|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
190-1449 |
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: 856.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 190 KEPLLSSAESSDNeevTAPFSKAGILSRMSFSWMSPLITLGNEKIIDIKDVPQLDRSDTTESLF------W--------- 254
Cdd:TIGR00957 188 KSPLFSETNHDPN---PCPESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVpvlvenWkkeckktrk 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 255 -----IFRSKLEWD---------DGERRITTFK---------LIKALFLSVWRDIVLSALLAFVYTVSCYVAPYLMDNFV 311
Cdd:TIGR00957 265 qpvsaVYGKKDPSKpkgssqldaNEEVEALIVKsphkprkpsLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLI 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 312 QYLNGNRQYKNQGYVLVTTFFVAKLVECQTQRQWFFRGQKAGLGMRSVLVSMIYEKGLTLPCHSKQGHTSGEIINLMAVD 391
Cdd:TIGR00957 345 RFVNDPMAPDWQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKSSTVGEIVNLMSVD 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 392 ADRISAFSWFMHDPWILVLQVSLALWILYKSLGLGSIAAFPATILVMLANYPFAKLEEKFQSSLMKSKDNRMKKTSEVLL 471
Cdd:TIGR00957 425 AQRFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILN 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 472 NMKILKLQGWEMKFLSKILELRHIEAGWLKKFVYnSSAINSVLWAAPSFISATAFGACLLLKIP---LESGKILAALATF 548
Cdd:TIGR00957 505 GIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAY-LHAVGTFTWVCTPFLVALITFAVYVTVDEnniLDAEKAFVSLALF 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 549 RILQGPIYKLPETISMIVQTKVSLNRIASFLCLDDLQQDVVGRLPSGSSEM-AVEISNGTFSWDDSSPiPTLRDMNFKVS 627
Cdd:TIGR00957 584 NILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGEGnSITVHNATFTWARDLP-PTLNGITFSIP 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 628 QGMNVAICGTVGSGKSSLLSSILGEVPKISGNLKVCGRKAYIAQSPWIQSGKVEENILFGKPMEREWYDRVLEACSLNKD 707
Cdd:TIGR00957 663 EGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALLPD 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 708 LEILPFHDQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEVL--LGLLRHKTVIYVTHQV 785
Cdd:TIGR00957 743 LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIgpEGVLKNKTRILVTHGI 822
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 786 EFLPEADLILVMKDGKITQAGKYHEILDSGTDFMELVGAHTEALATIDSCETGYASE----------------------- 842
Cdd:TIGR00957 823 SYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEQQGHLEDSWTALVsgegkeakliengmlvtdvvgkq 902
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 843 ------KSTTDKENEVLHHK--EKQENGSDNKPSGQLVQEEEREKGKVGFTVYKKYMAlAYGGAVIPLILVVQVLFQLLS 914
Cdd:TIGR00957 903 lqrqlsASSSDSGDQSRHHGssAELQKAEAKEETWKLMEADKAQTGQVELSVYWDYMK-AIGLFITFLSIFLFVCNHVSA 981
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 915 IGSNYWMT-WVTPVSKDVEPPVSGFTLIlVYVLLAVASSFCILIRALLVAMTGFKMATELFTQMHLRIFRASMSFFDATP 993
Cdd:TIGR00957 982 LASNYWLSlWTDDPMVNGTQNNTSLRLS-VYGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTP 1060
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 994 MGRILNRASTDQSVADLRLPGQFAYVAIAAINILGIIgVIVQVAWQVLIVFIPVVAACAWYRQ-YYISAARELARLAGIS 1072
Cdd:TIGR00957 1061 SGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGAL-IVILLATPIAAVIIPPLGLLYFFVQrFYVASSRQLKRLESVS 1139
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1073 RSPVVHHFSETLSGITTIRSFDQEPRFRGDIMRLSDCYSRLKFHSTGAMEWLCFRLEllstfaFASSLVILVSAPEGVI- 1151
Cdd:TIGR00957 1140 RSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLE------CVGNCIVLFAALFAVIs 1213
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1152 ----NPSLAGLAITYALNLNTLQATLIWTLCDLENKMISVERMLQYTNIPSEPPLVIETTRPEKSWPSRGEITICNLQVR 1227
Cdd:TIGR00957 1214 rhslSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSGWPPRGRVEFRNYCLR 1293
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1228 YGPHLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSIIPQDPTMFE 1307
Cdd:TIGR00957 1294 YREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFS 1373
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1308 GTIRSNLDPLEEYTDDQIWEALDNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEATASID 1387
Cdd:TIGR00957 1374 GSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30682479 1388 TATDNLIQETLRHHFADCTVITIAHRISSVIDSDMVLLLDQGLIKEHDSPARLLEDRSSLFS 1449
Cdd:TIGR00957 1454 LETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYS 1515
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
96-1458 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 823.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 96 LLLAALTWGSISVYLfgrytnSCEQKVLFLLRVWWVFFFVVscYHLVVD-----FVLYKKQ--EMVSVHFVISDLVgvCA 168
Cdd:PLN03130 115 LIVEALTWCSMLVMI------GVETKIYIREFRWYVRFAVI--YVLVGDavmlnLVLSVKEyySSFVLYLYISEVA--AQ 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 169 GLFLCCSCLWKKgegeriDLLKEPLLS--SAESSDNEEVTA--------PFSKAGILSRMSFSWMSPLITLGNEKIIDIK 238
Cdd:PLN03130 185 VLFGILLLVYFP------NLDPYPGYTpiGSESVDDYEYEElpggeqicPERHANIFSRIFFGWMTPLMQLGYKRPLTEK 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 239 DVPQLDRSDTTESLFWIFRSKleWDDgERRITTFKLIKALFLSVWRDIVLSALLAFVYTVSCYVAPYLMDNFVQYLNgNR 318
Cdd:PLN03130 259 DVWKLDTWDQTETLYRSFQKC--WDE-ELKKPKPWLLRALNNSLGGRFWLGGFFKIGNDLSQFVGPLLLNLLLESMQ-NG 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 319 QYKNQGYVLVTTFFVAKLVECQTQRQWFFRGQKAGLGMRSVLVSMIYEKGLTLPCHSKQGHTSGEIINLMAVDADRISAF 398
Cdd:PLN03130 335 EPAWIGYIYAFSIFVGVVLGVLCEAQYFQNVMRVGFRLRSTLVAAVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQI 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 399 SWFMHDPWILVLQVSLALWILYKSLGLGSIaaFPATILVML---ANYPFAKLEEKFQSSLMKSkDNRMKKTSEVLLNMKI 475
Cdd:PLN03130 415 CQQLHTLWSAPFRIIIAMVLLYQQLGVASL--IGSLMLVLMfpiQTFIISKMQKLTKEGLQRT-DKRIGLMNEVLAAMDT 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 476 LKLQGWEMKFLSKILELRHIEAGWLKKFVYnSSAINS-VLWAAPSFISATAFGACLLLKIPLESGKILAALATFRILQGP 554
Cdd:PLN03130 492 VKCYAWENSFQSKVQTVRDDELSWFRKAQL-LSAFNSfILNSIPVLVTVVSFGVFTLLGGDLTPARAFTSLSLFAVLRFP 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 555 IYKLPETISMIVQTKVSLNRIASFLCLDDLQqdVVGRLPSGSSEMAVEISNGTFSWDDSSPIPTLRDMNFKVSQGMNVAI 634
Cdd:PLN03130 571 LFMLPNLITQAVNANVSLKRLEELLLAEERV--LLPNPPLEPGLPAISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAI 648
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 635 CGTVGSGKSSLLSSILGEVPKIS-GNLKVCGRKAYIAQSPWIQSGKVEENILFGKPMEREWYDRVLEACSLNKDLEILPF 713
Cdd:PLN03130 649 VGSTGEGKTSLISAMLGELPPRSdASVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPG 728
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 714 HDQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEVLLGLLRHKTVIYVTHQVEFLPEADL 793
Cdd:PLN03130 729 GDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDR 808
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 794 ILVMKDGKITQAGKYHEILDSGTDF---MELVGAHTEALATIDSCETGYASEKsttDKENEVLHHKEKQENGSDNKPSGQ 870
Cdd:PLN03130 809 IILVHEGMIKEEGTYEELSNNGPLFqklMENAGKMEEYVEENGEEEDDQTSSK---PVANGNANNLKKDSSSKKKSKEGK 885
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 871 --LVQEEEREKGKVGFTVYKKYMAlAYGGA-VIPLILVVQVLFQLLSIGSNYWMT-WVTPVSKDVEPPvsGFtLILVYVL 946
Cdd:PLN03130 886 svLIKQEERETGVVSWKVLERYKN-ALGGAwVVMILFLCYVLTEVFRVSSSTWLSeWTDQGTPKTHGP--LF-YNLIYAL 961
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 947 LAVASSFCILIRALLVAMTGFKMATELFTQMHLRIFRASMSFFDATPMGRILNRASTDQSVADLRlpgqfayVAIAAINI 1026
Cdd:PLN03130 962 LSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRN-------VAVFVNMF 1034
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1027 LG----------IIGVIVQVA-WQVLIVFIPVVAAcawyRQYYISAARELARLAGISRSPVVHHFSETLSGITTIRSF-- 1093
Cdd:PLN03130 1035 LGqifqllstfvLIGIVSTISlWAIMPLLVLFYGA----YLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYka 1110
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1094 -DQEPRFRGDIMrlsDCYSRLKFHSTGAMEWLCFRLELLStfafasSLVILVSAPEGVI------NP----SLAGLAITY 1162
Cdd:PLN03130 1111 yDRMAEINGRSM---DNNIRFTLVNMSSNRWLAIRLETLG------GLMIWLTASFAVMqngraeNQaafaSTMGLLLSY 1181
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1163 ALNLNTLQATLIWTLCDLENKMISVERMLQYTNIPSEPPLVIETTRPEKSWPSRGEITICNLQVRYGPHLPMVLHGLTCT 1242
Cdd:PLN03130 1182 ALNITSLLTAVLRLASLAENSLNAVERVGTYIDLPSEAPLVIENNRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFE 1261
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1243 FPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSIIPQDPTMFEGTIRSNLDPLEEYTD 1322
Cdd:PLN03130 1262 ISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHND 1341
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1323 DQIWEALDNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTATDNLIQETLRHHF 1402
Cdd:PLN03130 1342 ADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEF 1421
|
1370 1380 1390 1400 1410 1420
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30682479 1403 ADCTVITIAHRISSVIDSDMVLLLDQGLIKEHDSPARLLEDRSSLFSKLV-------AEYTTS 1458
Cdd:PLN03130 1422 KSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKMVqstgaanAQYLRS 1484
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
67-1452 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 763.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 67 CCVSLSVFYSVLSL-LSCLHWHTNGWPF--LDLLLAALTWGSISVYLfgrytnSCEQKVLFLLRVWWVFFFVVscYHLVV 143
Cdd:PLN03232 83 YCVVEPVLRLVMGIsLFDMDEETDLPPFevASLMVEAFAWFSMLVLI------GLETKQYVKEFRWYVRFGVV--YVLVA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 144 DFVlykkqeMVSVHFVISDLVGVCAGLFL----CCSCLWkkgeG-------ERIDLLKEPLLSSAESSDNEEVTA----- 207
Cdd:PLN03232 155 DAV------LLDLVLPLKNSINRTALYLCissrCCQALF----GilllvyiPELDPYPGYHILNNESLDNVEYDAlrgge 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 208 ---PFSKAGILSRMSFSWMSPLITLGNEKIIDIKDVPQLDRSDTTESLfwIFRSKLEWDDGERRITTFkLIKALFLSVWR 284
Cdd:PLN03232 225 nicPERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETL--IKRFQRCWTEESRRPKPW-LLRALNNSLGG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 285 DIVLSALLAFVYTVSCYVAPYLMDNFVQYL-NGNRQYKnqGYVLVTTFFVAKLVECQTQRQWFFRGQKAGLGMRSVLVSM 363
Cdd:PLN03232 302 RFWLGGIFKIGHDLSQFVGPVILSHLLQSMqEGDPAWV--GYVYAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLVAA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 364 IYEKGLTLPCHSKQGHTSGEIINLMAVDADRISAFSWFMHDPWILVLQVSLALWILYKSLGLGSIaaFPATILVMLAnyP 443
Cdd:PLN03232 380 IFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASL--FGSLILFLLI--P 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 444 FAKLEEKFQSSLMKS----KDNRMKKTSEVLLNMKILKLQGWEMKFLSKILELRHIEAGWLKK----FVYNSSAINSVlw 515
Cdd:PLN03232 456 LQTLIVRKMRKLTKEglqwTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKaqllSAFNSFILNSI-- 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 516 aaPSFISATAFGACLLLKIPLESGKILAALATFRILQGPIYKLPETISMIVQTKVSLNRIASFLCLDD--LQQDVvgrlP 593
Cdd:PLN03232 534 --PVVVTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEEriLAQNP----P 607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 594 SGSSEMAVEISNGTFSWDDSSPIPTLRDMNFKVSQGMNVAICGTVGSGKSSLLSSILGEVPKI-SGNLKVCGRKAYIAQS 672
Cdd:PLN03232 608 LQPGAPAISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAeTSSVVIRGSVAYVPQV 687
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 673 PWIQSGKVEENILFGKPMEREWYDRVLEACSLNKDLEILPFHDQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDP 752
Cdd:PLN03232 688 SWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDP 767
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 753 FSAVDAHTGSHLFKEVLLGLLRHKTVIYVTHQVEFLPEADLILVMKDGKITQAGKYHEILDSGTDFMELVGAHTEALATI 832
Cdd:PLN03232 768 LSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGKMDATQ 847
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 833 DSCETG----YASEKSTTDKENEVLHHKEKQENGSDnkpsgQLVQEEEREKGKVGFTVYKKYMALAYGGAVIPLILVVQV 908
Cdd:PLN03232 848 EVNTNDenilKLGPTVTIDVSERNLGSTKQGKRGRS-----VLVKQEERETGIISWNVLMRYNKAVGGLWVVMILLVCYL 922
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 909 LFQLLSIGSNYWMTWVT--PVSKDVEPpvsGFtLILVYVLLAVASSFCILIRALLVAMTGFKMATELFTQMHLRIFRASM 986
Cdd:PLN03232 923 TTEVLRVSSSTWLSIWTdqSTPKSYSP---GF-YIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPM 998
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 987 SFFDATPMGRILNRASTD-----QSVADLRlpGQFAYVAIAAINILGIIGVIVQVA-WQVLIVFIPVVAACAwyrqYYIS 1060
Cdd:PLN03232 999 LFFHTNPTGRVINRFSKDigdidRNVANLM--NMFMNQLWQLLSTFALIGTVSTISlWAIMPLLILFYAAYL----YYQS 1072
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1061 AARELARLAGISRSPVVHHFSETLSGITTIRSF---DQEPRFRGDIMrlsDCYSRLKFHSTGAMEWLCFRLE-------- 1129
Cdd:PLN03232 1073 TSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYkayDRMAKINGKSM---DNNIRFTLANTSSNRWLTIRLEtlggvmiw 1149
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1130 LLSTFAFASSlvilVSAPEGVINPSLAGLAITYALNLNTLQATLIWTLCDLENKMISVERMLQYTNIPSEPPLVIETTRP 1209
Cdd:PLN03232 1150 LTATFAVLRN----GNAENQAGFASTMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIENNRP 1225
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1210 EKSWPSRGEITICNLQVRYGPHLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGL 1289
Cdd:PLN03232 1226 VSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGL 1305
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1290 HDLRSRLSIIPQDPTMFEGTIRSNLDPLEEYTDDQIWEALDNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRV 1369
Cdd:PLN03232 1306 TDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARA 1385
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1370 LLKRSKLLVLDEATASIDTATDNLIQETLRHHFADCTVITIAHRISSVIDSDMVLLLDQGLIKEHDSPARLLEDRSSLFS 1449
Cdd:PLN03232 1386 LLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFF 1465
|
...
gi 30682479 1450 KLV 1452
Cdd:PLN03232 1466 RMV 1468
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
274-1452 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 600.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 274 LIKALFLSVWRDIVLSALLAFVYTVSCYVAPYLMDNFVQYLNGNRQYKNQGYVLVTTFFVAKLVECQTQRQWFFRGQKAG 353
Cdd:PTZ00243 234 LLRTLFAALPYYVWWQIPFKLLSDVCTLTLPVLLKYFVKFLDADNATWGRGLGLVLTLFLTQLIQSVCLHRFYYISIRCG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 354 LGMRSVLVSMIYEKGLTLPCHSKQ--GHTSGEIINLMAVDADRISAFSWFMHDPWILVLQVSLALWILYKSLG---LGSI 428
Cdd:PTZ00243 314 LQYRSALNALIFEKCFTISSKSLAqpDMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGwcaLMAV 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 429 AAFPATILVmlaNYPFAKLEEKFQSSLMKSKDNRMKKTSEVLLNMKILKLQGWEMKFLSKILELRHIEAGWLKKfVYNSS 508
Cdd:PTZ00243 394 AVLLVTLPL---NGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRD-VQLAR 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 509 AINS-VLWAAPSFISATAFGACLLLKIPLESGKILAALATFRILQGPIYKLPETISMIVQTKVSLNRIASFLCLDDLQ-- 585
Cdd:PTZ00243 470 VATSfVNNATPTLMIAVVFTVYYLLGHELTPEVVFPTIALLGVLRMPFFMIPWVFTTVLQFLVSIKRISTFLECDNATcs 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 586 --QDVVG-----------------------------RLP----------------------------------------- 593
Cdd:PTZ00243 550 tvQDMEEywreqrehstacqlaavlenvdvtafvpvKLPrapkvktsllsralrmlcceqcrptkrhpspsvvvedtdyg 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 594 SGSSEMAVEISNGTFSWDDSSPIPT---------------------LRDMNFKVSQGMNVAICGTVGSGKSSLLSSILGE 652
Cdd:PTZ00243 630 SPSSASRHIVEGGTGGGHEATPTSErsaktpkmktddffelepkvlLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQ 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 653 VPKISGNLKVCGRKAYIAQSPWIQSGKVEENILFGKPMEREWYDRVLEACSLNKDLEILPFHDQTVIGERGINLSGGQKQ 732
Cdd:PTZ00243 710 FEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKA 789
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 733 RIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEVLLGLLRHKTVIYVTHQVEFLPEADLILVMKDGKITQAGKYheil 812
Cdd:PTZ00243 790 RVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSS---- 865
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 813 dsgTDFME---LVGAHTEALATIDSCETGYASEKSTTDKENEVLHHKEKQENGSDNKPS-----------GQLVQEEERE 878
Cdd:PTZ00243 866 ---ADFMRtslYATLAAELKENKDSKEGDADAEVAEVDAAPGGAVDHEPPVAKQEGNAEggdgaaldaaaGRLMTREEKA 942
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 879 KGKVGFTVYKKYMALAYGGAVIPLILVVQVLFQLLSIGSNYWMT-WVTPVSKdveppVSGFTLILVYVLLAVASSFCILI 957
Cdd:PTZ00243 943 SGSVPWSTYVAYLRFCGGLHAAGFVLATFAVTELVTVSSGVWLSmWSTRSFK-----LSAATYLYVYLGIVLLGTFSVPL 1017
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 958 RaLLVAMTGFKMATelfTQMH---LR-IFRASMSFFDATPMGRILNRASTDQSVADLRLPGQFAYVAIAAINILGIIgvI 1033
Cdd:PTZ00243 1018 R-FFLSYEAMRRGS---RNMHrdlLRsVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSI--L 1091
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1034 VQVAWQ--VLIVFIPVVAAcaWYR--QYYISAARELARLAGISRSPVVHHFSETLSGITTIRSFD------QEPRFRGDI 1103
Cdd:PTZ00243 1092 VTSASQpfVLVALVPCGYL--YYRlmQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGkahlvmQEALRRLDV 1169
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1104 MrlsdcysrlkfHSTGAME-----WLCFRLEllstfaFASSLVILVSAPEGVI---------NPSLAGLAITYALnlnTL 1169
Cdd:PTZ00243 1170 V-----------YSCSYLEnvanrWLGVRVE------FLSNIVVTVIALIGVIgtmlratsqEIGLVSLSLTMAM---QT 1229
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1170 QATLIWTL---CDLENKMISVERMLQYT-NIPSE--PPL---------------------VIETTRPEKSWP---SRGEI 1219
Cdd:PTZ00243 1230 TATLNWLVrqvATVEADMNSVERLLYYTdEVPHEdmPELdeevdalerrtgmaadvtgtvVIEPASPTSAAPhpvQAGSL 1309
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1220 TICNLQVRYGPHLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSII 1299
Cdd:PTZ00243 1310 VFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMI 1389
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1300 PQDPTMFEGTIRSNLDPLEEYTDDQIWEALDNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKR-SKLLV 1378
Cdd:PTZ00243 1390 PQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKgSGFIL 1469
|
1290 1300 1310 1320 1330 1340 1350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30682479 1379 LDEATASIDTATDNLIQETLRHHFADCTVITIAHRISSVIDSDMVLLLDQGLIKEHDSPARLLEDRSSLFSKLV 1452
Cdd:PTZ00243 1470 MDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMV 1543
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
207-1447 |
5.82e-138 |
|
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: 462.07 E-value: 5.82e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 207 APFSKAGILSRMSFSWMSPLITLGNEKIIDIKDVPQLDRSDTTESLFWifRSKLEWDdgeRRITTFK----LIKAL---F 279
Cdd:TIGR01271 4 SPVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSE--RLEREWD---RELASAKknpkLLNALrrcF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 280 LsvWRDIVLSALLAFVyTVSCYVAPYLMDNFVQYLNGNRQY-KNQGYVL---VTTFFVAKLVECQTQrqwFFRGQKAGLG 355
Cdd:TIGR01271 79 F--WRFVFYGILLYFG-EATKAVQPLLLGRIIASYDPFNAPeREIAYYLalgLCLLFIVRTLLLHPA---IFGLHHLGMQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 356 MRSVLVSMIYEKGLTLPCHSKQGHTSGEIINLMAVDADRISAFSWFMHDPWILVLQVSLALWILYKSLGLGSIAAFPATI 435
Cdd:TIGR01271 153 MRIALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 436 LVMLANYPFAKLEEKFQSSLMKSKDNRMKKTSEVLLNMKILKLQGWEMKFLSKILELRHIE------AGWLKKFvYNSSA 509
Cdd:TIGR01271 233 LLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDElkltrkIAYLRYF-YSSAF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 510 INSVLWAAPSFISATAFGACLLLKiplesgKILAALATFRILQGPIYK-LPETISMIVQTKVSLNRIASFLCLDDLQQdv 588
Cdd:TIGR01271 312 FFSGFFVVFLSVVPYALIKGIILR------RIFTTISYCIVLRMTVTRqFPGAIQTWYDSLGAITKIQDFLCKEEYKT-- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 589 vgrLPSGSSEMAVEISNGTFSWDDS-------------------------------SPIPTLRDMNFKVSQGMNVAICGT 637
Cdd:TIGR01271 384 ---LEYNLTTTEVEMVNVTASWDEGigelfekikqnnkarkqpngddglffsnfslYVTPVLKNISFKLEKGQLLAVAGS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 638 VGSGKSSLLSSILGEVPKISGNLKVCGRKAYIAQSPWIQSGKVEENILFGKPMEREWYDRVLEACSLNKDLEILPFHDQT 717
Cdd:TIGR01271 461 TGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKT 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 718 VIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEVLLGLLRHKTVIYVTHQVEFLPEADLILVM 797
Cdd:TIGR01271 541 VLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLL 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 798 KDGKITQAGKYHEILDSGTDFM-ELVGAH--------------TEAL--ATIDS-------CETGYASEKSTTDKENEvl 853
Cdd:TIGR01271 621 HEGVCYFYGTFSELQAKRPDFSsLLLGLEafdnfsaerrnsilTETLrrVSIDGdstvfsgPETIKQSFKQPPPEFAE-- 698
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 854 hhKEKQ----------------------------------------------ENGSDNKPSGQLVQ-------------- 873
Cdd:TIGR01271 699 --KRKQsiilnpiasarkfsfvqmgpqkaqattiedavrepserkfslvpedEQGEESLPRGNQYHhglqhqaqrrqsvl 776
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 874 ------------------------------------------------------------------EEEREKGKVGFTVY 887
Cdd:TIGR01271 777 qlmthsnrgenrreqlqtsfrkkssitqqnelaseldiysrrlskdsvyeiseeineedlkecfadERENVFETTTWNTY 856
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 888 KKYM----ALAYGGAVIPLILVVQVLFQLLSIgsnyWMTWVTPV-------------SKDVEPPV---SGFTLILVYVLL 947
Cdd:TIGR01271 857 LRYIttnrNLVFVLIFCLVIFLAEVAASLLGL----WLITDNPSapnyvdqqhanasSPDVQKPViitPTSAYYIFYIYV 932
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 948 AVASSFCIL--IRALLVAMTGFKMATELFTQMHLRIFRASMSFFDATPMGRILNRASTDQSVADLRLP-GQFAYVAIAAI 1024
Cdd:TIGR01271 933 GTADSVLALgfFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPlTLFDFIQLTLI 1012
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1025 nILGIIGVIVQVAWQVLIVFIPVVAACAWYRQYYISAARELARLAGISRSPVVHHFSETLSGITTIRSFDQEPRFRGDIM 1104
Cdd:TIGR01271 1013 -VLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFH 1091
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1105 RLSDCYSRLKFHSTGAMEWLCFRLELLSTFAFASSLVILVSAPEgvINPSLAGLAITYALN-LNTLQATLIWTLcDLENK 1183
Cdd:TIGR01271 1092 KALNLHTANWFLYLSTLRWFQMRIDIIFVFFFIAVTFIAIGTNQ--DGEGEVGIILTLAMNiLSTLQWAVNSSI-DVDGL 1168
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1184 MISVERMLQYTNIPSEPP--------------LVIETTRPEKSWPSRGEITICNLQVRYGPHLPMVLHGLTCTFPGGLKT 1249
Cdd:TIGR01271 1169 MRSVSRVFKFIDLPQEEPrpsggggkyqlstvLVIENPHAQKCWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRV 1248
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1250 GIVGRTGCGKSTLIQTLFRIVEpAAGEIRIDGINILSIGLHDLRSRLSIIPQDPTMFEGTIRSNLDPLEEYTDDQIWEAL 1329
Cdd:TIGR01271 1249 GLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVA 1327
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1330 DNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTATDNLIQETLRHHFADCTVIT 1409
Cdd:TIGR01271 1328 EEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVIL 1407
|
1450 1460 1470
....*....|....*....|....*....|....*...
