FekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKiiidgvditdkkVKLSDiRKKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 681 SYVSQVP--WLRNATIRDNILFDyPY--------IEERYKKVIQACGLltdlqsfvasDLTEIGEKG-VTLSGGQKQRIA 749
Cdd:PRK13637 86 GLVFQYPeyQLFEETIEKDIAFG-PInlglseeeIENRVKRAMNIVGL----------DYEDYKDKSpFELSGGQKRRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19115470 750 LARAVYSPTSIVLMDDVFSALDIHTSNWIYKHCFQSSLMENRTVILVTHNvhlfMDSAAFIV 811
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHS----MEDVAKLA 212
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1212-1433 |
4.21e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 52.65 E-value: 4.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRfthrisgeIYINGRETQSVNlnalrqrisf 1291
Cdd:COG2401 29 IVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG--------ALKGTPVAGCVD---------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1292 IPQDPILFSGTVRSNLDPFDELEDNFlnEALKTSGASSmimAHTDDQKPihitldthvasegSNFSQGQKQVLALARAIV 1371
Cdd:COG2401 91 VPDNQFGREASLIDAIGRKGDFKDAV--ELLNAVGLSD---AVLWLRRF-------------KELSTGQKFRFRLALLLA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19115470 1372 RRSKIIILDECTASVDDAMDQ----KIQKTLREAfgDATMLCIAHRlKTIVDY---DKVMVLDKGVLVE 1433
Cdd:COG2401 153 ERPKLLVIDEFCSHLDRQTAKrvarNLQKLARRA--GITLVVATHH-YDVIDDlqpDLLIFVGYGGVPE 218
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
630-798 |
4.34e-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: 52.11 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 630 CLRDLNIVFPRNKLSI-------VIGPTGSGKSSL---ISALL----GELSLNKGSYNLPR---SKGVSYVSQVPWLRNA 692
Cdd:cd03231 8 CERDGRALFSGLSFTLaagealqVTGPNGSGKTTLlriLAGLSpplaGRVLLNGGPLDFQRdsiARGLLYLGHAPGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 693 -TIRDNILFDYPYieerykkviqaCGLLTDLQSFVASDLTEIGEKGV-TLSGGQKQRIALARAVYSPTSIVLMDDVFSAL 770
Cdd:cd03231 88 lSVLENLRFWHAD-----------HSDEQVEEALARVGLNGFEDRPVaQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180
....*....|....*....|....*...
gi 19115470 771 DIHTSNWIYKHcFQSSLMENRTVILVTH 798
Cdd:cd03231 157 DKAGVARFAEA-MAGHCARGGMVVLTTH 183
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
648-801 |
4.99e-07 |
|
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: 52.55 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 648 GPTGSGKSSLISALLGELSLNKGSY--------NLPRSK----GVSYVSQVPWL-RNATIRDNIL----FDYPYIEERYK 710
Cdd:cd03218 33 GPNGAGKTTTFYMIVGLVKPDSGKIlldgqditKLPMHKrarlGIGYLPQEASIfRKLTVEENILavleIRGLSKKEREE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 711 KVIQacgLLTDLQsfvasdLTEI-GEKGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALD---IHTSNWIYKHcfqss 786
Cdd:cd03218 113 KLEE---LLEEFH------ITHLrKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDpiaVQDIQKIIKI----- 178
|
170
....*....|....*.
gi 19115470 787 LMENRTVILVT-HNVH 801
Cdd:cd03218 179 LKDRGIGVLITdHNVR 194
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
631-804 |
5.17e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 52.81 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYNLPRSKGVSYVSQVPWLrNATIrdnilfdyPYIEERYK 710
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYL-DTTL--------PLTVNRFL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 711 KV---IQACGLLTDLQSFVASDLTEIGEKgvTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKHCFQSSL 787
Cdd:PRK09544 91 RLrpgTKKEDILPALKRVQAGHLIDAPMQ--KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRR 168
|
170
....*....|....*..
gi 19115470 788 MENRTVILVTHNVHLFM 804
Cdd:PRK09544 169 ELDCAVLMVSHDLHLVM 185
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
611-816 |
5.77e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 52.81 E-value: 5.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 611 IGFFNASLTWVSNPSPGDFCLRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYNLPrSKGVSYVSQVPWLR 690
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG-DIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 691 NATIRDNILFDYP---YIEERYKKVI----QACGLLTDLQSFVASDLTEI-------GEKG-VTLSGGQKQRIALARAVY 755
Cdd:PRK13643 81 PVRKKVGVVFQFPesqLFEETVLKDVafgpQNFGIPKEKAEKIAAEKLEMvgladefWEKSpFELSGGQMRRVAIAGILA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19115470 756 SPTSIVLMDDVFSALDIHTSNWIYKhCFQSSLMENRTVILVTHNVHLFMDSAAFIVTVKNG 816
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARIEMMQ-LFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKG 220
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
633-819 |
6.54e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 52.32 E-value: 6.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 633 DLNIvfPRNKLSIVIGPTGSGKSSLISALLGELSLNK--GSY----------------NLPRSKG-VSYVSQVPWLRNA- 692
Cdd:PRK09984 24 DLNI--HHGEMVALLGPSGSGKSTLLRHLSGLITGDKsaGSHiellgrtvqregrlarDIRKSRAnTGYIFQQFNLVNRl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 693 TIRDNILFDYPYIEERYKKVIQACGLLTDLQSFVAsdLTEIG------EKGVTLSGGQKQRIALARAVYSPTSIVLMDDV 766
Cdd:PRK09984 102 SVLENVLIGALGSTPFWRTCFSWFTREQKQRALQA--LTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVILADEP 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 19115470 767 FSALDIHTSNWIYKHCFQSSLMENRTVILVTHNVHLFMDSAAFIVTVKNGSAF 819
Cdd:PRK09984 180 IASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVF 232
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
632-772 |
6.60e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 52.68 E-value: 6.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 632 RDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYNLPRSKGVSYVSQVPWLR------NATIRDNILFD---- 701
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRigllaqNATTPGDITVQelva 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19115470 702 ---YPY--IEERYKKVIQAcgllTDLQSFVASDLTEIGEKGV-TLSGGQKQRIALARAVYSPTSIVLMDDVFSALDI 772
Cdd:PRK10253 104 rgrYPHqpLFTRWRKEDEE----AVTKAMQATGITHLADQSVdTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1212-1440 |
7.26e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 52.89 E-value: 7.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAAgpTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNAlRQRISF 1291
Cdd:PRK13537 8 IDFRNVEKRYGDK--LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1292 IPQ----DPILfsgTVRSNLDPFDELednFlneALKTSGASSMIMAHTDDQKpihitLDTHVASEGSNFSQGQKQVLALA 1367
Cdd:PRK13537 85 VPQfdnlDPDF---TVRENLLVFGRY---F---GLSAAAARALVPPLLEFAK-----LENKADAKVGELSGGMKRRLTLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1368 RAIVRRSKIIILDECTASVDDAMDQKIQKTLRE--AFGDATMLCI-----AHRLktivdYDKVMVLDKGVLVEYGPPAVL 1440
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRSllARGKTILLTThfmeeAERL-----CDRLCVIEEGRKIAEGAPHAL 225
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
626-772 |
9.83e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 52.10 E-value: 9.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 626 PGDFCLRdlnivfPRNKLSIvIGPTGSGKSSLISALLG-------ELSLNK-----GSYNLpRSKGVSYVSQVPWLR-NA 692
Cdd:PRK15112 31 PLSFTLR------EGQTLAI-IGENGSGKSTLAKMLAGmieptsgELLIDDhplhfGDYSY-RSQRIRMIFQDPSTSlNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 693 TIRDNILFDYPYI-------EERYKKVIQA---CGLLTDLQSFVASdlteigekgvTLSGGQKQRIALARAVYSPTSIVL 762
Cdd:PRK15112 103 RQRISQILDFPLRlntdlepEQREKQIIETlrqVGLLPDHASYYPH----------MLAPGQKQRLGLARALILRPKVII 172
|
170
....*....|
gi 19115470 763 MDDVFSALDI 772
Cdd:PRK15112 173 ADEALASLDM 182
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
631-799 |
1.04e-06 |
|
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: 51.13 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELslnkgsynLPRSkGVSYVSQVPwlrnATIRDNILFDY-PyiEER- 708
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGII--------LPDS-GEVLFDGKP----LDIAARNRIGYlP--EERg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 709 -YKK--VIQACGLLTDLQSFVASD-------------LTEIGEKGV-TLSGGQKQRIALARAVYSPTSIVLMDDVFSALD 771
Cdd:cd03269 81 lYPKmkVIDQLVYLAQLKGLKKEEarrridewlerleLSEYANKRVeELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
170 180
....*....|....*....|....*...