gi 30682479 1410 IAHRISSVIDSDMVLLLDQGLIKEHDSPARLLEDRSSL 1447
Cdd:TIGR01271 1408 SEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLF 1445
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1217-1437 |
1.30e-120 |
|
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: 375.68 E-value: 1.30e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1217 GEITICNLQVRYGPHLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRL 1296
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1297 SIIPQDPTMFEGTIRSNLDPLEEYTDDQIWEALDNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKL 1376
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30682479 1377 LVLDEATASIDTATDNLIQETLRHHFADCTVITIAHRISSVIDSDMVLLLDQGLIKEHDSP 1437
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
938-1453 |
3.26e-103 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 341.76 E-value: 3.26e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 938 FTLILVYVLLAVASSFCILIRALLVAMTGFKMATELFTQMHLRIFRASMSFFDATPMGRILNRASTD-QSVADLrLPGQF 1016
Cdd:COG1132 61 LLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDvDAVEQF-LAHGL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1017 AYVAIAAINILGIIGVIVQVAWQ---VLIVFIPVVAACAWY-----RQYYISAARELARLAGisrspvvhHFSETLSGIT 1088
Cdd:COG1132 140 PQLVRSVVTLIGALVVLFVIDWRlalIVLLVLPLLLLVLRLfgrrlRKLFRRVQEALAELNG--------RLQESLSGIR 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1089 TIRSFDQEPRFRGDIMRLSDCYSRLKFHSTGAMEWLCFRLELLSTFAFASSLVI---LVSApeGVINPSLAGLAITYALN 1165
Cdd:COG1132 212 VVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVgglLVLS--GSLTVGDLVAFILYLLR 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1166 LNTLQATLIWTLCDLENKMISVERMLQYTNIPSEPPlviETTRPEKSWPSRGEITICNLQVRYGPHLPmVLHGLTCTFPG 1245
Cdd:COG1132 290 LFGPLRQLANVLNQLQRALASAERIFELLDEPPEIP---DPPGAVPLPPVRGEIEFENVSFSYPGDRP-VLKDISLTIPP 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1246 GLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSIIPQDPTMFEGTIRSNL---DPleEYTD 1322
Cdd:COG1132 366 GETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRP--DATD 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1323 DQIWEALDNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTATDNLIQETLRHHF 1402
Cdd:COG1132 444 EEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLM 523
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 30682479 1403 ADCTVITIAHRISSVIDSDMVLLLDQGLIKEHDSPARLLEdRSSLFSKLVA 1453
Cdd:COG1132 524 KGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLA-RGGLYARLYR 573
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1213-1437 |
2.22e-95 |
|
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: 305.49 E-value: 2.22e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1213 WPSRGEITICNLQVRYGPHLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDL 1292
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1293 RSRLSIIPQDPTMFEGTIRSNLDPLEEYTDDQIWEALDncqlgdevrkkelkldspVSENGQNWSVGQRQLVCLGRVLLK 1372
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30682479 1373 RSKLLVLDEATASIDTATDNLIQETLRHHFADCTVITIAHRISSVIDSDMVLLLDQGLIKEHDSP 1437
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
601-801 |
8.40e-92 |
|
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: 295.53 E-value: 8.40e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 601 VEISNGTFSWDD--SSPIPTLRDMNFKVSQGMNVAICGTVGSGKSSLLSSILGEVPKISGNLKVCGRKAYIAQSPWIQSG 678
Cdd:cd03250 1 ISVEDASFTWDSgeQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 679 KVEENILFGKPMEREWYDRVLEACSLNKDLEILPFHDQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDA 758
Cdd:cd03250 81 TIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 30682479 759 HTGSHLFKEVLLGLLR-HKTVIYVTHQVEFLPEADLILVMKDGK 801
Cdd:cd03250 161 HVGRHIFENCILGLLLnNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
938-1454 |
7.67e-91 |
|
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: 311.00 E-value: 7.67e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 938 FTLILVYVLLAVASSFCILIRALLVAMTGFKMATELFTQMHLRIFRASMSFFDATPMGRILNRASTDQSVADLrLPGQFA 1017
Cdd:COG2274 196 WVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRDVESIREF-LTGSLL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1018 YVAIAAINILGIIGVIVQVAWQ---VLIVFIPVVAACAWY-RQYYISAARELARLAGIsrspVVHHFSETLSGITTIRSF 1093
Cdd:COG2274 275 TALLDLLFVLIFLIVLFFYSPPlalVVLLLIPLYVLLGLLfQPRLRRLSREESEASAK----RQSLLVETLRGIETIKAL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1094 DQEPRFRGDIMRLSDCYSRLKFH--------STGAMewLCFRLELLSTFAFASSLVIlvsapEGVINP-------SLAGL 1158
Cdd:COG2274 351 GAESRFRRRWENLLAKYLNARFKlrrlsnllSTLSG--LLQQLATVALLWLGAYLVI-----DGQLTLgqliafnILSGR 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1159 AITYALNLNTLQATLIwtlcDLenkMISVERMLQYTNIPSEPPLVIETTRPEKSwpsRGEITICNLQVRYGPHLPMVLHG 1238
Cdd:COG2274 424 FLAPVAQLIGLLQRFQ----DA---KIALERLDDILDLPPEREEGRSKLSLPRL---KGDIELENVSFRYPGDSPPVLDN 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1239 LTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSIIPQDPTMFEGTIRSNL---D 1315
Cdd:COG2274 494 ISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItlgD 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1316 PleEYTDDQIWEALDNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTATDNLIQ 1395
Cdd:COG2274 574 P--DATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIIL 651
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 30682479 1396 ETLRHHFADCTVITIAHRISSVIDSDMVLLLDQGLIKEHDSPARLLEdRSSLFSKLVAE 1454
Cdd:COG2274 652 ENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLA-RKGLYAELVQQ 709
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
288-575 |
3.19e-88 |
|
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: 288.62 E-value: 3.19e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 288 LSALLAFVYTVSCYVAPYLMDNFVQYLNGNRQY-KNQGYVLVTTFFVAKLVECQTQRQWFFRGQKAGLGMRSVLVSMIYE 366
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEpLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 367 KGLTLPCHSKQGHTSGEIINLMAVDADRISAFSWFMHDPWILVLQVSLALWILYKSLGLGSIAAFPATILVMLANYPFAK 446
Cdd:cd18579 81 KALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 447 LEEKFQSSLMKSKDNRMKKTSEVLLNMKILKLQGWEMKFLSKILELRHIEAGWLKKFVYNSSAINSVLWAAPSFISATAF 526
Cdd:cd18579 161 LISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATF 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 30682479 527 GACLLLKIPLESGKILAALATFRILQGPIYKLPETISMIVQTKVSLNRI 575
Cdd:cd18579 241 ATYVLLGNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
900-1194 |
4.26e-88 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 288.63 E-value: 4.26e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 900 IPLILVVQVLFQLLSIGSNYWMTWVTPVSKDVEPPVSGFTLILVYVLLAVASSFCILIRALLVAMTGFKMATELFTQMHL 979
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 980 RIFRASMSFFDATPMGRILNRASTDQSVADLRLPGQFAYVAIAAINILGIIGVIVQVAWQVLIVFIPVVAACAWYRQYYI 1059
Cdd:cd18580 81 SVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1060 SAARELARLAGISRSPVVHHFSETLSGITTIRSFDQEPRFRGDIMRLSDCYSRLKFHSTGAMEWLCFRLELLSTFaFASS 1139
Cdd:cd18580 161 RTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGAL-LALV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 30682479 1140 LVILVSAPEGVINPSLAGLAITYALNLNTLQATLIWTLCDLENKMISVERMLQYT 1194
Cdd:cd18580 240 VALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
904-1442 |
2.26e-77 |
|
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: 267.78 E-value: 2.26e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 904 LVVQVLFQLLS----IGSNYWMTWVtpVSKDVEPPVSGFTLILVYVLLAVassfCILIRALLVAM---TGFKMAT----E 972
Cdd:COG4988 19 LALAVLLGLLSglliIAQAWLLASL--LAGLIIGGAPLSALLPLLGLLLA----VLLLRALLAWLrerAAFRAAArvkrR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 973 LFTQMHLRIFRASMSFFDATPMGRILNRAsTDQsVADLR------LPgQFAYVAIAAINILGiigVIVQVAWQ---VLIV 1043
Cdd:COG4988 93 LRRRLLEKLLALGPAWLRGKSTGELATLL-TEG-VEALDgyfaryLP-QLFLAALVPLLILV---AVFPLDWLsglILLV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1044 FIPVV----------AACAWYRQYyisaaRELARLAGisrspvvhHFSETLSGITTIRSFDQEPRFRGDIMRLSDCYS-- 1111
Cdd:COG4988 167 TAPLIplfmilvgkgAAKASRRQW-----RALARLSG--------HFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRkr 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1112 -----RLKFHSTGAMEW------------LCFRLeLLSTFAFASSLVILVSAPEgvinpslaglaitYALNLNTL----Q 1170
Cdd:COG4988 234 tmkvlRVAFLSSAVLEFfaslsialvavyIGFRL-LGGSLTLFAALFVLLLAPE-------------FFLPLRDLgsfyH 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1171 ATLiwtlcdleNKMISVERMLQytnIPSEPPLVIETTRPEKSWPSRGEITICNLQVRYGPHLPmVLHGLTCTFPGGLKTG 1250
Cdd:COG4988 300 ARA--------NGIAAAEKIFA---LLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRP-ALDGLSLTIPPGERVA 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1251 IVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSIIPQDPTMFEGTIRSNL---DPleEYTDDQIWE 1327
Cdd:COG4988 368 LVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLrlgRP--DASDEELEA 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1328 ALDNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTATDNLIQETLRHHFADCTV 1407
Cdd:COG4988 446 ALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTV 525
|
570 580 590
....*....|....*....|....*....|....*
gi 30682479 1408 ITIAHRISSVIDSDMVLLLDQGLIKEHDSPARLLE 1442
Cdd:COG4988 526 ILITHRLALLAQADRILVLDDGRIVEQGTHEELLA 560
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1217-1452 |
1.34e-74 |
|
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: 248.67 E-value: 1.34e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1217 GEITICNLQVRYGPHLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRL 1296
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1297 SIIPQDPTMFEGTIRSNLDPLEEYTDDQIWEALDNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKL 1376
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30682479 1377 LVLDEATASIDTATDNLIQETLRHHFADCTVITIAHRISSVIDSDMVLLLDQGLIKEHDSPARLLEDRSSLFSKLV 1452
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLV 253
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
902-1194 |
4.90e-70 |
|
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: 237.37 E-value: 4.90e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 902 LILVVQVLFQLLSIGSNYWMT-WVTPVSKDVEPPVSGFTL---ILVYVLLAVASSFCILIRALLVAMTGFKMATELFTQM 977
Cdd:cd18604 3 LLLLLFVLSQLLSVGQSWWLGiWASAYETSSALPPSEVSVlyyLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHERL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 978 HLRIFRASMSFFDATPMGRILNRASTDQSVADLRLPGQFAYVAIAAINILGIIGVIVQVAWQVLIVFIPVVAACAWYRQY 1057
Cdd:cd18604 83 LHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1058 YISAARELARLAGISRSPVVHHFSETLSGITTIRSFDQEPRFRGDIMRLSDCYSRLKFHSTGAMEWLCFRLELLSTFAFA 1137
Cdd:cd18604 163 YLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALFSF 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 30682479 1138 SSLVILVSAPegVINPSLAGLAITYALNLNTLQATLIWTLCDLENKMISVERMLQYT 1194
Cdd:cd18604 243 ATAALLVYGP--GIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
288-575 |
4.36e-67 |
|
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: 228.51 E-value: 4.36e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 288 LSALLAFVYTVSCYVAPYLMDNFVQYLNGNRQYKNQGYVLVTTFFVAKLVECQTQRQWFFRGQKAGLGMRSVLVSMIYEK 367
Cdd:cd18595 1 LAALLKLLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 368 GLTLPCHSKQGHTSGEIINLMAVDADRISAFSWFMHDPWILVLQVSLALWILYKSLGLGSIAAFPATILVMLANYPFAKL 447
Cdd:cd18595 81 ALRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 448 EEKFQSSLMKSKDNRMKKTSEVLLNMKILKLQGWEMKFLSKILELRHIEAGWLKKFVYnSSAINSVLW-AAPSFISATAF 526
Cdd:cd18595 161 IKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAY-LNAVSSFLWtCAPFLVSLATF 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 30682479 527 GACLLL--KIPLESGKILAALATFRILQGPIYKLPETISMIVQTKVSLNRI 575
Cdd:cd18595 240 ATYVLSdpDNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
902-1194 |
9.14e-66 |
|
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: 225.05 E-value: 9.14e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 902 LILVVQVLFQLLSIGSNYWMT-WVTPVSKDVEPPVSGFTL-ILVYVLLAVASSFCILIRALLVAMTGFKMATELFTQMHL 979
Cdd:cd18603 3 LILLLYLLSQAFSVGSNIWLSeWSDDPALNGTQDTEQRDYrLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHNKLLH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 980 RIFRASMSFFDATPMGRILNRASTDQSVADLRLPGQFAYVAIAAINILGIIGVIVQVAWQVLIVFIPVVAACAWYRQYYI 1059
Cdd:cd18603 83 NILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQRFYV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1060 SAARELARLAGISRSPVVHHFSETLSGITTIRSFDQEPRFRGDIMRLSDCYSRLKFHSTGAMEWLCFRLELLSTFA-FAS 1138
Cdd:cd18603 163 ATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLIvLFA 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 30682479 1139 SLVILVSapEGVINPSLAGLAITYALNLNtlqATLIW---TLCDLENKMISVERMLQYT 1194
Cdd:cd18603 243 ALFAVLS--RDSLSPGLVGLSISYALQIT---QTLNWlvrMTSELETNIVSVERIKEYS 296
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
900-1194 |
2.91e-64 |
|
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: 220.42 E-value: 2.91e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 900 IPLILVVQVLFQLLSIGSNYWMTWVTpvskDVEPPVSGFTLILVYVLLAVASSFCILIRALLVAMTGFKMATELFTQMHL 979
Cdd:cd18606 1 LPLLLLLLILSQFAQVFTNLWLSFWT----EDFFGLSQGFYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 980 RIFRASMSFFDATPMGRILNRASTDQSVADLRLPGQFAYVAIAAINILGIIG-VIVQVAWqVLIVFIPVVAACAWYRQYY 1058
Cdd:cd18606 77 RVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFIlIIIYLPW-FAIALPPLLVLYYFIANYY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1059 ISAARELARLAGISRSPVVHHFSETLSGITTIRSFDQEPRFRGDIMRLSDCYSRLKFHSTGAMEWLCFRLELL-STFAFA 1137
Cdd:cd18606 156 RASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLgSLLVLI 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 30682479 1138 SSLVILVSApeGVINPSLAGLAITYALNLNTLQATLIWTLCDLENKMISVERMLQYT 1194
Cdd:cd18606 236 VALLCVTRR--FSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHYA 290
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
902-1194 |
3.49e-64 |
|
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: 220.48 E-value: 3.49e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 902 LILVVQVLFQLLSIGSNYWMT-WVTPVSKDVEPPVSGFTL--ILVYVLLAVASSFCILIRALLVAMTGFKMATELFTQMH 978
Cdd:cd18605 3 LILLSLILMQASRNLIDFWLSyWVSHSNNSFFNFINDSFNffLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 979 LRIFRASMSFFDATPMGRILNRASTDQSVADLRLPGQFAYVAIAAINILGIIGVIVQVAWQVLIVFIPVVAACAWYRQYY 1058
Cdd:cd18605 83 SSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQRYY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1059 ISAARELARLAGISRSPVVHHFSETLSGITTIRSFDQEPRFRGDIMRLSDCYSRLKFHSTGAMEWLCFRLELLS--TFAF 1136
Cdd:cd18605 163 RATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGvlIVTF 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 30682479 1137 ASSLVILVSAPEGVINPSLAGLAITYALNLNTLQATLIWTLCDLENKMISVERMLQYT 1194
Cdd:cd18605 243 VALTAVVQHFFGLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1217-1444 |
1.34e-62 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 213.24 E-value: 1.34e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1217 GEITICNLQVRYGPHLPmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRL 1296
Cdd:cd03254 1 GEIEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1297 SIIPQDPTMFEGTIRSNLDPLEEY-TDDQIWEALDNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSK 1375
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNaTDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30682479 1376 LLVLDEATASIDTATDNLIQETLRHHFADCTVITIAHRISSVIDSDMVLLLDQGLIKEHDSPARLLEDR 1444
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
995-1444 |
4.56e-62 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 223.10 E-value: 4.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 995 GRILNRASTD-QSVAD--LRLpgqFAYVAIAAINILGIIGVIVQVAWQ----------VLIVFIPVVAACAWYRqyyisA 1061
Cdd:COG4987 112 GDLLNRLVADvDALDNlyLRV---LLPLLVALLVILAAVAFLAFFSPAlalvlalgllLAGLLLPLLAARLGRR-----A 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1062 ARELARLAGISRSpvvhHFSETLSGITTIRSFDQEPRFRGDIMRLSDCYSRLKFHS---TGAMEWLcfrLELLSTFAFAS 1138
Cdd:COG4987 184 GRRLAAARAALRA----RLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLarlSALAQAL---LQLAAGLAVVA 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1139 SLVILVSA-PEGVINPSLAGLAITYALNLNTLQATLIWTLCDLENKMISVERMLQytnIPSEPPLVIETTRPEKSwPSRG 1217
Cdd:COG4987 257 VLWLAAPLvAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNE---LLDAPPAVTEPAEPAPA-PGGP 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1218 EITICNLQVRYGPHLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLS 1297
Cdd:COG4987 333 SLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIA 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1298 IIPQDPTMFEGTIRSNL---DPleEYTDDQIWEALDNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRS 1374
Cdd:COG4987 413 VVPQRPHLFDTTLRENLrlaRP--DATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDA 490
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1375 KLLVLDEATASIDTATDNLIQETLRHHFADCTVITIAHRISSVIDSDMVLLLDQGLIKEHDSPARLLEDR 1444
Cdd:COG4987 491 PILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQN 560
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
288-575 |
1.12e-61 |
|
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: 213.51 E-value: 1.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 288 LSALLAFVYTVSCYVAPYLMDNFVQYL-NGNRQYKNQGYVLVTTFFVAKLVECQTQRQWFFRGQKAGLGMRSVLVSMIYE 366
Cdd:cd18596 1 LQALLAVLSSVLSFAPPFFLNRLLRYLeDPGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 367 KGLTLPCHS-------------------KQGHTSGEIINLMAVDADRISAFSWFMHDPWILVLQVSLALWILYKSLGLGS 427
Cdd:cd18596 81 KALRRRDKSgssksseskkkdkeededeKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 428 IAAFPATILVMLANYPFAKLEEKFQSSLMKSKDNRMKKTSEVLLNMKILKLQGWEMKFLSKILELRHIEAGWLKKFVYNS 507
Cdd:cd18596 161 LVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLD 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30682479 508 SAINSVLWAAPSFISATAFGA-CLLLKIPLESGKILAALATFRILQGPIYKLPETISMIVQTKVSLNRI 575
Cdd:cd18596 241 LLLSLLWFLIPILVTVVTFATyTLVMGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1219-1429 |
2.21e-58 |
|
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: 198.76 E-value: 2.21e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSI 1298
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1299 IPQDPTMFEGTIRSNLdpleeytddqiwealdncqlgdevrkkelkldspvsengqnWSVGQRQLVCLGRVLLKRSKLLV 1378
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 30682479 1379 LDEATASIDTATDNLIQETLRHHFADCTVITIAHRISSVIDSDMVLLLDQG 1429
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
902-1194 |
5.49e-57 |
|
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: 200.14 E-value: 5.49e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 902 LILVVQVLFQLLSIGSNYWMT-W----------VTPVSKDVEPPVSGFTLILVYVLLAVASSFCILIRALLVAMTGFKMA 970
Cdd:cd18602 3 LVLALALLKQGLRVATDFWLAdWteanhdvasvVFNITSSSLEDDEVSYYISVYAGLSLGAVILSLVTNLAGELAGLRAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 971 TELFTQMHLRIFRASMSFFDATPMGRILNRASTDQSVADLRLPGQFAYVAIAAINILGIIGVIVQVAWQVLIVFIPVVAA 1050
Cdd:cd18602 83 RRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIIIV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1051 CAWYRQYYISAARELARLAGISRSPVVHHFSETLSGITTIRSFDQEPRFRGDIMRLSD----CYSRLkfhsTGAMEWLCF 1126
Cdd:cd18602 163 YYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDrnntAFLFL----NTANRWLGI 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30682479 1127 RLELL-STFAFASSLVILVSAPEGVINPSLAGLAITYALNLNTLQATLIWTLCDLENKMISVERMLQYT 1194
Cdd:cd18602 239 RLDYLgAVIVFLAALSSLTAALAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEYT 307
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
601-800 |
1.02e-56 |
|
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: 196.01 E-value: 1.02e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 601 VEISNGTFSWddSSPIPTLRDMNFKVSQGMNVAICGTVGSGKSSLLSSILGEVPKISGNL-----------------KVC 663
Cdd:cd03290 1 VQVTNGYFSW--GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 664 GRKAYIAQSPWIQSGKVEENILFGKPMEREWYDRVLEACSLNKDLEILPFHDQTVIGERGINLSGGQKQRIQIARALYQD 743
Cdd:cd03290 79 YSVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 30682479 744 ADIYLFDDPFSAVDAHTGSHLFKEVLLGLLR--HKTVIYVTHQVEFLPEADLILVMKDG 800
Cdd:cd03290 159 TNIVFLDDPFSALDIHLSDHLMQEGILKFLQddKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
939-1451 |
1.40e-56 |
|
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: 207.26 E-value: 1.40e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 939 TLILVYVLLAVASSFCILIRALLVAMTGFKMATELFTQMHLRIFRASMSFFDATPMGRILNRASTDQsvadlrlpGQFAY 1018
Cdd:TIGR02203 55 WVPLVVIGLAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDS--------EQVAS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1019 VAIAAI--------NILGIIGVIVQVAWQVLIVFIPVVAACAWYRQYYISAARELARLAGISRSPVVHHFSETLSGITTI 1090
Cdd:TIGR02203 127 AATDAFivlvretlTVIGLFIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1091 RSFDQEPRFRGDIMRLSDCYSRLKFHSTGAMEWLCFRLELLSTFAFAssLVILVSAPEGVINPSLAGLAITYALNLNTLQ 1170
Cdd:TIGR02203 207 KLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASLALA--VVLFIALFQAQAGSLTAGDFTAFITAMIALI 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1171 ATlIWTLCDLENKMisvERMLQ-----YTNIPSEPPLVIETTRPEKSwpsRGEITICNLQVRYGPHLPMVLHGLTCTFPG 1245
Cdd:TIGR02203 285 RP-LKSLTNVNAPM---QRGLAaaeslFTLLDSPPEKDTGTRAIERA---RGDVEFRNVTFRYPGRDRPALDSISLVIEP 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1246 GLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSIIPQDPTMFEGTIRSNL--DPLEEYTDD 1323
Cdd:TIGR02203 358 GETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIayGRTEQADRA 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1324 QIWEALDNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTATDNLIQETLRHHFA 1403
Cdd:TIGR02203 438 EIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ 517
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 30682479 1404 DCTVITIAHRISSVIDSDMVLLLDQGLIKEHDSPARLLeDRSSLFSKL 1451
Cdd:TIGR02203 518 GRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELL-ARNGLYAQL 564
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
266-828 |
5.00e-55 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 202.70 E-value: 5.00e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 266 ERRITTFKLIKALFLSVWRDIVLSALLAFVYTVSCYVAPYLMDNFVQYLNGNRQYkNQGYVLVTTFFVAKLVE--CQ-TQ 342
Cdd:COG1132 3 KSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDL-SALLLLLLLLLGLALLRalLSyLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 343 RQWFFR-GQKAGLGMRSvlvsMIYEKGLTLP--CHSKqgHTSGEIINLMAVDADRIS-AFSWFMHDPWILVLQVSLALWI 418
Cdd:COG1132 82 RYLLARlAQRVVADLRR----DLFEHLLRLPlsFFDR--RRTGDLLSRLTNDVDAVEqFLAHGLPQLVRSVVTLIGALVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 419 LYK---SLGLGSIAAFPATILVMlanYPFAKLEEKFQSSLMKSKDNRMKKTSEVLLNMKILK---LQGWEM-KFLSKILE 491
Cdd:COG1132 156 LFVidwRLALIVLLVLPLLLLVL---RLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKafgREERELeRFREANEE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 492 LRHIEAGWLKKFVYNSSAINSVLWAApsFISATAFGACLLLKIPLESGKILAALATFRILQGPIYKLPETISMIVQTKVS 571
Cdd:COG1132 233 LRRANLRAARLSALFFPLMELLGNLG--LALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALAS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 572 LNRIASFLCLDDLQQDVVGRLPSGSSEMAVEISNGTFSWDDSSPIptLRDMNFKVSQGMNVAICGTvgsgkssllssilg 651
Cdd:COG1132 311 AERIFELLDEPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPV--LKDISLTIPPGETVALVGP-------------- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 652 evpkiSG-------NLkVCG------------------------RK--AYIAQSPWIQSGKVEENILFGKP---MEREWy 695
Cdd:COG1132 375 -----SGsgkstlvNL-LLRfydptsgrilidgvdirdltleslRRqiGVVPQDTFLFSGTIRENIRYGRPdatDEEVE- 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 696 dRVLEACSLNKDLEILPFHDQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFkEVLLGLLRH 775
Cdd:COG1132 448 -EAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQ-EALERLMKG 525
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 30682479 776 KTVIYVTHQVEFLPEADLILVMKDGKITQAGKYHEILDSGTDFMELVGAHTEA 828
Cdd:COG1132 526 RTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYRLQFGE 578
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1228-1451 |
1.99e-54 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 190.13 E-value: 1.99e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1228 YGPHLPmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSIIPQDPTMFE 1307
Cdd:cd03253 10 YDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDTVLFN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1308 GTIRSNLdpleEY-----TDDQIWEALDNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEA 1382
Cdd:cd03253 89 DTIGYNI----RYgrpdaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30682479 1383 TASIDTATDNLIQETLRHHFADCTVITIAHRISSVIDSDMVLLLDQGLIKEHDSPARLLEdRSSLFSKL 1451
Cdd:cd03253 165 TSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLA-KGGLYAEM 232
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
902-1194 |
4.99e-54 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 191.62 E-value: 4.99e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 902 LILVVQVLFQLLSIGSNYWMTW-------VTPVSKDVEPPVSGFTL--------ILVYVLLAVASSFCILIRALLVAMTG 966
Cdd:cd18599 7 FVLLLFILSVGSTVFSDWWLSYwlkqgsgNTTNNVDNSTVDSGNISdnpdlnfyQLVYGGSILVILLLSLIRGFVFVKVT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 967 FKMATELFTQMHLRIFRASMSFFDATPMGRILNRASTDQSVADLRLPGQFAYVAIAAINILGIIGVIVQVAWQVLIVFIP 1046
Cdd:cd18599 87 LRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWFLIALIP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1047 VVAACAWYRQYYISAARELARLAGISRSPVVHHFSETLSGITTIRSFDQEPRFRGDIMRLSDCYSRLKFHSTGAMEWLCF 1126
Cdd:cd18599 167 LAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCAMRWLAV 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30682479 1127 RLELLS---TFAFASSLVILvsapEGVINPSLAGLAITYALNLNTL-QATlIWTLCDLENKMISVERMLQYT 1194
Cdd:cd18599 247 RLDILAvliTLITALLVVLL----KGSISPAFAGLALSYALQLSGLfQFT-VRLASETEARFTSVERILEYI 313
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1219-1451 |
1.47e-53 |
|
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: 187.44 E-value: 1.47e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSI 1298
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1299 IPQDPTMFEGTIRSNLD-PLEEYTDDQIWEALDNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLL 1377
Cdd:cd03251 81 VSQDVFLFNDTVAENIAyGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30682479 1378 VLDEATASIDTATDNLIQETLRHHFADCTVITIAHRISSVIDSDMVLLLDQGLIKEHDSPARLLeDRSSLFSKL 1451
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELL-AQGGVYAKL 233
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
935-1444 |
1.77e-53 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 198.40 E-value: 1.77e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 935 VSGftLILVYVLLAVASSFCILIRALLVAMTGFKMATELFTQMHLRIFRASMSFFDATPMGRILNRASTDQSVA-DLrlp 1013
Cdd:PRK10790 64 VAG--LAAAYVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIrDL--- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1014 gqFAYVAIAAINILGIIGVIV--------QVAWQVLIVFIPVVAACAWYRQYYISAAREL-ARLAGISRSpvvhhFSETL 1084
Cdd:PRK10790 139 --YVTVVATVLRSAALIGAMLvamfsldwRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVrAYLADINDG-----FNEVI 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1085 SGITTIRSFDQEPRFrGDIMRLSdcySRLkfHSTGAMEWLcfRLE------LLSTFafaSSLV-----ILVS-APEGVIN 1152
Cdd:PRK10790 212 NGMSVIQQFRQQARF-GERMGEA---SRS--HYMARMQTL--RLDgfllrpLLSLF---SALIlcgllMLFGfSASGTIE 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1153 PSLAGLAITYALNLN------TLQATLiwtlcdLENKMISVERMLQYTNIPSEPplVIETTRPEKSwpsrGEITICNLQV 1226
Cdd:PRK10790 281 VGVLYAFISYLGRLNeplielTTQQSM------LQQAVVAGERVFELMDGPRQQ--YGNDDRPLQS----GRIDIDNVSF 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1227 RYGPHLPmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSIIPQDPTMF 1306
Cdd:PRK10790 349 AYRDDNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVL 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1307 EGTIRSNLDPLEEYTDDQIWEALDNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEATASI 1386
Cdd:PRK10790 428 ADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANI 507
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 30682479 1387 DTATDNLIQETLRHHFADCTVITIAHRISSVIDSDMVLLLDQGLIKEHDSPARLLEDR 1444
Cdd:PRK10790 508 DSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQ 565
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1184-1442 |
6.57e-48 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 181.94 E-value: 6.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1184 MISVERMLQYTNIPSE-------PPLVIettrpekswpSRGEITICNLQVRYGPHLPmVLHGLTCTFPGGLKTGIVGRTG 1256
Cdd:COG5265 326 LADMERMFDLLDQPPEvadapdaPPLVV----------GGGEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSG 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1257 CGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSIIPQDPTMFEGTIRSNLdpleEY-----TDDQIWEALDN 1331
Cdd:COG5265 395 AGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNI----AYgrpdaSEEEVEAAARA 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1332 CQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTATDNLIQETLRHHFADCTVITIA 1411
Cdd:COG5265 471 AQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIA 550
|
250 260 270
....*....|....*....|....*....|.
gi 30682479 1412 HRISSVIDSDMVLLLDQGLIKEHDSPARLLE 1442
Cdd:COG5265 551 HRLSTIVDADEILVLEAGRIVERGTHAELLA 581
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
290-575 |
9.14e-48 |
|
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: 172.74 E-value: 9.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 290 ALLAFVYTVSCYVAPYLMDNFVQYLNGNRQYKNQGYVLVTTFFVAKLVECQTQRQWFFRGQKAGLGMRSVLVSMIYEKGL 369
Cdd:cd18598 3 GLLKLLADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTAVYRKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 370 TLPCHSKQGHTSGEIINLMAVDADRISAFSWFMHDPWILVLQVSLALWILYKSLGLGSIAAFPATILVMLANYPFAKLEE 449
Cdd:cd18598 83 RVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAKRIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 450 KFQSSLMKSKDNRMKKTSEVLLNMKILKLQGWEMKFLSKILELRHIEAGWLKKFVYnSSAINSVLWAA-PSFISATAFGA 528
Cdd:cd18598 163 ALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKY-LDALCVYFWATtPVLISILTFAT 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 30682479 529 CLLLKIPLESGKILAALATFRILQGPIYKLPETISMIVQTKVSLNRI 575
Cdd:cd18598 242 YVLMGNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
896-1194 |
9.34e-48 |
|
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: 173.66 E-value: 9.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 896 GGAVIPLILVVQVLFQLLSIGSNYWMT-WV--------------TPVSKDVEPPVSG--FTLILVYVLLAVASSFCIlIR 958
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSyWAnleeklndttdrvqGENSTNVDIEDLDrdFNLGIYAGLTAATFVFGF-LR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 959 ALLVAMTGFKMATELFTQMHLRIFRASMSFFDATPMGRILNRASTDQSVADLRLPGQFAYVAIAAINILGIIGVIVQVAW 1038
Cdd:cd18601 80 SLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1039 QVLIVFIPVVAACAWYRQYYISAARELARLAGISRSPVVHHFSETLSGITTIRSFDQEPRFRGDIMRLSDCYSRLKFHST 1118
Cdd:cd18601 160 WVLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1119 GAMEWLCFRLELLST-FAFASSLVILVSAPEgvINPSLAGLAITYALnlnTLQATLIWTL---CDLENKMISVERMLQYT 1194
Cdd:cd18601 240 ATSRWLAVRLDALCAlFVTVVAFGSLFLAES--LDAGLVGLSLSYAL---TLMGTFQWCVrqsAEVENLMTSVERVLEYS 314
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1217-1447 |
1.84e-47 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 171.58 E-value: 1.84e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1217 GEITICNLQVRYGPHLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEpAAGEIRIDGINILSIGLHDLRSRL 1296
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1297 SIIPQDPTMFEGTIRSNLDPLEEYTDDQIWEALDNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKL 1376
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30682479 1377 LVLDEATASIDTATDNLIQETLRHHFADCTVITIAHRISSVIDSDMVLLLDQGLIKEHDSPARLLEDRSSL 1447
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1219-1452 |
3.79e-46 |
|
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: 166.18 E-value: 3.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYgPHLP--MVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRL 1296
Cdd:cd03249 1 IEFKNVSFRY-PSRPdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1297 SIIPQDPTMFEGTIRSNLD-PLEEYTDDQIWEALDNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSK 1375
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIRyGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30682479 1376 LLVLDEATASIDTATDNLIQETLRHHFADCTVITIAHRISSVIDSDMVLLLDQGLIKEHDSPARLLEdRSSLFSKLV 1452
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMA-QKGVYAKLV 235
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
256-822 |
4.33e-46 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 178.49 E-value: 4.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 256 FRSKLEWDDGERRITTFKLIKALFLSVWRDIVLSALLAFVYTVSCYVAPYLMDNFVQYLNGNRQYkNQGYVLVTTFFVAK 335
Cdd:COG2274 128 LEPTPEFDKRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDL-STLWVLAIGLLLAL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 336 LVEC--QTQRQWFFR--GQKAGLGMRSvlvsMIYEKGLTLPCHSKQGHTSGEIINLMAvDADRI-SAFSWFMHDPWILVL 410
Cdd:COG2274 207 LFEGllRLLRSYLLLrlGQRIDLRLSS----RFFRHLLRLPLSFFESRSVGDLASRFR-DVESIrEFLTGSLLTALLDLL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 411 QVSLALWILYK---SLGLGSIAAFPATILVMLA-NYPFAKLEEKfqssLMKSKDNRMKKTSEVLLNMKILKLQGWEMKFL 486
Cdd:COG2274 282 FVLIFLIVLFFyspPLALVVLLLIPLYVLLGLLfQPRLRRLSRE----ESEASAKRQSLLVETLRGIETIKALGAESRFR 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 487 SKILEL--RHIEAGwlkkfvYNSSAINSVLWAAPSFISATAFGACLLLKIPL-ESGKI-LAALATFRILQG----PIYKL 558
Cdd:COG2274 358 RRWENLlaKYLNAR------FKLRRLSNLLSTLSGLLQQLATVALLWLGAYLvIDGQLtLGQLIAFNILSGrflaPVAQL 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 559 PETISMIVQTKVSLNRIASFLCLDDLQQDVVGRLPSGSSEMAVEISNGTFSWDDSSPiPTLRDMNFKVSQGMNVAICG-- 636
Cdd:COG2274 432 IGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRLKGDIELENVSFRYPGDSP-PVLDNISLTIKPGERVAIVGrs 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 637 -----TVGsgkssllssilgevpKI--------SGNLKVCG-----------RK--AYIAQSPWIQSGKVEENILFGKP- 689
Cdd:COG2274 511 gsgksTLL---------------KLllglyeptSGRILIDGidlrqidpaslRRqiGVVLQDVFLFSGTIRENITLGDPd 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 690 MEREWYDRVLEACSLNKDLEILPFHDQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHlFKEVL 769
Cdd:COG2274 576 ATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAI-ILENL 654
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 30682479 770 LGLLRHKTVIYVTHQVEFLPEADLILVMKDGKITQAGKYHEILDSGTDFMELV 822
Cdd:COG2274 655 RRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELV 707
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1019-1426 |
1.80e-45 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 173.24 E-value: 1.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1019 VAIAAINIlgIIGVIVQVAWQVLIVFIPVV---AACAWYRQYyisaaRELARLAGisrspvvhHFSETLSGITTIRSFDQ 1095
Cdd:TIGR02857 137 AAVFPQDW--ISGLILLLTAPLIPIFMILIgwaAQAAARKQW-----AALSRLSG--------HFLDRLRGLPTLKLFGR 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1096 EPRFRGDIMRLSDCYS-------RLKFHSTGAMEWLC------------FRLeLLSTFAFASSLVILVSAPEgVINP--- 1153
Cdd:TIGR02857 202 AKAQAAAIRRSSEEYRertmrvlRIAFLSSAVLELFAtlsvalvavyigFRL-LAGDLDLATGLFVLLLAPE-FYLPlrq 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1154 -------SLAGLAityalNLNTLQATLiwtlcdlenkmisvermlqytnipSEPPLVIETTRPeKSWPSRGEITICNLQV 1226
Cdd:TIGR02857 280 lgaqyhaRADGVA-----AAEALFAVL------------------------DAAPRPLAGKAP-VTAAPASSLEFSGVSV 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1227 RYgPHLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSIIPQDPTMF 1306
Cdd:TIGR02857 330 AY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLF 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1307 EGTIRSNL---DPleEYTDDQIWEALDNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEAT 1383
Cdd:TIGR02857 409 AGTIAENIrlaRP--DASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPT 486
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 30682479 1384 ASIDTATDNLIQETLRHHFADCTVITIAHRISSVIDSDMVLLL 1426
Cdd:TIGR02857 487 AHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
287-575 |
7.33e-45 |
|
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: 164.55 E-value: 7.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 287 VLSALLAFVYTVscyVAPYLMD---NFVQ--YLNGNRQYKNQGYVLVTTFFVAKLVECQTQRQWFFRGQKAGLGMRSVLV 361
Cdd:cd18597 3 GLLKLLADVLQV---LSPLLLKyliNFVEdaYLGGPPPSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 362 SMIYEKGLTLPCHSKQGHTSGEIINLMAVDADRISAFSWFMHDPWILVLQVSLALWILYKSLGLGSIAAFpATILVMLA- 440
Cdd:cd18597 80 KAIYRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGI-GVLILSIPl 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 441 -NYPFAKLeEKFQSSLMKSKDNRMKKTSEVLLNMKILKLQGWEMKFLSKILELRHIEAGWLKKFVYNSSAINSVLWAAPS 519
Cdd:cd18597 159 qGFLMKKL-FKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 30682479 520 FISATAFGACLLLKIPLESGKILAALATFRILQGPIYKLPETISMIVQTKVSLNRI 575
Cdd:cd18597 238 LASMLSFITYYATGHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1217-1431 |
9.96e-43 |
|
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: 155.83 E-value: 9.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1217 GEITICNLQVRYGPHLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRL 1296
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1297 SIIPQDPTMFEGTIRSNL---DPleEYTDDQIWEALDNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKR 1373
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNItlgAP--LADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 30682479 1374 SKLLVLDEATASIDTATDNLIQETLRHHFADCTVITIAHRISSVIDSDMVLLLDQGLI 1431
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
617-818 |
1.25e-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: 157.71 E-value: 1.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 617 PTLRDMNFKVSQGMNVAICGTVGSGKSSLLSSILGEVPKISGNLKVCGRKAYIAQSPWIQSGKVEENILFGKPMEREWYD 696
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 697 RVLEACSLNKDLEILPFHDQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEVLLGLLRHK 776
Cdd:cd03291 131 SVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANK 210
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 30682479 777 TVIYVTHQVEFLPEADLILVMKDGKITQAGKYHEILDSGTDF 818
Cdd:cd03291 211 TRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDF 252
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
288-575 |
1.31e-41 |
|
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: 155.86 E-value: 1.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 288 LSALLAFVYTVSCYVAPYLMDNFVQYLNGNRQYKNQ------------------GYVLVTTFFVAKLVECQTQRQWFFRG 349
Cdd:cd18591 1 LGGILKLLGDLLGFVGPLCISGIVDYVEENTYSSSNstdklsvsyvtveeffsnGYVLAVILFLALLLQATFSQASYHIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 350 QKAGLGMRSVLVSMIYEKGLTLP--CHSKQGHTSGEIINLMAVDADRISAFSWFMHDPWILVLQVSLALWILYKSLGLGS 427
Cdd:cd18591 81 IREGIRLKTALQAMIYEKALRLSswNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 428 IAAFpATILVML-ANYPFAKLEEKFQSSLMKSKDNRMKKTSEVLLNMKILKLQGWEMKFLSKILELRHIEAGWLKKFVYN 506
Cdd:cd18591 161 LIGA-ALILVMTpLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVY 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 507 SSAINSVLWAAPSFISATAFGACLLLK-IPLESGKILAALATFRILQGPIYKLPETISMIVQTKVSLNRI 575
Cdd:cd18591 240 WSLMTFLTQASPILVTLVTFGLYPYLEgEPLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
574-815 |
1.88e-39 |
|
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: 155.69 E-value: 1.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 574 RIASFLCLDDLQQDVVGRLPSGSSEMAVEISNGTFSWDDSSPIptLRDMNFKVSQGMNVAICG-------TVGSGKSSLl 646
Cdd:COG4988 310 KIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPA--LDGLSLTIPPGERVALVGpsgagksTLLNLLLGF- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 647 ssilgeVPKISGNLKVCGRK-------------AYIAQSPWIQSGKVEENILFGKP-MEREWYDRVLEACSLNKDLEILP 712
Cdd:COG4988 387 ------LPPYSGSILINGVDlsdldpaswrrqiAWVPQNPYLFAGTIRENLRLGRPdASDEELEAALEAAGLDEFVAALP 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 713 FHDQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLfKEVLLGLLRHKTVIYVTHQVEFLPEAD 792
Cdd:COG4988 461 DGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEI-LQALRRLAKGRTVILITHRLALLAQAD 539
|
250 260
....*....|....*....|...
gi 30682479 793 LILVMKDGKITQAGKYHEILDSG 815
Cdd:COG4988 540 RILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1219-1453 |
3.39e-39 |
|
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: 146.48 E-value: 3.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSI 1298
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1299 IPQDPTMFEGTIRSNLDPLEEYTD-DQIWEALDNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLL 1377
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSmERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30682479 1378 VLDEATASIDTATDNLIQETLRHHFADCTVITIAHRISSVIDSDMVLLLDQGLIKEHDSPARLLeDRSSLFSKLVA 1453
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELL-AENGLYAYLYQ 235
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
904-1413 |
1.67e-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: 152.51 E-value: 1.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 904 LVVQVLFQLLSIGSNYWMTWVTP--VSKDVE-PPVsgftlilVYVLLAVAS--SFCILiRAL------LVAM-TGFKMAT 971
Cdd:TIGR02868 15 LALAVLLGALALGSAVALLGVSAwlISRAAEmPPV-------LYLSVAAVAvrAFGIG-RAVfrylerLVGHdAALRSLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 972 ELFTQMHLRIFRASMSFFDATPMGRILNRASTD-QSVADLRLPGQFAyVAIAAINILGIIGVIVQVAWQVLIVFIpVVAA 1050
Cdd:TIGR02868 87 ALRVRVYERLARQALAGRRRLRRGDLLGRLGADvDALQDLYVRVIVP-AGVALVVGAAAVAAIAVLSVPAALILA-AGLL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1051 CAWYRQYYISAAreLARLAGISRSPVVHHFS----ETLSGITTIRSFDQEPRFRGDIMRLSDCYSRLkfhSTGAMEWLCF 1126
Cdd:TIGR02868 165 LAGFVAPLVSLR--AARAAEQALARLRGELAaqltDALDGAAELVASGALPAALAQVEEADRELTRA---ERRAAAATAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1127 RLELLSTFAFASSLVILVSAPEGVINPSLAGLAITyALNLNTLQAT-----LIWTLCDLENKMISVERMLQytnIPSEPP 1201
Cdd:TIGR02868 240 GAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLA-VLVLLPLAAFeafaaLPAAAQQLTRVRAAAERIVE---VLDAAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1202 LVIETTRPEKSWPSRGEITICNLQVRYG-PHLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRID 1280
Cdd:TIGR02868 316 PVAEGSAPAAGAVGLGKPTLELRDLSAGyPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1281 GINILSIGLHDLRSRLSIIPQDPTMFEGTIRSNLD-PLEEYTDDQIWEALDNCQLGDEVRKKELKLDSPVSENGQNWSVG 1359
Cdd:TIGR02868 396 GVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRlARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGG 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 30682479 1360 QRQLVCLGRVLLKRSKLLVLDEATASIDTATDNLIQETLRHHFADCTVITIAHR 1413
Cdd:TIGR02868 476 ERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
941-1443 |
1.87e-36 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 148.72 E-value: 1.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 941 ILVYVLLAVASSFciliralLVAMTG--FKMATELFT-QMHLRIFRA----SMSFFDATPMGRILNRASTDQSVADLRLP 1013
Cdd:TIGR00958 204 IFFMCLLSIASSV-------SAGLRGgsFNYTMARINlRIREDLFRSllrqDLGFFDENKTGELTSRLSSDTQTMSRSLS 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1014 GQFAYVAIAAINILGIIGVIVQVAWQ---VLIVFIPVV-AACAWYRQYYISAAREL----ARLAGISRspvvhhfsETLS 1085
Cdd:TIGR00958 277 LNVNVLLRNLVMLLGLLGFMLWLSPRltmVTLINLPLVfLAEKVFGKRYQLLSEELqeavAKANQVAE--------EALS 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1086 GITTIRSFDQE----PRFRGdimRLSDCysrLKFHSTGAMEWLCFrLELLSTFAFASSLVILVSAPEGVINPSLA-GLAI 1160
Cdd:TIGR00958 349 GMRTVRSFAAEegeaSRFKE---ALEET---LQLNKRKALAYAGY-LWTTSVLGMLIQVLVLYYGGQLVLTGKVSsGNLV 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1161 TYAL-------NLNTLQAtlIWTlcDLENKMISVERMLQYTN-IPSEPPLVieTTRPEkswPSRGEITICNLQVRYG--P 1230
Cdd:TIGR00958 422 SFLLyqeqlgeAVRVLSY--VYS--GMMQAVGASEKVFEYLDrKPNIPLTG--TLAPL---NLEGLIEFQDVSFSYPnrP 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1231 HLPmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSIIPQDPTMFEGTI 1310
Cdd:TIGR00958 493 DVP-VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSV 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1311 RSNLD-PLEEYTDDQIWEALDNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTA 1389
Cdd:TIGR00958 572 RENIAyGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAE 651
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 30682479 1390 TDNLIQETLRhhFADCTVITIAHRISSVIDSDMVLLLDQGLIKEHDSPARLLED 1443
Cdd:TIGR00958 652 CEQLLQESRS--RASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMED 703
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1236-1452 |
3.25e-36 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 146.64 E-value: 3.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1236 LHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSIIPQDPTMFEGTIRSNLD 1315
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1316 -PLEEYTDDQIWEALDNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTATDNLI 1394
Cdd:PRK13657 431 vGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKV 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30682479 1395 Q---ETLRHhfaDCTVITIAHRISSVIDSDMVLLLDQGLIKEHDSPARLLeDRSSLFSKLV 1452
Cdd:PRK13657 511 KaalDELMK---GRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELV-ARGGRFAALL 567
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1239-1454 |
2.42e-35 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 143.83 E-value: 2.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1239 LTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVePAAGEIRIDGINILSIGLHDLRSRLSIIPQDPTMFEGTIRSNL---D 1315
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVllgN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1316 PleEYTDDQIWEALDNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTATDNLIQ 1395
Cdd:PRK11174 448 P--DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVM 525
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 30682479 1396 ETLRHHFADCTVITIAHRISSVIDSDMVLLLDQGLIKEHDSPARLLEDrSSLFSKLVAE 1454
Cdd:PRK11174 526 QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQA-GGLFATLLAH 583
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
942-1453 |
3.84e-35 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 144.33 E-value: 3.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 942 LVYVLLAVASSFCILIRALLVamtgFKMAT--ELFTQMHL--RIFRASMSFFDATPMGRILNRAStdqSVADLR--LPGQ 1015
Cdd:TIGR03797 180 LALLAAAVGAAAFQLAQSLAV----LRLETrmDASLQAAVwdRLLRLPVSFFRQYSTGDLASRAM---GISQIRriLSGS 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1016 FAYVAIAAINILGIIGVIVQVAWQ------VLIVFIPVVAACAWYRQyyISAARELARLAGISRSPVVhhfsETLSGITT 1089
Cdd:TIGR03797 253 TLTTLLSGIFALLNLGLMFYYSWKlalvavALALVAIAVTLVLGLLQ--VRKERRLLELSGKISGLTV----QLINGISK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1090 IRSFDQEPRFRGDIMRLsdcYSRLK--FHSTGAMEwlcfrlELLSTF-----AFASSLVI-LVSAPEGVINPSLAG-LAI 1160
Cdd:TIGR03797 327 LRVAGAENRAFARWAKL---FSRQRklELSAQRIE------NLLTVFnavlpVLTSAALFaAAISLLGGAGLSLGSfLAF 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1161 TYALNlNTLQATLiwtlcDLENKMISV-------ERMLqytniP---SEPPLVIETTRPEKSwpsRGEITICNLQVRYGP 1230
Cdd:TIGR03797 398 NTAFG-SFSGAVT-----QLSNTLISIlaviplwERAK-----PileALPEVDEAKTDPGKL---SGAIEVDRVTFRYRP 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1231 HLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSIIPQDPTMFEGTI 1310
Cdd:TIGR03797 464 DGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSI 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1311 RSNLDPLEEYTDDQIWEALDNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTAT 1390
Cdd:TIGR03797 544 FENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRT 623
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30682479 1391 DNLIQETLRHHFAdcTVITIAHRISSVIDSDMVLLLDQGLIKEHDSPARLLEdRSSLFSKLVA 1453
Cdd:TIGR03797 624 QAIVSESLERLKV--TRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMA-REGLFAQLAR 683
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
934-1442 |
2.40e-34 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 140.54 E-value: 2.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 934 PVSGFTLILVYVLLAVASSFCILIRALLVAMtgfkmatelftQMHLRIFRASM----SFFDATPMGRILNRASTD-QSVA 1008
Cdd:PRK11176 68 PLVVIGLMILRGITSFISSYCISWVSGKVVM-----------TMRRRLFGHMMgmpvSFFDKQSTGTLLSRITYDsEQVA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1009 DlrlPGQFAYVAIA--AINILGIIGVIVQVAWQ---VLIVFIPVVAacaWYRQYYISAARELARLAGISRSPVVHHFSET 1083
Cdd:PRK11176 137 S---SSSGALITVVreGASIIGLFIMMFYYSWQlslILIVIAPIVS---IAIRVVSKRFRNISKNMQNTMGQVTTSAEQM 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1084 LSGITTIRSFD----QEPRFR--GDIMRLSDcysrlkfhstgamewlcfrLELLSTFAFASSLVILVSapegvinpSLAG 1157
Cdd:PRK11176 211 LKGHKEVLIFGgqevETKRFDkvSNRMRQQG-------------------MKMVSASSISDPIIQLIA--------SLAL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1158 LAITYALNLNTLQATLI-WTLCDLENKMISVERMLQ-YTNIPSE------------PPLVIETTRPE---KSWPSRGEIT 1220
Cdd:PRK11176 264 AFVLYAASFPSVMDTLTaGTITVVFSSMIALMRPLKsLTNVNAQfqrgmaacqtlfAILDLEQEKDEgkrVIERAKGDIE 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1221 ICNLQVRY-GPHLPmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSII 1299
Cdd:PRK11176 344 FRNVTFTYpGKEVP-ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALV 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1300 PQDPTMFEGTIRSNLD--PLEEYTDDQIWEALDNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLL 1377
Cdd:PRK11176 423 SQNVHLFNDTIANNIAyaRTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPIL 502
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30682479 1378 VLDEATASIDTATDNLIQETLRHHFADCTVITIAHRISSVIDSDMVLLLDQGLIKEHDSPARLLE 1442
Cdd:PRK11176 503 ILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLA 567
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1219-1429 |
1.61e-33 |
|
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: 127.72 E-value: 1.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSI 1298
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1299 IPQDPTMFEGTIRSNLdpleeytddqiwealdncqlgdevrkkelkldspvsengqnWSVGQRQLVCLGRVLLKRSKLLV 1378
Cdd:cd03246 81 LPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 30682479 1379 LDEATASIDTATDNLIQETLRH-HFADCTVITIAHRISSVIDSDMVLLLDQG 1429
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAAlKAAGATRIVIAHRPETLASADRILVLEDG 171
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
364-812 |
1.84e-33 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 137.59 E-value: 1.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 364 IYEKGLTLPCHSKQGHTSGEIINLMAVDADR------------ISAfswfmhdpWILVLQVSLALWILykSLGLGSIAAF 431
Cdd:COG4987 94 LYRRLEPLAPAGLARLRSGDLLNRLVADVDAldnlylrvllplLVA--------LLVILAAVAFLAFF--SPALALVLAL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 432 PATILVMLANYPFAKLEEKFQSSLMKSKDNRMKKTSEVLLNMKILKLQGWEMKFLSKileLRHIEAGWLKKfVYNSSAIN 511
Cdd:COG4987 164 GLLLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALAR---LDAAEARLAAA-QRRLARLS 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 512 SVLWAAPSFISATAFGACLLLKIPL-ESGKI---------LAALATFRILQGpiykLPETISMIVQTKVSLNRIASFLCL 581
Cdd:COG4987 240 ALAQALLQLAAGLAVVAVLWLAAPLvAAGALsgpllallvLAALALFEALAP----LPAAAQHLGRVRAAARRLNELLDA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 582 DDLQQDVVGRLPSgSSEMAVEISNGTFSWDDSSPiPTLRDMNFKVSQGMNVAICG-------TVGSGKSSLlssilgeVP 654
Cdd:COG4987 316 PPAVTEPAEPAPA-PGGPSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGpsgsgksTLLALLLRF-------LD 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 655 KISGNLKVCGRK-------------AYIAQSPWIQSGKVEENILFGKPM---EREWydRVLEACSLNKDLEILPFHDQTV 718
Cdd:COG4987 387 PQSGSITLGGVDlrdldeddlrrriAVVPQRPHLFDTTLRENLRLARPDatdEELW--AALERVGLGDWLAALPDGLDTW 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 719 IGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEvLLGLLRHKTVIYVTHQVEFLPEADLILVMK 798
Cdd:COG4987 465 LGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLAD-LLEALAGRTVLLITHRLAGLERMDRILVLE 543
|
490
....*....|....
gi 30682479 799 DGKITQAGKYHEIL 812
Cdd:COG4987 544 DGRIVEQGTHEELL 557
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1214-1449 |
2.32e-33 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 137.65 E-value: 2.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1214 PSRGEITICNLQVRYGPHLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLR 1293
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1294 SRLSIIPQDPTMFEGTIRSNLD-PLEEYTDDQIWEALDNCQLGDEVRKKElKLDSPVSENGQNWSVGQRQLVCLGRVLLK 1372
Cdd:PRK11160 414 QAISVVSQRVHLFSATLRDNLLlAAPNASDEALIEVLQQVGLEKLLEDDK-GLNAWLGEGGRQLSGGEQRRLGIARALLH 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30682479 1373 RSKLLVLDEATASIDTATDNLIQETLRHHFADCTVITIAHRISSVIDSDMVLLLDQGLIKEHDSPARLLEDRSSLFS 1449
Cdd:PRK11160 493 DAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQ 569
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
1236-1452 |
3.53e-33 |
|
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: 137.33 E-value: 3.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1236 LHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSIIPQDPTMFEGTIRSNLD 1315
Cdd:TIGR01192 351 VFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1316 -PLEEYTDDQIWEALDNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTATDNLI 1394
Cdd:TIGR01192 431 lGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARV 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 30682479 1395 QETLRHHFADCTVITIAHRISSVIDSDMVLLLDQGLIKEHDSPARLLEdRSSLFSKLV 1452
Cdd:TIGR01192 511 KNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQ-KDGRFYKLL 567
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1236-1384 |
1.26e-32 |
|
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: 124.30 E-value: 1.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1236 LHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSIIPQDPTMF-EGTIRSNL 1314
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30682479 1315 -------DPLEEYTDDQIWEALDNCQLGDevrkkelKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEATA 1384
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEKLGLGD-------LADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
289-575 |
1.27e-32 |
|
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: 128.87 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 289 SALLAFVYTVSCYVAPYLMDNFVQYLNGNRQYKNQGYVLVTTFFVAKLVECQTQRQWFFRGQKAGLGMRSVLVSMIYEKG 368
Cdd:cd18559 2 FLLIKLVLCNHVFSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 369 LTLPCHSKQGHTSGEIINLMAVDADRISAFSWFMHDPWILVLQVSLALWILYKSLGLGSIAAFPATILVMLANYPFAKLE 448
Cdd:cd18559 82 LRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 449 EKFQSSLMKSKDNRMKKTSEVLLNMKILKLQGWEMKFLSKILELRHIEAGWLKKFVYNsSAINSVLWAAPSFISATAFGA 528
Cdd:cd18559 162 RQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYL-RALAVRLWCVGPCIVLFASFF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 30682479 529 CLLLK---IPLESGKILAALATFRILQGPIYKLPETISMIVQTKVSLNRI 575
Cdd:cd18559 241 AYVSRhslAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
601-821 |
3.35e-32 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 125.81 E-value: 3.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 601 VEISNGTFSWDDSSPiPTLRDMNFKVSQGMNVAICG-------TVGSGkssllssilgeVPKI----SGNLKVCG----- 664
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGpsgsgksTLVNL-----------IPRFydvdSGRILIDGhdvrd 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 665 ------RK--AYIAQSPWIQSGKVEENILFGKP-MEREWYDRVLEACSLNKDLEILPFHDQTVIGERGINLSGGQKQRIQ 735
Cdd:cd03251 69 ytlaslRRqiGLVSQDVFLFNDTVAENIAYGRPgATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 736 IARALYQDADIYLFDDPFSAVDAHTgSHLFKEVLLGLLRHKTVIYVTHQVEFLPEADLILVMKDGKITQAGKYHEILDSG 815
Cdd:cd03251 149 IARALLKDPPILILDEATSALDTES-ERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQG 227
|
....*.
gi 30682479 816 TDFMEL 821
Cdd:cd03251 228 GVYAKL 233
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1219-1447 |
7.31e-32 |
|
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: 124.75 E-value: 7.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHLPmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSI 1298
Cdd:COG1122 1 IELENLSFSYPGGTP-ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1299 IPQDPT--MFEGTIRS-------NLDPLEEYTDDQIWEALDNCQLGDevrkkelKLDSPVSEngqnWSVGQRQLVCLGRV 1369
Cdd:COG1122 80 VFQNPDdqLFAPTVEEdvafgpeNLGLPREEIRERVEEALELVGLEH-------LADRPPHE----LSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1370 LLKRSKLLVLDEATASIDTATDNLIQETLRH-HFADCTVITIAHRISSVID-SDMVLLLDQGLIKEHDSPARLLEDRSSL 1447
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSDYELL 228
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1230-1431 |
3.89e-31 |
|
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: 122.58 E-value: 3.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1230 PHLPmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSIIPQDPTMFEGT 1309
Cdd:cd03248 25 PDTL-VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFARS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1310 IRSNLD-PLEEYTDDQIWEALDNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDT 1388
Cdd:cd03248 104 LQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 30682479 1389 ATDNLIQETLRHHFADCTVITIAHRISSVIDSDMVLLLDQGLI 1431
Cdd:cd03248 184 ESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
291-575 |
1.64e-30 |
|
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent.
Pssm-ID: 350038 [Multi-domain] Cd Length: 291 Bit Score: 122.74 E-value: 1.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 291 LLAFVYTVSCYVAPYLMDNFVQYLN-GNRQYKNQGYVLVTTFFVAKLVECQTQRQWFFRGQKAGLGMRSVLVSMIYEKGL 369
Cdd:cd18594 4 ILLFLEESLKIVQPLLLGRLVAYFVpDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKKTL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 370 TLPCHSKQGHTSGEIINLMAVDADRISAFSWFMHDPWILVLQVSLALWILYKSLGLGSIAAFPATILVMLANYPFAKLEE 449
Cdd:cd18594 84 KLSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 450 KFQSSLMKSKDNRMKKTSEVLLNMKILKLQGWEMKFLSKILELRHIEAGWLKKFVYNSSAINSVLWAAPSFISATAFGAC 529
Cdd:cd18594 164 KYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPY 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 30682479 530 LLLKIPLESGKILAALATFRILQGPI-YKLPETISMIVQTKVSLNRI 575
Cdd:cd18594 244 VLTGNTLTARKVFTVISLLNALRMTItRFFPESIQTLSESRVSLKRI 290
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
601-815 |
1.98e-30 |
|
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: 120.79 E-value: 1.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 601 VEISNGTFSWDdsSPIPTLRDMNFKVSQGMNVAICG-------TVGSGKSSLLSSILGEVpKISG-NLKVCGRK------ 666
Cdd:cd03254 3 IEFENVNFSYD--EKKPVLKDINFSIKPGETVAIVGptgagktTLINLLMRFYDPQKGQI-LIDGiDIRDISRKslrsmi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 667 AYIAQSPWIQSGKVEENILFGKPMEREwyDRVLEACS-LNKDLEI--LPFHDQTVIGERGINLSGGQKQRIQIARALYQD 743
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATD--EEVIEAAKeAGAHDFImkLPNGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30682479 744 ADIYLFDDPFSAVDAHTGShLFKEVLLGLLRHKTVIYVTHQVEFLPEADLILVMKDGKITQAGKYHEILDSG 815
Cdd:cd03254 158 PKILILDEATSNIDTETEK-LIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
601-821 |
2.87e-30 |
|
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: 120.41 E-value: 2.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 601 VEISNGTFSWDDSSPIptLRDMNFKVSQGMNVAICG-------TVGsgkssllssilgevpKI--------SGNLKVCG- 664
Cdd:cd03253 1 IEFENVTFAYDPGRPV--LKDVSFTIPAGKKVAIVGpsgsgksTIL---------------RLlfrfydvsSGSILIDGq 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 665 ----------RKA--YIAQSPWIQSGKVEENILFGKPMEREwyDRVLEAC---SLNKDLEILPFHDQTVIGERGINLSGG 729
Cdd:cd03253 64 direvtldslRRAigVVPQDTVLFNDTIGYNIRYGRPDATD--EEVIEAAkaaQIHDKIMRFPDGYDTIVGERGLKLSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 730 QKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEvLLGLLRHKTVIYVTHQVEFLPEADLILVMKDGKITQAGKYH 809
Cdd:cd03253 142 EKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAA-LRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHE 220
|
250
....*....|..
gi 30682479 810 EILDSGTDFMEL 821
Cdd:cd03253 221 ELLAKGGLYAEM 232
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1219-1433 |
2.95e-30 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 118.57 E-value: 2.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGlHDLRSRLSI 1298
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1299 IPQDPTMFEGTIRSNLdpleeytddqiwealdncqlgdevrkkelkldspvsenGQNWSVGQRQLVCLGRVLLKRSKLLV 1378
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 30682479 1379 LDEATASIDTATDNLIQETLRHHFADCTVITIAHRISSVIDSDMVLLLDQGLIKE 1433
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1220-1429 |
6.22e-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: 116.58 E-value: 6.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1220 TICNLQVRYGPHLpmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSII 1299
Cdd:cd00267 1 EIENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1300 PQdptmfegtirsnLdpleeytddqiwealdncqlgdevrkkelkldspvsengqnwSVGQRQLVCLGRVLLKRSKLLVL 1379
Cdd:cd00267 79 PQ------------L------------------------------------------SGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 30682479 1380 DEATASIDTATDNLIQETLRHHFAD-CTVITIAHRISSVID-SDMVLLLDQG 1429
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELaADRVIVLKDG 156
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1219-1447 |
1.96e-29 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 124.63 E-value: 1.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAA---GEIRIDGINILSIGLHDLRSR 1295
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1296 LSIIPQDPTmfegtirSNLDPLeeYTDDQIWEALDNCQL-GDEVRKK------ELKLDSPVSENGQNWSVGQRQLVCLGR 1368
Cdd:COG1123 85 IGMVFQDPM-------TQLNPV--TVGDQIAEALENLGLsRAEARARvlelleAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1369 VLLKRSKLLVLDEATASIDTATDNLIQETLR--HHFADCTVITIAHRISSVID-SDMVLLLDQGLIKEHDSPARLLEDRS 1445
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
..
gi 30682479 1446 SL 1447
Cdd:COG1123 236 AL 237
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
601-801 |
4.03e-29 |
|
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: 114.79 E-value: 4.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 601 VEISNGTFSWDDSSPiPTLRDMNFKVSQGMNVAICG-------TVGsgkssllssilgevpKI--------SGNLKVCG- 664
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGpsgsgksTLL---------------KLllrlydptSGEILIDGv 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 665 ----------RK--AYIAQSPWIQSGKVEENILfgkpmerewydrvleacslnkdleilpfhdqtvigerginlSGGQKQ 732
Cdd:cd03228 65 dlrdldleslRKniAYVPQDPFLFSGTIRENIL-----------------------------------------SGGQRQ 103
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30682479 733 RIQIARALYQDADIYLFDDPFSAVDAHTgSHLFKEVLLGLLRHKTVIYVTHQVEFLPEADLILVMKDGK 801
Cdd:cd03228 104 RIAIARALLRDPPILILDEATSALDPET-EALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1219-1440 |
5.16e-29 |
|
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: 116.51 E-value: 5.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHlpMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVE-----PAAGEIRIDGINILSIGLHD-- 1291
Cdd:cd03260 1 IELRDLNVYYGDK--HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1292 LRSRLSIIPQDPTMFEGTIRSNLD--------PLEEYTDDQIWEALDNCQLGDEV--RKKELKLdspvsengqnwSVGQR 1361
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAyglrlhgiKLKEELDERVEEALRKAALWDEVkdRLHALGL-----------SGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1362 QLVCLGRVLLKRSKLLVLDEATASIDTATDNLIQETLRHHFADCTVITIAH------RIssvidSDMVLLLDQGLIKEHD 1435
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHnmqqaaRV-----ADRTAFLLNGRLVEFG 222
|
....*
gi 30682479 1436 SPARL 1440
Cdd:cd03260 223 PTEQI 227
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1219-1450 |
7.10e-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: 116.83 E-value: 7.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGP--HLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRL 1296
Cdd:COG1124 2 LEVRNLSVSYGQggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1297 SIIPQDPtmfegtiRSNLDP-------LEE--------YTDDQIWEALDNCQLGDEVRKK---ELkldspvsengqnwSV 1358
Cdd:COG1124 82 QMVFQDP-------YASLHPrhtvdriLAEplrihglpDREERIAELLEQVGLPPSFLDRyphQL-------------SG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1359 GQRQLVCLGRVLLKRSKLLVLDEATASIDTATD----NLIQETLRHHfaDCTVITIAHRIsSVID--SDMVLLLDQGLIK 1432
Cdd:COG1124 142 GQRQRVAIARALILEPELLLLDEPTSALDVSVQaeilNLLKDLREER--GLTYLFVSHDL-AVVAhlCDRVAVMQNGRIV 218
|
250
....*....|....*...
gi 30682479 1433 EHDSPARLLEDRSSLFSK 1450
Cdd:COG1124 219 EELTVADLLAGPKHPYTR 236
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
271-813 |
1.14e-28 |
|
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: 122.90 E-value: 1.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 271 TFKLIKALFLSVWRDIVLSALLAFVYTVSCYVAPYLMDNFVQYLNGNRqykNQGYVLVTTFFVAKLVECQTQRQWF---F 347
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGR---DRSVLWWVPLVVIGLAVLRGICSFVstyL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 348 RGQKAGLGMRSVLVSMiYEKGLTLPCHSKQGHTSGEIINLMAVDADRISAFSwfmHDPWILVLQ-----VSLALWILYKS 422
Cdd:TIGR02203 78 LSWVSNKVVRDIRVRM-FEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAA---TDAFIVLVRetltvIGLFIVLLYYS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 423 LGLGSIAAFPATILVMLANYpFAKLEEKFQSSLMKSKDNRMKKTSEVLLNMKILKLQGWEMKFLSKILELRHIEAGWLKK 502
Cdd:TIGR02203 154 WQLTLIVVVMLPVLSILMRR-VSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 503 FVYNSSAINSVLwaapSFISATAFGACLLLKI------PLESGKILAALATFRILQGPIYKLPETISMIVQTKVSLNRIA 576
Cdd:TIGR02203 233 MTSAGSISSPIT----QLIASLALAVVLFIALfqaqagSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 577 SFLclDDLQQDVVGRLPSGSSEMAVEISNGTFSWDDSSpIPTLRDMNFKVSQGMNVAICGTVGSGKSSLLSSILGEVPKI 656
Cdd:TIGR02203 309 TLL--DSPPEKDTGTRAIERARGDVEFRNVTFRYPGRD-RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 657 SGNLKVCG-----------RK--AYIAQSPWIQSGKVEENILFGKPME--REWYDRVLEACSLNKDLEILPFHDQTVIGE 721
Cdd:TIGR02203 386 SGQILLDGhdladytlaslRRqvALVSQDVVLFNDTIANNIAYGRTEQadRAEIERALAAAYAQDFVDKLPLGLDTPIGE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 722 RGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLfKEVLLGLLRHKTVIYVTHQVEFLPEADLILVMKDGK 801
Cdd:TIGR02203 466 NGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLV-QAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGR 544
|
570
....*....|..
gi 30682479 802 ITQAGKYHEILD 813
Cdd:TIGR02203 545 IVERGTHNELLA 556
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
711-1452 |
2.71e-28 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 124.37 E-value: 2.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 711 LPFHDQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDaHTGSHLFKEVLLGLL--RHKTVIYVTHQVEFL 788
Cdd:PTZ00265 565 LPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINNLKgnENRITIIIAHRLSTI 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 789 PEADLILVM----------------------------------------KDGKITQAGKY------HEILDSGTDFMELV 822
Cdd:PTZ00265 644 RYANTIFVLsnrergstvdvdiigedptkdnkennnknnkddnnnnnnnNNNKINNAGSYiieqgtHDALMKNKNGIYYT 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 823 GAHTEALATIDSCETG-----------YASEKSTTDKENEVLHHKEKQENGSDNKpSGQLVQEEEREK---GKVGF---- 884
Cdd:PTZ00265 724 MINNQKVSSKKSSNNDndkdsdmkssaYKDSERGYDPDEMNGNSKHENESASNKK-SCKMSDENASENnagGKLPFlrnl 802
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 885 ------------TVYKKYMALAYGGAVIPL-ILVVQVLFQLLSIgsnYWMTWVTPVSK--DVEPPVSGFTLilvYVLLAV 949
Cdd:PTZ00265 803 fkrkpkapnnlrIVYREIFSYKKDVTIIALsILVAGGLYPVFAL---LYAKYVSTLFDfaNLEANSNKYSL---YILVIA 876
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 950 ASSFcilIRALLVAMTGFKMATELFTQMHLRIFR----ASMSFFDATPMGRILNRASTDQSVADLRLPGQFAYVAIAAIN 1025
Cdd:PTZ00265 877 IAMF---ISETLKNYYNNVIGEKVEKTMKRRLFEnilyQEISFFDQDKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFI 953
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1026 ILGIIGVIVQvawqvlIVFIPVVAACAWYrQYYISAaRELARLAGISRSPVVHHFSETLSGITTIRSFDQE----PRFRG 1101
Cdd:PTZ00265 954 VLFLVSMVMS------FYFCPIVAAVLTG-TYFIFM-RVFAIRARLTANKDVEKKEINQPGTVFAYNSDDEifkdPSFLI 1025
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1102 D----------IMRLSDCYSRL-----KFHSTG--------AMEWlCFRLE---LLSTFA--FASSLVILVSAPEGVINP 1153
Cdd:PTZ00265 1026 QeafynmntviIYGLEDYFCNLiekaiDYSNKGqkrktlvnSMLW-GFSQSaqlFINSFAywFGSFLIRRGTILVDDFMK 1104
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1154 SLAGLAIT--YALNLNTLQAtliwtlcDLENKMISVER----MLQYTNIPSEPPLVIettRPEKSWPSRGEITICNLQVR 1227
Cdd:PTZ00265 1105 SLFTFLFTgsYAGKLMSLKG-------DSENAKLSFEKyyplIIRKSNIDVRDNGGI---RIKNKNDIKGKIEIMDVNFR 1174
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1228 Y--GPHLPmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRI------------------------------------ 1269
Cdd:PTZ00265 1175 YisRPNVP-IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtndmtneqdyqgdeeqnvgmk 1253
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1270 ------------------VEPAAGEIRIDGINILSIGLHDLRSRLSIIPQDPTMFEGTIRSNLD-PLEEYTDDQIWEALD 1330
Cdd:PTZ00265 1254 nvnefsltkeggsgedstVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKfGKEDATREDVKRACK 1333
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1331 NCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTATDNLIQETLR--HHFADCTVI 1408
Cdd:PTZ00265 1334 FAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdiKDKADKTII 1413
|
890 900 910 920
....*....|....*....|....*....|....*....|....*....
gi 30682479 1409 TIAHRISSVIDSDMVLLLDQ-----GLIKEHDSPARLLEDRSSLFSKLV 1452
Cdd:PTZ00265 1414 TIAHRIASIKRSDKIVVFNNpdrtgSFVQAHGTHEELLSVQDGVYKKYV 1462
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
574-812 |
5.85e-28 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 120.97 E-value: 5.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 574 RIASFLCLDDLQQDVVGRLPSGSSEMAVEISngTFSWDDSSPiPTLRDMNFKVSQGMNVAICG-------TVGSGKSSLL 646
Cdd:PRK10789 289 RIRAMLAEAPVVKDGSEPVPEGRGELDVNIR--QFTYPQTDH-PALENVNFTLKPGQMLGICGptgsgksTLLSLIQRHF 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 647 SSILGEVPKISGNLKVC------GRKAYIAQSPWIQSGKVEENILFGKP-MEREWYDRVLEACSLNKDLEILPFHDQTVI 719
Cdd:PRK10789 366 DVSEGDIRFHDIPLTKLqldswrSRLAVVSQTPFLFSDTVANNIALGRPdATQQEIEHVARLASVHDDILRLPQGYDTEV 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 720 GERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEvLLGLLRHKTVIYVTHQVEFLPEADLILVMKD 799
Cdd:PRK10789 446 GERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHN-LRQWGEGRTVIISAHRLSALTEASEILVMQH 524
|
250
....*....|...
gi 30682479 800 GKITQAGKyHEIL 812
Cdd:PRK10789 525 GHIAQRGN-HDQL 536
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1223-1443 |
8.59e-28 |
|
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: 119.62 E-value: 8.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1223 NLQVRY---GPHLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIG---LHDLRSRL 1296
Cdd:COG1123 265 NLSKRYpvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRELRRRV 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1297 SIIPQDPT------MfegTIRSNL-DPL-------EEYTDDQIWEALDNCQLGDEVRKK---ELkldspvsengqnwSVG 1359
Cdd:COG1123 345 QMVFQDPYsslnprM---TVGDIIaEPLrlhgllsRAERRERVAELLERVGLPPDLADRyphEL-------------SGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1360 QRQLVCLGRVLLKRSKLLVLDEATASIDTATD----NLIQEtLRHHFaDCTVITIAHRISSVID-SDMVLLLDQGLIKEH 1434
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVSVQaqilNLLRD-LQREL-GLTYLFISHDLAVVRYiADRVAVMYDGRIVED 486
|
....*....
gi 30682479 1435 DSPARLLED 1443
Cdd:COG1123 487 GPTEEVFAN 495
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
658-829 |
1.57e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 119.56 E-value: 1.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 658 GNLKVCG-----------RK--AYIAQSPWIQSGKVEENILFGKP-MEREWYDRVLEACSLNKDLEILPFHDQTVIGERG 723
Cdd:PRK11174 404 GSLKINGielreldpeswRKhlSWVGQNPQLPHGTLRDNVLLGNPdASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQA 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 724 INLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgSHLFKEVLLGLLRHKTVIYVTHQVEFLPEADLILVMKDGKIT 803
Cdd:PRK11174 484 AGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS-EQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIV 562
|
170 180
....*....|....*....|....*.
gi 30682479 804 QAGKYHEILDSGTDFMELVGAHTEAL 829
Cdd:PRK11174 563 QQGDYAELSQAGGLFATLLAHRQEEI 588
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
581-797 |
2.02e-27 |
|
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: 118.54 E-value: 2.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 581 LDDLQQDVVGRLPSGS-SEMAVEISNGTFSWDDSSPIptLRDMNFKVSQGMNVAICGTVGSGKSSLLSSILGEVPKISGN 659
Cdd:TIGR02857 301 LDAAPRPLAGKAPVTAaPASSLEFSGVSVAYPGRRPA--LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGS 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 660 LKVCGRK-------------AYIAQSPWIQSGKVEENILFGKP-MEREWYDRVLEACSLNKDLEILPFHDQTVIGERGIN 725
Cdd:TIGR02857 379 IAVNGVPladadadswrdqiAWVPQHPFLFAGTIAENIRLARPdASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAG 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLfKEVLLGLLRHKTVIYVTHQVEFLPEADLILVM 797
Cdd:TIGR02857 459 LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEV-LEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1219-1454 |
2.77e-27 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 111.69 E-value: 2.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHLpmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSiGLHDLRSRLSI 1298
Cdd:COG1131 1 IEVRGLTKRYGDKT--ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1299 IPQDPTMFEG-TIRSNLD--------PLEEyTDDQIWEALDNCQLGDevrkkelKLDSPVSengqNWSVGQRQLVCLGRV 1369
Cdd:COG1131 78 VPQEPALYPDlTVRENLRffarlyglPRKE-ARERIDELLELFGLTD-------AADRKVG----TLSGGMKQRLGLALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1370 LLKRSKLLVLDEATASIDTATDNLIQETLRHHFAD-CTVItiahrISS-VID-----SDMVLLLDQGLIKEHDSP----A 1438
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLRELAAEgKTVL-----LSThYLEeaerlCDRVAIIDKGRIVADGTPdelkA 220
|
250
....*....|....*.
gi 30682479 1439 RLLEDrssLFSKLVAE 1454
Cdd:COG1131 221 RLLED---VFLELTGE 233
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1219-1441 |
3.67e-27 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 111.72 E-value: 3.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHLpmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINIlsiglHDLRSRLSI 1298
Cdd:COG1121 7 IELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----RRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1299 IPQ----DPTM----FEgTIRSNLDPL---------EEYtdDQIWEALDNCQLGDevrkkelKLDSPVSEngqnWSVGQR 1361
Cdd:COG1121 80 VPQraevDWDFpitvRD-VVLMGRYGRrglfrrpsrADR--EAVDEALERVGLED-------LADRPIGE----LSGGQQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1362 QLVCLGRVLLKRSKLLVLDEATASIDTATDNLIQETLRH-HFADCTVITIAHRISSVID-SDMVLLLDQGLIKeHDSPAR 1439
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRGLVA-HGPPEE 224
|
..
gi 30682479 1440 LL 1441
Cdd:COG1121 225 VL 226
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1219-1441 |
5.29e-27 |
|
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: 111.67 E-value: 5.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHLpmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSI 1298
Cdd:COG1120 2 LEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1299 IPQDPTM-FEGTIR-----------SNLDPLEEYTDDQIWEALDNCQLGDevrkkeLKlDSPVSEngqnWSVGQRQLVCL 1366
Cdd:COG1120 80 VPQEPPApFGLTVRelvalgryphlGLFGRPSAEDREAVEEALERTGLEH------LA-DRPVDE----LSGGERQRVLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1367 GRVLLKRSKLLVLDEATASIDTATDNLIQETLRH--HFADCTVITIAHrissviD-------SDMVLLLDQGLIKEHDSP 1437
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLH------DlnlaaryADRLVLLKDGRIVAQGPP 222
|
....