gi 19115470 772 IhTSNWIYKHCFQSSLMENRTVILVTHN 799
Cdd:cd03269 161 P-VNVELLKDVIRELARAGKTVILSTHQ 187
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
572-820 |
1.09e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.33 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 572 AYLMRQIVQIFVSIGRVSDFLNDPDEVDPVNTIEDTSQE--IGFFNASLTWVSNPspgdFCLRDLNIVFPRNKLSIVIGP 649
Cdd:PLN03073 468 ASLVQSRIKALDRLGHVDAVVNDPDYKFEFPTPDDRPGPpiISFSDASFGYPGGP----LLFKNLNFGIDLDSRIAMVGP 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 650 TGSGKSSLISALLGELSLNKGSynLPRSKGVSY------------VSQVPWLRNATIrdnilfdYPYIEERykkviqacG 717
Cdd:PLN03073 544 NGIGKSTILKLISGELQPSSGT--VFRSAKVRMavfsqhhvdgldLSSNPLLYMMRC-------FPGVPEQ--------K 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 718 LLTDLQSF-VASDLTEigEKGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIykhcFQSSLMENRTVILV 796
Cdd:PLN03073 607 LRAHLGSFgVTGNLAL--QPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEAL----IQGLVLFQGGVLMV 680
|
250 260
....*....|....*....|....
gi 19115470 797 THNVHLFMDSAAFIVTVKNGSAFP 820
Cdd:PLN03073 681 SHDEHLISGSVDELWVVSEGKVTP 704
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
636-802 |
1.10e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 51.32 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 636 IVFPRNKLSIvIGPTGSGKSSLISALLG-------ELSL--------NKGSYNLPRSKGVSYVSQ----VPWLrNAtiRD 696
Cdd:PRK10584 32 VVKRGETIAL-IGESGSGKSTLLAILAGlddgssgEVSLvgqplhqmDEEARAKLRAKHVGFVFQsfmlIPTL-NA--LE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 697 NIlfDYPYI---EERYKKVIQACGLLTDLQsfvasdlteIGEK----GVTLSGGQKQRIALARAVYSPTSIVLMDDVFSA 769
Cdd:PRK10584 108 NV--ELPALlrgESSRQSRNGAKALLEQLG---------LGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
170 180 190
....*....|....*....|....*....|...
gi 19115470 770 LDIHTSNWIYKHCFQSSLMENRTVILVTHNVHL 802
Cdd:PRK10584 177 LDRQTGDKIADLLFSLNREHGTTLILVTHDLQL 209
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1227-1429 |
1.41e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 52.96 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1227 TILKDVNLHINPSEKVAVVGRTGSGKSTL--GLTLLRFTHRISGEIYINGRETQSVNLnalrQRISFIPQDPILFSG-TV 1303
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLlnALAGRIQGNNFTGTILANNRKPTKQIL----KRTGFVTQDDILYPHlTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1304 RSNLDPFDELE-DNFLNEALKTSGASSMI--MAHTDDQKPIhitldthvasEGSNF----SQGQKQVLALARAIVRRSKI 1376
Cdd:PLN03211 158 RETLVFCSLLRlPKSLTKQEKILVAESVIseLGLTKCENTI----------IGNSFirgiSGGERKRVSIAHEMLINPSL 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115470 1377 IILDECTASVDDAMDQKIQKTLreafgdatmLCIAHRLKTIVD------------YDKVMVLDKG 1429
Cdd:PLN03211 228 LILDEPTSGLDATAAYRLVLTL---------GSLAQKGKTIVTsmhqpssrvyqmFDSVLVLSEG 283
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1219-1386 |
1.47e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.81 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1219 VSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQ-SVNLNALRQRISFIPQDpi 1297
Cdd:PRK10982 4 ISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQE-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1298 LFSGTVRSNLDpfdelednflNEALKTSGASSMIMAHT---DDQKPIHITLDTHV--ASEGSNFSQGQKQVLALARAIVR 1372
Cdd:PRK10982 82 LNLVLQRSVMD----------NMWLGRYPTKGMFVDQDkmyRDTKAIFDELDIDIdpRAKVATLSVSQMQMIEIAKAFSY 151
|
170
....*....|....
gi 19115470 1373 RSKIIILDECTASV 1386
Cdd:PRK10982 152 NAKIVIMDEPTSSL 165
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1207-1440 |
1.47e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 51.33 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1207 PKEGDIVFNHVSVSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALR 1286
Cdd:PRK10575 5 TNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1287 QRISFIPQD-PILFSGTVRS-----------NLDPFDELEDNFLNEALKTSGAssmimahtddqKPI-HITLDThvaseg 1353
Cdd:PRK10575 85 RKVAYLPQQlPAAEGMTVRElvaigrypwhgALGRFGAADREKVEEAISLVGL-----------KPLaHRLVDS------ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1354 snFSQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQK----IQKTLREAfgDATMLCIAHRLKTIVDY-DKVMVLDK 1428
Cdd:PRK10575 148 --LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDvlalVHRLSQER--GLTVIAVLHDINMAARYcDYLVALRG 223
|
250
....*....|..
gi 19115470 1429 GVLVEYGPPAVL 1440
Cdd:PRK10575 224 GEMIAQGTPAEL 235
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
645-798 |
1.51e-06 |
|
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: 50.43 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 645 IVIGPTGSGKSSL---ISALL----GELSLNKGSYNLPR---SKGVSYVSQVPWLRNA-TIRDNILFdypyieerykkvi 713
Cdd:TIGR01189 30 QVTGPNGIGKTTLlriLAGLLrpdsGEVRWNGTPLAEQRdepHENILYLGHLPGLKPElSALENLHF------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 714 qACGLLTDLQSFVASDLTEIGEKGVT------LSGGQKQRIALARAVYSPTSIVLMDDVFSALDIhTSNWIYKHCFQSSL 787
Cdd:TIGR01189 97 -WAAIHGGAQRTIEDALAAVGLTGFEdlpaaqLSAGQQRRLALARLWLSRRPLWILDEPTTALDK-AGVALLAGLLRAHL 174
|
170
....*....|.
gi 19115470 788 MENRTVILVTH 798
Cdd:TIGR01189 175 ARGGIVLLTTH 185
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1229-1400 |
1.58e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 51.17 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1229 LKDVNLHINPSEKVAVVGRTGSGKSTLgltLLRFTHRISGE------IYINGRETQ-----SVNLNALRQRISFIPQDPI 1297
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTL---LRHLSGLITGDksagshIELLGRTVQregrlARDIRKSRANTGYIFQQFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1298 LFSG-TVRSNL-------DPFDELEDNFLNEALKTSGASSMI---MAHTDDQKPihitldthvasegSNFSQGQKQVLAL 1366
Cdd:PRK09984 97 LVNRlSVLENVligalgsTPFWRTCFSWFTREQKQRALQALTrvgMVHFAHQRV-------------STLSGGQQQRVAI 163
|
170 180 190
....*....|....*....|....*....|....
gi 19115470 1367 ARAIVRRSKIIILDECTASVDDAMDQKIQKTLRE 1400
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRD 197
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
631-805 |
1.58e-06 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 50.86 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSL---ISALL----GELSLNKGSYNLPRSK--------GVSYvSQVPWLRNATIR 695
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLlrcINKLEeitsGDLIVDGLKVNDPKVDerlirqeaGMVF-QQFYLFPHLTAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 696 DNILFDyPyIEERYKKVIQACGLLTDLqsfvasdLTEIG--EKG----VTLSGGQKQRIALARAVYSPTSIVLMDDVFSA 769
Cdd:PRK09493 96 ENVMFG-P-LRVRGASKEEAEKQAREL-------LAKVGlaERAhhypSELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 19115470 770 LDIHTSNWIYKhCFQSSLMENRTVILVTHNVH---------LFMD 805
Cdd:PRK09493 167 LDPELRHEVLK-VMQDLAEEGMTMVIVTHEIGfaekvasrlIFID 210
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1229-1432 |
1.66e-06 |
|
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: 50.79 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1229 LKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGretqsvnLNALRQRISFIPQDPILFS--GTVRSN 1306
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-------LVPWKRRKKFLRRIGVVFGqkTQLWWD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1307 LDPFDELEdnfLNEA---LKTSGASSMIMAHTDDQKPIHItLDTHVasegSNFSQGQKQVLALARAIVRRSKIIILDECT 1383
Cdd:cd03267 110 LPVIDSFY---LLAAiydLPPARFKKRLDELSELLDLEEL-LDTPV----RQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 19115470 1384 ASVDDAMDQKIQKTLREAFGD--ATMLCIAHRLKTIVDY-DKVMVLDKGVLV 1432
Cdd:cd03267 182 IGLDVVAQENIRNFLKEYNRErgTTVLLTSHYMKDIEALaRRVLVIDKGRLL 233
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1227-1437 |
1.69e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 51.14 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1227 TILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNALRQRISFIPQDP-----ILFSG 1301
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNAttpgdITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1302 TVRSNLDPFDEL-------EDNFLNEALKTSGASSMIMAHTDdqkpihitldthvasegsNFSQGQKQVLALARAIVRRS 1374
Cdd:PRK10253 101 LVARGRYPHQPLftrwrkeDEEAVTKAMQATGITHLADQSVD------------------TLSGGQRQRAWIAMVLAQET 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115470 1375 KIIILDECTASVDDAMDQKIQKTLREAFGDA--TMLCIAHRLKTIVDY-DKVMVLDKGVLVEYGPP 1437
Cdd:PRK10253 163 AIMLLDEPTTWLDISHQIDLLELLSELNREKgyTLAAVLHDLNQACRYaSHLIALREGKIVAQGAP 228
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1228-1435 |
1.75e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.18 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1228 ILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLrfTHR----ISGEIYINGRETQSVNLNALRQRISFIP-QDPILFSG- 1301
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIA--GHPaykiLEGDILFKGESILDLEPEERAHLGIFLAfQYPIEIPGv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1302 -----------TVR-----SNLDPFDELEdnFLNEALKTSGASSMImahtddqkpihitLDTHVaSEGsnFSQGQKQVLA 1365
Cdd:CHL00131 100 snadflrlaynSKRkfqglPELDPLEFLE--IINEKLKLVGMDPSF-------------LSRNV-NEG--FSGGEKKRNE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19115470 1366 LARAIVRRSKIIILDECTASVD-DAMdqkiqKTLREAFG-----DATMLCIAH--RLKTIVDYDKVMVLDKGVLVEYG 1435
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLDiDAL-----KIIAEGINklmtsENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTG 234
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
643-827 |
1.94e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 51.27 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 643 LSIvIGPTGSGKSS---LISALL----------GELSLNKGSYNLPRSKGVsyVSQVP--WLRNATIRDNILF------- 700
Cdd:PRK13650 36 LSI-IGHNGSGKSTtvrLIDGLLeaesgqiiidGDLLTEENVWDIRHKIGM--VFQNPdnQFVGATVEDDVAFglenkgi 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 701 DYPYIEERYKKVIQacglLTDLQSFVASDLTEigekgvtLSGGQKQRIALARAVYSPTSIVLMDDVFSALD-------IH 773
Cdd:PRK13650 113 PHEEMKERVNEALE----LVGMQDFKEREPAR-------LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDpegrlelIK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 19115470 774 TSNWIYKHcfqsslmENRTVILVTHNvhlfMDSAAF---IVTVKNGSafpVTDKSSP 827
Cdd:PRK13650 182 TIKGIRDD-------YQMTVISITHD----LDEVALsdrVLVMKNGQ---VESTSTP 224
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1215-1438 |
2.18e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 50.70 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1215 NHVSVSysaagpTILKDVNLHINPSEKVAVVGRTGSGKSTLgLTLLRFTHRISGEIYINGRETQSVNLNAL-RQRISFIP 1293
Cdd:PRK03695 4 NDVAVS------TRLGPLSAEVRAGEILHLVGPNGAGKSTL-LARMAGLLPGSGSIQFAGQPLEAWSAAELaRHRAYLSQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1294 QDPILFSGTV-------RSNLDPFDELED--NFLNEALKtsgassmimahtddqkpihitLDTHVASEGSNFSQGQKQVL 1364
Cdd:PRK03695 77 QQTPPFAMPVfqyltlhQPDKTRTEAVASalNEVAEALG---------------------LDDKLGRSVNQLSGGEWQRV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1365 ALARAIVR-------RSKIIILDECTASVDDAMDQKIQKTLRE--AFGDATMLCiAHRL-KTIVDYDKVMVLDKGVLVEY 1434
Cdd:PRK03695 136 RLAAVVLQvwpdinpAGQLLLLDEPMNSLDVAQQAALDRLLSElcQQGIAVVMS-SHDLnHTLRHADRVWLLKQGKLLAS 214
|
....
gi 19115470 1435 GPPA 1438
Cdd:PRK03695 215 GRRD 218
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
646-827 |
2.72e-06 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 51.38 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 646 VIGPTGSGKSSLISALLGELSLNKGSYNLP-------RSKGVS-YVSQVPwlRNATIRDNilFDYPYIEE--------RY 709
Cdd:PRK09536 34 LVGPNGAGKTTLLRAINGTLTPTAGTVLVAgddvealSARAASrRVASVP--QDTSLSFE--FDVRQVVEmgrtphrsRF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 710 -------KKVIQACGLLTDLQSFVASDLTeigekgvTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHtsnwiykHC 782
Cdd:PRK09536 110 dtwtetdRAAVERAMERTGVAQFADRPVT-------SLSGGERQRVLLARALAQATPVLLLDEPTASLDIN-------HQ 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 19115470 783 FQS-----SLMEN-RTVILVTHNVHLFMDSAAFIVTVKNGSafpVTDKSSP 827
Cdd:PRK09536 176 VRTlelvrRLVDDgKTAVAAIHDLDLAARYCDELVLLADGR---VRAAGPP 223
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1216-1400 |
3.23e-06 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 50.03 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1216 HVSVSYSaaGPTILKDVNLHINPSEKVAVVGRTGSGKSTL-----GLtllrfthrI---SGEIYINGRE--TQSVNLNAl 1285
Cdd:COG1137 8 NLVKSYG--KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTfymivGL--------VkpdSGRIFLDGEDitHLPMHKRA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1286 RQRISFIPQDPILFSG-TVrsnldpfdelEDNflnealktsgassmIMA----HTDDQKPIHITLD--------THVA-S 1351
Cdd:COG1137 77 RLGIGYLPQEASIFRKlTV----------EDN--------------ILAvlelRKLSKKEREERLEelleefgiTHLRkS 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 19115470 1352 EGSNFSQGQKQVLALARAIVRRSKIIILDECTASVD-----DAmdQKIQKTLRE 1400
Cdd:COG1137 133 KAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDpiavaDI--QKIIRHLKE 184
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
630-798 |
3.58e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 49.42 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 630 CLRDLNIVFPRNKLSI-------VIGPTGSGKSSL---ISALL----GELSLNkgsyNLPRSK-GVSYVSQVPWLRNAT- 693
Cdd:PRK13538 9 CERDERILFSGLSFTLnagelvqIEGPNGAGKTSLlriLAGLArpdaGEVLWQ----GEPIRRqRDEYHQDLLYLGHQPg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 694 IRD------NILFdypyieerykkviqACGLLTDLQSFVASD-LTEIGEKGV------TLSGGQKQRIALARAVYSPTSI 760
Cdd:PRK13538 85 IKTeltaleNLRF--------------YQRLHGPGDDEALWEaLAQVGLAGFedvpvrQLSAGQQRRVALARLWLTRAPL 150
|
170 180 190
....*....|....*....|....*....|....*...