gi 30682479 1438 ARLL 1441
Cdd:COG1120 223 EEVL 226
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1173-1442 |
1.38e-26 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 116.74 E-value: 1.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1173 LIWTLCDLENKMISVER-MLQYTNIPS---EPPLVIETTRPEKSwpSRGEITICNLQVRYGPHLPMVLHGLTCTFPGGLK 1248
Cdd:PRK10789 266 MIWPMLALAWMFNIVERgSAAYSRIRAmlaEAPVVKDGSEPVPE--GRGELDVNIRQFTYPQTDHPALENVNFTLKPGQM 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1249 TGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSIIPQDPTMFEGTIRSNL---DPleEYTDDQI 1325
Cdd:PRK10789 344 LGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIalgRP--DATQQEI 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1326 WEALDNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTATDNLIQETLRHHFADC 1405
Cdd:PRK10789 422 EHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGR 501
|
250 260 270
....*....|....*....|....*....|....*..
gi 30682479 1406 TVITIAHRISSVIDSDMVLLLDQGLIKEHDSPARLLE 1442
Cdd:PRK10789 502 TVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQ 538
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1219-1442 |
3.50e-26 |
|
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: 108.79 E-value: 3.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPhlPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHdLRSRLSI 1298
Cdd:COG4555 2 IEVENLSKKYGK--VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1299 IPQDPTMFEG-TIRSNLD---PLEEYTDDQIWEALDncqlgdEVRKKeLKLDSPVSENGQNWSVGQRQLVCLGRVLLKRS 1374
Cdd:COG4555 79 LPDERGLYDRlTVRENIRyfaELYGLFDEELKKRIE------ELIEL-LGLEEFLDRRVGELSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30682479 1375 KLLVLDEATASIDTATDNLIQETLRHHFAD--CTVITiAHRISSVID-SDMVLLLDQGLIKEHDSPARLLE 1442
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRALKKEgkTVLFS-SHIMQEVEAlCDRVVILHKGKVVAQGSLDELRE 221
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1223-1431 |
5.62e-26 |
|
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: 107.23 E-value: 5.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1223 NLQVRYGPHLpmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINIlsiglHDLRSRLSIIPQ- 1301
Cdd:cd03235 4 DLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-----EKERKRIGYVPQr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1302 ---DPTmFEGTIR--------SNLDPLEEYTDDQ---IWEALDNCQLGDevrkkelKLDSPVSEngqnWSVGQRQLVCLG 1367
Cdd:cd03235 77 rsiDRD-FPISVRdvvlmglyGHKGLFRRLSKADkakVDEALERVGLSE-------LADRQIGE----LSGGQQQRVLLA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30682479 1368 RVLLKRSKLLVLDEATASIDTATDNLIQETLRH-HFADCTVITIAHRISSVIDS-DMVLLLDQGLI 1431
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYfDRVLLLNRTVV 210
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1223-1429 |
7.60e-26 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 106.78 E-value: 7.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1223 NLQVRYGPHLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSIIPQD 1302
Cdd:cd03225 4 NLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1303 P-TMFegtirSNLDPLEE---------YTDDQIWEALDncQLGDEVRKKELKLDSPvsengQNWSVGQRQLVCLGRVLLK 1372
Cdd:cd03225 84 PdDQF-----FGPTVEEEvafglenlgLPEEEIEERVE--EALELVGLEGLRDRSP-----FTLSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 30682479 1373 RSKLLVLDEATASIDTATDNLIQETLRH-HFADCTVITIAHRISSVID-SDMVLLLDQG 1429
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
600-802 |
8.31e-26 |
|
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: 106.91 E-value: 8.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 600 AVEISNGTFSWDDSsPIPTLRDMNFKVSQGMNVAICGTVGSGKSSLLSSILGEVPKISGNLKVCG-----------RK-- 666
Cdd:cd03245 2 RIEFRNVSFSYPNQ-EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlRRni 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 667 AYIAQSPWIQSGKVEENILFGKPMEREwyDRVLEACSL---NKDLEILPFHDQTVIGERGINLSGGQKQRIQIARALYQD 743
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADD--ERILRAAELagvTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 30682479 744 ADIYLFDDPFSAVDaHTGSHLFKEVLLGLLRHKTVIYVTHQVEFLPEADLILVMKDGKI 802
Cdd:cd03245 159 PPILLLDEPTSAMD-MNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1216-1432 |
1.18e-25 |
|
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: 113.69 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1216 RGEITICNLQVRY-GPHLPmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRS 1294
Cdd:COG4618 328 KGRLSVENLTVVPpGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1295 RLSIIPQDPTMFEGTIRSNLDPLEEYTDDQIWEAldnCQLGDeVRKKELKL----DSPVSENGQNWSVGQRQLVCLGRVL 1370
Cdd:COG4618 407 HIGYLPQDVELFDGTIAENIARFGDADPEKVVAA---AKLAG-VHEMILRLpdgyDTRIGEGGARLSGGQRQRIGLARAL 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30682479 1371 LKRSKLLVLDEATASIDTATDNLIQETLRHHFAD-CTVITIAHRISSVIDSDMVLLLDQGLIK 1432
Cdd:COG4618 483 YGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHRPSLLAAVDKLLVLRDGRVQ 545
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
601-822 |
2.79e-25 |
|
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: 106.08 E-value: 2.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 601 VEISNGTFSWDDSSPIPTLRDMNFKVSQGMNVAICG-------TVGSGKSSLLSSILGEVPkISG----NLKVCGRK--- 666
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGssgcgksTVVSLLERFYDPTSGEIL-LDGvdirDLNLRWLRsqi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 667 AYIAQSPWIQSGKVEENILFGKP-MEREWYDRVLEACSLNKDLEILPFHDQTVIGERGINLSGGQKQRIQIARALYQDAD 745
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIRYGKPdATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30682479 746 IYLFDDPFSAVDAHTgSHLFKEVLLGLLRHKTVIYVTHQVEFLPEADLILVMKDGKITQAGKYHEILDSGTDFMELV 822
Cdd:cd03249 160 ILLLDEATSALDAES-EKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLV 235
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1223-1429 |
8.29e-25 |
|
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: 102.90 E-value: 8.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1223 NLQVRYGPHlpMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSIIPQd 1302
Cdd:cd03214 4 NLSVGYGGR--TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1303 ptmfegtirsnldpleeytddqiweALDNCQLGDevrkkelKLDSPVSEngqnWSVGQRQLVCLGRVLLKRSKLLVLDEA 1382
Cdd:cd03214 81 -------------------------ALELLGLAH-------LADRPFNE----LSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 30682479 1383 TASID----TATDNLIQETLRHHfaDCTVITIAHRISSVID-SDMVLLLDQG 1429
Cdd:cd03214 125 TSHLDiahqIELLELLRRLARER--GKTVVMVLHDLNLAARyADRVILLKDG 174
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
601-822 |
8.74e-25 |
|
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: 104.49 E-value: 8.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 601 VEISNGTFSWDDSSPIpTLRDMNFKVSQGMNVAICGTVGSGKSSLLSSILGEVPKISGNLKVCGRKAYIAQSPWIQ---- 676
Cdd:cd03252 1 ITFEHVRFRYKPDGPV-ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRrqvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 677 ---------SGKVEENILFGKP-MEREwydRVLEACSLNKDLEI---LPFHDQTVIGERGINLSGGQKQRIQIARALYQD 743
Cdd:cd03252 80 vvlqenvlfNRSIRDNIALADPgMSME---RVIEAAKLAGAHDFiseLPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30682479 744 ADIYLFDDPFSAVDAHTgSHLFKEVLLGLLRHKTVIYVTHQVEFLPEADLILVMKDGKITQAGKYHEILDSGTDFMELV 822
Cdd:cd03252 157 PRILIFDEATSALDYES-EHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLY 234
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1219-1401 |
1.00e-24 |
|
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: 103.33 E-value: 1.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHLpmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINIlSIGLHDLRSRLSI 1298
Cdd:COG4133 3 LEAENLSCRRGERL--LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI-RDAREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1299 IPQDPTMFEG-TIRSNLDPL-----EEYTDDQIWEALDNCQLGDEvrkkelkLDSPVSengqNWSVGQRQLVCLGRVLLK 1372
Cdd:COG4133 80 LGHADGLKPElTVRENLRFWaalygLRADREAIDEALEAVGLAGL-------ADLPVR----QLSAGQKRRVALARLLLS 148
|
170 180
....*....|....*....|....*....
gi 30682479 1373 RSKLLVLDEATASIDTATDNLIQETLRHH 1401
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIAAH 177
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1216-1432 |
1.06e-24 |
|
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: 110.52 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1216 RGEITICNLQVRYGPHLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSR 1295
Cdd:TIGR01842 314 EGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKH 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1296 LSIIPQDPTMFEGTIRSNLDPLEEYTDDQ-IWEALDNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRS 1374
Cdd:TIGR01842 394 IGYLPQDVELFPGTVAENIARFGENADPEkIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDP 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 30682479 1375 KLLVLDEATASIDTATDNLIQETLRH-HFADCTVITIAHRISSVIDSDMVLLLDQGLIK 1432
Cdd:TIGR01842 474 KLVVLDEPNSNLDEEGEQALANAIKAlKARGITVVVITHRPSLLGCVDKILVLQDGRIA 532
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1219-1434 |
1.26e-24 |
|
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: 103.74 E-value: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHLPMV--LHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDL---R 1293
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1294 SRLSIIPQDPtmfegtiRSNLDPLeeYT-DDQIWEAL-DNCQLGDEVRKKELKLDSPVS-ENGQNW--------SVGQRQ 1362
Cdd:cd03257 82 KEIQMVFQDP-------MSSLNPR--MTiGEQIAEPLrIHGKLSKKEARKEAVLLLLVGvGLPEEVlnryphelSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30682479 1363 LVCLGRVLLKRSKLLVLDEATASIDTATDNLIQETLRH----HfaDCTVITIAHRISSV-IDSDMVLLLDQGLIKEH 1434
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKlqeeL--GLTLLFITHDLGVVaKIADRVAVMYAGKIVEE 227
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
665-822 |
1.28e-24 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 110.56 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 665 RKAYIAQSPWIQSGKVEENILFGKPMEREwyDRVLEACSLNKDLEI---LPFHDQTVIGERGINLSGGQKQRIQIARALY 741
Cdd:TIGR02204 415 RMALVPQDPVLFAASVMENIRYGRPDATD--EEVEAAARAAHAHEFisaLPEGYDTYLGERGVTLSGGQRQRIAIARAIL 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 742 QDADIYLFDDPFSAVDAHTgSHLFKEVLLGLLRHKTVIYVTHQVEFLPEADLILVMKDGKITQAGKYHEILDSGTDFMEL 821
Cdd:TIGR02204 493 KDAPILLLDEATSALDAES-EQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARL 571
|
.
gi 30682479 822 V 822
Cdd:TIGR02204 572 A 572
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
902-1173 |
4.11e-24 |
|
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: 103.88 E-value: 4.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 902 LILVVQVLFQLLSIGSNYWMTWVTPVSKDVEPPVSGFtlILVYVLLAVASSFCILIRALLVAMTGFKMATELFTQMHLRI 981
Cdd:pfam00664 7 LAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVY--SLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 982 FRASMSFFDATPMGRILNRASTD-QSVADLrLPGQFAYVAIAAINILGIIGVIVQVAWQVLIVFIPVVAACAWYRQYYIS 1060
Cdd:pfam00664 85 LRQPMSFFDTNSVGELLSRLTNDtSKIRDG-LGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1061 AARELARLAGISRSPVVHHFSETLSGITTIRSFDQEPRFRGDIMRLSDCYSRLKFHSTGAMEWLCFRLELLSTFAFASSL 1140
Cdd:pfam00664 164 ILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALAL 243
|
250 260 270
....*....|....*....|....*....|....*.
gi 30682479 1141 VI---LVSapEGVINPslaGLAITYALNLNTLQATL 1173
Cdd:pfam00664 244 WFgayLVI--SGELSV---GDLVAFLSLFAQLFGPL 274
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1219-1429 |
1.06e-23 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 99.57 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHLpmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINI--LSIGLHDLRSRL 1296
Cdd:cd03229 1 LELKNVSKRYGQKT--VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdLEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1297 SIIPQDPTMFegtirSNLDpleeytddqiweALDNCQLGdevrkkelkldspvsengqnWSVGQRQLVCLGRVLLKRSKL 1376
Cdd:cd03229 79 GMVFQDFALF-----PHLT------------VLENIALG--------------------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 30682479 1377 LVLDEATASIDTATDNLIQETLRHHFAD--CTVITIAHRISSVID-SDMVLLLDQG 1429
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
680-806 |
2.27e-23 |
|
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: 99.90 E-value: 2.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 680 VEENILFG----KPMEREWYDRVLEACSLnkdLEILPFHDQTVIGerginLSGGQKQRIQIARALYQDADIYLFDDPFSA 755
Cdd:cd03259 89 VAENIAFGlklrGVPKAEIRARVRELLEL---VGLEGLLNRYPHE-----LSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 30682479 756 VDAHTGSHLFKEvLLGLLR--HKTVIYVTH-QVEFLPEADLILVMKDGKITQAG 806
Cdd:cd03259 161 LDAKLREELREE-LKELQRelGITTIYVTHdQEEALALADRIAVMNEGRIVQVG 213
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
668-822 |
9.12e-23 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 105.21 E-value: 9.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 668 YIAQSPWIQSGKVEENILFG-KP-MEREWYDRVLEACSLNKDLEILPFHDQTVIGERGINLSGGQKQRIQIARALYQDAD 745
Cdd:TIGR01193 552 YLPQEPYIFSGSILENLLLGaKEnVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSK 631
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30682479 746 IYLFDDPFSAVDAHTGSHLFKEVLlgLLRHKTVIYVTHQVEFLPEADLILVMKDGKITQAGKYHEILDSGTDFMELV 822
Cdd:TIGR01193 632 VLILDESTSNLDTITEKKIVNNLL--NLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
509-824 |
9.95e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 104.66 E-value: 9.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 509 AINSVLWAAPSFISATA---FGACLLLKIPLESGKILA--ALATFRIlqgpiYKLPETISMIVQTKVSLNRIASFLCLDD 583
Cdd:PRK13657 240 ALASVLNRAASTITMLAilvLGAALVQKGQLRVGEVVAfvGFATLLI-----GRLDQVVAFINQVFMAAPKLEEFFEVED 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 584 LQQDVvgRLPSGSSEM-----AVEISNGTFSWDDSSPipTLRDMNFKVSQGMNVAICGTVGSGKSSLLSSILGEVPKISG 658
Cdd:PRK13657 315 AVPDV--RDPPGAIDLgrvkgAVEFDDVSFSYDNSRQ--GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSG 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 659 NLKVCG-----------RKAyIA---QSPWIQSGKVEENILFGKP--MEREWYdRVLEACSLNKDLEILPFHDQTVIGER 722
Cdd:PRK13657 391 RILIDGtdirtvtraslRRN-IAvvfQDAGLFNRSIEDNIRVGRPdaTDEEMR-AAAERAQAHDFIERKPDGYDTVVGER 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 723 GINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLfKEVLLGLLRHKTVIYVTHQVEFLPEADLILVMKDGKI 802
Cdd:PRK13657 469 GRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKV-KAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRV 547
|
330 340
....*....|....*....|..
gi 30682479 803 TQAGKYHEILDSGTDFMELVGA 824
Cdd:PRK13657 548 VESGSFDELVARGGRFAALLRA 569
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1217-1413 |
1.34e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 104.12 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1217 GEITICNLQVRygphLP---MVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRI-DGINILsiglhdl 1292
Cdd:COG4178 361 GALALEDLTLR----TPdgrPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVL------- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1293 rsrlsIIPQDPTMFEGTIRSNL---DPLEEYTDDQIWEALDNCQLGDEVRKkelkLDspvseNGQNW----SVGQRQLVC 1365
Cdd:COG4178 430 -----FLPQRPYLPLGTLREALlypATAEAFSDAELREALEAVGLGHLAER----LD-----EEADWdqvlSLGEQQRLA 495
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 30682479 1366 LGRVLLKRSKLLVLDEATASIDTATDNLIQETLRHHFADCTVITIAHR 1413
Cdd:COG4178 496 FARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1219-1442 |
1.36e-22 |
|
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: 98.51 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHlpMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIG---LHDLRSR 1295
Cdd:COG1127 6 IEVRNLTKSFGDR--VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1296 LSIIPQDPTMFEG-TIRSNLD-PLEEYTD-------DQIWEALDNCQLGDeVRKK---ELkldspvsengqnwSVGQRQL 1363
Cdd:COG1127 84 IGMLFQGGALFDSlTVFENVAfPLREHTDlseaeirELVLEKLELVGLPG-AADKmpsEL-------------SGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1364 VCLGRVLLKRSKLLVLDEATASID----TATDNLIQEtLRHHFaDCTVITIAHRISSVID-SDMVLLLDQGLIKEHDSPA 1438
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDpitsAVIDELIRE-LRDEL-GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPE 227
|
....
gi 30682479 1439 RLLE 1442
Cdd:COG1127 228 ELLA 231
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
288-575 |
1.55e-22 |
|
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: 99.56 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 288 LSALLAFVYTVSCYVAP-YLMDNFVQYLNGNRQYKNQGYVLVTTFFVAKLVECQTQRQWFFRGQKAGLGMRSVLVSMIYE 366
Cdd:cd18592 1 FSILLLLISLIFGFIGPtILIRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 367 KGLTLpcHSKQGHTSGEIINLMAVDADRIsaFSWFMHDPWILVLQVSLALWILYKSLGLGSIAAfpATILVMLANYPF-- 444
Cdd:cd18592 81 KILRL--RSLGDKSVGELINIFSNDGQRL--FDAAVFGPLVIGGPVVLILGIVYSTYLLGPWAL--LGMLVFLLFYPLqa 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 445 --AKLEEKFQSSLMKSKDNRMKKTSEVLLNMKILKLQGWEMKFLSKILELRHIEAGWLKKFVYNSSAINSVLWAAPSFIS 522
Cdd:cd18592 155 fiAKLTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIAS 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 30682479 523 ATAFGACLLLKIPLESGKILAALATFRILQGPIYKLPETISMIVQTKVSLNRI 575
Cdd:cd18592 235 VVTFLAHVALGNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
899-1193 |
1.79e-22 |
|
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: 100.26 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 899 VIPLILVVQVLFQLLSIGSNYWMTWVTP--VSKDVEPPVSGFT--LILVYVLLAVASSFCIL--IRALLVAMTGFKMATE 972
Cdd:cd18600 25 VIFAIEVAASLVGLWLLRSQADRVNTTRpeSSSNTYAVIVTFTssYYVFYIYVGVADSLLAMgfFRGLPLVHTLITVSKT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 973 LFTQMHLRIFRASMSFFDATPMGRILNRASTDQSVADLRLP-GQFAYVAIAAInILGIIGVIVQVAWQVLIVFIPVVAAC 1051
Cdd:cd18600 105 LHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPlTIFDFIQLFLI-VIGAITVVSILQPYIFLATVPVIIAF 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1052 AWYRQYYISAARELARLAGISRSPVVHHFSETLSGITTIRSFDQEPRFRGDIMRLSDCYSRLKFHSTGAMEWLCFRLELL 1131
Cdd:cd18600 184 IVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMI 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30682479 1132 STFAFasSLVILVSAPEGVINPSLAGLAITYALN-LNTLQATlIWTLCDLENKMISVERMLQY 1193
Cdd:cd18600 264 FVIFF--TAVTFISIGTTGDGEGRVGIILTLAMNiMSTLQWA-VNTSIDVDSLMRSVSRIFKF 323
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1219-1431 |
2.02e-22 |
|
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: 95.93 E-value: 2.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHlpMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGlHDLRSRLSI 1298
Cdd:cd03230 1 IEVRNLSKRYGKK--TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1299 IPQDPTMFEG-TIRSNLDpleeYtddqiwealdncqlgdevrkkelkldspvsengqnwSVGQRQLVCLGRVLLKRSKLL 1377
Cdd:cd03230 78 LPEEPSLYENlTVRENLK----L------------------------------------SGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 30682479 1378 VLDEATASIDTATDNLIQETLRHHFAD-CTVITIAHRISSVID-SDMVLLLDQGLI 1431
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKEgKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
596-814 |
3.41e-22 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 97.47 E-value: 3.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 596 SSEMAVEISNGTFSWDDSspiPTLRDMNFKVSQGMNVAICG-----------TVGSgkssllssilgEVPKISGNLKVCG 664
Cdd:COG1121 2 MMMPAIELENLTVSYGGR---PVLEDVSLTIPPGEFVAIVGpngagkstllkAILG-----------LLPPTSGTVRLFG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 665 RK--------AYIAQSPWIQSG---KVEENILFG--------KPMEREWYDRVLEAcsLnKDLEILPFHDQTvIGErgin 725
Cdd:COG1121 68 KPprrarrriGYVPQRAEVDWDfpiTVRDVVLMGrygrrglfRRPSRADREAVDEA--L-ERVGLEDLADRP-IGE---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgshlfKEVLLGLLRH-----KTVIYVTHQVEFLPE-ADLILVMKD 799
Cdd:COG1121 140 LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAAT-----EEALYELLRElrregKTILVVTHDLGAVREyFDRVLLLNR 214
|
250
....*....|....*
gi 30682479 800 GKITqAGKYHEILDS 814
Cdd:COG1121 215 GLVA-HGPPEEVLTP 228
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1233-1429 |
3.67e-22 |
|
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: 96.00 E-value: 3.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1233 PMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLfrivepaAGEIRidginiLSIGLHDLRSRLSIIPQDPTMFEGTIRS 1312
Cdd:cd03250 18 SFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL-------LGELE------KLSGSVSVPGSIAYVSQEPWIQNGTIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1313 NLDPLEEYTDDQIWEALDNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTAT-D 1391
Cdd:cd03250 85 NILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVgR 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 30682479 1392 NLIQETLRHHFADC-TVITIAHRISSVIDSDMVLLLDQG 1429
Cdd:cd03250 165 HIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
526-821 |
4.64e-22 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 102.90 E-value: 4.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 526 FGACLLLKIPLESGKILAalatFRILQG----PIYKLPETISMIVQTKVSLNRIASFLClDDLQQDVVGRLPSGSSEMAV 601
Cdd:TIGR01846 382 FGAHLVIGGALSPGQLVA----FNMLAGrvtqPVLRLAQLWQDFQQTGIALERLGDILN-SPTEPRSAGLAALPELRGAI 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 602 EISNGTFSWDDSSPiPTLRDMNFKVSQGMNVAICGTVGSGKSSLLSSILGEVPKISGNLKVCGRKAYIAQSPWIQ----- 676
Cdd:TIGR01846 457 TFENIRFRYAPDSP-EVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRrqmgv 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 677 --------SGKVEENILFGKPMEREwyDRVLEACSLNKDLEI---LPFHDQTVIGERGINLSGGQKQRIQIARALYQDAD 745
Cdd:TIGR01846 536 vlqenvlfSRSIRDNIALCNPGAPF--EHVIHAAKLAGAHDFiseLPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPR 613
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30682479 746 IYLFDDPFSAVDAHTgSHLFKEVLLGLLRHKTVIYVTHQVEFLPEADLILVMKDGKITQAGKYHEILDSGTDFMEL 821
Cdd:TIGR01846 614 ILIFDEATSALDYES-EALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARL 688
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
401-812 |
6.74e-22 |
|
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: 101.66 E-value: 6.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 401 FMHDPWILVLqvSLALWILYKSLGLgsIAAFPATILVMLAnypfaKLEEKF-QSSLMKSKDNRMKKTSEV---LLNMKIL 476
Cdd:TIGR01842 123 FFDAPWMPIY--LLVCFLLHPWIGI--LALGGAVVLVGLA-----LLNNRAtKKPLKEATEASIRANNLAdsaLRNAEVI 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 477 KLQGWeMKFLSKILELRHIEAgwLKKFVYNSSAINSVLWAAPSF-----ISATAFGACLLLKIPLESGKILAA-LATFRI 550
Cdd:TIGR01842 194 EAMGM-MGNLTKRWGRFHSKY--LSAQSAASDRAGMLSNLSKYFrivlqSLVLGLGAYLAIDGEITPGMMIAGsILVGRA 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 551 LqGPIYKLPETISMIVQTKVSLNRIASFLCLDDLQQDVVgRLPSGSSEMAVEisNGTFSwddsSPI---PTLRDMNFKVS 627
Cdd:TIGR01842 271 L-APIDGAIGGWKQFSGARQAYKRLNELLANYPSRDPAM-PLPEPEGHLSVE--NVTIV----PPGgkkPTLRGISFSLQ 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 628 QGMNVAICGTVGSGKSSLLSSILGEVPKISGNLKVCG-------------RKAYIAQSPWIQSGKVEENIL-FGKPMERE 693
Cdd:TIGR01842 343 AGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGadlkqwdretfgkHIGYLPQDVELFPGTVAENIArFGENADPE 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 694 wydRVLEACSLNKDLE-ILPFHD--QTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEVLL 770
Cdd:TIGR01842 423 ---KIIEAAKLAGVHElILRLPDgyDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKA 499
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 30682479 771 GLLRHKTVIYVTHQVEFLPEADLILVMKDGKITQAGKYHEIL 812
Cdd:TIGR01842 500 LKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVL 541
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1219-1434 |
1.39e-21 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 94.57 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHlpMVLHGLTCTFPGGLkTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGlHDLRSRLSI 1298
Cdd:cd03264 1 LQLENLTKRYGKK--RALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1299 IPQDPTMFEG-TIRSNLDPL-------EEYTDDQIWEALDNCQLGDEVRKKELKLdspvsengqnwSVGQRQLVCLGRVL 1370
Cdd:cd03264 77 LPQEFGVYPNfTVREFLDYIawlkgipSKEVKARVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVGIAQAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30682479 1371 LKRSKLLVLDEATASIDTATdnliQETLRHHF----ADCTVITIAHRISSVIDS-DMVLLLDQGLIKEH 1434
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEE----RIRFRNLLselgEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFE 210
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1219-1437 |
1.47e-21 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 95.26 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHlpMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILS---IGLHDLRSR 1295
Cdd:cd03261 1 IELRGLTKSFGGR--TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1296 LSIIPQDPTMFEG-TIRSNLD-PLEEYT-------DDQIWEALDNCQLGDEVRKK--ELkldspvsengqnwSVGQRQLV 1364
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVAfPLREHTrlseeeiREIVLEKLEAVGLRGAEDLYpaEL-------------SGGMKKRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30682479 1365 CLGRVLLKRSKLLVLDEATASID----TATDNLIQETLRHHfaDCTVITIAHRISSVID-SDMVLLLDQGLIKEHDSP 1437
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLDpiasGVIDDLIRSLKKEL--GLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTP 221
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
288-575 |
2.02e-21 |
|
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: 96.14 E-value: 2.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 288 LSALLAFVYTVSCYVAPYLMDNFVQYLNGNRQ-------YKNQGYVLVTTFFVAklvecQTQRQWFFRGQKAGLGMRSVL 360
Cdd:cd18593 1 LLGIFLFLEEAIRVVQPIFLGKLIRYFEGNGSsislteaYLYAGGVSLCSFLFI-----ITHHPYFFGMQRIGMRLRVAC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 361 VSMIYEKGLTLPCHSKQGHTSGEIINLMAVDADRISAFSWFMHDPWILVLQVSLALWILYKSLGLGSIAAFPATILVMLA 440
Cdd:cd18593 76 SSLIYRKALRLSQAALGKTTVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 441 NYPFAKLEEKFQSSLMKSKDNRMKKTSEVLLNMKILKLQGWEMKFLSKILELRHIEAGWLKKFVYNSSAINSVLWAAPSF 520
Cdd:cd18593 156 QSFFGKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 30682479 521 ISATAFGACLLLKIPLESGKILAALATFRILQGPI-YKLPETISMIVQTKVSLNRI 575
Cdd:cd18593 236 ILFLTFLAYILLGNILTAERVFVTMALYNAVRLTMtLFFPFAIQFGSELSVSIRRI 291
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
541-784 |
3.29e-21 |
|
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: 99.36 E-value: 3.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 541 ILAALATFRILqGPiykLPETISMIVQTKVSLNRIASFLCLDDLQQDVV--GRLPSGSSEMAVEISNGTFSWDDSSPIpt 618
Cdd:TIGR02868 277 VLLPLAAFEAF-AA---LPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSapAAGAVGLGKPTLELRDLSAGYPGAPPV-- 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 619 LRDMNFKVSQGMNVAICGTVGSGKSSLLSSILGEVPKISGNLKVCG-------------RKAYIAQSPWIQSGKVEENIL 685
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGvpvssldqdevrrRVSVCAQDAHLFDTTVRENLR 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 686 FGKP--MEREWYDrVLEACSLNKDLEILPFHDQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSH 763
Cdd:TIGR02868 431 LARPdaTDEELWA-ALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADE 509
|
250 260
....*....|....*....|.
gi 30682479 764 LFkEVLLGLLRHKTVIYVTHQ 784
Cdd:TIGR02868 510 LL-EDLLAALSGRTVVLITHH 529
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1219-1435 |
4.82e-21 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 94.33 E-value: 4.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHLpmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVE--PAA---GEIRIDGINILS--IGLHD 1291
Cdd:COG1117 12 IEVRNLNVYYGDKQ--ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGArveGEILLDGEDIYDpdVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1292 LRSRLSIIPQDPTMFEGTI---------------RSNLDPLEEytddqiwEALDNCQLGDEVrKKELKldspvsENGQNW 1356
Cdd:COG1117 90 LRRRVGMVFQKPNPFPKSIydnvayglrlhgiksKSELDEIVE-------ESLRKAALWDEV-KDRLK------KSALGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1357 SVGQRQLVCLGRVLLKRSKLLVLDEATASID-TATD---NLIQEtLRHHFadcTVITIAH------RIssvidSDMVLLL 1426
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDpISTAkieELILE-LKKDY---TIVIVTHnmqqaaRV-----SDYTAFF 226
|
....*....
gi 30682479 1427 DQGLIKEHD 1435
Cdd:COG1117 227 YLGELVEFG 235
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1082-1426 |
5.80e-21 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 100.49 E-value: 5.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1082 ETLSGITTIRSFDQEPRFRGDIMRLSDCYSR--LKFHSTGAMEWLCFRLELLSTFAFA---SSLVILVSAPEGVINPSLA 1156
Cdd:PTZ00265 241 EALVGIRTVVSYCGEKTILKKFNLSEKLYSKyiLKANFMESLHIGMINGFILASYAFGfwyGTRIIISDLSNQQPNNDFH 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1157 GLAITYALnLNTLQATLIWT--LCDLENKMISVERMLQYTNIPSEPPLViETTRPEKSWPSRGEITICNLQVRYGPHLPM 1234
Cdd:PTZ00265 321 GGSVISIL-LGVLISMFMLTiiLPNITEYMKSLEATNSLYEIINRKPLV-ENNDDGKKLKDIKKIQFKNVRFHYDTRKDV 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1235 VLH-GLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRI-DGINILSIGLHDLRSRLSIIPQDPTMFEGTIRS 1312
Cdd:PTZ00265 399 EIYkDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKN 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1313 N----------LDPLEEY---------------------------------TDDQIWEALDNCQLGDE-----VRKKEL- 1343
Cdd:PTZ00265 479 NikyslyslkdLEALSNYynedgndsqenknkrnscrakcagdlndmsnttDSNELIEMRKNYQTIKDsevvdVSKKVLi 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1344 ---------KLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTATDNLIQETLRHHFADCTVIT--IAH 1412
Cdd:PTZ00265 559 hdfvsalpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITiiIAH 638
|
410
....*....|....
gi 30682479 1413 RISSVIDSDMVLLL 1426
Cdd:PTZ00265 639 RLSTIRYANTIFVL 652
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
680-813 |
1.51e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 95.14 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 680 VEENILFG----KPMEREWYDRVLEACSLnkdLEILPFHDQTViGErginLSGGQKQRIQIARALYQDADIYLFDDPFSA 755
Cdd:COG3839 92 VYENIAFPlklrKVPKAEIDRRVREAAEL---LGLEDLLDRKP-KQ----LSGGQRQRVALGRALVREPKVFLLDEPLSN 163
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30682479 756 VDAHtgshlFKEVLLGLLR--HK----TVIYVTH-QVEFLPEADLILVMKDGKITQAGKYHEILD 813
Cdd:COG3839 164 LDAK-----LRVEMRAEIKrlHRrlgtTTIYVTHdQVEAMTLADRIAVMNDGRIQQVGTPEELYD 223
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
602-802 |
3.66e-20 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 90.67 E-value: 3.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 602 EISNGTFSWDDSspiPTLRDMNFKVSQGMNVAICG-----------TVGSGkssllssilgeVPKISGNLKVCGRK---- 666
Cdd:cd03235 1 EVEDLTVSYGGH---PVLEDVSFEVKPGEFLAIVGpngagkstllkAILGL-----------LKPTSGSIRVFGKPleke 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 667 ----AYIAQSPWIQSG---KVEENIL--------FGKPMEREWYDRVLEACslnKDLEILPFHDQTvIGErginLSGGQK 731
Cdd:cd03235 67 rkriGYVPQRRSIDRDfpiSVRDVVLmglyghkgLFRRLSKADKAKVDEAL---ERVGLSELADRQ-IGE----LSGGQQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30682479 732 QRIQIARALYQDADIYLFDDPFSAVDAHTgshlfKEVLLGLLRH-----KTVIYVTHQVEFLPE-ADLILVMKDGKI 802
Cdd:cd03235 139 QRVLLARALVQDPDLLLLDEPFAGVDPKT-----QEDIYELLRElrregMTILVVTHDLGLVLEyFDRVLLLNRTVV 210
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
725-823 |
6.01e-20 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 93.29 E-value: 6.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 725 NLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEvLLGLLR--HKTVIYVTH-QVEFLPEADLILVMKDGK 801
Cdd:COG1118 133 QLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRW-LRRLHDelGGTTVFVTHdQEEALELADRVVVMNQGR 211
|
90 100
....*....|....*....|....
gi 30682479 802 ITQAGKYHEILDS-GTDF-MELVG 823
Cdd:COG1118 212 IEQVGTPDEVYDRpATPFvARFLG 235
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
377-822 |
9.39e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 95.56 E-value: 9.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 377 QGHTSGEIINLMAVDADRISafSWfmhdpwiLVLQVSLALWILYKSLGLG----------SIAAFPATILVMLANYPFAK 446
Cdd:TIGR00958 253 DENKTGELTSRLSSDTQTMS--RS-------LSLNVNVLLRNLVMLLGLLgfmlwlsprlTMVTLINLPLVFLAEKVFGK 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 447 ----LEEKFQSSLMKSkdNRMKKtsEVLLNMKILKLQGWEMKFLSKILE-LRHI-EAGWLKKFVYNSSAINSVLWAAPSF 520
Cdd:TIGR00958 324 ryqlLSEELQEAVAKA--NQVAE--EALSGMRTVRSFAAEEGEASRFKEaLEETlQLNKRKALAYAGYLWTTSVLGMLIQ 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 521 ISATAFGACLLLKIPLESGKILAALATFRILQGPIYKLPETISMIVQTKVSLNRIASFLclddlqqDVVGRLPSGSSEMA 600
Cdd:TIGR00958 400 VLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYL-------DRKPNIPLTGTLAP 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 601 ------VEISNGTFSWDDSSPIPTLRDMNFKVSQGMNVAICG-------TVGSGKSSLLSSILGEV-----PKISGNLKV 662
Cdd:TIGR00958 473 lnleglIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGpsgsgksTVAALLQNLYQPTGGQVlldgvPLVQYDHHY 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 663 CGRK-AYIAQSPWIQSGKVEENILFG---KPMErEWYDRVLEACSLNKDLEiLPFHDQTVIGERGINLSGGQKQRIQIAR 738
Cdd:TIGR00958 553 LHRQvALVGQEPVLFSGSVRENIAYGltdTPDE-EIMAAAKAANAHDFIME-FPNGYDTEVGEKGSQLSGGQKQRIAIAR 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 739 ALYQDADIYLFDDPFSAVDAHTgshlfkEVLLGLLRH---KTVIYVTHQVEFLPEADLILVMKDGKITQAGKYHEILDSG 815
Cdd:TIGR00958 631 ALVRKPRVLILDEATSALDAEC------EQLLQESRSrasRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
....*..