gi 19115470 761 VLMDDVFSALDIHTSNWIYKHcFQSSLMENRTVILVTH 798
Cdd:PRK13538 151 WILDEPFTAIDKQGVARLEAL-LAQHAEQGGMVILTTH 187
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
642-816 |
3.93e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 49.49 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 642 KLSIVIGPTGSGKSSLISALLG--ELSLNK---GSYNLPRSKGvsyvSQVPWLRNATirDNILFDYPYIEER--YKKV-- 712
Cdd:PRK10908 29 EMAFLTGHSGAGKSTLLKLICGieRPSAGKiwfSGHDITRLKN----REVPFLRRQI--GMIFQDHHLLMDRtvYDNVai 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 713 --IQACGLLTDLQSFVASDLTEIG--EKG----VTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKhcfq 784
Cdd:PRK10908 103 plIIAGASGDDIRRRVSAALDKVGllDKAknfpIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILR---- 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 19115470 785 ssLME--NR---TVILVTHNVHLFMDSAAFIVTVKNG 816
Cdd:PRK10908 179 --LFEefNRvgvTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
631-799 |
4.05e-06 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 49.69 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKlSI-VIGPTGSGKSSLISALLGELSLNKGSYnlpRSKGvsyvsQVPWL--------RNATIRDNILF- 700
Cdd:COG1134 42 LKDVSFEVERGE-SVgIIGRNGAGKSTLLKLIAGILEPTSGRV---EVNG-----RVSALlelgagfhPELTGRENIYLn 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 701 ------DYPYIEERYKKVIqacglltdlqsfvasDLTEIGE------KgvTLSGGQKQRIALARAVYSPTSIVLMDDVFS 768
Cdd:COG1134 113 grllglSRKEIDEKFDEIV---------------EFAELGDfidqpvK--TYSSGMRARLAFAVATAVDPDILLVDEVLA 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 19115470 769 ALDIHtsnwiykhcFQ-------SSLMEN-RTVILVTHN 799
Cdd:COG1134 176 VGDAA---------FQkkclariRELRESgRTVIFVSHS 205
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1212-1443 |
5.59e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 50.23 E-value: 5.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAAGPTIlKDVNLHINPSEKVAVVGRTGSGKSTL-----GLtllrftHRI-SGEIYINGRetqsvNLNAL 1285
Cdd:PRK11650 4 LKLQAVRKSYDGKTQVI-KGIDLDVADGEFIVLVGPSGCGKSTLlrmvaGL------ERItSGEIWIGGR-----VVNEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1286 --RQR-ISFIPQDPILFSG-TVRSNLD--------PFDELEDNfLNEALKTSGASSMImahtdDQKPihitldthvaseg 1353
Cdd:PRK11650 72 epADRdIAMVFQNYALYPHmSVRENMAyglkirgmPKAEIEER-VAEAARILELEPLL-----DRKP------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1354 SNFSQGQKQVLALARAIVRRSKIIILDECTASVDD----AMDQKIQKTLReafgdatmlciahRLKTIVDY--------- 1420
Cdd:PRK11650 133 RELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAklrvQMRLEIQRLHR-------------RLKTTSLYvthdqveam 199
|
250 260
....*....|....*....|....*.
gi 19115470 1421 ---DKVMVLDKGVLVEYGPPAVLYHN 1443
Cdd:PRK11650 200 tlaDRVVVMNGGVAEQIGTPVEVYEK 225
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
631-817 |
5.79e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 49.80 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYnLPRS------------KGVSYVSQVP--WLRNATIRD 696
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSV-LIRGepitkenirevrKFVGLVFQNPddQIFSPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 697 NILF-------DYPYIEERYKKVIQACGlLTDLQSFVASDlteigekgvtLSGGQKQRIALARAVYSPTSIVLMDDVFSA 769
Cdd:PRK13652 99 DIAFgpinlglDEETVAHRVSSALHMLG-LEELRDRVPHH----------LSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 19115470 770 LDIHTSNWIYKhcFQSSLMEN--RTVILVTHNVHLFMDSAAFIVTVKNGS 817
Cdd:PRK13652 168 LDPQGVKELID--FLNDLPETygMTVIFSTHQLDLVPEMADYIYVMDKGR 215
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
740-798 |
6.15e-06 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 50.33 E-value: 6.15e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19115470 740 LSGGQKQRIALARAVYSPTSIVLMDDVFSALDihtsnwiYK--HCFQSSLME-----NRTVILVTH 798
Cdd:PRK09452 145 LSGGQQQRVAIARAVVNKPKVLLLDESLSALD-------YKlrKQMQNELKAlqrklGITFVFVTH 203
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
633-827 |
6.60e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 49.38 E-value: 6.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 633 DLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSY-----NLP---RS------KGVSYVSQvpwlRNATIRDNI 698
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEIlfdgeNIPamsRSrlytvrKRMSMLFQ----SGALFTDMN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 699 LFD---YPYIEE-RYKKVIqacglltdLQSFVASDLTEIGEKGVT------LSGGQKQRIALARAVYSPTSIVLMDDVFS 768
Cdd:PRK11831 101 VFDnvaYPLREHtQLPAPL--------LHSTVMMKLEAVGLRGAAklmpseLSGGMARRAALARAIALEPDLIMFDEPFV 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115470 769 ALDIHTSNWIYKHCFQSSLMENRTVILVTHNVHLFMDSA--AFIVT----VKNGSAFPVTDKSSP 827
Cdd:PRK11831 173 GQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIAdhAYIVAdkkiVAHGSAQALQANPDP 237
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
740-801 |
6.77e-06 |
|
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: 47.81 E-value: 6.77e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19115470 740 LSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKhcfqssLMEN-----RTVILVTHNVH 801
Cdd:cd03216 83 LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK------VIRRlraqgVAVIFISHRLD 143
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1227-1436 |
7.12e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.88 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1227 TILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTH----RISGEIYINGReTQSVNLNALRQRISFIPQDPILF-SG 1301
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDGI-TPEEIKKHYRGDVVYNAETDVHFpHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1302 TVRSNLDpfdelednfLNEALKTSGASSMIMAHTDDQKPI----------HITLDTHVaseGSNF----SQGQKQVLALA 1367
Cdd:TIGR00956 154 TVGETLD---------FAARCKTPQNRPDGVSREEYAKHIadvymatyglSHTRNTKV---GNDFvrgvSGGERKRVSIA 221
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19115470 1368 RAIVRRSKIIILDECTASVDDAMDQKIQKTLREA--FGDATMLCIAHRL--KTIVDYDKVMVLDKGVLVEYGP 1436
Cdd:TIGR00956 222 EASLGGAKIQCWDNATRGLDSATALEFIRALKTSanILDTTPLVAIYQCsqDAYELFDKVIVLYEGYQIYFGP 294
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
631-802 |
7.52e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 49.04 E-value: 7.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISaLLGELslnkgsyNLPRSKGVSY----VSQVPWLRNATIRDNIL-FDYPY- 704
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLH-LLGGL-------DTPTSGDVIFngqpMSKLSSAAKAELRNQKLgFIYQFh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 705 -------------------------IEERYKKVIQACGLLTDLQsfvasdlteigEKGVTLSGGQKQRIALARAVYSPTS 759
Cdd:PRK11629 97 hllpdftalenvamplligkkkpaeINSRALEMLAAVGLEHRAN-----------HRPSELSGGERQRVAIARALVNNPR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 19115470 760 IVLMDDVFSALDIHTSNWIYKHCFQSSLMENRTVILVTHNVHL 802
Cdd:PRK11629 166 LVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQL 208
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1219-1429 |
7.74e-06 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 48.01 E-value: 7.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1219 VSYSAAGPT----ILKDVNLHINPSEKVAVVGRTGSGKSTLgLTLL---RFTHRISGEIYINGREtqsvNLNALRQRISF 1291
Cdd:cd03232 9 LNYTVPVKGgkrqLLNNISGYVKPGTLTALMGESGAGKTTL-LDVLagrKTAGVITGEILINGRP----LDKNFQRSTGY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1292 IPQDPILFSG-TVRsnldpfdelednflnEALKTSGASSMImahtddqkpihitldthvasegsnfSQGQKQVLALARAI 1370
Cdd:cd03232 84 VEQQDVHSPNlTVR---------------EALRFSALLRGL-------------------------SVEQRKRLTIGVEL 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19115470 1371 VRRSKIIILDECTASVDDAMDQKIQKTLRE-AFGDATMLCIAHR-LKTIVDY-DKVMVLDKG 1429
Cdd:cd03232 124 AAKPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQpSASIFEKfDRLLLLKRG 185
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
646-807 |
7.96e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 49.42 E-value: 7.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 646 VIGPTGSGKSSLISALLGELSLNKGSYNL---------PRSKgvSYVSQVPWLRNA----TIRDNILfdypyIEERY--K 710
Cdd:PRK13537 38 LLGPNGAGKTTTLRMLLGLTHPDAGSISLcgepvpsraRHAR--QRVGVVPQFDNLdpdfTVRENLL-----VFGRYfgL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 711 KVIQACGLLTDLQSFvaSDLTEIGEKGVT-LSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKHcFQSSLME 789
Cdd:PRK13537 111 SAAAARALVPPLLEF--AKLENKADAKVGeLSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWER-LRSLLAR 187
|
170
....*....|....*...
gi 19115470 790 NRTVILVTHnvhlFMDSA 807
Cdd:PRK13537 188 GKTILLTTH----FMEEA 201
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
646-798 |
8.12e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 49.20 E-value: 8.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 646 VIGPTGSGKSSLISAL-------LGELSLNKGSYNLPRSK-GVSYVSQVPWLRNATIRDNILFDY-------PYIEERYK 710
Cdd:PRK10619 36 IIGSSGSGKSTFLRCInflekpsEGSIVVNGQTINLVRDKdGQLKVADKNQLRLLRTRLTMVFQHfnlwshmTVLENVME 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 711 KVIQACGLL-TDLQSFVASDLTEIGEKG-------VTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKhC 782
Cdd:PRK10619 116 APIQVLGLSkQEARERAVKYLAKVGIDEraqgkypVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR-I 194
|
170
....*....|....*.
gi 19115470 783 FQSSLMENRTVILVTH 798
Cdd:PRK10619 195 MQQLAEEGKTMVVVTH 210
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
627-771 |
1.00e-05 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 49.45 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 627 GDFCLRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYNLprsKGVSYVSQVPWLR--NATIRDNILFDYPY 704
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML---DGVDLSHVPPYQRpiNMMFQSYALFPHMT 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19115470 705 IEERYkkviqACGLLTD------LQSFVASDLTEI------GEKGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALD 771
Cdd:PRK11607 108 VEQNI-----AFGLKQDklpkaeIASRVNEMLGLVhmqefaKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
646-818 |
1.14e-05 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 48.59 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 646 VIGPTGSGKSSLISAL------------LGELSLNkGSYNLPRSKG--------VSYVSQ----VPwlrNATIRDNILfD 701
Cdd:PRK11264 34 IIGPSGSGKTTLLRCInlleqpeagtirVGDITID-TARSLSQQKGlirqlrqhVGFVFQnfnlFP---HRTVLENII-E 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 702 YPYIEERYKKViQACGLLTDLqsfvasdLTEIGEKGVT------LSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTS 775
Cdd:PRK11264 109 GPVIVKGEPKE-EATARAREL-------LAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELV 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 19115470 776 NWIYkHCFQSSLMENRTVILVTH---------NVHLFMDSAafiVTVKNGSA 818
Cdd:PRK11264 181 GEVL-NTIRQLAQEKRTMVIVTHemsfardvaDRAIFMDQG---RIVEQGPA 228
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
627-811 |
1.19e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 48.83 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 627 GDFCLRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYnLPRSKGVSYVSQVPWLRNATirdNILFDYPYIE 706
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKV-LVSGIDTGDFSKLQGIRKLV---GIVFQNPETQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 707 ERYKKVIQ--------ACGLLTDLQSFVASDLTEIG-EK-----GVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDI 772
Cdd:PRK13644 90 FVGRTVEEdlafgpenLCLPPIEIRKRVDRALAEIGlEKyrhrsPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 19115470 773 HTSNWIYKHCfqSSLMEN-RTVILVTHNVHLFMDSAAFIV 811
Cdd:PRK13644 170 DSGIAVLERI--KKLHEKgKTIVYITHNLEELHDADRIIV 207
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
740-798 |
1.21e-05 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 49.03 E-value: 1.21e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115470 740 LSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKhcfqssLME--NR----TVILVTH 798
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILE------LLKdiNRelglTIVLITH 199
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
631-816 |
1.21e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 48.93 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYN-------------------------LPRSKGVSYVSQ 685
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeknkkktkekekvleklviqKTRFKKIKKIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 686 VP------------WLRNATIRDNILF-------DYPYIEERYKKVIQACGLltdlqsfvasDLTEIGEKGVTLSGGQKQ 746
Cdd:PRK13651 103 IRrrvgvvfqfaeyQLFEQTIEKDIIFgpvsmgvSKEEAKKRAAKYIELVGL----------DESYLQRSPFELSGGQKR 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 747 RIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKhCFQSSLMENRTVILVTHNVHLFMDSAAFIVTVKNG 816
Cdd:PRK13651 173 RVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE-IFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1212-1442 |
1.83e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 47.80 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAAgpTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIyingRETQSVNLNALRQRISF 1291
Cdd:PRK09544 5 VSLENVSVSFGQR--RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI----KRNGKLRIGYVPQKLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1292 IPQDPILFSGTVRsnLDPFDELEDnfLNEALKTSGASSMImahtddQKPIHitldthvasegsNFSQGQKQVLALARAIV 1371
Cdd:PRK09544 79 DTTLPLTVNRFLR--LRPGTKKED--ILPALKRVQAGHLI------DAPMQ------------KLSGGETQRVLLARALL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1372 RRSKIIILDECTASVD--------DAMDQkiqktLREAFGDAtMLCIAHRLKTIV-DYDKVMVLDKGVLVEYGPPAVLYH 1442
Cdd:PRK09544 137 NRPQLLVLDEPTQGVDvngqvalyDLIDQ-----LRRELDCA-VLMVSHDLHLVMaKTDEVLCLNHHICCSGTPEVVSLH 210
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1238-1419 |
1.85e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 46.21 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1238 PSEKVAVVGRTGSGKSTLGLTLLRFTHRISGE-IYINGRETQSVNLNALRQRIsfipqdpilfsgtvrsnldpfdeledn 1316
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1317 flnealktsgassmimahtddqkpihitldthVASEGSNFSQGQKQVLALARAIVRRSKIIILDECTASVDDAMDQKIQK 1396
Cdd:smart00382 54 --------------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLL 101
|
170 180 190
....*....|....*....|....*....|
gi 19115470 1397 TLR-------EAFGDATMLCIAHRLKTIVD 1419
Cdd:smart00382 102 LEElrlllllKSEKNLTVILTTNDEKDLGP 131
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1212-1387 |
2.21e-05 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 48.78 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVF--NHVSVSYsAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLgltlLRFTHRISGEIyiNGRETQSVNLNalrqrI 1289
Cdd:TIGR03719 3 YIYtmNRVSKVV-PPKKEILKDISLSFFPGAKIGVLGLNGAGKSTL----LRIMAGVDKDF--NGEARPQPGIK-----V 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1290 SFIPQDPIL-FSGTVRSN-----------LDPFDELEDNF------LNEALKTSGASSMIMAHTD----DQKpIHITLDT 1347
Cdd:TIGR03719 71 GYLPQEPQLdPTKTVRENveegvaeikdaLDRFNEISAKYaepdadFDKLAAEQAELQEIIDAADawdlDSQ-LEIAMDA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 19115470 1348 HVASEG----SNFSQGQKQVLALARAIVRRSKIIILDECTASVD 1387
Cdd:TIGR03719 150 LRCPPWdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
740-771 |
3.66e-05 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 46.91 E-value: 3.66e-05
10 20 30
....*....|....*....|....*....|...
gi 19115470 740 LSGGQKQRIALARA-VYSPtSIVLMDDVFSALD 771
Cdd:COG1126 137 LSGGQQQRVAIARAlAMEP-KVMLFDEPTSALD 168
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
648-771 |
4.49e-05 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 46.56 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 648 GPTGSGKSSLISALLGELSLNKGSY--------NLP---RS-KGVSYVSQVPWL-RNATIRDNIL----FDYPYIEERYK 710
Cdd:COG1137 36 GPNGAGKTTTFYMIVGLVKPDSGRIfldgeditHLPmhkRArLGIGYLPQEASIfRKLTVEDNILavleLRKLSKKEREE 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19115470 711 KVIQacgLLTDLQsfvasdLTEIGE-KGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALD 771
Cdd:COG1137 116 RLEE---LLEEFG------ITHLRKsKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1236-1439 |
4.73e-05 |
|
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: 46.63 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1236 INPSEKVAVVGRTGSGKSTlgltllrFTHRISGEIYINGRETQSvnlnaLRQRISFIPQDPIL-FSGTVRSnldpfdele 1314
Cdd:cd03237 22 ISESEVIGILGPNGIGKTT-------FIKMLAGVLKPDEGDIEI-----ELDTVSYKPQYIKAdYEGTVRD--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1315 dnFLNEALKTSGASSMImaHTDDQKPIHI--TLDTHVasegSNFSQGQKQVLALARAIVRRSKIIILDECTASVDD---A 1389
Cdd:cd03237 81 --LLSSITKDFYTHPYF--KTEIAKPLQIeqILDREV----PELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 19115470 1390 MDQKIQKTLREAfGDATMLCIAHRLKTIvDY--DKVMVLDkgvlveyGPPAV 1439
Cdd:cd03237 153 MASKVIRRFAEN-NEKTAFVVEHDIIMI-DYlaDRLIVFE-------GEPSV 195
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
627-800 |
5.04e-05 |
|
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: 46.63 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 627 GDFCLRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYNLPRSKgVSYVSQvpwlrnatirdnilfdypYIE 706
Cdd:cd03237 11 GEFTLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-VSYKPQ------------------YIK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 707 ERYKKVIQAcgLLTDL------QSFVASD------LTEIGEKGV-TLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIH 773
Cdd:cd03237 72 ADYEGTVRD--LLSSItkdfytHPYFKTEiakplqIEQILDREVpELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE 149
|
170 180
....*....|....*....|....*..