gi 30682479 816 TDFMELV 822
Cdd:TIGR00958 705 GCYKHLV 711
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
679-820 |
1.21e-19 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 89.67 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 679 KVEENI-----LFGKPMEREwYDRVLEACSLnKDLEILPFHDQTViGErginLSGGQKQRIQIARALYQDADIYLFDDPF 753
Cdd:cd03295 91 TVEENIalvpkLLKWPKEKI-RERADELLAL-VGLDPAEFADRYP-HE----LSGGQQQRVGVARALAADPPLLLMDEPF 163
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 754 SAVDAHTGSHLFKEVL-LGLLRHKTVIYVTHQV-EFLPEADLILVMKDGKITQAGKYHEILDS-GTDFME 820
Cdd:cd03295 164 GALDPITRDQLQEEFKrLQQELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRSpANDFVA 233
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1250-1417 |
1.29e-19 |
|
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: 91.65 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1250 GIVGRTGCGKSTLIQTLFRIVEP---AAGEIRIDGINILSIGLHDLR----SRLSIIPQDPTmfegtirSNLDPLeeYT- 1321
Cdd:COG0444 35 GLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRkirgREIQMIFQDPM-------TSLNPV--MTv 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1322 DDQIWEALDNCQLGD--EVRKK--EL----KLDSPVSENGQ---NWSVGQRQLVCLGRVLLKRSKLLVLDEATasidTAT 1390
Cdd:COG0444 106 GDQIAEPLRIHGGLSkaEARERaiELlervGLPDPERRLDRyphELSGGMRQRVMIARALALEPKLLIADEPT----TAL 181
|
170 180 190
....*....|....*....|....*....|....*
gi 30682479 1391 D--------NLIQEtLRHHFaDCTVITIAHRISSV 1417
Cdd:COG0444 182 DvtiqaqilNLLKD-LQREL-GLAILFITHDLGVV 214
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
596-800 |
1.79e-19 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 89.76 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 596 SSEMAVEISNGTFSWD-DSSPIPTLRDMNFKVSQGMNVAI-----CG--TVGsgkssllssilgevpKI--------SGN 659
Cdd:COG1116 3 AAAPALELRGVSKRFPtGGGGVTALDDVSLTVAAGEFVALvgpsgCGksTLL---------------RLiaglekptSGE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 660 LKVCGRK--------AYIAQS----PWIqsgKVEENILFG-----KPME--REWYDRVLEACSLNKDLEILPFhdqtvig 720
Cdd:COG1116 68 VLVDGKPvtgpgpdrGVVFQEpallPWL---TVLDNVALGlelrgVPKAerRERARELLELVGLAGFEDAYPH------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 721 ergiNLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLfKEVLLGLLR--HKTVIYVTHQVE---FLpeADLIL 795
Cdd:COG1116 138 ----QLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERL-QDELLRLWQetGKTVLFVTHDVDeavFL--ADRVV 210
|
....*
gi 30682479 796 VMKDG 800
Cdd:COG1116 211 VLSAR 215
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1219-1399 |
3.65e-19 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 88.39 E-value: 3.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYgPHLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIG---LHDLRSR 1295
Cdd:cd03256 1 IEVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1296 LSIIPQDPTMFE----------------GTIRS--NLDPLEEYtdDQIWEALDNCQLGDEVRKKELKLdspvsengqnwS 1357
Cdd:cd03256 80 IGMIFQQFNLIErlsvlenvlsgrlgrrSTWRSlfGLFPKEEK--QRALAALERVGLLDKAYQRADQL-----------S 146
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 30682479 1358 VGQRQLVCLGRVLLKRSKLLVLDEATASIDTATDNLIQETLR 1399
Cdd:cd03256 147 GGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLK 188
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
726-801 |
5.64e-19 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 85.37 E-value: 5.64e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGsHLFKEVLLGLL-RHKTVIYVTHQVEFLPEA-DLILVMKDGK 801
Cdd:cd00267 81 LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR-ERLLELLRELAeEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
938-1146 |
5.70e-19 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 89.09 E-value: 5.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 938 FTLILVYVLLAVASSFCILIRALLVAMTGFKMateLFTqMHLRIF----RASMSFFDATPMGRILNRASTD-QSVADLrL 1012
Cdd:cd18546 39 LLAAAAYLAVVLAGWVAQRAQTRLTGRTGERL---LYD-LRLRVFahlqRLSLDFHERETSGRIMTRMTSDiDALSEL-L 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1013 PGQFAYVAIAAINILGIIGVIVQVAWQ----VLIVFIPVVAACAWYRQY----YiSAARELarlagISRspVVHHFSETL 1084
Cdd:cd18546 114 QTGLVQLVVSLLTLVGIAVVLLVLDPRlalvALAALPPLALATRWFRRRssraY-RRARER-----IAA--VNADLQETL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30682479 1085 SGITTIRSFDQEPRFRGDIMRLSDCYSRLKFHSTGAMEWLCFRLELLSTFAFAssLVILVSA 1146
Cdd:cd18546 186 AGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATA--AVLLVGA 245
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1216-1433 |
7.42e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 87.66 E-value: 7.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1216 RGEITICNLQVRYGPhlPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVE--PAA---GEIRIDGINILSIGLH 1290
Cdd:PRK14247 1 MNKIEIRDLKVSFGQ--VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEArvsGEVYLDGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1291 DLRSRLSIIPQDP------TMFE----GTIRSNLDPLEEYTDDQIWEALDNCQLGDEVRKkelKLDSPVSEngqnWSVGQ 1360
Cdd:PRK14247 79 ELRRRVQMVFQIPnpipnlSIFEnvalGLKLNRLVKSKKELQERVRWALEKAQLWDEVKD---RLDAPAGK----LSGGQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30682479 1361 RQLVCLGRVLLKRSKLLVLDEATASIDTATDNLIQETLRHHFADCTVITIAH------RIssvidSDMVLLLDQGLIKE 1433
Cdd:PRK14247 152 QQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRI-----SDYVAFLYKGQIVE 225
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1219-1443 |
9.39e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 88.12 E-value: 9.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSI 1298
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1299 IPQDP-TMFEGTIrsnldpleeyTDDQIWEALDNCQLGDEVRK-------KELKLDSPVSENGQNWSVGQRQLVCLGRVL 1370
Cdd:PRK13632 88 IFQNPdNQFIGAT----------VEDDIAFGLENKKVPPKKMKdiiddlaKKVGMEDYLDKEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30682479 1371 LKRSKLLVLDEATASIDTATDNLIQETLR--HHFADCTVITIAHRISSVIDSDMVLLLDQGLIKEHDSPARLLED 1443
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVdlRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1219-1429 |
1.44e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 87.80 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHLPM---VLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINIL--SIGLHDLR 1293
Cdd:PRK13637 3 IKIENLTHIYMEGTPFekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1294 SRLSIIPQDP--TMFEGTIR-------SNLDPLEEYTDDQIWEALDNCQLGDEvrkkELKLDSPVSENGqnwsvGQRQLV 1364
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEkdiafgpINLGLSEEEIENRVKRAMNIVGLDYE----DYKDKSPFELSG-----GQKRRV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30682479 1365 CLGRVLLKRSKLLVLDEATASIDTATDNLIQETLR--HHFADCTVITIAHRISSVID-SDMVLLLDQG 1429
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKelHKEYNMTIILVSHSMEDVAKlADRIIVMNKG 221
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1219-1435 |
2.13e-18 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 85.26 E-value: 2.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHLpmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHdlRSRLSI 1298
Cdd:cd03259 1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1299 IPQDPTMF-----EGTI----RSNLDPLEEyTDDQIWEALDncQLGDevrkkELKLDSPVSEngqnWSVGQRQLVCLGRV 1369
Cdd:cd03259 77 VFQDYALFphltvAENIafglKLRGVPKAE-IRARVRELLE--LVGL-----EGLLNRYPHE----LSGGQQQRVALARA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30682479 1370 LLKRSKLLVLDEATASIDTATDNLIQETLR--HHFADCTVITIAHRISSVID-SDMVLLLDQGLIKEHD 1435
Cdd:cd03259 145 LAREPSLLLLDEPLSALDAKLREELREELKelQRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
601-806 |
2.72e-18 |
|
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: 85.24 E-value: 2.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 601 VEISNGTFSWDDSSPiPTLRDMNFKVSQGMNVAICG-------TVGSGKSSLLSSILGEVpKISG-NLKVCGRKAY---- 668
Cdd:cd03244 3 IEFKNVSLRYRPNLP-PVLKNISFSIKPGEKVGIVGrtgsgksSLLLALFRLVELSSGSI-LIDGvDISKIGLHDLrsri 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 669 --IAQSPWIQSGKVEENI-LFGkpmerEWYD----RVLEACSLNKDLEILPFHDQTVIGERGINLSGGQKQRIQIARALY 741
Cdd:cd03244 81 siIPQDPVLFSGTIRSNLdPFG-----EYSDeelwQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30682479 742 QDADIYLFDDPFSAVDAHTGSHLfKEVLLGLLRHKTVIYVTHQVEFLPEADLILVMKDGKITQAG 806
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALI-QKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFD 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1235-1431 |
2.94e-18 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 85.23 E-value: 2.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1235 VLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDL----RSRLSIIPQD----PTMf 1306
Cdd:cd03255 19 ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafrRRHIGFVFQSfnllPDL- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1307 egTIRSNLD-PLE------EYTDDQIWEALDNCQLGDEVRKKELKLdspvsengqnwSVGQRQLVCLGRVLLKRSKLLVL 1379
Cdd:cd03255 98 --TALENVElPLLlagvpkKERRERAEELLERVGLGDRLNHYPSEL-----------SGGQQQRVAIARALANDPKIILA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 30682479 1380 DEATASIDTATDNLIQETLR--HHFADCTVITIAHRISSVIDSDMVLLLDQGLI 1431
Cdd:cd03255 165 DEPTGNLDSETGKEVMELLRelNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1223-1443 |
3.54e-18 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 85.18 E-value: 3.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1223 NLQVRYGP-HlpmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDlRSRLSI--I 1299
Cdd:cd03224 5 NLNAGYGKsQ---ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE-RARAGIgyV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1300 PQDPTMFEG-TIRSNLDpLEEYT--DDQIWEALdncqlgDEV-----RKKElKLDSPvsenGQNWSVGQRQLVCLGRVLL 1371
Cdd:cd03224 81 PEGRRIFPElTVEENLL-LGAYArrRAKRKARL------ERVyelfpRLKE-RRKQL----AGTLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30682479 1372 KRSKLLVLDEATASIDTATDNLIQETLRhHFADcTVITI------AHRISSVidSDMVLLLDQGLIKEHDSPARLLED 1443
Cdd:cd03224 149 SRPKLLLLDEPSEGLAPKIVEEIFEAIR-ELRD-EGVTIllveqnARFALEI--ADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
602-801 |
3.78e-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: 84.44 E-value: 3.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 602 EISNGTFSWDDSSPiPTLRDMNFKVSQGMNVAICG-------TVGSGKSSLLssilgevPKISGNLKVCGRKayIAQSPW 674
Cdd:cd03225 1 ELKNLSFSYPDGAR-PALDDISLTIKKGEFVLIVGpngsgksTLLRLLNGLL-------GPTSGEVLVDGKD--LTKLSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 675 IQSGK-----------------VEENILFG---KPMEREWYDR----VLEACSLNKDLEILPFHdqtvigerginLSGGQ 730
Cdd:cd03225 71 KELRRkvglvfqnpddqffgptVEEEVAFGlenLGLPEEEIEErveeALELVGLEGLRDRSPFT-----------LSGGQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30682479 731 KQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFkEVLLGLLR-HKTVIYVTHQVEFLPE-ADLILVMKDGK 801
Cdd:cd03225 140 KQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELL-ELLKKLKAeGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1219-1431 |
3.90e-18 |
|
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: 84.50 E-value: 3.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHLpmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINIL--SIGLHDLRSRL 1296
Cdd:cd03262 1 IEIKNLHKSFGDFH--VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1297 SIIPQDPTMFEgtirsNLDPLEEYTDDQIW-------EALDNC-QLGDEVRKKELKLDSPVSENGqnwsvGQRQLVCLGR 1368
Cdd:cd03262 79 GMVFQQFNLFP-----HLTVLENITLAPIKvkgmskaEAEERAlELLEKVGLADKADAYPAQLSG-----GQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30682479 1369 VLLKRSKLLVLDEATASIDTATDNLIQETLRHHFAD-CTVITIAHRISSVID-SDMVLLLDQGLI 1431
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEgMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
657-827 |
7.16e-18 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 84.34 E-value: 7.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 657 SGNLKVCGRK------------AYIAQSPWIQSG-KVEENI-----LFGKPME--REWYDRVLEACSLNKdleilpfhdq 716
Cdd:COG1131 54 SGEVRVLGEDvardpaevrrriGYVPQEPALYPDlTVRENLrffarLYGLPRKeaRERIDELLELFGLTD---------- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 717 tVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHtGSHLFKEVLLGLLRH-KTVIYVTHQ---VEFLpeAD 792
Cdd:COG1131 124 -AADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPE-ARRELWELLRELAAEgKTVLLSTHYleeAERL--CD 199
|
170 180 190
....*....|....*....|....*....|....*..
gi 30682479 793 LILVMKDGKITQAGKYHEILDSGTD--FMELVGAHTE 827
Cdd:COG1131 200 RVAIIDKGRIVADGTPDELKARLLEdvFLELTGEEAR 236
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
657-797 |
8.90e-18 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 83.68 E-value: 8.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 657 SGNLKVCGRK--------AYIAQS----PWIqsgKVEENILFG----KPMEREWYDRV---LEACSLNKDLEILPfHDqt 717
Cdd:cd03293 58 SGEVLVDGEPvtgpgpdrGYVFQQdallPWL---TVLDNVALGlelqGVPKAEARERAeelLELVGLSGFENAYP-HQ-- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 718 vigerginLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLfKEVLLGLLRH--KTVIYVTHQVE---FLpeAD 792
Cdd:cd03293 132 --------LSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQL-QEELLDIWREtgKTVLLVTHDIDeavFL--AD 200
|
....*
gi 30682479 793 LILVM 797
Cdd:cd03293 201 RVVVL 205
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
680-813 |
1.54e-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: 85.92 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 680 VEENILFG------KPMEREwyDRVLEACSLnkdLEILPFhdqtviGERGIN-LSGGQKQRIQIARALYQDADIYLFDDP 752
Cdd:COG3842 94 VAENVAFGlrmrgvPKAEIR--ARVAELLEL---VGLEGL------ADRYPHqLSGGQQQRVALARALAPEPRVLLLDEP 162
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30682479 753 FSAVDAHTGSHLFKEvLLGLLRH--KTVIYVTH-QVEFLPEADLILVMKDGKITQAGKYHEILD 813
Cdd:COG3842 163 LSALDAKLREEMREE-LRRLQRElgITFIYVTHdQEEALALADRIAVMNDGRIEQVGTPEEIYE 225
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1223-1458 |
1.69e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 84.50 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1223 NLQVRYGPHLPMVLHGLT-CTFP--GGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINIL----SIGLHDLRSR 1295
Cdd:PRK13641 7 NVDYIYSPGTPMEKKGLDnISFEleEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKKLRKK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1296 LSIIPQDP--TMFEGTIRS-------NLDPLEEYTDDQIWEALDNCQLGDEVRKKelkldSPVSENGqnwsvGQRQLVCL 1366
Cdd:PRK13641 87 VSLVFQFPeaQLFENTVLKdvefgpkNFGFSEDEAKEKALKWLKKVGLSEDLISK-----SPFELSG-----GQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1367 GRVLLKRSKLLVLDEATASID-TATDNLIQETLRHHFADCTVITIAHRISSVID-SDMVLLLDQGLIKEHDSPARLLEDR 1444
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDpEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSDK 236
|
250
....*....|....
gi 30682479 1445 SSLFSKLVAEYTTS 1458
Cdd:PRK13641 237 EWLKKHYLDEPATS 250
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1219-1412 |
1.71e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 83.74 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHlpMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVE--PAA---GEIRIDGINILSIGLH--D 1291
Cdd:PRK14267 5 IETVNLRVYYGSN--HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElnEEArveGEVRLFGRNIYSPDVDpiE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1292 LRSRLSIIPQDP------TMFE----GTIRSNLDPLEEYTDDQIWEALDNCQLGDEVrKKELKlDSPvsengQNWSVGQR 1361
Cdd:PRK14267 83 VRREVGMVFQYPnpfphlTIYDnvaiGVKLNGLVKSKKELDERVEWALKKAALWDEV-KDRLN-DYP-----SNLSGGQR 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 30682479 1362 QLVCLGRVLLKRSKLLVLDEATASIDTATDNLIQETLRHHFADCTVITIAH 1412
Cdd:PRK14267 156 QRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
680-806 |
1.81e-17 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 82.69 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 680 VEENILFG----KPMEREWYDRVLEACSLnkdLEIlpfhdQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSA 755
Cdd:cd03301 89 VYDNIAFGlklrKVPKDEIDERVREVAEL---LQI-----EHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 30682479 756 VDAhtgsHLFKEVLLGLLR-HK----TVIYVTH-QVEFLPEADLILVMKDGKITQAG 806
Cdd:cd03301 161 LDA----KLRVQMRAELKRlQQrlgtTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
601-812 |
2.94e-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: 82.38 E-value: 2.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 601 VEISNGTFSWDDSSPIptLRDMNFKVSQGMNVAICG-------TVGsgkssllssilgevpKI--------SGNLKVCGR 665
Cdd:COG1122 1 IELENLSFSYPGGTPA--LDDVSLSIEKGEFVAIIGpngsgksTLL---------------RLlngllkptSGEVLVDGK 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 666 K-------------AYIAQSPWIQ--SGKVEENILFGkPM-----EREWYDRVLEACslnKDLEILPFHDQTVIgergiN 725
Cdd:COG1122 64 DitkknlrelrrkvGLVFQNPDDQlfAPTVEEDVAFG-PEnlglpREEIRERVEEAL---ELVGLEHLADRPPH-----E 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHtGSHLFKEVLLGL-LRHKTVIYVTHQVEFLPE-ADLILVMKDGKIT 803
Cdd:COG1122 135 LSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPR-GRRELLELLKRLnKEGKTVIIVTHDLDLVAElADRVIVLDDGRIV 213
|
....*....
gi 30682479 804 QAGKYHEIL 812
Cdd:COG1122 214 ADGTPREVF 222
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
680-812 |
3.90e-17 |
|
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: 83.08 E-value: 3.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 680 VEENILFG-------KPMEREWYDRVLEACSLNKDLEILPfhDQtvigerginLSGGQKQRIQIARALYQDADIYLFDDP 752
Cdd:cd03294 119 VLENVAFGlevqgvpRAEREERAAEALELVGLEGWEHKYP--DE---------LSGGMQQRVGLARALAVDPDILLMDEA 187
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 753 FSAVDAhtgshLFK----EVLLGLLR--HKTVIYVTHQvefLPEA----DLILVMKDGKITQAGKYHEIL 812
Cdd:cd03294 188 FSALDP-----LIRremqDELLRLQAelQKTIVFITHD---LDEAlrlgDRIAIMKDGRLVQVGTPEEIL 249
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
668-812 |
4.86e-17 |
|
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: 86.34 E-value: 4.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 668 YIAQSPWIQSGKVEENI-LFGKPMErewyDRVLEACSLN--KDLeILPFHD--QTVIGERGINLSGGQKQRIQIARALYQ 742
Cdd:COG4618 410 YLPQDVELFDGTIAENIaRFGDADP----EKVVAAAKLAgvHEM-ILRLPDgyDTRIGEGGARLSGGQRQRIGLARALYG 484
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30682479 743 DADIYLFDDPFSAVDAhTGSHLFKEVLLGL-LRHKTVIYVTHQVEFLPEADLILVMKDGKITQAGKYHEIL 812
Cdd:COG4618 485 DPRLVVLDEPNSNLDD-EGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
286-555 |
5.05e-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: 83.08 E-value: 5.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 286 IVLSALLAFVYTVSCYVAPYLMDNFVQYLNGNRQYKNQGYVLVTTFFVAKLVECQTQrqwFFRGQKAGLGMRSVLVSMIY 365
Cdd:pfam00664 5 ILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQ---SYLLNHTGERLSRRLRRKLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 366 EKGLTLPCHSKQGHTSGEIINLMAVDADRISAFSWFMHDPWILVLQVSLAL--WILYKSLGLgSIAAFPATILVMLANYP 443
Cdd:pfam00664 82 KKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGiiVMFYYGWKL-TLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 444 FAKLEEKFQSSLMKSKDNRMKKTSEVLLNMKILKLQGWEMKFLSKILELRHIE-AGWLKKFVYNsSAINSVLWAAPSFIS 522
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEAlKAGIKKAVAN-GLSFGITQFIGYLSY 239
|
250 260 270
....*....|....*....|....*....|....*
gi 30682479 523 ATA--FGACLLLKIPLESGKILAALATFRILQGPI 555
Cdd:pfam00664 240 ALAlwFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
680-812 |
5.68e-17 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 82.00 E-value: 5.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 680 VEENILFG----KPMEREWYDRVLEacsLNKDLEIlpfhdQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSA 755
Cdd:cd03299 88 VYKNIAYGlkkrKVDKKEIERKVLE---IAEMLGI-----DHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30682479 756 VDAHTGSHLFKEvlLGLLRHK---TVIYVTH-QVEFLPEADLILVMKDGKITQAGKYHEIL 812
Cdd:cd03299 160 LDVRTKEKLREE--LKKIRKEfgvTVLHVTHdFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1219-1461 |
8.48e-17 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 81.58 E-value: 8.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGpHLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSI 1298
Cdd:cd03295 1 IEFENVTKRYG-GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1299 IPQD----PTMfegTIRSN--LDP-LEEYTDDQIwealdncqlgdEVRKKEL--KLDSPVSENGQNW----SVGQRQLVC 1365
Cdd:cd03295 80 VIQQiglfPHM---TVEENiaLVPkLLKWPKEKI-----------RERADELlaLVGLDPAEFADRYphelSGGQQQRVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1366 LGRVLLKRSKLLVLDEATASIDTAT-DNLIQETLR-HHFADCTVITIAHRISSVID-SDMVLLLDQGLIKEHDSPARLLE 1442
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPITrDQLQEEFKRlQQELGKTIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEILR 225
|
250
....*....|....*....
gi 30682479 1443 DRSSLFsklVAEYTTSSES 1461
Cdd:cd03295 226 SPANDF---VAEFVGADRL 241
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
667-802 |
8.94e-17 |
|
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: 80.98 E-value: 8.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 667 AYIAQSPWIQSGKVEENILFGkpMEREWYDRVLEACS-LNKDLEILPFHD--QTVIGERGINLSGGQKQRIQIARALYQD 743
Cdd:cd03248 91 SLVGQEPVLFARSLQDNIAYG--LQSCSFECVKEAAQkAHAHSFISELASgyDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 30682479 744 ADIYLFDDPFSAVDAHTgSHLFKEVLLGLLRHKTVIYVTHQVEFLPEADLILVMKDGKI 802
Cdd:cd03248 169 PQVLILDEATSALDAES-EQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
723-806 |
1.22e-16 |
|
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: 79.28 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 723 GINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFkEVLLGLLRHKTVIYVTHQVEFLPEADLILVMKDGKI 802
Cdd:cd03247 96 GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLL-SLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKI 174
|
....
gi 30682479 803 TQAG 806
Cdd:cd03247 175 IMQG 178
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
597-814 |
1.38e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 81.58 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 597 SEMAVEISNGTFSWDDSSPiPTLRDMNFKVSQGMNVAICG-------TVGSGKSSLLSSILGEVpKISG------NLKVC 663
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSEN-NALKNVSFEINEGEYVAILGhngsgksTISKILTGLLKPQSGEI-KIDGitiskeNLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 664 GRK-AYIAQSPWIQ--SGKVEENILFG---KPMEREWYDRVLEACSLNKDLE-ILPFHDQtvigergiNLSGGQKQRIQI 736
Cdd:PRK13632 82 RKKiGIIFQNPDNQfiGATVEDDIAFGlenKKVPPKKMKDIIDDLAKKVGMEdYLDKEPQ--------NLSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 737 ARALYQDADIYLFDDPFSAVDAhTGSHLFKEVLLGL--LRHKTVIYVTHQVEFLPEADLILVMKDGKITQAGKYHEILDS 814
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDP-KGKREIKKIMVDLrkTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
940-1146 |
1.55e-16 |
|
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: 82.05 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 940 LILVYVLLAVASSFCILIRALLVAMTG----FKMATELFTQMHlrifRASMSFFDATPMGRILNRASTD-QSVADLrlpg 1014
Cdd:cd18544 43 LALLYLGLLLLSFLLQYLQTYLLQKLGqriiYDLRRDLFSHIQ----RLPLSFFDRTPVGRLVTRVTNDtEALNEL---- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1015 qFAYVAIAAIN----ILGIIGVIVQVAWQ---VLIVFIPVVAACAWYRQYYISAARELARLAgISRspVVHHFSETLSGI 1087
Cdd:cd18544 115 -FTSGLVTLIGdlllLIGILIAMFLLNWRlalISLLVLPLLLLATYLFRKKSRKAYREVREK-LSR--LNAFLQESISGM 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30682479 1088 TTIRSFDQEPRFRGDIMRLSDCY--SRLKFHSTGAMewlcFR--LELLSTFAFAssLVILVSA 1146
Cdd:cd18544 191 SVIQLFNREKREFEEFDEINQEYrkANLKSIKLFAL----FRplVELLSSLALA--LVLWYGG 247
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
721-806 |
1.82e-16 |
|
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: 79.02 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 721 ERGIN-LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHlfkevLLGLLRH------KTVIYVTHQVEF-LPEAD 792
Cdd:cd03214 92 DRPFNeLSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIE-----LLELLRRlarergKTVVMVLHDLNLaARYAD 166
|
90
....*....|....
gi 30682479 793 LILVMKDGKITQAG 806
Cdd:cd03214 167 RVILLKDGRIVAQG 180
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
669-812 |
1.95e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 84.49 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 669 IAQSPWIQSGKVEENILFGKPMEREwyDRVLEAcsLNK-DLEILPFHDQ---TVIGERGINLSGGQKQRIQIARALYQDA 744
Cdd:PRK11160 419 VSQRVHLFSATLRDNLLLAAPNASD--EALIEV--LQQvGLEKLLEDDKglnAWLGEGGRQLSGGEQRRLGIARALLHDA 494
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30682479 745 DIYLFDDPFSAVDAHTGSHLFkEVLLGLLRHKTVIYVTHQVEFLPEADLILVMKDGKITQAGKYHEIL 812
Cdd:PRK11160 495 PLLLLDEPTEGLDAETERQIL-ELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELL 561
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
667-816 |
1.98e-16 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 80.86 E-value: 1.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 667 AYIAQSPWIQSG-KVEENILFG--------KPMEREWYDRVLEACSLnkdLEILPFHDQTViGErginLSGGQKQRIQIA 737
Cdd:COG1120 78 AYVPQEPPAPFGlTVRELVALGryphlglfGRPSAEDREAVEEALER---TGLEHLADRPV-DE----LSGGERQRVLIA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 738 RALYQDADIYLFDDPFSAVDAHtgsHLFKevLLGLLRH------KTVIYVTHQVEF-LPEADLILVMKDGKITQAGKYHE 810
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDLA---HQLE--VLELLRRlarergRTVVMVLHDLNLaARYADRLVLLKDGRIVAQGPPEE 224
|
....*.
gi 30682479 811 ILDSGT 816
Cdd:COG1120 225 VLTPEL 230
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1219-1446 |
2.37e-16 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 79.80 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGpHLPMvlhGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDlrsR-LS 1297
Cdd:COG3840 2 LRLDDLTYRYG-DFPL---RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE---RpVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1298 IIPQDPTMFEG-TIRSN----LDPLEEYTDDQ---IWEALDNCQLGD-EVRK-KELkldspvsengqnwSVGQRQLVCLG 1367
Cdd:COG3840 75 MLFQENNLFPHlTVAQNiglgLRPGLKLTAEQraqVEQALERVGLAGlLDRLpGQL-------------SGGQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1368 RVLLKRSKLLVLDEATASIDTATD----NLIQETLRHHFAdcTVITIAHRISSVID-SDMVLLLDQGLIKEHDSPARLLE 1442
Cdd:COG3840 142 RCLVRKRPILLLDEPFSALDPALRqemlDLVDELCRERGL--TVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLD 219
|
....
gi 30682479 1443 DRSS 1446
Cdd:COG3840 220 GEPP 223
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1227-1426 |
3.08e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 78.43 E-value: 3.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1227 RYGPHlpMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGinilsiglhdlRSRLSIIPQ---DP 1303
Cdd:NF040873 1 GYGGR--PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQrseVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1304 TMFEGTIR--------SNLDPLEEYT-DDQ--IWEALDNCQLGD-EVRkkelkldsPVSEngqnWSVGQRQLVCLGRVLL 1371
Cdd:NF040873 68 DSLPLTVRdlvamgrwARRGLWRRLTrDDRaaVDDALERVGLADlAGR--------QLGE----LSGGQRQRALLAQGLA 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 30682479 1372 KRSKLLVLDEATASIDTATDNLIQETLRH-HFADCTVITIAHRISSVIDSDMVLLL 1426
Cdd:NF040873 136 QEADLLLLDEPTTGLDAESRERIIALLAEeHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
717-812 |
3.34e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 83.91 E-value: 3.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 717 TVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDahTGS-HLFKEVLLGLLRHKTVIYVTHQVEFLPEADLIL 795
Cdd:PRK11176 472 TVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALD--TESeRAIQAALDELQKNRTSLVIAHRLSTIEKADEIL 549
|
90
....*....|....*..
gi 30682479 796 VMKDGKITQAGKYHEIL 812
Cdd:PRK11176 550 VVEDGEIVERGTHAELL 566
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
680-806 |
3.39e-16 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 78.88 E-value: 3.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 680 VEENILFGKPMEREWYDRVLEAcslnkdlEILPFHDQTVIGERGI-NLSGGQKQRIQIARALYQDADIYLFDDPFSAVDA 758
Cdd:cd03297 92 VRENLAFGLKRKRNREDRISVD-------ELLDLLGLDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 30682479 759 HTgshlfKEVLLGLLR------HKTVIYVTH---QVEFLpeADLILVMKDGKITQAG 806
Cdd:cd03297 165 AL-----RLQLLPELKqikknlNIPVIFVTHdlsEAEYL--ADRIVVMEDGRLQYIG 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
680-813 |
3.41e-16 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 79.59 E-value: 3.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 680 VEENILFGKPMER----EWYDRVLEACSLNKDLEilpfHDQTVIGErginLSGGQKQRIQIARALYQDADIYLFDDPFSA 755
Cdd:cd03300 89 VFENIAFGLRLKKlpkaEIKERVAEALDLVQLEG----YANRKPSQ----LSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30682479 756 VDAhtgsHLFKEVLLGLLR-HK----TVIYVTH-QVEFLPEADLILVMKDGKITQAGKYHEILD 813
Cdd:cd03300 161 LDL----KLRKDMQLELKRlQKelgiTFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1228-1429 |
3.64e-16 |
|
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: 79.30 E-value: 3.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1228 YGPHLPmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSR----LSIIPQDP 1303
Cdd:cd03290 10 WGSGLA-TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1304 TMFEGTIRSNLDPLEEYTDDQIWEALDNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEAT 1383
Cdd:cd03290 89 WLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 30682479 1384 ASIDT-ATDNLIQETLRHHFAD--CTVITIAHRISSVIDSDMVLLLDQG 1429
Cdd:cd03290 169 SALDIhLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1219-1442 |
3.65e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 80.44 E-value: 3.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSI 1298
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1299 IPQDP-TMFEGTIrsnldpleeyTDDQIWEALDNCQLG------------DEVRKKELKLDSPVSENGqnwsvGQRQLVC 1365
Cdd:PRK13635 86 VFQNPdNQFVGAT----------VQDDVAFGLENIGVPreemvervdqalRQVGMEDFLNREPHRLSG-----GQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30682479 1366 LGRVLLKRSKLLVLDEATASIDTATDNLIQETLRH--HFADCTVITIAHRISSVIDSDMVLLLDQGLIKEHDSPARLLE 1442
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
717-801 |
4.29e-16 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 77.61 E-value: 4.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 717 TVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSH---LFKEV--LLGllrhKTVIYVTHQVEFLPE- 790
Cdd:cd03229 92 TVLENIALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREvraLLKSLqaQLG----ITVVLVTHDLDEAARl 167
|
90
....*....|.
gi 30682479 791 ADLILVMKDGK 801
Cdd:cd03229 168 ADRVVVLRDGK 178
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
680-815 |
4.36e-16 |
|
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: 83.72 E-value: 4.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 680 VEENILFGKP-MEREWYDRVLEACSLNKDLEILPFHDQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDA 758
Cdd:COG5265 448 IAYNIAYGRPdASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDS 527
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 30682479 759 HTgSHLFKEVLLGLLRHKTVIYVTHQVEFLPEADLILVMKDGKITQAGKYHEILDSG 815
Cdd:COG5265 528 RT-ERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQG 583
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
721-803 |
4.86e-16 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 77.08 E-value: 4.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 721 ERGIN----LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKevLLGLLR--HKTVIYVTHQVEFLPE-ADL 793
Cdd:cd03216 74 RAGIAmvyqLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK--VIRRLRaqGVAVIFISHRLDEVFEiADR 151
|
90
....*....|
gi 30682479 794 ILVMKDGKIT 803
Cdd:cd03216 152 VTVLRDGRVV 161
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
680-802 |
5.00e-16 |
|
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: 78.69 E-value: 5.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 680 VEENILFgkPME---------REWYDRVLEACSLNKDLEILPFhdqtvigergiNLSGGQKQRIQIARALYQDADIYLFD 750
Cdd:cd03255 99 ALENVEL--PLLlagvpkkerRERAEELLERVGLGDRLNHYPS-----------ELSGGQQQRVAIARALANDPKIILAD 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 30682479 751 DPFSAVDAHTGS---HLFKEvlLGLLRHKTVIYVTHQVEFLPEADLILVMKDGKI 802
Cdd:cd03255 166 EPTGNLDSETGKevmELLRE--LNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
679-823 |
5.36e-16 |
|
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: 79.13 E-value: 5.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 679 KVEENILF---GKPMEREWYDRVLEacSLNKDLEILPFHDQTVIGerginLSGGQKQRIQIARALYQDADIYLFDDPFSA 755
Cdd:COG4555 90 TVRENIRYfaeLYGLFDEELKKRIE--ELIELLGLEEFLDRRVGE-----LSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30682479 756 VDAHTgSHLFKEVLLGLLRH-KTVIYVTHQVEFLPE-ADLILVMKDGKITQAGKYHEILDSGTD------FMELVG 823
Cdd:COG4555 163 LDVMA-RRLLREILRALKKEgKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIGEenledaFVALIG 237
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1218-1412 |
7.46e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 78.90 E-value: 7.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1218 EITICNLQVRYGPHlpMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLS 1297
Cdd:PRK11231 2 TLRTENLTVGYGTK--RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1298 IIPQDPTMFEG-TIRSnldpLEEY-------------TDDQ--IWEALDNCQLGDEVrkkelklDSPVSEngqnWSVGQR 1361
Cdd:PRK11231 80 LLPQHHLTPEGiTVRE----LVAYgrspwlslwgrlsAEDNarVNQAMEQTRINHLA-------DRRLTD----LSGGQR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 30682479 1362 QLVCLGRVLLKRSKLLVLDEATASIDTATD----NLIQEtLRHhfADCTVITIAH 1412
Cdd:PRK11231 145 QRAFLAMVLAQDTPVVLLDEPTTYLDINHQvelmRLMRE-LNT--QGKTVVTVLH 196
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1220-1432 |
1.00e-15 |
|
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: 77.30 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1220 TICNLQVRYGpHLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINilsIGLHDLRSRLSII 1299
Cdd:cd03226 1 RIENISFSYK-KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP---IKAKERRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1300 PQDPT--MFEGTIRSNLDPLEEYTDDQIWEAldNCQLgdevrkKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLL 1377
Cdd:cd03226 77 MQDVDyqLFTDSVREELLLGLKELDAGNEQA--ETVL------KDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 30682479 1378 VLDEATASIDTATDNLIQETLRHHFA-DCTVITIAHR---ISSVidSDMVLLLDQGLIK 1432
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAAqGKAVIVITHDyefLAKV--CDRVLLLANGAIV 205
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
724-802 |
1.27e-15 |
|
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: 76.28 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 724 INLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgSHLFKEVLLGLLRH-KTVIYVTHQVEFLPE-ADLILVMKDGK 801
Cdd:cd03230 94 LKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPES-RREFWELLRELKKEgKTILLSSHILEEAERlCDRVAILNNGR 172
|
.
gi 30682479 802 I 802
Cdd:cd03230 173 I 173
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1219-1433 |
1.36e-15 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 77.78 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRY--GPHLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDL---- 1292
Cdd:COG1136 5 LELRNLTKSYgtGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1293 RSRLSIIPQD----PTMfegTIRSNLD-PLE------EYTDDQIWEALDNCQLGDEVRKK--ELkldspvsengqnwSVG 1359
Cdd:COG1136 85 RRHIGFVFQFfnllPEL---TALENVAlPLLlagvsrKERRERARELLERVGLGDRLDHRpsQL-------------SGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30682479 1360 QRQLVCLGRVLLKRSKLLVLDEATASIDTATDNLIQETLR--HHFADCTVITIAH--RISSVidSDMVLLLDQGLIKE 1433
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRelNRELGTTIVMVTHdpELAAR--ADRVIRLRDGRIVS 224
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1219-1408 |
1.71e-15 |
|
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: 77.16 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSiGLHDLRSRLSI 1298
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1299 IPQDPTMFEG-TIRSNLD--------PLEEYTDDQIWEaLDNCQLGDevrkkelKLDSPVSengqNWSVGQRQLVCLGRV 1369
Cdd:cd03263 80 CPQFDALFDElTVREHLRfyarlkglPKSEIKEEVELL-LRVLGLTD-------KANKRAR----TLSGGMKRKLSLAIA 147
|
170 180 190
....*....|....*....|....*....|....*....
gi 30682479 1370 LLKRSKLLVLDEATASIDTATDNLIQETLRHHFADCTVI 1408
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSII 186
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1219-1447 |
1.99e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 78.25 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSI 1298
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1299 IPQDP-TMFEGTI---------RSNLDPLEEyTDDQIWEALDncqlgdEVRKKELKLDSPVSENGqnwsvGQRQLVCLGR 1368
Cdd:PRK13648 88 VFQNPdNQFVGSIvkydvafglENHAVPYDE-MHRRVSEALK------QVDMLERADYEPNALSG-----GQKQRVAIAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1369 VLLKRSKLLVLDEATASIDTATD----NLIQETLRHHfaDCTVITIAHRISSVIDSDMVLLLDQGLIKEHDSPARLLEDR 1444
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARqnllDLVRKVKSEH--NITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHA 233
|
...
gi 30682479 1445 SSL 1447
Cdd:PRK13648 234 EEL 236
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1219-1417 |
2.27e-15 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 76.64 E-value: 2.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHLPMV--LHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLhDLRSRL 1296
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPA-EARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1297 SIIPQDPTMFEG-TIRSNLD---PLEEYTDDQIWEALDncQLGDEVRKKELkLDSPVSEngqnWSVGQRQLVCLGRVLLK 1372
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEyfaGLYGLKGDELTARLE--ELADRLGMEEL-LDRRVGG----FSTGMRQKVAIARALVH 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 30682479 1373 RSKLLVLDEATASIDTATDNLIQETLRHHFAD-CTVITIAHRISSV 1417
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEV 199
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1223-1429 |
2.55e-15 |
|
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: 77.09 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1223 NLQVRYGPHLpmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDlRSRLSIIP-- 1300
Cdd:cd03219 5 GLTKRFGGLV--ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHE-IARLGIGRtf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1301 QDPTMFEG-TIRSNLD-----------------PLEEYTDDQIWEALDNCQLGDevrkkelKLDSPVSengqNWSVGQRQ 1362
Cdd:cd03219 82 QIPRLFPElTVLENVMvaaqartgsglllararREEREARERAEELLERVGLAD-------LADRPAG----ELSYGQQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30682479 1363 LVCLGRVLLKRSKLLVLDEATASIDTA-TDNLIQ--ETLRHHfaDCTVITIAHRISSVID-SDMVLLLDQG 1429
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAAGLNPEeTEELAEliRELRER--GITVLLVEHDMDVVMSlADRVTVLDQG 219
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1234-1403 |
2.90e-15 |
|
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: 75.86 E-value: 2.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1234 MVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSIIPQDPTMFEGTIRSN 1313
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1314 LD---PLEEYTDDQIWEALDNCQLGDEVrkkelklDSPVSEngqnWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTAT 1390
Cdd:TIGR01189 94 LHfwaAIHGGAQRTIEDALAAVGLTGFE-------DLPAAQ----LSAGQQRRLALARLWLSRRPLWILDEPTTALDKAG 162
|
170
....*....|...
gi 30682479 1391 DNLIQETLRHHFA 1403
Cdd:TIGR01189 163 VALLAGLLRAHLA 175
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
667-802 |
3.07e-15 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 76.01 E-value: 3.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 667 AYIAQSPWIQSGKVEENILF-----GKPMEREWYDRVLEAcsLNKDLEILpfhDQTVIgergiNLSGGQKQRIQIARALY 741
Cdd:COG4619 77 AYVPQEPALWGGTVRDNLPFpfqlrERKFDRERALELLER--LGLPPDIL---DKPVE-----RLSGGERQRLALIRALL 146
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30682479 742 QDADIYLFDDPFSAVDAHTgSHLFKEVLLGLLRHK--TVIYVTH---QVEFLpeADLILVMKDGKI 802
Cdd:COG4619 147 LQPDVLLLDEPTSALDPEN-TRRVEELLREYLAEEgrAVLWVSHdpeQIERV--ADRVLTLEAGRL 209
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1219-1433 |
3.47e-15 |
|
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: 76.47 E-value: 3.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHLPMV--LHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSI---GLHDLR 1293
Cdd:cd03258 2 IELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLsgkELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1294 SRLSIIPQDPTMFEG-TIRSNLD-PLE------EYTDDQIWEALDNCQLGDEVRKKELKLdspvsengqnwSVGQRQLVC 1365
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVAlPLEiagvpkAEIEERVLELLELVGLEDKADAYPAQL-----------SGGQKQRVG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30682479 1366 LGRVLLKRSKLLVLDEATASIDTATDNLIQETLR--HHFADCTVITIAHRISSVID-SDMVLLLDQGLIKE 1433
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRdiNRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVE 221
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1219-1432 |
4.07e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 76.74 E-value: 4.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHlpMVLHGLTCTF-PGGLkTGIVGRTGCGKSTLIQTLFRI--VEP---AAGEIRIDGINILS--IGLH 1290
Cdd:PRK14239 6 LQVSDLSVYYNKK--KALNSVSLDFyPNEI-TALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIYSprTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1291 DLRSRLSIIPQDPTMFEGTIRSNL----------DplEEYTDDQIWEALDNCQLGDEVrkKELKLDSPVSENGqnwsvGQ 1360
Cdd:PRK14239 83 DLRKEIGMVFQQPNPFPMSIYENVvyglrlkgikD--KQVLDEAVEKSLKGASIWDEV--KDRLHDSALGLSG-----GQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30682479 1361 RQLVCLGRVLLKRSKLLVLDEATASIDTATDNLIQETLRHHFADCTVITIAHRI--SSVIDSDMVLLLDQGLIK 1432
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMqqASRISDRTGFFLDGDLIE 227
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
551-838 |
5.35e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 80.15 E-value: 5.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 551 LQGPIYKLPETISMIVQTKVSLNRIasFLCLDDLQQ---DVVGRLPSGSsemaVEISNGTFSWDDSSPIptLRDMNFKVS 627
Cdd:PRK10790 294 LNEPLIELTTQQSMLQQAVVAGERV--FELMDGPRQqygNDDRPLQSGR----IDIDNVSFAYRDDNLV--LQNINLSVP 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 628 QGMNVAICGTVGSGKSSLLSSILGEVPKISGNLKVCGRK-------------AYIAQSPWIQSGKVEENILFGKPMEREW 694
Cdd:PRK10790 366 SRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPlsslshsvlrqgvAMVQQDPVVLADTFLANVTLGRDISEEQ 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 695 YDRVLEACSLNKDLEILPFHDQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEvlLGLLR 774
Cdd:PRK10790 446 VWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQA--LAAVR 523
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 775 -HKTVIYVTHQVEFLPEADLILVMKDGKITQAGKYHEILDSGTDF-----MELVGahtEALATIDSCETG 838
Cdd:PRK10790 524 eHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYwqmyqLQLAG---EELAASVREEES 590
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1235-1429 |
5.50e-15 |
|
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: 74.89 E-value: 5.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1235 VLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTL--FRIVEPAAGEIRIDGINIlsiGLHDLRSRLSIIPQDpTMFegtirs 1312
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPL---DKRSFRKIIGYVPQD-DIL------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1313 nldpLEEYTddqIWEALDncqlgdevrkkelkldspVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTATDN 1392
Cdd:cd03213 94 ----HPTLT---VRETLM------------------FAAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 30682479 1393 LIQETLRhHFAD--CTVITIAHRISSVIDS--DMVLLLDQG 1429
Cdd:cd03213 149 QVMSLLR-RLADtgRTIICSIHQPSSEIFElfDKLLLLSQG 188
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
917-1193 |
5.96e-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: 77.25 E-value: 5.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 917 SNYWMTwVTPVSKDVEPPVSGFTLILVYVLLAVASSFCILIRALLVAMTGFKMATELFTQMHLRIFRASMSFFDATPMGR 996
Cdd:cd18559 18 SNLWLL-LWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSGE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 997 ILNRASTDQSVADlRLPGQFA-------YVAIAAINILGIIGVIVQVAWQVLIVFIPVvaacawyRQYYISAARELARLA 1069
Cdd:cd18559 97 LVNLFSKDLDRVD-SMAPQVIkmwmgplQNVIGLYLLILLAGPMAAVGIPLGLLYVPV-------NRVYAASSRQLKRLE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1070 GISRSPVVHHFSETLSGITTIRSFDQEPRFrgdIMRLSDCYSRLK--FHSTGAMEWLCFRLELLSTFAFA-SSLVILVSA 1146
Cdd:cd18559 169 SVSKDPRYKLFNETLLGISVIKAFEWEEAF---IRQVDAKRDNELayLPSIVYLRALAVRLWCVGPCIVLfASFFAYVSR 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 30682479 1147 PEgviNPSLAGLAITYALNLNTLQATLIWTLCDLENKMISVERMLQY 1193
Cdd:cd18559 246 HS---LAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLER 289
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
940-1155 |
6.51e-15 |
|
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: 77.21 E-value: 6.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 940 LILVYVLLAVASSFCILIRALLVAMTGFKMATELFTQMHLRIFRASMSFFDATPMGRILNRASTD-QSVADLrLPGQFAY 1018
Cdd:cd07346 41 IALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDvDAVQNL-VSSGLLQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1019 VAIAAINILGIIGVIVQVAWQ---VLIVFIPVVAACAWYrqyYISAARELARLAGISRSPVVHHFSETLSGITTIRSFDQ 1095
Cdd:cd07346 120 LLSDVLTLIGALVILFYLNWKltlVALLLLPLYVLILRY---FRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAA 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1096 EPRFRGDIMRLSDCYSRLKFHSTGAMEWLCFRLELLSTFAFAssLVILVSAPEgVINPSL 1155
Cdd:cd07346 197 EEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTA--LVLLYGGYL-VLQGSL 253
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1219-1431 |
6.67e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 76.25 E-value: 6.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHlpMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDginilSIGLHDLRSRLSI 1298
Cdd:PRK11247 13 LLLNAVSKRYGER--TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-----TAPLAEAREDTRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1299 IPQDptmfegtirSNLDPleeytddqiWEA-LDNCQLG--DEVRKKELKLDSPV--SENGQNW----SVGQRQLVCLGRV 1369
Cdd:PRK11247 86 MFQD---------ARLLP---------WKKvIDNVGLGlkGQWRDAALQALAAVglADRANEWpaalSGGQKQRVALARA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30682479 1370 LLKRSKLLVLDEATASIDTAT----DNLIqETL--RHHFadcTVITIAHRIS-SVIDSDMVLLLDQGLI 1431
Cdd:PRK11247 148 LIHRPGLLLLDEPLGALDALTriemQDLI-ESLwqQHGF---TVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
726-824 |
8.31e-15 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 75.45 E-value: 8.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgshlfKEVLLGLLR------HKTVIYVTH-QVEFLPEADLILVMK 798
Cdd:cd03296 137 LSGGQRQRVALARALAVEPKVLLLDEPFGALDAKV-----RKELRRWLRrlhdelHVTTVFVTHdQEEALEVADRVVVMN 211
|
90 100
....*....|....*....|....*...
gi 30682479 799 DGKITQAGKYHEILDS-GTDF-MELVGA 824
Cdd:cd03296 212 KGRIEQVGTPDEVYDHpASPFvYSFLGE 239
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
286-575 |
9.01e-15 |
|
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: 76.44 E-value: 9.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 286 IVLSALLAFVYTVSCYVAPYLM----DNFVqyLNGNRQYKNQGYVLVTTFFVAKLVeCQTQRQWFFR--GQKAGLGMRSV 359
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTklliDDVI--PAGDLSLLLWIALLLLLLALLRAL-LSYLRRYLAArlGQRVVFDLRRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 360 LvsmiYEKGLTLPCHSKQGHTSGEIINLMAVDADRISAF-SWFMHDPWILVLQVSLALWILYK---SLGLGSIAAFPati 435
Cdd:cd07346 78 L----FRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLvSSGLLQLLSDVLTLIGALVILFYlnwKLTLVALLLLP--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 436 LVMLANYPFAKLEEKFQSSLMKSKDNRMKKTSEVLLNMKILKLQGWEMKFLSKILELRHieagWLKKFVYNSSAINSVLW 515
Cdd:cd07346 151 LYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANR----DLRDANLRAARLSALFS 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30682479 516 AAPSFISATA------FGACLLLKIPLESGKILAALATFRILQGPIYKLPETISMIVQTKVSLNRI 575
Cdd:cd07346 227 PLIGLLTALGtalvllYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1236-1414 |
1.00e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 78.91 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1236 LHGLTCTFPG---------GLKTG----IVGRTGCGKSTLIQTLFRIVEPAAGEIRIDG--INILSIgLHDLRSRLSIIP 1300
Cdd:COG1129 7 MRGISKSFGGvkaldgvslELRPGevhaLLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSP-RDAQAAGIAIIH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1301 QDPTMFEG-TIRSNldpleeytddqIWealdncqLGDEVRKK---------------------ELKLDSPVSEngqnWSV 1358
Cdd:COG1129 86 QELNLVPNlSVAEN-----------IF-------LGREPRRGglidwramrrrarellarlglDIDPDTPVGD----LSV 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 30682479 1359 GQRQLVCLGRVLLKRSKLLVLDEATASIDTA-TDNLIQ--ETLRHHfaDCTVITIAHRI 1414
Cdd:COG1129 144 AQQQLVEIARALSRDARVLILDEPTASLTEReVERLFRiiRRLKAQ--GVAIIYISHRL 200
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
726-802 |
1.12e-14 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 73.40 E-value: 1.12e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDaHTGSHLFKEVLLGL-LRHKTVIYVTHQVEFLPEADLILVMKDGKI 802
Cdd:cd03246 97 LSGGQRQRLGLARALYGNPRILVLDEPNSHLD-VEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1250-1423 |
1.12e-14 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 77.08 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1250 GIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIG---LHDLRSRLSIIPQDPT------MfegTIRSNL-DPLEE 1319
Cdd:COG4608 48 GLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDPYaslnprM---TVGDIIaEPLRI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1320 YT-------DDQIWEALDNCQLGDEVRKK---ELkldspvsengqnwSVGQRQLVCLGRVLLKRSKLLVLDEATA----S 1385
Cdd:COG4608 125 HGlaskaerRERVAELLELVGLRPEHADRyphEF-------------SGGQRQRIGIARALALNPKLIVCDEPVSaldvS 191
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 30682479 1386 IDTATDNLIQEtLRHHFaDCTVITIAHRISSV--IdSDMV 1423
Cdd:COG4608 192 IQAQVLNLLED-LQDEL-GLTYLFISHDLSVVrhI-SDRV 228
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
669-817 |
1.46e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 79.30 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 669 IAQSPWIQSGKVEENILFGKP-MEREWYDRVLEACSLNKDLEILPFHDQTVIGERGINLSGGQKQRIQIARALYQDADIY 747
Cdd:PTZ00265 1301 VSQEPMLFNMSIYENIKFGKEdATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKIL 1380
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30682479 748 LFDDPFSAVDAHTGSHLFKEVL-LGLLRHKTVIYVTHQVEFLPEADLILVM----KDGKITQAGKYHEILDSGTD 817
Cdd:PTZ00265 1381 LLDEATSSLDSNSEKLIEKTIVdIKDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQAHGTHEELLSVQD 1455
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
680-811 |
1.58e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 77.29 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 680 VEENILFGKPMER----EWYDRVLEACSLNKdLEILpfhdqtviGERGI-NLSGGQKQRIQIARALYQDADIYLFDDPFS 754
Cdd:PRK09452 103 VFENVAFGLRMQKtpaaEITPRVMEALRMVQ-LEEF--------AQRKPhQLSGGQQQRVAIARAVVNKPKVLLLDESLS 173
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30682479 755 AVDAhtgsHLFKEVLLGL--LRHK---TVIYVTH-QVEFLPEADLILVMKDGKITQAGKYHEI 811
Cdd:PRK09452 174 ALDY----KLRKQMQNELkaLQRKlgiTFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1218-1447 |
1.61e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 75.83 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1218 EITICNLQVRYGPHLPM---VLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIdGINILSIG-----L 1289
Cdd:PRK13634 2 DITFQKVEHRYQYKTPFerrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGkknkkL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1290 HDLRSRLSIIPQDP--TMFEGTIR-------SNLDPLEEYTDDQIWEALDNCQLGDEVRKKelkldSPVSENGqnwsvGQ 1360
Cdd:PRK13634 81 KPLRKKVGIVFQFPehQLFEETVEkdicfgpMNFGVSEEDAKQKAREMIELVGLPEELLAR-----SPFELSG-----GQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1361 RQLVCLGRVLLKRSKLLVLDEATASIDTATDNLIQETLR--HHFADCTVITIAHRISSVID-SDMVLLLDQGLIKEHDSP 1437
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYklHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTP 230
|
250
....*....|
gi 30682479 1438 ARLLEDRSSL 1447
Cdd:PRK13634 231 REIFADPDEL 240
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
725-802 |
1.68e-14 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 75.09 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 725 NLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGshlfkEVLLGLLRH------KTVIYVTHQVEFLPE-ADLILVM 797
Cdd:COG3638 146 QLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTA-----RQVMDLLRRiaredgITVVVNLHQVDLARRyADRIIGL 220
|
....*
gi 30682479 798 KDGKI 802
Cdd:COG3638 221 RDGRV 225
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1214-1443 |
2.19e-14 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 74.74 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1214 PSRGEITICNLQVRY----GPHLpmVLHGLTCTFPGGLKTGIVGRTGCGKStliqTLFRIV----EPAAGEIRIDGINIl 1285
Cdd:COG1116 3 AAAPALELRGVSKRFptggGGVT--ALDDVSLTVAAGEFVALVGPSGCGKS----TLLRLIagleKPTSGEVLVDGKPV- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1286 siglHDLRSRLSIIPQDPTMFE-GTIRSNLD-PLE------EYTDDQIWEALDNCQLGDEVRK--KELkldspvsengqn 1355
Cdd:COG1116 76 ----TGPGPDRGVVFQEPALLPwLTVLDNVAlGLElrgvpkAERRERARELLELVGLAGFEDAypHQL------------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1356 wSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTATDNLIQETLRHHFAD--CTVITIAHRIS-SVIDSDMVLLLDQGlik 1432
Cdd:COG1116 140 -SGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQEtgKTVLFVTHDVDeAVFLADRVVVLSAR--- 215
|
250
....*....|.
gi 30682479 1433 ehdsPARLLED 1443
Cdd:COG1116 216 ----PGRIVEE 222
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1235-1447 |
2.36e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 75.22 E-value: 2.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1235 VLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEP---AAGEIRIDGINILSIGLHDLRSRLSIIPQDP-TMFEGTI 1310
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIREKVGIVFQNPdNQFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1311 rsnldpleeyTDDQIWEALDNCQLGDEVRKKELK--------LDSPVSENgQNWSVGQRQLVCLGRVLLKRSKLLVLDEA 1382
Cdd:PRK13640 102 ----------VGDDVAFGLENRAVPRPEMIKIVRdvladvgmLDYIDSEP-ANLSGGQKQRVAIAGILAVEPKIIILDES 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30682479 1383 TASIDTATDNLIQETLRHHFAD--CTVITIAHRISSVIDSDMVLLLDQGLIKEHDSPARLLEDRSSL 1447
Cdd:PRK13640 171 TSMLDPAGKEQILKLIRKLKKKnnLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKVEML 237
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1223-1429 |
2.50e-14 |
|
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: 72.08 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1223 NLQVRYGPHLpmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDG--INILSIGlHDLRSRLSIIP 1300
Cdd:cd03216 5 GITKRFGGVK--ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGkeVSFASPR-DARRAGIAMVY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1301 QdptmfegtirsnLdpleeytddqiwealdncqlgdevrkkelkldspvsengqnwSVGQRQLVCLGRVLLKRSKLLVLD 1380
Cdd:cd03216 82 Q------------L------------------------------------------SVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 30682479 1381 EATASIDTA-TDNLIQ--ETLRHhfADCTVITIAHRISSVID-SDMVLLLDQG 1429
Cdd:cd03216 108 EPTAALTPAeVERLFKviRRLRA--QGVAVIFISHRLDEVFEiADRVTVLRDG 158
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1219-1426 |
2.59e-14 |
|
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: 73.66 E-value: 2.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHLP--MVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINIlsiglHDLRSRL 1296
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV-----TGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1297 SIIPQDPTMFE-GTIRSN-LDPLE------EYTDDQIWEALDNCQLGDEVRK--KELkldspvsengqnwSVGQRQLVCL 1366
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNvALGLElqgvpkAEARERAEELLELVGLSGFENAypHQL-------------SGGMRQRVAL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30682479 1367 GRVLLKRSKLLVLDEATASIDTATDNLIQETL-----RHHFadcTVITIAHRIS-SVIDSDMVLLL 1426
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELldiwrETGK---TVLLVTHDIDeAVFLADRVVVL 205
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
680-802 |
3.06e-14 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 74.14 E-value: 3.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 680 VEENILFG--------KPMEREWYDR-VLEACSLNKDLEILPFHDQtvigeRGINLSGGQKQRIQIARALYQDADIYLFD 750
Cdd:cd03256 95 VLENVLSGrlgrrstwRSLFGLFPKEeKQRALAALERVGLLDKAYQ-----RADQLSGGQQQRVAIARALMQQPKLILAD 169
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 30682479 751 DPFSAVD---AHTGSHLFKEvlLGLLRHKTVIYVTHQVEFLPE-ADLILVMKDGKI 802
Cdd:cd03256 170 EPVASLDpasSRQVMDLLKR--INREEGITVIVSLHQVDLAREyADRIVGLKDGRI 223
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
726-803 |
3.48e-14 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 73.54 E-value: 3.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFkEVLLGLLR--HKTVIYVTHQVEFLPEADLILVMKDGKIT 803
Cdd:COG1136 145 LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVL-ELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIV 223
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1236-1445 |
3.63e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 74.64 E-value: 3.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1236 LHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIG-LHDLRSRLSIIPQDP-TMFEGTIrsn 1313
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGIVFQNPeTQFVGRT--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1314 ldpLEEytdDQIWEALDNCQLGDEVRKK------ELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEATASID 1387
Cdd:PRK13644 95 ---VEE---DLAFGPENLCLPPIEIRKRvdralaEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 30682479 1388 TATDNLIQETLRH-HFADCTVITIAHRISSVIDSDMVLLLDQGLIKEHDSPARLLEDRS 1445
Cdd:PRK13644 169 PDSGIAVLERIKKlHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1236-1447 |
3.80e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 74.50 E-value: 3.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1236 LHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDG--INILSIGLHDLRSRLSIIPQDP--TMFEGTIr 1311
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESVGMVFQDPdnQLFSASV- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1312 snldpleeYTDdqIWEALDNCQL-GDEVRKK-----ELKLDSPVSENGQNW-SVGQRQLVCLGRVLLKRSKLLVLDEATA 1384
Cdd:PRK13636 101 --------YQD--VSFGAVNLKLpEDEVRKRvdnalKRTGIEHLKDKPTHClSFGQKKRVAIAGVLVMEPKVLVLDEPTA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30682479 1385 SID----TATDNLIQETLRHhfADCTVITIAHRISSV-IDSDMVLLLDQGLIKEHDSPARLLEDRSSL 1447
Cdd:PRK13636 171 GLDpmgvSEIMKLLVEMQKE--LGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEVFAEKEML 236
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
936-1098 |
6.84e-14 |
|
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: 73.75 E-value: 6.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 936 SGFTLILVYVLLAVASSFciliRALLVAMTGFKMATELFTQMHLRIFRASMSFFDATPMGRILNRASTDQSVADLRLPGQ 1015
Cdd:cd18557 38 LALILLAIYLLQSVFTFV----RYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1016 FAYVAIAAINILGIIGVIVQVAWQ---VLIVFIPVVA-ACAWYRQYYISAAREL-ARLAGISrspvvHHFSETLSGITTI 1090
Cdd:cd18557 114 LSQLLRNILQVIGGLIILFILSWKltlVLLLVIPLLLiASKIYGRYIRKLSKEVqDALAKAG-----QVAEESLSNIRTV 188
|
....*...
gi 30682479 1091 RSFDQEPR 1098
Cdd:cd18557 189 RSFSAEEK 196
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1249-1417 |
6.90e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 73.53 E-value: 6.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1249 TGIVGRTGCGKSTLIQTLFRIVEpAAGEIRIDG--------INILSIGLHDLRSRLSIIPQDPTMFEGTIRSNL------ 1314
Cdd:PRK14258 36 TAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGrveffnqnIYERRVNLNRLRRQVSMVHPKPNLFPMSVYDNVaygvki 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1315 ---DPLEEyTDDQIWEALDNCQLGDEVRKKelkldspVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTATD 1391
Cdd:PRK14258 115 vgwRPKLE-IDDIVESALKDADLWDEIKHK-------IHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIAS 186
|
170 180
....*....|....*....|....*....
gi 30682479 1392 NLIqETLRHHF---ADCTVITIAHRISSV 1417
Cdd:PRK14258 187 MKV-ESLIQSLrlrSELTMVIVSHNLHQV 214
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
680-812 |
7.23e-14 |
|
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: 74.75 E-value: 7.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 680 VEENILFG-----KPMEREWYDRVLEAcslnkdLEILPFHDQTVIgergiNLSGGQKQRIQIARALYQDADIYLFDDPFS 754
Cdd:COG4148 94 VRGNLLYGrkrapRAERRISFDEVVEL------LGIGHLLDRRPA-----TLSGGERQRVAIGRALLSSPRLLLMDEPLA 162
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30682479 755 AVDAHTgshlfKEVLLGLLR--HKT----VIYVTHQVEflpE----ADLILVMKDGKITQAGKYHEIL 812
Cdd:COG4148 163 ALDLAR-----KAEILPYLErlRDEldipILYVSHSLD---EvarlADHVVLLEQGRVVASGPLAEVL 222
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
726-802 |
7.95e-14 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 72.18 E-value: 7.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDahtgSHLFKEVlLGLLR-----HKTVIYVTHQVEFLPE-ADLILVMKD 799
Cdd:cd03262 136 LSGGQQQRVAIARALAMNPKVMLFDEPTSALD----PELVGEV-LDVMKdlaeeGMTMVVVTHEMGFAREvADRVIFMDD 210
|
...
gi 30682479 800 GKI 802
Cdd:cd03262 211 GRI 213
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1219-1387 |
8.87e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 75.26 E-value: 8.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHlpMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSI 1298
Cdd:PRK09536 4 IDVSDLSVEFGDT--TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1299 IPQDPTM-FEGTIR-----------SNLDPLEEYTDDQIWEALDNCQLGDEVrkkelklDSPVSEngqnWSVGQRQLVCL 1366
Cdd:PRK09536 82 VPQDTSLsFEFDVRqvvemgrtphrSRFDTWTETDRAAVERAMERTGVAQFA-------DRPVTS----LSGGERQRVLL 150
|
170 180
....*....|....*....|.
gi 30682479 1367 GRVLLKRSKLLVLDEATASID 1387
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLD 171
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1235-1433 |
1.01e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 73.21 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1235 VLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAG-----EIRIDGINILSI-GLHDLRSRLSIIPQDPTMFEG 1308
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1309 TIRSN---------LDPLEEY--------TDDQIWEALdncqlgdevrkKELKLDSPVSENGqnwsvGQRQLVCLGRVLL 1371
Cdd:PRK14271 116 SIMDNvlagvrahkLVPRKEFrgvaqarlTEVGLWDAV-----------KDRLSDSPFRLSG-----GQQQLLCLARTLA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30682479 1372 KRSKLLVLDEATASIDTATDNLIQETLRHHFADCTVITIAHRISSV--IDSDMVLLLDQGLIKE 1433
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAarISDRAALFFDGRLVEE 243
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1235-1441 |
1.23e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 72.73 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1235 VLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDG--INILSIGLHDLRSRLSIIPQDP--TMFEGTI 1310
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQDPeqQIFYTDI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1311 RS-------NLDPLEEYTDDQIWEALdncQLGDEVRKKElkldSPVsengQNWSVGQRQLVCLGRVLLKRSKLLVLDEAT 1383
Cdd:PRK13638 96 DSdiafslrNLGVPEAEITRRVDEAL---TLVDAQHFRH----QPI----QCLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1384 ASIDTATDNLIQETLRHHFADCT-VITIAHRISSVID-SDMVLLLDQGLIKEHDSPARLL 1441
Cdd:PRK13638 165 AGLDPAGRTQMIAIIRRIVAQGNhVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVF 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
598-814 |
1.25e-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: 75.32 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 598 EMAVEISNGTFSWDDSsPIPTLRDMNFKVSQGMNVAICG------TVGSGKSSLLSSILGEvpkISGNLKVCG------- 664
Cdd:COG1123 2 TPLLEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGesgsgkSTLALALMGLLPHGGR---ISGEVLLDGrdllels 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 665 ------RKAYIAQSPWIQ--SGKVEENILFG-------KPMEREWYDRVLEACSLNKDLEILPFHdqtvigerginLSGG 729
Cdd:COG1123 78 ealrgrRIGMVFQDPMTQlnPVTVGDQIAEAlenlglsRAEARARVLELLEAVGLERRLDRYPHQ-----------LSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 730 QKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEVL-LGLLRHKTVIYVTHQVEFLPE-ADLILVMKDGKITQAGK 807
Cdd:COG1123 147 QRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLReLQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGP 226
|
....*..
gi 30682479 808 YHEILDS 814
Cdd:COG1123 227 PEEILAA 233
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
667-754 |
1.80e-13 |
|
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: 69.21 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 667 AYIAQSPWIQSGK-VEENILFGKPME---REWYDRVLEAcSLNKdLEILPFHDqTVIGERGINLSGGQKQRIQIARALYQ 742
Cdd:pfam00005 62 GYVFQDPQLFPRLtVRENLRLGLLLKglsKREKDARAEE-ALEK-LGLGDLAD-RPVGERPGTLSGGQRQRVAIARALLT 138
|
90
....*....|..
gi 30682479 743 DADIYLFDDPFS 754
Cdd:pfam00005 139 KPKLLLLDEPTA 150
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1234-1430 |
2.18e-13 |
|
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: 70.60 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1234 MVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSIIPQDptmfegTIRSN 1313
Cdd:cd03231 14 ALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAP------GIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1314 LDPLEEYT-------DDQIWEALDNCQL-GDEvrkkelklDSPVSEngqnWSVGQRQLVCLGRVLLKRSKLLVLDEATAS 1385
Cdd:cd03231 88 LSVLENLRfwhadhsDEQVEEALARVGLnGFE--------DRPVAQ----LSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 30682479 1386 IDTATDNLIQETLRHHFADCTVITIAHRISSVIDSDMVLLLDQGL 1430
Cdd:cd03231 156 LDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDLGF 200
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1250-1443 |
2.49e-13 |
|
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: 74.34 E-value: 2.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1250 GIVGRTGCGKSTLIQTLFRIVePAAGEIRIDGINILSIG---LHDLRSRLSIIPQDPtmF--------------EG--TI 1310
Cdd:COG4172 316 GLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--FgslsprmtvgqiiaEGlrVH 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1311 RSNLDPLEeyTDDQIWEALDNCQLGDEVRKK---ELkldspvsengqnwSVGQRQLVCLGRVLLKRSKLLVLDEATASID 1387
Cdd:COG4172 393 GPGLSAAE--RRARVAEALEEVGLDPAARHRyphEF-------------SGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30682479 1388 TATDNLIQETLR-----HHFA------DCTVI-TIAHRIssvidsdMVllLDQGLIKEHDSPARLLED 1443
Cdd:COG4172 458 VSVQAQILDLLRdlqreHGLAylfishDLAVVrALAHRV-------MV--MKDGKVVEQGPTEQVFDA 516
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1230-1412 |
2.62e-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: 70.51 E-value: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1230 PHLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINIlsIGLHD-----LRSRLSIIPQD-- 1302
Cdd:cd03292 11 PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDV--SDLRGraipyLRRKIGVVFQDfr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1303 --PTMfegTIRSNLD-PLE-EYTDDQIW-----EALDNCQLGDEVRKKELKLdspvsengqnwSVGQRQLVCLGRVLLKR 1373
Cdd:cd03292 89 llPDR---NVYENVAfALEvTGVPPREIrkrvpAALELVGLSHKHRALPAEL-----------SGGEQQRVAIARAIVNS 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 30682479 1374 SKLLVLDEATASIDTATDNLIQETLRH-HFADCTVITIAH 1412
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIMNLLKKiNKAGTTVVVATH 194
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1242-1415 |
2.92e-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: 70.40 E-value: 2.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1242 TFPGGLkTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINIL----SIGLHDLRSRLSIIPQDPTMFEG-TIRSNLD- 1315
Cdd:cd03297 20 DLNEEV-TGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFdsrkKINLPPQQRKIGLVFQQYALFPHlNVRENLAf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1316 --PLEEYTDDQIW--EALDNCQLGDEVRKKELKLdspvsengqnwSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTATD 1391
Cdd:cd03297 99 glKRKRNREDRISvdELLDLLGLDHLLNRYPAQL-----------SGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180
....*....|....*....|....*.