gi 19115470 774 TSNWIYKHCFQSSLMENRTVILVTHNV 800
Cdd:cd03237 150 QRLMASKVIRRFAENNEKTAFVVEHDI 176
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
646-801 |
5.68e-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: 46.23 E-value: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 646 VIGPTGSGKSSLISALLGEL---SLN--------KGSYNLP--RSKgVSYVS---QVPWLRNATIRDNIL---FD----Y 702
Cdd:COG1119 34 ILGPNGAGKSTLLSLITGDLpptYGNdvrlfgerRGGEDVWelRKR-IGLVSpalQLRFPRDETVLDVVLsgfFDsiglY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 703 PYIEERYKKviQACGLLTDLqsfvasDLTEIGEKGV-TLSGGQKQRIALARA-VYSPTSIVLmDDVFSALDIHtsnwiYK 780
Cdd:COG1119 113 REPTDEQRE--RARELLELL------GLAHLADRPFgTLSQGEQRRVLIARAlVKDPELLIL-DEPTAGLDLG-----AR 178
|
170 180
....*....|....*....|....*.
gi 19115470 781 HCFQSSL-----MENRTVILVTHNVH 801
Cdd:COG1119 179 ELLLALLdklaaEGAPTLVLVTHHVE 204
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
646-808 |
8.03e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 46.24 E-value: 8.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 646 VIGPTGSGKSS---LISALL----------GELSLNKGSYNLPRSKGVSYVSQVPWLRNATIRDNILFDYPYI----EER 708
Cdd:PRK13642 38 IIGQNGSGKSTtarLIDGLFeefegkvkidGELLTAENVWNLRRKIGMVFQNPDNQFVGATVEDDVAFGMENQgiprEEM 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 709 YKKVIQACgLLTDLQSFVASDLTEigekgvtLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKHCFQSSLM 788
Cdd:PRK13642 118 IKRVDEAL-LAVNMLDFKTREPAR-------LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEK 189
|
170 180
....*....|....*....|
gi 19115470 789 ENRTVILVTHNvhlfMDSAA 808
Cdd:PRK13642 190 YQLTVLSITHD----LDEAA 205
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1210-1387 |
1.37e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.48 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1210 GDIVFNHVSVSYSAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYIngretqsvnlnALRQRI 1289
Cdd:PRK11147 316 GKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-----------GTKLEV 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1290 SFIPQdpilfsgtVRSNLDPFDELEDNfLNEALKTsgassmIMAHTDDQkpihitldtHVASEGSNF------------- 1356
Cdd:PRK11147 385 AYFDQ--------HRAELDPEKTVMDN-LAEGKQE------VMVNGRPR---------HVLGYLQDFlfhpkramtpvka 440
|
170 180 190
....*....|....*....|....*....|..
gi 19115470 1357 -SQGQKQVLALARAIVRRSKIIILDECTASVD 1387
Cdd:PRK11147 441 lSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
630-810 |
2.26e-04 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 43.45 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 630 CLRDLNIVFPRNKLSIVIGPTGSGKSSLISAL---LGE--LSLNKGSYNLPRSKGVSyvsqvPWLRNATIRdnILFDypy 704
Cdd:cd03239 11 SYRDETVVGGSNSFNAIVGPNGSGKSNIVDAIcfvLGGkaAKLRRGSLLFLAGGGVK-----AGINSASVE--ITFD--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 705 ieERYKKVIQacglltdlqsfvasdlteiGEKGVTLSGGQKQRIALARAV----YSPTSIVLMDDVFSALDI-HTSNwiy 779
Cdd:cd03239 81 --KSYFLVLQ-------------------GKVEQILSGGEKSLSALALIFalqeIKPSPFYVLDEIDAALDPtNRRR--- 136
|
170 180 190
....*....|....*....|....*....|....*
gi 19115470 780 khcFQSSLMENRT----VILVTHNVHLFMDSAAFI 810
Cdd:cd03239 137 ---VSDMIKEMAKhtsqFIVITLKKEMFENADKLI 168
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1215-1398 |
2.40e-04 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 44.69 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1215 NHVSVSYsaAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLgLTLLR-FTHRISGEIYINGRETqsvnlnalrqrisfip 1293
Cdd:PRK11248 5 SHLYADY--GGKPALEDINLTLESGELLVVLGPSGCGKTTL-LNLIAgFVPYQHGSITLDGKPV---------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1294 QDPILFSGTVRSN--LDPFDELEDNfLNEALKTSGASSMIMAHTDDQKPIHITLDTHVASEGSNFSQGQKQVLALARAIV 1371
Cdd:PRK11248 66 EGPGAERGVVFQNegLLPWRNVQDN-VAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALA 144
|
170 180
....*....|....*....|....*..
gi 19115470 1372 RRSKIIILDECTASVDDAMDQKIQKTL 1398
Cdd:PRK11248 145 ANPQLLLLDEPFGALDAFTREQMQTLL 171
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
640-667 |
2.46e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 43.93 E-value: 2.46e-04
10 20
....*....|....*....|....*...
gi 19115470 640 RNKLSIVIGPTGSGKSSLISALLGELSL 667
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLPELVL 111
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1207-1296 |
2.51e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 45.40 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1207 PKEGDIVF--NHVSVSySAAGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRETQSVNLNA 1284
Cdd:COG3845 251 AEPGEVVLevENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRE 329
|
90
....*....|...
gi 19115470 1285 LRQR-ISFIPQDP 1296
Cdd:COG3845 330 RRRLgVAYIPEDR 342
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
632-816 |
2.59e-04 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 45.02 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 632 RDLNIVFPRNKLSIVIGPTGSGKSSL---ISAL----LGELSLNKGSYN-LPRSK-GVSYVSQ----VPWLrnaTIRDNI 698
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLlrmIAGLeditSGDLFIGEKRMNdVPPAErGVGMVFQsyalYPHL---SVAENM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 699 LFDYPYI----EERYKKVIQACGLLTdlqsfvASDLTEIGEKgvTLSGGQKQRIALARAVYSPTSIVLMDDVFSALD--- 771
Cdd:PRK11000 97 SFGLKLAgakkEEINQRVNQVAEVLQ------LAHLLDRKPK--ALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaal 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 19115470 772 -----IHTSNwiykhcFQSSLmeNRTVILVTHNVHLFMDSAAFIVTVKNG 816
Cdd:PRK11000 169 rvqmrIEISR------LHKRL--GRTMIYVTHDQVEAMTLADKIVVLDAG 210
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
740-816 |
3.03e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 45.49 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 740 LSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSN---WIYKHCFQsslmENRTVILVTHNVHLfMDSAAFIVTVKNG 816
Cdd:PRK10535 145 LSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEevmAILHQLRD----RGHTVIIVTHDPQV-AAQAERVIEIRDG 219
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
634-807 |
3.78e-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: 45.39 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 634 LNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYNLPRSKGVSYVSQVPWLRNATIRDNILFDYPYIEERYKKVI 713
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYA 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 714 QACGLLTD-LQSFVASDLTEIG------EKGVTLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKHCFQss 786
Cdd:TIGR01257 1029 QLKGRSWEeAQLEMEAMLEDTGlhhkrnEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLK-- 1106
|
170 180
....*....|....*....|.
gi 19115470 787 LMENRTVILVTHNvhlfMDSA 807
Cdd:TIGR01257 1107 YRSGRTIIMSTHH----MDEA 1123
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1212-1434 |
3.98e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.94 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1212 IVFNHVSVSYSAAgPtILKDVNLHINPSEKVAVVGRTGSGKStlglTLLRFthrISGEIYIN-GRETQSVNLnalrqRIS 1290
Cdd:PRK11147 4 ISIHGAWLSFSDA-P-LLDNAELHIEDNERVCLVGRNGAGKS----TLMKI---LNGEVLLDdGRIIYEQDL-----IVA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1291 FIPQDPIL-FSGTVrsnldpFDELEDNF--LNEALKTSGASSMIMAHTDDQK------PIHITLDTHVA----------- 1350
Cdd:PRK11147 70 RLQQDPPRnVEGTV------YDFVAEGIeeQAEYLKRYHDISHLVETDPSEKnlnelaKLQEQLDHHNLwqlenrinevl 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1351 --------SEGSNFSQGQKQVLALARAIVRRSKIIILDECTASVD-DAMD--QKIQKTLReafgdATMLCIAH------R 1413
Cdd:PRK11147 144 aqlgldpdAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDiETIEwlEGFLKTFQ-----GSIIFISHdrsfirN 218
|
250 260
....*....|....*....|..
gi 19115470 1414 LKT-IVDydkvmvLDKGVLVEY 1434
Cdd:PRK11147 219 MATrIVD------LDRGKLVSY 234
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
631-657 |
4.52e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.02 E-value: 4.52e-04
10 20
....*....|....*....|....*...