gi 30682479 1392 NLIQETLRHHFAD--CTVITIAHRIS 1415
Cdd:cd03297 168 LQLLPELKQIKKNlnIPVIFVTHDLS 193
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
601-812 |
3.05e-13 |
|
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: 71.69 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 601 VEISNGTFSWDDSSPiPTLRDMNFKVSQGMNVAICG-------TVGsgkssllssilgevpKI--------SGNLKVCGR 665
Cdd:TIGR04520 1 IEVENVSFSYPESEK-PALKNVSLSIEKGEFVAIIGhngsgksTLA---------------KLlnglllptSGKVTVDGL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 666 KAYIAQSPW----------------IQSGKVEENILFGkpME------REWYDRVLEACslnKDLEILPFHDQTVIgerg 723
Cdd:TIGR04520 65 DTLDEENLWeirkkvgmvfqnpdnqFVGATVEDDVAFG--LEnlgvprEEMRKRVDEAL---KLVGMEDFRDREPH---- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 724 iNLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAhTGShlfKEVLLGLLR-----HKTVIYVTHQVEFLPEADLILVMK 798
Cdd:TIGR04520 136 -LLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDP-KGR---KEVLETIRKlnkeeGITVISITHDMEEAVLADRVIVMN 210
|
250
....*....|....
gi 30682479 799 DGKITQAGKYHEIL 812
Cdd:TIGR04520 211 KGKIVAEGTPREIF 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
679-814 |
4.59e-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: 73.40 E-value: 4.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 679 KVEENI-----LFGKPMEREWYDRV---LEACSLNKD-LEILPFHdqtvigerginLSGGQKQRIQIARALYQDADIYLF 749
Cdd:COG1123 360 TVGDIIaeplrLHGLLSRAERRERVaelLERVGLPPDlADRYPHE-----------LSGGQRQRVAIARALALEPKLLIL 428
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30682479 750 DDPFSAVDAHTGSHlfkevLLGLLRH------KTVIYVTHQ---VEFLpeADLILVMKDGKITQAGKYHEILDS 814
Cdd:COG1123 429 DEPTSALDVSVQAQ-----ILNLLRDlqrelgLTYLFISHDlavVRYI--ADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1219-1444 |
5.53e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 70.92 E-value: 5.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRY--GPHlpmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRL 1296
Cdd:PRK13647 5 IEVEDLHFRYkdGTK---ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1297 SIIPQDP-------TMFE----GTIRSNLDPLEeyTDDQIWEALdncqlgDEVRKKELKLDSPvsengQNWSVGQRQLVC 1365
Cdd:PRK13647 82 GLVFQDPddqvfssTVWDdvafGPVNMGLDKDE--VERRVEEAL------KAVRMWDFRDKPP-----YHLSYGQKKRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1366 LGRVLLKRSKLLVLDEATASIDTATDNLIQETL-RHHFADCTVITIAHRISSVID-SDMVLLLDQGLIKEHDSPaRLLED 1443
Cdd:PRK13647 149 IAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILdRLHNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDK-SLLTD 227
|
.
gi 30682479 1444 R 1444
Cdd:PRK13647 228 E 228
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1251-1441 |
6.66e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 70.59 E-value: 6.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1251 IVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGiNILSIGLHDLRS-RLSIIPQDPTmfegtirSNLDPLEeytddQIWEAL 1329
Cdd:PRK15112 44 IIGENGSGKSTLAKMLAGMIEPTSGELLIDD-HPLHFGDYSYRSqRIRMIFQDPS-------TSLNPRQ-----RISQIL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1330 D-----NCQLGDEVRKKELK--------LDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTATD----N 1392
Cdd:PRK15112 111 DfplrlNTDLEPEQREKQIIetlrqvglLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRsqliN 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 30682479 1393 LIQETLRHHFADCTVITIAHRISSVIdSDMVLLLDQGLIKEHDSPARLL 1441
Cdd:PRK15112 191 LMLELQEKQGISYIYVTQHLGMMKHI-SDQVLVMHQGEVVERGSTADVL 238
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
657-803 |
8.23e-13 |
|
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: 68.82 E-value: 8.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 657 SGNLKVCGRKA----------YIAQSPWIQ--SGKVEENILFGKPmerEWYDRVLEACSLNKDLEILPFHDQtvigeRGI 724
Cdd:cd03226 54 SGSILLNGKPIkakerrksigYVMQDVDYQlfTDSVREELLLGLK---ELDAGNEQAETVLKDLDLYALKER-----HPL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 725 NLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgshlfKEVLLGLLRH-----KTVIYVTHQVEFLPE-ADLILVMK 798
Cdd:cd03226 126 SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKN-----MERVGELIRElaaqgKAVIVITHDYEFLAKvCDRVLLLA 200
|
....*
gi 30682479 799 DGKIT 803
Cdd:cd03226 201 NGAIV 205
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
726-809 |
8.63e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 71.60 E-value: 8.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAhtgshlfkevllgLLR----------HK----TVIYVTH-QVEFLPE 790
Cdd:PRK11000 134 LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA-------------ALRvqmrieisrlHKrlgrTMIYVTHdQVEAMTL 200
|
90 100
....*....|....*....|...
gi 30682479 791 ADLILVMKDGKITQAGK----YH 809
Cdd:PRK11000 201 ADKIVVLDAGRVAQVGKplelYH 223
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
725-812 |
1.06e-12 |
|
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: 69.15 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 725 NLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgshlfKEVLLGLLR--HK----TVIYVTHQVEFLPE-ADLILVM 797
Cdd:cd03258 140 QLSGGQKQRVGIARALANNPKVLLCDEATSALDPET-----TQSILALLRdiNRelglTIVLITHEMEVVKRiCDRVAVM 214
|
90
....*....|....*
gi 30682479 798 KDGKITQAGKYHEIL 812
Cdd:cd03258 215 EKGEVVEEGTVEEVF 229
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1231-1466 |
1.07e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 73.41 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1231 HLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGinilsiglhdlrsRLSIIPQDPTMFEGTI 1310
Cdd:TIGR01271 437 YVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1311 RSNLDPLEEYTDDQIWEALDNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTAT 1390
Cdd:TIGR01271 504 KDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30682479 1391 DNLIQET-LRHHFADCTVITIAHRISSVIDSDMVLLLDQGLIKEHDSPARLLEDRSSLFSKLVAEYTTSSESKSKRS 1466
Cdd:TIGR01271 584 EKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLLGLEAFDNFSAERRN 660
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1231-1429 |
1.15e-12 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 70.27 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1231 HLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGinilsiglhdlrsRLSIIPQDPTMFEGTI 1310
Cdd:cd03291 48 VGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1311 RSNLDPLEEYTDDQIWEALDNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTAT 1390
Cdd:cd03291 115 KENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 30682479 1391 DNLIQET-LRHHFADCTVITIAHRISSVIDSDMVLLLDQG 1429
Cdd:cd03291 195 EKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
726-814 |
1.58e-12 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 68.96 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHtGSHLFKEVLLGLLRH--KTVIYVTHQVEFLPEA-DLILVMKDGKI 802
Cdd:COG1119 143 LSQGEQRRVLIARALVKDPELLILDEPTAGLDLG-ARELLLALLDKLAAEgaPTLVLVTHHVEEIPPGiTHVLLLKDGRV 221
|
90
....*....|..
gi 30682479 803 TQAGKYHEILDS 814
Cdd:COG1119 222 VAAGPKEEVLTS 233
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1251-1427 |
1.95e-12 |
|
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: 66.79 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1251 IVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGinilsiglhdlRSRLSIIPQDPTMFEGTIRsnldpleeytdDQI---WE 1327
Cdd:cd03223 32 ITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLFLPQRPYLPLGTLR-----------EQLiypWD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1328 aldncqlgdevrkKELkldspvsengqnwSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTATDNLIQETLRHHFAdcTV 1407
Cdd:cd03223 90 -------------DVL-------------SGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGI--TV 141
|
170 180
....*....|....*....|
gi 30682479 1408 ITIAHRISSVIDSDMVLLLD 1427
Cdd:cd03223 142 ISVGHRPSLWKFHDRVLDLD 161
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
726-814 |
1.99e-12 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 68.48 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAhtgsHLFKEVlLGLLR-----HKTVIYVTHQVEFLPE-ADLILVMKD 799
Cdd:COG1126 137 LSGGQQQRVAIARALAMEPKVMLFDEPTSALDP----ELVGEV-LDVMRdlakeGMTMVVVTHEMGFAREvADRVVFMDG 211
|
90
....*....|....*
gi 30682479 800 GKITQAGKYHEILDS 814
Cdd:COG1126 212 GRIVEEGPPEEFFEN 226
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
726-823 |
2.55e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 70.11 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAhtgsHLFKEvLLGLLR--HK----TVIYVTH-QVEFLPEADLILVMK 798
Cdd:PRK10851 137 LSGGQKQRVALARALAVEPQILLLDEPFGALDA----QVRKE-LRRWLRqlHEelkfTSVFVTHdQEEAMEVADRVVVMS 211
|
90 100
....*....|....*....|....*..
gi 30682479 799 DGKITQAGKYHEIL-DSGTDF-MELVG 823
Cdd:PRK10851 212 QGNIEQAGTPDQVWrEPATRFvLEFMG 238
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1219-1429 |
2.82e-12 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 68.19 E-value: 2.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHLpmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAG-EIRIDGINILSIGLHDLRSRLS 1297
Cdd:COG1119 4 LELRNVTVRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1298 IIpqDPTMFEgTIRSNLDPLE--------------EYTDDQI---WEALDNCQLGDevrkkelKLDSPVSEngqnWSVGQ 1360
Cdd:COG1119 82 LV--SPALQL-RFPRDETVLDvvlsgffdsiglyrEPTDEQReraRELLELLGLAH-------LADRPFGT----LSQGE 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30682479 1361 RQLVCLGRVLLKRSKLLVLDEATASID-TATDNLIQ--ETLRHHfADCTVITIAHRISSVIDS-DMVLLLDQG 1429
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDlGARELLLAllDKLAAE-GAPTLVLVTHHVEEIPPGiTHVLLLKDG 219
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1227-1431 |
2.82e-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: 67.52 E-value: 2.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1227 RYGpHLPMvlhGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINilsIGLHDLRSR-LSIIPQDPTM 1305
Cdd:cd03298 9 SYG-EQPM---HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVD---VTAAPPADRpVSMLFQENNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1306 FEG-TIRSNLD----P---LEEYTDDQIWEALDNCQLGDEVRKKELKLdspvsengqnwSVGQRQLVCLGRVLLKRSKLL 1377
Cdd:cd03298 82 FAHlTVEQNVGlglsPglkLTAEDRQAIEVALARVGLAGLEKRLPGEL-----------SGGERQRVALARVLVRDKPVL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 30682479 1378 VLDEATASIDTATDNLIQETLR--HHFADCTVITIAHRISSVID-SDMVLLLDQGLI 1431
Cdd:cd03298 151 LLDEPFAALDPALRAEMLDLVLdlHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1223-1435 |
3.48e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.86 E-value: 3.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1223 NLQVRYGPHLpmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIdGINIlsiglhdlrsRLSIIPQD 1302
Cdd:COG0488 320 GLSKSYGDKT--LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGYFDQH 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1303 ptmfegtiRSNLDPleeytDDQIWEALdnCQLGDEVRKKEL------------KLDSPVSengqNWSVGQRQLVCLGRVL 1370
Cdd:COG0488 387 --------QEELDP-----DKTVLDEL--RDGAPGGTEQEVrgylgrflfsgdDAFKPVG----VLSGGEKARLALAKLL 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30682479 1371 LKRSKLLVLDEATASIDTATDNLIQETLRhHFaDCTVITIAH-R--ISSVIDSdmVLLLDQGLIKEHD 1435
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDIETLEALEEALD-DF-PGTVLLVSHdRyfLDRVATR--ILEFEDGGVREYP 511
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1216-1387 |
4.70e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 68.09 E-value: 4.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1216 RGEiticNLQVRYGPHlpMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSR 1295
Cdd:PRK10253 9 RGE----QLTLGYGKY--TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1296 LSIIPQDPTMFEGTIRSNLDPLEEYTDDQI---WEALDNCQLGDEVRKKelKLDSPVSENGQNWSVGQRQLVCLGRVLLK 1372
Cdd:PRK10253 83 IGLLAQNATTPGDITVQELVARGRYPHQPLftrWRKEDEEAVTKAMQAT--GITHLADQSVDTLSGGQRQRAWIAMVLAQ 160
|
170
....*....|....*
gi 30682479 1373 RSKLLVLDEATASID 1387
Cdd:PRK10253 161 ETAIMLLDEPTTWLD 175
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
726-802 |
4.78e-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: 67.15 E-value: 4.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgshlfKEVLLGLLRH------KTVIYVTHQVEFLPE-ADLILVMK 798
Cdd:cd03257 146 LSGGQRQRVAIARALALNPKLLIADEPTSALDVSV-----QAQILDLLKKlqeelgLTLLFITHDLGVVAKiADRVAVMY 220
|
....
gi 30682479 799 DGKI 802
Cdd:cd03257 221 AGKI 224
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
726-807 |
5.20e-12 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 66.81 E-value: 5.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAhtgshLFKEVLLGLL------RHKTVIYVTHQVEFLPE-ADLILVMK 798
Cdd:TIGR01277 129 LSGGQRQRVALARCLVRPNPILLLDEPFSALDP-----LLREEMLALVkqlcseRQRTLLMVTHHLSDARAiASQIAVVS 203
|
....*....
gi 30682479 799 DGKITQAGK 807
Cdd:TIGR01277 204 QGKIKVVSD 212
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
939-1108 |
5.31e-12 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 68.28 E-value: 5.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 939 TLILVYVLLAVASSFCILIRALLVAMTGFKMATELFTQMHLRIFRASMSFFDATPMGRILNRASTdqsvaDLRLPGQF-A 1017
Cdd:cd18543 40 PLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATS-----DLSLVQRFlA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1018 YVAIAAINILGIIGVIVQVAWQ-------VLIVFIPVVAACAWYRQYYISAARELARLAGIsrspVVHHFSETLSGITTI 1090
Cdd:cd18543 115 FGPFLLGNLLTLVVGLVVMLVLspplalvALASLPPLVLVARRFRRRYFPASRRAQDQAGD----LATVVEESVTGIRVV 190
|
170
....*....|....*...
gi 30682479 1091 RSFDQEPRFRGDIMRLSD 1108
Cdd:cd18543 191 KAFGRERRELDRFEAAAR 208
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
680-811 |
5.99e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 68.72 E-value: 5.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 680 VEENILFG-------KPMEREWYDRVLEACSLNKD-LEILPFhdqtvigergiNLSGGQKQRIQIARALYQDADIYLFDD 751
Cdd:PRK13631 134 IEKDIMFGpvalgvkKSEAKKLAKFYLNKMGLDDSyLERSPF-----------GLSGGQKRRVAIAGILAIQPEILIFDE 202
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30682479 752 PFSAVDAHTGSHLFKEVLLGLLRHKTVIYVTHQVEFLPE-ADLILVMKDGKITQAGKYHEI 811
Cdd:PRK13631 203 PTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEI 263
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
940-1098 |
6.59e-12 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 67.92 E-value: 6.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 940 LILVYVLLAVASSFCILIRALLVAMTGFKMATELFTQMHLRIFRASMSFFDATPMGRILNRASTDQSVADLRLPGQFAYV 1019
Cdd:cd18563 45 LVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDF 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1020 AIAAINILGIIGVIVQVAWQV-LIVFIP---VVAACAWYRQYyisaARELARLAGISRSPVVHHFSETLSGITTIRSFDQ 1095
Cdd:cd18563 125 LTNILMIIGIGVVLFSLNWKLaLLVLIPvplVVWGSYFFWKK----IRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQ 200
|
...
gi 30682479 1096 EPR 1098
Cdd:cd18563 201 EKR 203
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1223-1412 |
7.32e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 67.50 E-value: 7.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1223 NLQVRYGPHLpmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVE-----PAAGEIRIDGINILSIGLH--DLRSR 1295
Cdd:PRK14243 15 NLNVYYGSFL--AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYAPDVDpvEVRRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1296 LSIIPQDPTMFEGTIRSNL------DPLEEYTDDQIWEALDNCQLGDEVRKKelkldspVSENGQNWSVGQRQLVCLGRV 1369
Cdd:PRK14243 93 IGMVFQKPNPFPKSIYDNIaygariNGYKGDMDELVERSLRQAALWDEVKDK-------LKQSGLSLSGGQQQRLCIARA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 30682479 1370 LLKRSKLLVLDEATASIDTATDNLIQETLRHHFADCTVITIAH 1412
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTH 208
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
682-806 |
7.68e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 68.59 E-value: 7.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 682 ENILFGKPM----EREWYDRVLEACSLnKDLEilPFHDQTVIgergiNLSGGQKQRIQIARALYQDADIYLFDDPFSAVD 757
Cdd:PRK11432 97 ENVGYGLKMlgvpKEERKQRVKEALEL-VDLA--GFEDRYVD-----QISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 758 AHtgshlfkevLLGLLRHK----------TVIYVTH-QVEFLPEADLILVMKDGKITQAG 806
Cdd:PRK11432 169 AN---------LRRSMREKirelqqqfniTSLYVTHdQSEAFAVSDTVIVMNKGKIMQIG 219
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1219-1399 |
8.43e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 67.91 E-value: 8.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHLpmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHdLRSRLSI 1298
Cdd:PRK13537 8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH-ARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1299 IPQ----DPTMfegTIRSNLDPLEEYTDDQIWEALDNCQLGDEVRKKELKLDSPVSEngqnWSVGQRQLVCLGRVLLKRS 1374
Cdd:PRK13537 85 VPQfdnlDPDF---TVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGE----LSGGMKRRLTLARALVNDP 157
|
170 180
....*....|....*....|....*
gi 30682479 1375 KLLVLDEATASIDTATDNLIQETLR 1399
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLR 182
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
726-804 |
8.47e-12 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 67.19 E-value: 8.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLfKEVLLGLLR--HKTVIYVTHQVE---FLpeADLILVMKD- 799
Cdd:COG4525 135 LSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQM-QELLLDVWQrtGKGVFLITHSVEealFL--ATRLVVMSPg 211
|
....*.
gi 30682479 800 -GKITQ 804
Cdd:COG4525 212 pGRIVE 217
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1235-1433 |
9.91e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 66.99 E-value: 9.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1235 VLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRID------GINILSIGLHDLRSRLSIIPQDPTMFEG 1308
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDgkvlyfGKDIFQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1309 -TIRSNLD-PLEEYTDDQ-------IWEALDNCQLGDEVRKkelKLDSPVSEngqnWSVGQRQLVCLGRVLLKRSKLLVL 1379
Cdd:PRK14246 105 lSIYDNIAyPLKSHGIKEkreikkiVEECLRKVGLWKEVYD---RLNSPASQ----LSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 30682479 1380 DEATASIDTATDNLIQETLRHHFADCTVITIAHRISSVID-SDMVLLLDQGLIKE 1433
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVE 232
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1219-1400 |
1.26e-11 |
|
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: 66.03 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHLpmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDlRSRLSI 1298
Cdd:cd03218 1 LRAENLSKRYGKRK--VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1299 I--PQDPTMFEG-TIRSNLDPLEEYT--DDQIWEALDNCQLgdevrkKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKR 1373
Cdd:cd03218 78 GylPQEASIFRKlTVEENILAVLEIRglSKKEREEKLEELL------EEFHITHLRKSKASSLSGGERRRVEIARALATN 151
|
170 180
....*....|....*....|....*..
gi 30682479 1374 SKLLVLDEATASIDTATDNLIQETLRH 1400
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIKI 178
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
726-803 |
1.39e-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: 66.37 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKevLLGLLRHK---TVIYVTHQ---VEFLpeADLILVMKD 799
Cdd:COG1124 139 LSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILN--LLKDLREErglTYLFVSHDlavVAHL--CDRVAVMQN 214
|
....
gi 30682479 800 GKIT 803
Cdd:COG1124 215 GRIV 218
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
612-825 |
1.54e-11 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 66.47 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 612 DSSPIPTLRDMNFKVSQGMNVAICGTVGSGKSSLLSSILGEVPKISGNLKVCG-------------RKAYIAQSPWIQSG 678
Cdd:cd03288 30 ENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtlrsRLSIILQDPILFSG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 679 KVEENIlfgKPMEREWYDRV---LEACSLNKDLEILPFHDQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSA 755
Cdd:cd03288 110 SIRFNL---DPECKCTDDRLweaLEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATAS 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30682479 756 VDAHTgSHLFKEVLLGLLRHKTVIYVTHQVEFLPEADLILVMKDGKITQAGKYHEIL-DSGTDFMELVGAH 825
Cdd:cd03288 187 IDMAT-ENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLVRTD 256
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
726-813 |
2.02e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 65.55 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVD-AhtgshLFKEvLLGLLRH------KTVIYVTHQVE-FLPEADLILVM 797
Cdd:COG3840 130 LSGGQRQRVALARCLVRKRPILLLDEPFSALDpA-----LRQE-MLDLVDElcrergLTVLMVTHDPEdAARIADRVLLV 203
|
90
....*....|....*.
gi 30682479 798 KDGKITQAGKYHEILD 813
Cdd:COG3840 204 ADGRIAADGPTAALLD 219
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1236-1441 |
2.88e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 65.88 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1236 LHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSIIPQDP-TMFEG-TIRSN 1313
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPdNQFVGaTVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1314 LD--------PLEEYTdDQIWEALDNCQLGDevrkkeLKLDSPVSENGqnwsvGQRQLVCLGRVLLKRSKLLVLDEATAS 1385
Cdd:PRK13642 103 VAfgmenqgiPREEMI-KRVDEALLAVNMLD------FKTREPARLSG-----GQKQRVAVAGIIALRPEIIILDESTSM 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 30682479 1386 IDTATDNLIQETLrHHFAD---CTVITIAHRISSVIDSDMVLLLDQGLIKEHDSPARLL 1441
Cdd:PRK13642 171 LDPTGRQEIMRVI-HEIKEkyqLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
725-812 |
3.21e-11 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 66.64 E-value: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 725 NLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGshlfKEVL---------LGLlrhkTVIYVTHQVEFLPE-ADLI 794
Cdd:COG1135 140 QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETT----RSILdllkdinreLGL----TIVLITHEMDVVRRiCDRV 211
|
90
....*....|....*...
gi 30682479 795 LVMKDGKITQAGKYHEIL 812
Cdd:COG1135 212 AVLENGRIVEQGPVLDVF 229
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
938-1096 |
3.48e-11 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 65.95 E-value: 3.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 938 FTLILVYVLLAVASSFCILIRALLVAMTG----FKMATELFTqmHLRifRASMSFFDATPMGRILNRASTD-QSVADLrL 1012
Cdd:cd18545 40 LIIALLFLALNLVNWVASRLRIYLMAKVGqrilYDLRQDLFS--HLQ--KLSFSFFDSRPVGKILSRVINDvNSLSDL-L 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1013 PGQFAYVAIAAINILGIIGVIVQVAWQ---VLIVFIPVVAACAWYRQYYisaARELARLAGISRSPVVHHFSETLSGITT 1089
Cdd:cd18545 115 SNGLINLIPDLLTLVGIVIIMFSLNVRlalVTLAVLPLLVLVVFLLRRR---ARKAWQRVRKKISNLNAYLHESISGIRV 191
|
....*..
gi 30682479 1090 IRSFDQE 1096
Cdd:cd18545 192 IQSFARE 198
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
601-806 |
4.08e-11 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 63.97 E-value: 4.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 601 VEISNGTFSWDDSSPiPTLRDMNFKVSQGMNVAICGTVGSGKSSLLSSILGEVPKISGNLKVCG-------------RKA 667
Cdd:cd03369 7 IEVENLSVRYAPDLP-PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 668 YIAQSPWIQSGKVEENI-LFGKPMEREWYdrvlEACSlnkdleilpfhdqtvIGERGINLSGGQKQRIQIARALYQDADI 746
Cdd:cd03369 86 IIPQDPTLFSGTIRSNLdPFDEYSDEEIY----GALR---------------VSEGGLNLSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 747 YLFDDPFSAVDAHTgSHLFKEVLLGLLRHKTVIYVTHQVEFLPEADLILVMKDGKITQAG 806
Cdd:cd03369 147 LVLDEATASIDYAT-DALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
726-829 |
4.13e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 67.44 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGshlfKEVL--LGLLRHK--TVIYVTHQVEFLPEADLILVMKDGK 801
Cdd:PRK10535 145 LSGGQQQRVSIARALMNGGQVILADEPTGALDSHSG----EEVMaiLHQLRDRghTVIIVTHDPQVAAQAERVIEIRDGE 220
|
90 100 110
....*....|....*....|....*....|....*...
gi 30682479 802 ITQ----------AGKYHEILDSGTDFMELVGAHTEAL 829
Cdd:PRK10535 221 IVRnppaqekvnvAGGTEPVVNTASGWRQFVSGFREAL 258
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
726-821 |
5.48e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 64.77 E-value: 5.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgshlfKEVLLGLLRHK------TVIYVTHQVEFLPEADLILVMKD 799
Cdd:PRK13648 143 LSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA-----RQNLLDLVRKVksehniTIISITHDLSEAMEADHVIVMNK 217
|
90 100
....*....|....*....|..
gi 30682479 800 GKITQAGKYHEILDSGTDFMEL 821
Cdd:PRK13648 218 GTVYKEGTPTEIFDHAEELTRI 239
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
726-829 |
6.09e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 65.21 E-value: 6.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHtGSHLFKEVLLGLL-RHKTVIYVTHqveFLPEA----DLILVMKDG 800
Cdd:PRK13537 139 LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ-ARHLMWERLRSLLaRGKTILLTTH---FMEEAerlcDRLCVIEEG 214
|
90 100 110
....*....|....*....|....*....|.
gi 30682479 801 KITQAGKYHEILDS--GTDFMELVGAHTEAL 829
Cdd:PRK13537 215 RKIAEGAPHALIESeiGCDVIEIYGPDPVAL 245
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1251-1440 |
6.12e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 64.75 E-value: 6.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1251 IVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSIIPQDP-TMFEG-TIRSNLD--------PLEEY 1320
Cdd:PRK13650 38 IIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPdNQFVGaTVEDDVAfglenkgiPHEEM 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1321 TDdQIWEALDNCQLGDEVRKKELKLdspvsengqnwSVGQRQLVCLGRVLLKRSKLLVLDEATASID-TATDNLIQ--ET 1397
Cdd:PRK13650 118 KE-RVNEALELVGMQDFKEREPARL-----------SGGQKQRVAIAGAVAMRPKIIILDEATSMLDpEGRLELIKtiKG 185
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 30682479 1398 LRHHFaDCTVITIAHRISSVIDSDMVLLLDQGLIKEHDSPARL 1440
Cdd:PRK13650 186 IRDDY-QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
726-806 |
6.16e-11 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 63.67 E-value: 6.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgSHLFKEVLLGLLRHK--TVIYVTHQVE-FLPEADLILVMKDGKI 802
Cdd:cd03298 129 LSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL-RAEMLDLVLDLHAETkmTVLMVTHQPEdAKRLAQRVVFLDNGRI 207
|
....
gi 30682479 803 TQAG 806
Cdd:cd03298 208 AAQG 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
726-814 |
7.37e-11 |
|
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: 64.06 E-value: 7.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgSHLFKEVLLGLLRHK--TVIYVTHQVEFLPE-ADLILVMKDGKI 802
Cdd:cd03261 137 LSGGMKKRVALARALALDPELLLYDEPTAGLDPIA-SGVIDDLIRSLKKELglTSIMVTHDLDTAFAiADRIAVLYDGKI 215
|
90
....*....|..
gi 30682479 803 TQAGKYHEILDS 814
Cdd:cd03261 216 VAEGTPEELRAS 227
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1248-1387 |
7.62e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 65.37 E-value: 7.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1248 KT-GIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILS---IGLHDLRSRLSIIPQDPTmfegtirSNLDPLEEyTDD 1323
Cdd:PRK11308 42 KTlAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpEAQKLLRQKIQIVFQNPY-------GSLNPRKK-VGQ 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30682479 1324 QIWEALD-NCQLG-DEVRKKELKLDSPV---SENGQNW----SVGQRQLVCLGRVLLKRSKLLVLDEATASID 1387
Cdd:PRK11308 114 ILEEPLLiNTSLSaAERREKALAMMAKVglrPEHYDRYphmfSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
892-1144 |
9.11e-11 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 64.75 E-value: 9.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 892 ALAYGGAVIPLILVVQVLFQLLSIGSNYWMTWVTPvskdveppvsgFTLILVYVLLAVASsfciLIRALLVAMTGFKMAT 971
Cdd:cd18552 8 MILVAATTAALAWLLKPLLDDIFVEKDLEALLLVP-----------LAIIGLFLLRGLAS----YLQTYLMAYVGQRVVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 972 ELFTQMHLRIFRASMSFFDATPMGRILNRASTDqsvadlrlPGQFAYVAIAAIN--------ILGIIGVIVQVAWQ---V 1040
Cdd:cd18552 73 DLRNDLFDKLLRLPLSFFDRNSSGDLISRITND--------VNQVQNALTSALTvlvrdpltVIGLLGVLFYLDWKltlI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1041 LIVFIPVVAACAWY-----RQYyisAARELARLAGISrspvvHHFSETLSGITTIRSFDQEPRFRGDIMRLSDCYSRLKF 1115
Cdd:cd18552 145 ALVVLPLAALPIRRigkrlRKI---SRRSQESMGDLT-----SVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSM 216
|
250 260
....*....|....*....|....*....
gi 30682479 1116 HSTGAMEWLCFRLELLSTFAFAssLVILV 1144
Cdd:cd18552 217 KIARARALSSPLMELLGAIAIA--LVLWY 243
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
941-1133 |
9.29e-11 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 64.49 E-value: 9.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 941 ILVYVLLAVASSFCILIRALLVAMTGFKMATELFTQMHLRIFRASMSFFDATPMGRILNRASTD-QSVADlRLPGQFAYV 1019
Cdd:cd18572 39 VLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDcQKVSD-PLSTNLNVF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1020 AIAAINILGIIGVIVQVAWQ----VLIVFIPVVAACAWYRQYYISAAREL-ARLAGISRspVVHhfsETLSGITTIRSFD 1094
Cdd:cd18572 118 LRNLVQLVGGLAFMFSLSWRltllAFITVPVIALITKVYGRYYRKLSKEIqDALAEANQ--VAE---EALSNIRTVRSFA 192
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 30682479 1095 QEP----RFRGDIMRLSDCYSRLKFHSTGAMeWLCFRLELLST 1133
Cdd:cd18572 193 TEErearRYERALDKALKLSVRQALAYAGYV-AVNTLLQNGTQ 234
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
680-811 |
1.01e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 65.24 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 680 VEENILFGKPMER----EWYDRVLEACSLnkdleilpFHDQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSA 755
Cdd:PRK11607 108 VEQNIAFGLKQDKlpkaEIASRVNEMLGL--------VHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 30682479 756 VDAHTGSHLFKEVLLGLLR-HKTVIYVTH-QVEFLPEADLILVMKDGKITQAGKYHEI 811
Cdd:PRK11607 180 LDKKLRDRMQLEVVDILERvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1219-1443 |
1.08e-10 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 63.64 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHLpmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSI 1298
Cdd:PRK13548 3 LEARNLSVRLGGRT--LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1299 IPQDPTM-F----EGTIRSNLDPL-EEYTDDQ--IWEALDNCQLGDEVRKKELKLdspvsengqnwSVGQRQLVCLGRVL 1370
Cdd:PRK13548 81 LPQHSSLsFpftvEEVVAMGRAPHgLSRAEDDalVAAALAQVDLAHLAGRDYPQL-----------SGGEQQRVQLARVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1371 LKRS------KLLVLDEATASIDTATDnliQETLR--HHFAD---CTVITIAHrissviD-------SDMVLLLDQGLIK 1432
Cdd:PRK13548 150 AQLWepdgppRWLLLDEPTSALDLAHQ---HHVLRlaRQLAHergLAVIVVLH------DlnlaaryADRIVLLHQGRLV 220
|
250
....*....|.
gi 30682479 1433 EHDSPARLLED 1443
Cdd:PRK13548 221 ADGTPAEVLTP 231
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1235-1431 |
1.23e-10 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 63.06 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1235 VLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAA---GEIRIDGINiLSIGLhdLRSRLSIIPQDPTMFEG-TI 1310
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQP-RKPDQ--FQKCVAYVRQDDILLPGlTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1311 R-----SNLDPLEEYTDDQIWEALDncqlgDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEATAS 1385
Cdd:cd03234 99 RetltyTAILRLPRKSSDAIRKKRV-----EDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 30682479 1386 IDTATDNLIQETLRHHFA-DCTVITIAHRISSVIDS--DMVLLLDQGLI 1431
Cdd:cd03234 174 LDSFTALNLVSTLSQLARrNRIVILTIHQPRSDLFRlfDRILLLSSGEI 222
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
680-820 |
1.48e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 63.95 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 680 VEENILFGkPM-----EREWYDRVLEACSL-NKDLEIL---PFhdqtvigergiNLSGGQKQRIQIARALYQDADIYLFD 750
Cdd:PRK13651 123 IEKDIIFG-PVsmgvsKEEAKKRAAKYIELvGLDESYLqrsPF-----------ELSGGQKRRVALAGILAMEPDFLVFD 190
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30682479 751 DPFSAVDAHtGShlfKEVLLgLLRH-----KTVIYVTHQVE-FLPEADLILVMKDGKITQAGKYHEILdSGTDFME 820
Cdd:PRK13651 191 EPTAGLDPQ-GV---KEILE-IFDNlnkqgKTIILVTHDLDnVLEWTKRTIFFKDGKIIKDGDTYDIL-SDNKFLI 260
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1219-1455 |
1.57e-10 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 63.02 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHLpmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHdlRSRLSI 1298
Cdd:cd03300 1 IELENVSKFYGGFV--ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1299 IPQDPTMFEG-TIRSNLD-PL------EEYTDDQIWEALDNCQLGDEVRKKELKLdspvsengqnwSVGQRQLVCLGRVL 1370
Cdd:cd03300 77 VFQNYALFPHlTVFENIAfGLrlkklpKAEIKERVAEALDLVQLEGYANRKPSQL-----------SGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1371 LKRSKLLVLDEATASIDTATDNLIQETLR--HHFADCTVITIAHRISSVID-SDMVLLLDQGLIKEHDSPARLLEDRSSL 1447
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQLELKrlQKELGITFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEIYEEPANR 225
|
....*...
gi 30682479 1448 FsklVAEY 1455
Cdd:cd03300 226 F---VADF 230
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
601-812 |
1.63e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 63.47 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 601 VEISNGTFSWDDSSPipTLRDMNFKVSQGMNVAICG-------TVGSGKSSLLSSILGEV----------PKISGNLKVC 663
Cdd:PRK13644 2 IRLENVSYSYPDGTP--ALENINLVIKKGEYIGIIGkngsgksTLALHLNGLLRPQKGKVlvsgidtgdfSKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 664 GrkaYIAQSPWIQ--SGKVEENILFGK------PME-REWYDRVLEACSLNKDLEILPfhdqtvigergINLSGGQKQRI 734
Cdd:PRK13644 80 G---IVFQNPETQfvGRTVEEDLAFGPenlclpPIEiRKRVDRALAEIGLEKYRHRSP-----------KTLSGGQGQCV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30682479 735 QIARALYQDADIYLFDDPFSAVDAHTGSHLFKEVLLGLLRHKTVIYVTHQVEFLPEADLILVMKDGKITQAGKYHEIL 812
Cdd:PRK13644 146 ALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1235-1403 |
1.63e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 62.81 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1235 VLHGLTCTF-PGGLKTgIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSIIPQDPTMFEGTIRSN 1313
Cdd:PRK10247 22 ILNNISFSLrAGEFKL-ITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1314 L-----------DPleeytdDQIWEALDNCQLGDEVrkkelkLDSPVSEngqnWSVGQRQLVCLGRVLLKRSKLLVLDEA 1382
Cdd:PRK10247 101 LifpwqirnqqpDP------AIFLDDLERFALPDTI------LTKNIAE----LSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180
....*....|....*....|.