gi 19115470 631 LRDLNIVFPRNKLsIVI-GPTGSGKSSL 657
Cdd:COG0178 16 LKNIDVDIPRNKL-VVItGLSGSGKSSL 42
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
891-1104 |
4.58e-04 |
|
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: 44.00 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 891 FGSGfyVAAVLLFFVTTQATSILIDLWVAFWTNSSVNSpDVNNNKFLFVY---GTMLLAYSLLDFLRTVSyDRgawwASR 967
Cdd:cd18577 9 IAAG--AALPLMTIVFGDLFDAFTDFGSGESSPDEFLD-DVNKYALYFVYlgiGSFVLSYIQTACWTITG-ER----QAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 968 KLHDSMLESVFGTFASWFDKTPTGRIVNRFAKDIRSIDMNLS---GWLFFSINCFlsVAGGILS----------VSSAMP 1034
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGeklGLLIQSLSTF--IAGFIIAfiyswkltlvLLATLP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1035 IFMIpavivclAGYYFGLLYTRAQvgvKRLISIYTSPIfSLLGESIVGVSVIRAFNRQTIFKQMFSERLD 1104
Cdd:cd18577 159 LIAI-------VGGIMGKLLSKYT---KKEQEAYAKAG-SIAEEALSSIRTVKAFGGEEKEIKRYSKALE 217
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
651-797 |
4.61e-04 |
|
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: 42.80 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 651 GSGKSSLISALLGELSLNKGSYNL------------PRSKGVSYVSqvpwlrnatirdnilfdypyiEERYKKviqacGL 718
Cdd:cd03215 36 GNGQTELAEALFGLRPPASGEITLdgkpvtrrsprdAIRAGIAYVP---------------------EDRKRE-----GL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 719 LTDL---QSFVASDLteigekgvtLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKHCFQSSlMENRTVIL 795
Cdd:cd03215 90 VLDLsvaENIALSSL---------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELA-DAGKAVLL 159
|
..
gi 19115470 796 VT 797
Cdd:cd03215 160 IS 161
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1230-1433 |
5.71e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 44.39 E-value: 5.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1230 KDVNLHINPSEKVAVVGRTGSGKSTLGLTLLRFTHRISGEIYINGRE-TQSVNLNALRQRISFIPQdpilfsgTVRSN-- 1306
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDiSPRSPLDAVKKGMAYITE-------SRRDNgf 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1307 LDPFDELEDNFLNEALKTSG-ASSMIMAHTDDQKPI----HITLDTHVASEGSN---FSQGQKQVLALARAIVRRSKIII 1378
Cdd:PRK09700 353 FPNFSIAQNMAISRSLKDGGyKGAMGLFHEVDEQRTaenqRELLALKCHSVNQNiteLSGGNQQKVLISKWLCCCPEVII 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 19115470 1379 LDECTASVDDAMDQKIQKTLREAFGDA-TMLCIAHRLKTIVDY-DKVMVLDKGVLVE 1433
Cdd:PRK09700 433 FDEPTRGIDVGAKAEIYKVMRQLADDGkVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
631-771 |
5.85e-04 |
|
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: 42.97 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKGSYNLprsKGVSYVSQVPWLR-------------NATIRDN 697
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITF---DGKSYQKNIEALRrigalieapgfypNLTAREN 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115470 698 ILFDYPYIEERYKKVIQACGLLtdlqsfvasDLTEIGEKGV-TLSGGQKQRIALARAVYSPTSIVLMDDVFSALD 771
Cdd:cd03268 93 LRLLARLLGIRKKRIDEVLDVV---------GLKDSAKKKVkGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
301-594 |
7.92e-04 |
|
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: 43.32 E-value: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 301 VSSFMVSVCQFLSPIALNRLLKHL-ESPSSSSVNPLVWIVLLLTgpFLTSLFTQFYLFMSTRYLARSYTTLVQQIYNKVI 379
Cdd:cd18557 3 LFLLISSAAQLLLPYLIGRLIDTIiKGGDLDVLNELALILLAIY--LLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 380 R---SRFVQNKSGDSkvgrsNNLISTDVDDIGE-IREFIHIIVRAPVEIAGSIYLLQkLLGWSayvgLALTVLtCSVPIV 455
Cdd:cd18557 81 RqeiAFFDKHKTGEL-----TSRLSSDTSVLQSaVTDNLSQLLRNILQVIGGLIILF-ILSWK----LTLVLL-LVIPLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 456 L--GPLVAKLTLRANRATDSRI----ELMSELLQSIRITKFFGWELPMLDRVKQrrqvELNRTWKLLLMEICIQVLVESl 529
Cdd:cd18557 150 LiaSKIYGRYIRKLSKEVQDALakagQVAEESLSNIRTVRSFSAEEKEIRRYSE----ALDRSYRLARKKALANALFQG- 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19115470 530 pvFSMFATFVVFTTIM--GQTITPSIAFTSISLFSFirtqfswIAYLMrqivQIFVSIGRVSDFLND 594
Cdd:cd18557 225 --ITSLLIYLSLLLVLwyGGYLVLSGQLTVGELTSF-------ILYTI----MVASSVGGLSSLLAD 278
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
631-802 |
9.02e-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: 42.99 E-value: 9.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSLIS-----ALLGELSLNKGSY-NLPRSKG------VSYVSQVPWLRN-----AT 693
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdtlypALARRLHLKKEQPgNHDRIEGlehidkVIVIDQSPIGRTprsnpAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 694 -------IRDniLF---------DYPYIEERYK-KVI-------------------QACGLLTDLQSfVASDLTEIGEKG 737
Cdd:cd03271 91 ytgvfdeIRE--LFcevckgkryNRETLEVRYKgKSIadvldmtveealeffenipKIARKLQTLCD-VGLGYIKLGQPA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19115470 738 VTLSGGQKQRIALA---------RAVY---SPTSIVLMDDVFSALDIhtsnwiykhcFQSSLMENRTVILVTHNVHL 802
Cdd:cd03271 168 TTLSGGEAQRIKLAkelskrstgKTLYildEPTTGLHFHDVKKLLEV----------LQRLVDKGNTVVVIEHNLDV 234
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
739-798 |
9.40e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 9.40e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19115470 739 TLSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIykhcfQSSLME-NRTVILVTH 798
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWL-----ETYLLKwPKTFIVVSH 399
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
640-667 |
9.43e-04 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 41.76 E-value: 9.43e-04
10 20
....*....|....*....|....*...
gi 19115470 640 RNKLSIVIGPTGSGKSSLISALLGELSL 667
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNALLPELDL 132
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1216-1276 |
1.06e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.47 E-value: 1.06e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19115470 1216 HVSVSysaaGPTILKDVNLHINPSEKVAVVGRTGSGKSTLGLTLL-RFTHRI-SGEIYINGRE 1276
Cdd:PRK09580 8 HVSVE----DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgREDYEVtGGTVEFKGKD 66
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
741-772 |
1.12e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 43.03 E-value: 1.12e-03
10 20 30
....*....|....*....|....*....|..
gi 19115470 741 SGGQKQRIALARAVYSPTSIVLMDDVFSALDI 772
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDV 187
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1173-1264 |
1.22e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.08 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1173 SLQAEMNSYERvLEYSKLPQEPAPTIAGQVPATWPKegdIVFNHVSVSYSAAgpTILKDVNLHINPSEKVAVVGRTGSGK 1252
Cdd:PRK10938 226 ALVAQLAHSEQ-LEGVQLPEPDEPSARHALPANEPR---IVLNNGVVSYNDR--PILHNLSWQVNPGEHWQIVGPNGAGK 299
|
90
....*....|..
gi 19115470 1253 STLgLTLLRFTH 1264
Cdd:PRK10938 300 STL-LSLITGDH 310
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
633-771 |
1.46e-03 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 42.78 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 633 DLNIVFPRNKLSIVIGPTGSGKSSLISALLGELSLNKG---------SYNLPRSKGVSYVSQVPWL-RNATIRDNILFDY 702
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGqifidgedvTHRSIQQRDICMVFQSYALfPHMSLGENVGYGL 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19115470 703 PYI----EERYKKVIQACGLLtDLQSFVASDLTEIgekgvtlSGGQKQRIALARAVYSPTSIVLMDDVFSALD 771
Cdd:PRK11432 104 KMLgvpkEERKQRVKEALELV-DLAGFEDRYVDQI-------SGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
706-771 |
1.63e-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: 42.75 E-value: 1.63e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115470 706 EERYKKVIQAcglltdlqsfvasdLTEIGEKGVTL-------SGGQKQRIALARA-VYSPTSIVLmDDVFSALD 771
Cdd:COG4172 399 AERRARVAEA--------------LEEVGLDPAARhryphefSGGQRQRIAIARAlILEPKLLVL-DEPTSALD 457
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
631-657 |
1.85e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.75 E-value: 1.85e-03
10 20
....*....|....*....|....*...
gi 19115470 631 LRDLNIVFPRNKLsIVI-GPTGSGKSSL 657
Cdd:PRK00349 16 LKNIDLDIPRDKL-VVFtGLSGSGKSSL 42
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
740-802 |
2.42e-03 |
|
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: 41.27 E-value: 2.42e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19115470 740 LSGGQKQRIALARAVYSPTSIVLMDDVFSALDIHTSNWIYKhcfqssLME--NR----TVILVTHNVHL 802
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIID------LLFelNRergtTLVLVTHDPAL 209
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
646-771 |
2.75e-03 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 42.17 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 646 VIGPTGSGKSSLISALLGELS---------LNKGSYNLPRSKGVSYVSQvpwlrnatirDNILfdYPYIEERYKKVIqaC 716
Cdd:PLN03211 99 VLGPSGSGKSTLLNALAGRIQgnnftgtilANNRKPTKQILKRTGFVTQ----------DDIL--YPHLTVRETLVF--C 164
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115470 717 GLLTDLQSFVASDLTE-----IGEKGVT--------------LSGGQKQRIALARAVYSPTSIVLMDDVFSALD 771
Cdd:PLN03211 165 SLLRLPKSLTKQEKILvaesvISELGLTkcentiignsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
647-764 |
2.76e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 41.93 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 647 IGPTGSGKSSLISALLGELSLNKGSYNL---------PR---SKGVSYVSQ----VPWLrnaTIRDNI----------LF 700
Cdd:COG1129 36 LGENGAGKSTLMKILSGVYQPDSGEILLdgepvrfrsPRdaqAAGIAIIHQelnlVPNL---SVAENIflgreprrggLI 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19115470 701 DYPYIEERYKKVIQACGLLTDLQSFVASdlteigekgvtLSGGQKQRIALARAVYSPTSIVLMD 764
Cdd:COG1129 113 DWRAMRRRARELLARLGLDIDPDTPVGD-----------LSVAQQQLVEIARALSRDARVLILD 165
|
|
| DotB_TraJ |
cd19516 |
dot/icm secretion system protein DotB-like; Defect in organelle trafficking (Dot)B is part of ... |
634-665 |
3.56e-03 |
|
dot/icm secretion system protein DotB-like; Defect in organelle trafficking (Dot)B is part of the type IVb secretion (T4bS) system, also known as the dot/icm system, and is the main energy supplier of the secretion system. It is an ATPase, similar to the VirB11 component of the T4aS systems. This family also includes Escherichia coli IncI plasmid-encoded conjugative transfer ATPase TraJ encoded on the tra (transfer) operon.
Pssm-ID: 410924 [Multi-domain] Cd Length: 179 Bit Score: 40.05 E-value: 3.56e-03
10 20 30
....*....|....*....|....*....|..
gi 19115470 634 LNIVFPRNKLSIVIGPTGSGKSSLISALLGEL 665
Cdd:cd19516 4 VEALFPREGLVYVAGATGSGKSTLLAAIYRYI 35
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
631-657 |
3.67e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 40.70 E-value: 3.67e-03
10 20
....*....|....*....|....*..
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSL 657
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSL 37
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1228-1317 |
4.63e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.26 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 1228 ILKDVNLHINPSEKVAVVGRTGSGKStlglTLLRFTHRISGEiyINGRETQSVNLnalrqRISFIPQDPIL-FSGTVRSN 1306
Cdd:PRK11819 22 ILKDISLSFFPGAKIGVLGLNGAGKS----TLLRIMAGVDKE--FEGEARPAPGI-----KVGYLPQEPQLdPEKTVREN 90
|
90 100
....*....|....*....|..
gi 19115470 1307 -----------LDPFDELEDNF 1317
Cdd:PRK11819 91 veegvaevkaaLDRFNEIYAAY 112
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
646-812 |
4.69e-03 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 40.65 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 646 VIGPTGSGKSSLISALLGELSLNKGSYN--------LP----RSKGVSYVSQVPWL-RNATIRDNILF-----DYPYIEE 707
Cdd:PRK10895 34 LLGPNGAGKTTTFYMVVGIVPRDAGNIIiddedislLPlharARRGIGYLPQEASIfRRLSVYDNLMAvlqirDDLSAEQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 708 RYKKVIQAcglltdLQSFVASDLTEigEKGVTLSGGQKQRIALARAVYSPTSIVLMDDVF------SALDIHTsnwIYKH 781
Cdd:PRK10895 114 REDRANEL------MEEFHIEHLRD--SMGQSLSGGERRRVEIARALAANPKFILLDEPFagvdpiSVIDIKR---IIEH 182
|
170 180 190
....*....|....*....|....*....|...
gi 19115470 782 CFQSSLmenrTVILVTHNVHLFMD--SAAFIVT 812
Cdd:PRK10895 183 LRDSGL----GVLITDHNVRETLAvcERAYIVS 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
691-816 |
4.95e-03 |
|
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: 41.33 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 691 NATIRDNILFDYPYIEERYKKVIQ-ACGLLTDLQsfVASDLTEIGEKgvtLSGGQKQRIALARAVYSPTSIVLMDDVFSA 769
Cdd:TIGR03269 124 DDTVLDNVLEALEEIGYEGKEAVGrAVDLIEMVQ--LSHRITHIARD---LSGGEKQRVVLARQLAKEPFLFLADEPTGT 198
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 19115470 770 LDIHTSNWIYKHCFQSSLMENRTVILVTHNVHLFMDSAAFIVTVKNG 816
Cdd:TIGR03269 199 LDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENG 245
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
631-657 |
5.27e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.54 E-value: 5.27e-03
10 20
....*....|....*....|....*..
gi 19115470 631 LRDLNIVFPRNKLSIVIGPTGSGKSSL 657
Cdd:TIGR00630 12 LKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1231-1296 |
6.08e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 40.29 E-value: 6.08e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19115470 1231 DVNLHINPSEKVAVVGRTGSGKSTLgLTLLrfTHRI---SGEIYINGRETQSVNLNAL---------RQRISFIPQDP 1296
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTL-LNAL--SARLapdAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVHQHP 98
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
740-771 |
6.10e-03 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 40.49 E-value: 6.10e-03
10 20 30
....*....|....*....|....*....|...
gi 19115470 740 LSGGQKQRIALARA-VYSPTSIVLmDDVFSALD 771
Cdd:COG4608 158 FSGGQRQRIGIARAlALNPKLIVC-DEPVSALD 189
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
982-1110 |
6.69e-03 |
|
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: 40.19 E-value: 6.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115470 982 ASWFDKTPTGRIVNRFAKDI----RSIDMNLS-GwlffsINCFLSVAGGI---LSVSSAMPIFMIPAV-IVCLAGYYFGL 1052
Cdd:cd18573 89 AAFFDKNKTGELVSRLSSDTsvvgKSLTQNLSdG-----LRSLVSGVGGIgmmLYISPKLTLVMLLVVpPIAVGAVFYGR 163
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19115470 1053 LytraqvgVKRLisiyTSPIFSLLG-------ESIVGVSVIRAFNRQTIFKQMFSERLDNLVRLQ 1110
Cdd:cd18573 164 Y-------VRKL----SKQVQDALAdatkvaeERLSNIRTVRAFAAERKEVERYAKKVDEVFDLA 217
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
640-670 |
6.79e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 40.19 E-value: 6.79e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 19115470 640 RNKLSIVIGPTGSGKSSLISALLGEL---------SLNKG 670
Cdd:PRK00098 163 AGKVTVLAGQSGVGKSTLLNALAPDLelktgeiseALGRG 202
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
630-661 |
7.97e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 40.30 E-value: 7.97e-03
10 20 30
....*....|....*....|....*....|..
gi 19115470 630 CLRDLNIVFPRnkLSIVIGPTGSGKSSLISAL 661
Cdd:COG4637 12 SLRDLELPLGP--LTVLIGANGSGKSNLLDAL 41
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
630-661 |
8.38e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 39.02 E-value: 8.38e-03
10 20 30
....*....|....*....|....*....|..
gi 19115470 630 CLRDLNIVFPRNkLSIVIGPTGSGKSSLISAL 661
Cdd:pfam13476 8 SFRDQTIDFSKG-LTLITGPNGSGKTTILDAI 38
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
646-707 |
9.85e-03 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 38.59 E-value: 9.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19115470 646 VIGPTGSGKSSLISALLGELSLNKGSYNLPRSKGVSYVsqvpWLRNATIRDNILFDYPYIEE 707
Cdd:cd00882 2 VVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDPDVYV----KELDKGKVKLVLVDTPGLDE 59
|
|
| |