gi 30682479 1383 TASIDTATDNLIQETLrHHFA 1403
Cdd:PRK10247 165 TSALDESNKHNVNEII-HRYV 184
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1219-1454 |
1.66e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 63.18 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHLP---MVLHGLTCTfpggLKTG----IVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHD 1291
Cdd:COG1101 2 LELKNLSKTFNPGTVnekRALDGLNLT----IEEGdfvtVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1292 lRSRL-SIIPQDPTMfeGT-----IRSNL------------------DPLEEYTddqiwEALDNCQLGDEVRkkelkLDS 1347
Cdd:COG1101 78 -RAKYiGRVFQDPMM--GTapsmtIEENLalayrrgkrrglrrgltkKRRELFR-----ELLATLGLGLENR-----LDT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1348 PVSengqNWSVGQRQLVCLGRVLLKRSKLLVLDEATASID--TA------TDNLIQEtlrHHfadCTVITIAHRISSVID 1419
Cdd:COG1101 145 KVG----LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDpkTAalvlelTEKIVEE---NN---LTTLMVTHNMEQALD 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 30682479 1420 -SDMVLLLDQGLI--------KEHDSPARLLEdrssLFSKLVAE 1454
Cdd:COG1101 215 yGNRLIMMHEGRIildvsgeeKKKLTVEDLLE----LFEEIRGE 254
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1219-1428 |
1.73e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.21 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHlpMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRidginilsiglHDLRSRLSI 1298
Cdd:PRK09544 5 VSLENVSVSFGQR--RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-----------RNGKLRIGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1299 IPQ----DPTMFEGTIR-SNLDPLEEYTDdqIWEALDNCQLGDevrkkelKLDSPVsengQNWSVGQRQLVCLGRVLLKR 1373
Cdd:PRK09544 72 VPQklylDTTLPLTVNRfLRLRPGTKKED--ILPALKRVQAGH-------LIDAPM----QKLSGGETQRVLLARALLNR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1374 SKLLVLDEATASIDT----ATDNLIQEtLRHHFaDCTVITIAHRISSVI-DSDMVLLLDQ 1428
Cdd:PRK09544 139 PQLLVLDEPTQGVDVngqvALYDLIDQ-LRREL-DCAVLMVSHDLHLVMaKTDEVLCLNH 196
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1223-1412 |
1.73e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 65.47 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1223 NLQVRYGPHLpmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGinilsiGLhdlrsRLSIIPQD 1302
Cdd:COG0488 3 NLSKSFGGRP--LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK------GL-----RIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1303 PTMFEG-TIRSNL-------------------------DPLEEYTDDQ-IWEALDNCQLGDEVRK-------KELKLDSP 1348
Cdd:COG0488 70 PPLDDDlTVLDTVldgdaelraleaeleeleaklaepdEDLERLAELQeEFEALGGWEAEARAEEilsglgfPEEDLDRP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30682479 1349 VSEngqnWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTATDNLIQETLRHHfaDCTVITIAH 1412
Cdd:COG0488 150 VSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNY--PGTVLVVSH 207
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
726-806 |
1.76e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 63.23 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDahtgSHLFKEVL---LGLLRHK-TVIYVTHQVEFLPE-ADLILVMKDG 800
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALD----PELVGEVLntiRQLAQEKrTMVIVTHEMSFARDvADRAIFMDQG 220
|
....*.
gi 30682479 801 KITQAG 806
Cdd:PRK11264 221 RIVEQG 226
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1226-1443 |
1.83e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 63.17 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1226 VRYGPHLpMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSI---GLHDLRSRLSIIPQD 1302
Cdd:PRK10419 19 SGKHQHQ-TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1303 -PTMF--EGTIRSNLD-PLEEYTDdqiweaLDncQLGDEVRKKELKL-----DSPVSENGQNWSVGQRQLVCLGRVLLKR 1373
Cdd:PRK10419 98 sISAVnpRKTVREIIRePLRHLLS------LD--KAERLARASEMLRavdldDSVLDKRPPQLSGGQLQRVCLARALAVE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1374 SKLLVLDEATASIDTatdnLIQ-------ETLRHHFAD-CTVIT--------IAHRissvidsdmVLLLDQGLIKEH--- 1434
Cdd:PRK10419 170 PKLLILDEAVSNLDL----VLQagvirllKKLQQQFGTaCLFIThdlrlverFCQR---------VMVMDNGQIVETqpv 236
|
250
....*....|....*.
gi 30682479 1435 ------DSPA-RLLED 1443
Cdd:PRK10419 237 gdkltfSSPAgRVLQN 252
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1217-1453 |
1.88e-10 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 64.32 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1217 GEITICNLQVRYGPHLpmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIqtlfRIV----EPAAGEIRIDGINILsiGLHDL 1292
Cdd:COG3839 2 ASLELENVSKSYGGVE--ALKDIDLDIEDGEFLVLLGPSGCGKSTLL----RMIagleDPTSGEILIGGRDVT--DLPPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1293 RSRLSIIPQD----PTMfegTIRSNLD-PLE------EYTDDQIWEALDNCQLGD--EVRKKELkldspvsengqnwSVG 1359
Cdd:COG3839 74 DRNIAMVFQSyalyPHM---TVYENIAfPLKlrkvpkAEIDRRVREAAELLGLEDllDRKPKQL-------------SGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1360 QRQLVCLGRVLLKRSKLLVLDEATASIDTAtdnlIQETLRHHFAD------CTVI----------TIAHRIssvidsdmv 1423
Cdd:COG3839 138 QRQRVALGRALVREPKVFLLDEPLSNLDAK----LRVEMRAEIKRlhrrlgTTTIyvthdqveamTLADRI--------- 204
|
250 260 270
....*....|....*....|....*....|
gi 30682479 1424 LLLDQGLIKEHDSPARLLEDRSSLFsklVA 1453
Cdd:COG3839 205 AVMNDGRIQQVGTPEELYDRPANLF---VA 231
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
679-834 |
1.93e-10 |
|
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: 64.36 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 679 KVEENILFGK-----PMEREWYDRVLEACSLNKDLEILPFhdqtvigergiNLSGGQKQRIQIARALYQDADIYLFDDPF 753
Cdd:TIGR02142 91 SVRGNLRYGMkrarpSERRISFERVIELLGIGHLLGRLPG-----------RLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 754 SAVDahtgSHLFKEVL--LGLLRHKT---VIYVTHQV-EFLPEADLILVMKDGKITQAGKYHEILDSGtdfmELVGAHTE 827
Cdd:TIGR02142 160 AALD----DPRKYEILpyLERLHAEFgipILYVSHSLqEVLRLADRVVVLEDGRVAAAGPIAEVWASP----DLPWLARE 231
|
....*..
gi 30682479 828 ALATIDS 834
Cdd:TIGR02142 232 DQGSLIE 238
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
673-811 |
2.68e-10 |
|
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: 62.10 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 673 PWIQsgkVEENILFGkpmerewYDRVLEACSLNKDLEILPFHDQTV-----IGERGINLSGGQKQRIQIARALYQDADIY 747
Cdd:TIGR01184 67 PWLT---VRENIALA-------VDRVLPDLSKSERRAIVEEHIALVglteaADKRPGQLSGGMKQRVAIARALSIRPKVL 136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30682479 748 LFDDPFSAVDAHTGSHLfKEVLLGLLR--HKTVIYVTHQV-EFLPEADLILVMKDGKITQAGKYHEI 811
Cdd:TIGR01184 137 LLDEPFGALDALTRGNL-QEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1236-1447 |
2.78e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 62.87 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1236 LHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIG----LHDLRSRLSIIPQDP--TMFEGT 1309
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyIRPVRKRIGMVFQFPesQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1310 IRS-----------NLDPLEEYTDDQIwealdnCQLGDEvrkKELKLDSPVSENGqnwsvGQRQLVCLGRVLLKRSKLLV 1378
Cdd:PRK13646 103 VEReiifgpknfkmNLDEVKNYAHRLL------MDLGFS---RDVMSQSPFQMSG-----GQMRKIAIVSILAMNPDIIV 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30682479 1379 LDEATASIDTATDNLIQETLRHHFAD--CTVITIAHRISSVID-SDMVLLLDQGLIKEHDSPARLLEDRSSL 1447
Cdd:PRK13646 169 LDEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKDKKKL 240
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1250-1426 |
2.81e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 63.57 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1250 GIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIG---LHDLRSRLSIIPQD------PTMFEGTIRSnlDPLEEY 1320
Cdd:PRK15079 51 GVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKddeWRAVRSDIQMIFQDplaslnPRMTIGEIIA--EPLRTY 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1321 TDDqiweaLDNCQLGDEVRKKELK---LDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTATD----NL 1393
Cdd:PRK15079 129 HPK-----LSRQEVKDRVKAMMLKvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQaqvvNL 203
|
170 180 190
....*....|....*....|....*....|....*
gi 30682479 1394 IQETLRHhfADCTVITIAHRISSV--IdSDMVLLL 1426
Cdd:PRK15079 204 LQQLQRE--MGLSLIFIAHDLAVVkhI-SDRVLVM 235
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
680-806 |
3.33e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 63.71 E-value: 3.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 680 VEENILFG---KPMEREWYD-RVLEACslnKDLEILPFHDQtvigeRGINLSGGQKQRIQIARALYQDADIYLFDDPFSA 755
Cdd:PRK11650 93 VRENMAYGlkiRGMPKAEIEeRVAEAA---RILELEPLLDR-----KPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSN 164
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30682479 756 VDAHtgshlfkevllglLR----------HK----TVIYVTH-QVEFLPEADLILVMKDGKITQAG 806
Cdd:PRK11650 165 LDAK-------------LRvqmrleiqrlHRrlktTSLYVTHdQVEAMTLADRVVVMNGGVAEQIG 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
680-802 |
3.45e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 64.27 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 680 VEENILFGK-PMEREWYDR---------VLEACSLNKDLEilpfhdqTVIGErginLSGGQKQRIQIARALYQDADIYLF 749
Cdd:COG1129 96 VAENIFLGRePRRGGLIDWramrrrareLLARLGLDIDPD-------TPVGD----LSVAQQQLVEIARALSRDARVLIL 164
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 30682479 750 DDPFSAVDAHTGSHLFKevLLGLLRHK--TVIYVTHqveFLPE----ADLILVMKDGKI 802
Cdd:COG1129 165 DEPTASLTEREVERLFR--IIRRLKAQgvAIIYISH---RLDEvfeiADRVTVLRDGRL 218
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1223-1429 |
3.62e-10 |
|
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: 61.14 E-value: 3.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1223 NLQVRYGPHlpMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGiNILSIglhDLRSRLSIIPQD 1302
Cdd:cd03269 5 NVTKRFGRV--TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG-KPLDI---AARNRIGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1303 ----PTMfegTIRSNLDPLEEYTDDQIWEALDncQLGDEVRKKEL--KLDSPVSEngqnWSVGQRQLVCLGRVLLKRSKL 1376
Cdd:cd03269 79 rglyPKM---KVIDQLVYLAQLKGLKKEEARR--RIDEWLERLELseYANKRVEE----LSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 30682479 1377 LVLDEATASIDTATDNLIQETLRHHF-ADCTVITIAHRISSVID-SDMVLLLDQG 1429
Cdd:cd03269 150 LILDEPFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELVEElCDRVLLLNKG 204
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
673-802 |
3.74e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 62.39 E-value: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 673 PWiqsGKVEENILFGkpMEREWYDRVLEAcslnkdLEILPFHDQTviGERGINLSGGQKQRIQIARALYQDADIYLFDDP 752
Cdd:PRK11247 94 PW---KKVIDNVGLG--LKGQWRDAALQA------LAAVGLADRA--NEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 30682479 753 FSAVDAHTGSHLfKEVLLGLLR--HKTVIYVTHQV-EFLPEADLILVMKDGKI 802
Cdd:PRK11247 161 LGALDALTRIEM-QDLIESLWQqhGFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
726-813 |
4.06e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 61.65 E-value: 4.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDahtgSHLFKEVLL--------GLlrhkTVIYVTHQVEFLPE-ADLILV 796
Cdd:PRK09493 137 LSGGQQQRVAIARALAVKPKLMLFDEPTSALD----PELRHEVLKvmqdlaeeGM----TMVIVTHEIGFAEKvASRLIF 208
|
90
....*....|....*..
gi 30682479 797 MKDGKITQAGKYHEILD 813
Cdd:PRK09493 209 IDKGRIAEDGDPQVLIK 225
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
715-814 |
4.07e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 62.29 E-value: 4.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 715 DQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDahtgSHLFKEVLLGLLR----HKTVIYVTHQVEFLPE 790
Cdd:PRK10619 142 DERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALD----PELVGEVLRIMQQlaeeGKTMVVVTHEMGFARH 217
|
90 100
....*....|....*....|....*
gi 30682479 791 -ADLILVMKDGKITQAGKYHEILDS 814
Cdd:PRK10619 218 vSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1215-1446 |
4.39e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 61.91 E-value: 4.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1215 SRGEITICNLQVRYGPHlpMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSI------- 1287
Cdd:PRK10619 2 SENKLNVIDLHKRYGEH--EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgql 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1288 ------GLHDLRSRLSIIPQD------PTMFEGTIRSNLDPL---EEYTDDQIWEALDNCQLGDEVRKKelkldSPVSEN 1352
Cdd:PRK10619 80 kvadknQLRLLRTRLTMVFQHfnlwshMTVLENVMEAPIQVLglsKQEARERAVKYLAKVGIDERAQGK-----YPVHLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1353 GqnwsvGQRQLVCLGRVLLKRSKLLVLDEATASIDTatdNLIQETLR--HHFAD--CTVITIAHRISSVID-SDMVLLLD 1427
Cdd:PRK10619 155 G-----GQQQRVSIARALAMEPEVLLFDEPTSALDP---ELVGEVLRimQQLAEegKTMVVVTHEMGFARHvSSHVIFLH 226
|
250
....*....|....*....
gi 30682479 1428 QGLIKEHDSPARLLEDRSS 1446
Cdd:PRK10619 227 QGKIEEEGAPEQLFGNPQS 245
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
726-832 |
4.81e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 62.93 E-value: 4.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHtGSHLFKEVLLGLL-RHKTVIYVTHqveFLPEA----DLILVMKDG 800
Cdd:PRK13536 173 LSGGMKRRLTLARALINDPQLLILDEPTTGLDPH-ARHLIWERLRSLLaRGKTILLTTH---FMEEAerlcDRLCVLEAG 248
|
90 100 110
....*....|....*....|....*....|....
gi 30682479 801 KITQAGKYHEILDS--GTDFMELVGAHTEALATI 832
Cdd:PRK13536 249 RKIAEGRPHALIDEhiGCQVIEIYGGDPHELSSL 282
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1251-1389 |
4.97e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 64.11 E-value: 4.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1251 IVGRTGCGKSTLIQTLFRIVEPAAGEIRIDG--INILSIG-LHDLRSRLSIIPQDPTmfegtirSNLDPlEEYTDDQIWE 1327
Cdd:PRK10261 355 LVGESGSGKSTTGRALLRLVESQGGEIIFNGqrIDTLSPGkLQALRRDIQFIFQDPY-------ASLDP-RQTVGDSIME 426
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30682479 1328 ALDNCQL--GDEVRKKELKLDSPVS---ENG----QNWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTA 1389
Cdd:PRK10261 427 PLRVHGLlpGKAAAARVAWLLERVGllpEHAwrypHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
720-796 |
5.11e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 61.64 E-value: 5.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 720 GERGI-NLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLfKEVLLGLLRH--KTVIYVTHQVE---FLPeADL 793
Cdd:PRK11248 122 EKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQM-QTLLLKLWQEtgKQVLLITHDIEeavFMA-TEL 199
|
...
gi 30682479 794 ILV 796
Cdd:PRK11248 200 VLL 202
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
671-811 |
5.21e-10 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 61.04 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 671 QSPWIQSGKVEENILFGKPMEREWYDRVLEAcSLNKDLEI--LP--FHDQTvigeRGINLSGGQKQRIQIARALYQDADI 746
Cdd:cd03260 88 QKPNPFPGSIYDNVAYGLRLHGIKLKEELDE-RVEEALRKaaLWdeVKDRL----HALGLSGGQQQRLCLARALANEPEV 162
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30682479 747 YLFDDPFSAVDAHTGSHLfkEVLLGLLRHK-TVIYVTH---QVEFLpeADLILVMKDGKITQAGKYHEI 811
Cdd:cd03260 163 LLLDEPTSALDPISTAKI--EELIAELKKEyTIVIVTHnmqQAARV--ADRTAFLLNGRLVEFGPTEQI 227
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1234-1409 |
5.30e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.59 E-value: 5.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1234 MVLHGLTCTF-PGGLkTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGlHDLRSRLsiipqdptMFEG---T 1309
Cdd:PRK13538 15 ILFSGLSFTLnAGEL-VQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR-DEYHQDL--------LYLGhqpG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1310 IRSNLDPLE----------EYTDDQIWEALDncQLGdeVRKKElklDSPVSengqNWSVGQRQLVCLGRVLLKRSKLLVL 1379
Cdd:PRK13538 85 IKTELTALEnlrfyqrlhgPGDDEALWEALA--QVG--LAGFE---DVPVR----QLSAGQQRRVALARLWLTRAPLWIL 153
|
170 180 190
....*....|....*....|....*....|..
gi 30682479 1380 DEATASIDTATDNLIQETLRHHFAD--CTVIT 1409
Cdd:PRK13538 154 DEPFTAIDKQGVARLEALLAQHAEQggMVILT 185
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
726-821 |
5.52e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 61.95 E-value: 5.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgshlfKEVLLGLLRH------KTVIYVTHQVEFLPEADLILVMKD 799
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRG-----RREVLETVRQlkeqkgITVLSITHDLDEAAQADRVIVMNK 215
|
90 100
....*....|....*....|..
gi 30682479 800 GKITQAGKYHEILDSGTDFMEL 821
Cdd:PRK13635 216 GEILEEGTPEEIFKSGHMLQEI 237
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1235-1403 |
5.84e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 60.66 E-value: 5.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1235 VLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINilsIGLHDLRSRLSII-PQDPTMFEGTIRSN 1313
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD---IDDPDVAEACHYLgHRNAMKPALTVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1314 LDPLEEY---TDDQIWEALDNCQLGD--EVRKKELkldspvsengqnwSVGQRQLVCLGRVLLKRSKLLVLDEATASIDT 1388
Cdd:PRK13539 94 LEFWAAFlggEELDIAAALEAVGLAPlaHLPFGYL-------------SAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
170
....*....|....*
gi 30682479 1389 ATDNLIQETLRHHFA 1403
Cdd:PRK13539 161 AAVALFAELIRAHLA 175
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
725-802 |
6.76e-10 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 60.60 E-value: 6.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 725 NLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFkEVLLGLLRHKTVIYVTHQVEflpEADL----ILVMKDG 800
Cdd:cd03263 133 TLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIW-DLILEVRKGRSIILTTHSMD---EAEAlcdrIAIMSDG 208
|
..
gi 30682479 801 KI 802
Cdd:cd03263 209 KL 210
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1235-1399 |
7.06e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 62.54 E-value: 7.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1235 VLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGlHDLRSRLSIIPQ-DPTMFEGTIRSN 1313
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA-RLARARIGVVPQfDNLDLEFTVREN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1314 LDPLEEY---TDDQIwEALDNCQLgdEVRKKELKLDSPVSEngqnWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTAT 1390
Cdd:PRK13536 135 LLVFGRYfgmSTREI-EAVIPSLL--EFARLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHA 207
|
....*....
gi 30682479 1391 DNLIQETLR 1399
Cdd:PRK13536 208 RHLIWERLR 216
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1235-1442 |
7.87e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 61.34 E-value: 7.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1235 VLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSIIPQDPTMFEGTIRSNL 1314
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1315 DPLEEYTddqiWE-ALDncQLGDEVRKkelKLDSPVSENG---------QNWSVGQRQLVCLGRVLLKRSKLLVLDEATA 1384
Cdd:PRK10575 106 VAIGRYP----WHgALG--RFGAADRE---KVEEAISLVGlkplahrlvDSLSGGERQRAWIAMLVAQDSRCLLLDEPTS 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30682479 1385 SIDTATD----NLIQETLRHHfaDCTVITIAHRISSVID-SDMVLLLDQGLIKEHDSPARLLE 1442
Cdd:PRK10575 177 ALDIAHQvdvlALVHRLSQER--GLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMR 237
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
680-814 |
9.81e-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: 60.76 E-value: 9.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 680 VEENILFgkPM-------EREWYDRV---LEACSLNKDLEILPfhdqtviGErginLSGGQKQRIQIARALYQDADIYLF 749
Cdd:COG1127 99 VFENVAF--PLrehtdlsEAEIRELVlekLELVGLPGAADKMP-------SE----LSGGMRKRVALARALALDPEILLY 165
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30682479 750 DDPFSAVDAHTgSHLFKEVLLGlLRHK---TVIYVTHQVEFLPE-ADLILVMKDGKITQAGKYHEILDS 814
Cdd:COG1127 166 DEPTAGLDPIT-SAVIDELIRE-LRDElglTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLAS 232
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
726-806 |
1.08e-09 |
|
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: 59.99 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAhTGSHLFKEVLLGLLRH-KTVIYVTHQVEFLPE-ADLILVMKDGKIT 803
Cdd:cd03269 129 LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VNVELLKDVIRELARAgKTVILSTHQMELVEElCDRVLLLNKGRAV 207
|
...
gi 30682479 804 QAG 806
Cdd:cd03269 208 LYG 210
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1235-1443 |
1.19e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 60.29 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1235 VLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDlRSRLSI--IPQDPTMFEG-TIR 1311
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA-RARRGIgyLPQEASIFRRlSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1312 SNLDPLEEYTDDQIWEAldncqlgDEVRKKELKLDSPVSE----NGQNWSVGQRQLVCLGRVLLKRSKLLVLDEATASID 1387
Cdd:PRK10895 97 DNLMAVLQIRDDLSAEQ-------REDRANELMEEFHIEHlrdsMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 30682479 1388 TATDNLIQETLRH-HFADCTVITIAHRISSVID-SDMVLLLDQGLIKEHDSPARLLED 1443
Cdd:PRK10895 170 PISVIDIKRIIEHlRDSGLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
726-812 |
1.32e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 60.62 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEVL-----LGLlrhkTVIYVTHQ---VEFLpeADLILVM 797
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLelqekLGI----SYIYVSQHlgiVKHI--SDKVLVM 223
|
90
....*....|....*
gi 30682479 798 KDGKITQAGKYHEIL 812
Cdd:COG4167 224 HQGEVVEYGKTAEVF 238
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
597-806 |
1.32e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 60.67 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 597 SEMAVEISNGTFSWDDSSPipTLRDMNFKVSQGMNVAICGTVGSGKSSLLSSILGEVPKISGNLKVCGRK---------- 666
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNGHT--ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPtrqalqknlv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 667 AYIAQSP---WIQSGKVEENILFGKPMEREW------YDRVLEACSLNKdLEILPF-HDQtvIGErginLSGGQKQRIQI 736
Cdd:PRK15056 81 AYVPQSEevdWSFPVLVEDVVMMGRYGHMGWlrrakkRDRQIVTAALAR-VDMVEFrHRQ--IGE----LSGGQKKRVFL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30682479 737 ARALYQDADIYLFDDPFSAVDAHTGSHLFKevLLGLLRH--KTVIYVTHQVEFLPEADLILVMKDGKITQAG 806
Cdd:PRK15056 154 ARAIAQQGQVILLDEPFTGVDVKTEARIIS--LLRELRDegKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1219-1454 |
1.40e-09 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 61.65 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHLpmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTL--FriVEPAAGEIRIDGINILSIGLHDlRsRL 1296
Cdd:COG3842 6 LELENVSKRYGDVT--ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIagF--ETPDSGRILLDGRDVTGLPPEK-R-NV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1297 SIIPQD----PTMfegTIRSNLD-PLE------EYTDDQIWEALDNCQLGD-EVRK-KELkldspvsengqnwSVGQRQL 1363
Cdd:COG3842 80 GMVFQDyalfPHL---TVAENVAfGLRmrgvpkAEIRARVAELLELVGLEGlADRYpHQL-------------SGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1364 VCLGRVLLKRSKLLVLDEATASIDTATDNLIQETLRHHFADC--TVITIAHrissviD-------SDMVLLLDQGLIKEH 1434
Cdd:COG3842 144 VALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELgiTFIYVTH------DqeealalADRIAVMNDGRIEQV 217
|
250 260
....*....|....*....|
gi 30682479 1435 DSPARLLEDRSSLFsklVAE 1454
Cdd:COG3842 218 GTPEEIYERPATRF---VAD 234
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
942-1146 |
1.49e-09 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 61.31 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 942 LVYVLLAVASSFCILIRALLVAMTGFKMATELFTQMHLRIFRASMSFFDA---TPmGRILNRASTDqsVADLR-LPGQF- 1016
Cdd:cd18578 56 LMFLVLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDDpenST-GALTSRLSTD--ASDVRgLVGDRl 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1017 AYVAIAAINILG--IIGVIvqVAWQ---VLIVFIPVVAACAWYRQYYIS-----AARELARLAGIsrspvvhhFSETLSG 1086
Cdd:cd18578 133 GLILQAIVTLVAglIIAFV--YGWKlalVGLATVPLLLLAGYLRMRLLSgfeekNKKAYEESSKI--------ASEAVSN 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30682479 1087 ITTIRSFDQEPRFRGDIMR-LSDCY--SRLKFHSTGAmewlcfrlellsTFAFASSLVILVSA 1146
Cdd:cd18578 203 IRTVASLTLEDYFLEKYEEaLEEPLkkGLRRALISGL------------GFGLSQSLTFFAYA 253
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
680-811 |
1.65e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 60.48 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 680 VEENILFGkPM-----EREWYDRVLEAcsLNK----DLEILPFHdqtvigergiNLSGGQKQRIQIARALYQDADIYLFD 750
Cdd:PRK13639 96 VEEDVAFG-PLnlglsKEEVEKRVKEA--LKAvgmeGFENKPPH----------HLSGGQKKRVAIAGILAMKPEIIVLD 162
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30682479 751 DPFSAVDAHTGSHLFKevLLGLLRHK--TVIYVTHQVEFLPE-ADLILVMKDGKITQAGKYHEI 811
Cdd:PRK13639 163 EPTSGLDPMGASQIMK--LLYDLNKEgiTIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEV 224
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
726-806 |
1.80e-09 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 60.03 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVD--------------AHTGShlfkevllgllrhkTVIYVTHQVEFLPE- 790
Cdd:COG4161 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeitaqvveiirelSQTGI--------------TQVIVTHEVEFARKv 207
|
90
....*....|....*.
gi 30682479 791 ADLILVMKDGKITQAG 806
Cdd:COG4161 208 ASQVVYMEKGRIIEQG 223
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
601-821 |
1.87e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 60.52 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 601 VEISNGTFSWDDSSPIPTLRDMNFKVSQGMNVAICGTVGSGKSSLLSSILGEVPKISGNLKVCGRK-------------A 667
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLlteenvwdirhkiG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 668 YIAQSPWIQ--SGKVEENILFG---KPMER-EWYDRVLEACSLnkdLEILPFHDQtvigeRGINLSGGQKQRIQIARALY 741
Cdd:PRK13650 85 MVFQNPDNQfvGATVEDDVAFGlenKGIPHeEMKERVNEALEL---VGMQDFKER-----EPARLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 742 QDADIYLFDDPFSAVDAHTGSHLFKEVllGLLRHK---TVIYVTHQVEFLPEADLILVMKDGKITQAGKYHEILDSGTDF 818
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTI--KGIRDDyqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGNDL 234
|
...
gi 30682479 819 MEL 821
Cdd:PRK13650 235 LQL 237
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
726-814 |
2.03e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 61.59 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEVLLGLLRH-KTVIYVTHQV-EFLPEADLILVMKDGKIT 803
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHqRTIVFISHDLdEAMRIGDRIAIMQNGEVV 244
|
90
....*....|.
gi 30682479 804 QAGKYHEILDS 814
Cdd:PRK10070 245 QVGTPDEILNN 255
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
726-814 |
2.04e-09 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 59.81 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDahtgSHLFKEVlLGLLR-----HKTVIYVTHQVEFLPE-ADLILVMKD 799
Cdd:COG4598 155 LSGGQQQRAAIARALAMEPEVMLFDEPTSALD----PELVGEV-LKVMRdlaeeGRTMLVVTHEMGFARDvSSHVVFLHQ 229
|
90
....*....|....*
gi 30682479 800 GKITQAGKYHEILDS 814
Cdd:COG4598 230 GRIEEQGPPAEVFGN 244
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1236-1417 |
2.07e-09 |
|
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: 61.76 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1236 LHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAA--GEIRIDGINILSIGLHDL-RSRLSIIPQDPTMF-EGTIR 1311
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVpELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1312 SNLDPLEEYTDDQIWEALDNCQLGDEVRKKELKLD-SPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEATASIdTAT 1390
Cdd:TIGR02633 97 ENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDaDNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL-TEK 175
|
170 180 190
....*....|....*....|....*....|..
gi 30682479 1391 D-----NLIQETLRHHFAdCtvITIAHRISSV 1417
Cdd:TIGR02633 176 EteillDIIRDLKAHGVA-C--VYISHKLNEV 204
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
928-1098 |
2.52e-09 |
|
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: 60.22 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 928 SKDVEPPVSGFTLILVYVLLA---VASSFCILIRALLVAMTGFKMATELFTQMHLRIFRASMSFFDATPMGRILNRASTD 1004
Cdd:cd18573 28 KESGDIEIFGLSLKTFALALLgvfVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1005 QSVADLRLPGQFAYVAIAAINILGIIGVIVQVAWQ---VLIVFIPVVAACAWyrqYYISAARELAR-----LAGISRSPv 1076
Cdd:cd18573 108 TSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKltlVMLLVVPPIAVGAV---FYGRYVRKLSKqvqdaLADATKVA- 183
|
170 180
....*....|....*....|..
gi 30682479 1077 vhhfSETLSGITTIRSFDQEPR 1098
Cdd:cd18573 184 ----EERLSNIRTVRAFAAERK 201
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1218-1448 |
2.92e-09 |
|
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: 59.28 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1218 EITICNLQVRYGPHlpMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSiglHDLRSR-L 1296
Cdd:cd03296 2 SIEVRNVSKRFGDF--VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATD---VPVQERnV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1297 SIIPQDPTMFEG-TIRsnldpleeytddqiwealDNCQLGDEVRKK-----ELKLDSPVSENGQ----NW---------S 1357
Cdd:cd03296 77 GFVFQHYALFRHmTVF------------------DNVAFGLRVKPRserppEAEIRAKVHELLKlvqlDWladrypaqlS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1358 VGQRQLVCLGRVLLKRSKLLVLDEATASIDTATDNLIQETLR--HHFADCTVITIAHRISSVID-SDMVLLLDQGLIKEH 1434
Cdd:cd03296 139 GGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRrlHDELHVTTVFVTHDQEEALEvADRVVVMNKGRIEQV 218
|
250
....*....|....
gi 30682479 1435 DSPARLLEDRSSLF 1448
Cdd:cd03296 219 GTPDEVYDHPASPF 232
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
725-811 |
3.15e-09 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 60.58 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 725 NLSGGQKQRIQIARALYQDADIYLFDDPFSAVD-AHTGS--HLFKEV--LLGLlrhkTVIYVTHQVEFLPE-ADLILVMK 798
Cdd:PRK11153 140 QLSGGQKQRVAIARALASNPKVLLCDEATSALDpATTRSilELLKDInrELGL----TIVLITHEMDVVKRiCDRVAVID 215
|
90
....*....|...
gi 30682479 799 DGKITQAGKYHEI 811
Cdd:PRK11153 216 AGRLVEQGTVSEV 228
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1250-1437 |
3.62e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 59.72 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1250 GIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIG-LHDLRSRLSIIPQDP------TMFEGTIR---SNL--DPL 1317
Cdd:PRK13633 40 VILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIRNKAGMVFQNPdnqivaTIVEEDVAfgpENLgiPPE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1318 EeytddqIWEALDNCQlgDEVRKKELKLDSPVSENGqnwsvGQRQLVCLGRVLLKRSKLLVLDEATASIDTATD----NL 1393
Cdd:PRK13633 120 E------IRERVDESL--KKVGMYEYRRHAPHLLSG-----GQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRrevvNT 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 30682479 1394 IQETLRHHfaDCTVITIAHRISSVIDSDMVLLLDQGLIKEHDSP 1437
Cdd:PRK13633 187 IKELNKKY--GITIILITHYMEEAVEADRIIVMDSGKVVMEGTP 228
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1250-1429 |
3.88e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.10 E-value: 3.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1250 GIVGRTGCGKSTLIQTLFRiVEPAA---GEIRIDGINILSIGLHDL-RSRLSIIPQdptmfEGTIRSNLDPLEeytddqi 1325
Cdd:PRK13549 35 SLCGENGAGKSTLMKVLSG-VYPHGtyeGEIIFEGEELQASNIRDTeRAGIAIIHQ-----ELALVKELSVLE------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1326 wealdNCQLGDEVRK-----------------KELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEATASIdT 1388
Cdd:PRK13549 102 -----NIFLGNEITPggimdydamylraqkllAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASL-T 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 30682479 1389 ATD-----NLIQEtLRHHFADCtvITIAHRISSVID-SDMVLLLDQG 1429
Cdd:PRK13549 176 ESEtavllDIIRD-LKAHGIAC--IYISHKLNEVKAiSDTICVIRDG 219
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
726-812 |
4.40e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 58.87 E-value: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAhtgSHLFKevLLGLLRH-----KTVIYVTHQvefLPEA----DLILV 796
Cdd:PRK11231 139 LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDI---NHQVE--LMRLMRElntqgKTVVTVLHD---LNQAsrycDHLVV 210
|
90
....*....|....*.
gi 30682479 797 MKDGKITQAGKYHEIL 812
Cdd:PRK11231 211 LANGHVMAQGTPEEVM 226
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
679-814 |
5.63e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 59.89 E-value: 5.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 679 KVEENILFG-KPMEREWYDRVLEACSLNKDLEILPfhdqtvigergINLSGGQKQRIQIARALYQDADIYLFDDPFSAVD 757
Cdd:PRK11144 92 KVRGNLRYGmAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30682479 758 AHTGshlfKEVL--LGLLRHKT---VIYVTHQV-EFLPEADLILVMKDGKITQAGKYHEILDS 814
Cdd:PRK11144 161 LPRK----RELLpyLERLAREInipILYVSHSLdEILRLADRVVVLEQGKVKAFGPLEEVWAS 219
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1208-1435 |
6.60e-09 |
|
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: 57.93 E-value: 6.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1208 RPEKSWPSRGEITICNLQVRYGPHlpMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGiNI--- 1284
Cdd:cd03220 12 TYKGGSSSLKKLGILGRKGEVGEF--WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVssl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1285 --LSIGLH-DLRSRlsiipqDPTMFEGTIrSNLDPleEYTDDQIWEALDNCQLGDevrkkelKLDSPVSengqNWSVGQR 1361
Cdd:cd03220 89 lgLGGGFNpELTGR------ENIYLNGRL-LGLSR--KEIDEKIDEIIEFSELGD-------FIDLPVK----TYSSGMK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30682479 1362 QLVCLGRVLLKRSKLLVLDEATASIDTATDNLIQETLRHHFADC-TVITIAHRISSVID-SDMVLLLDQGLIKEHD 1435
Cdd:cd03220 149 ARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGkTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
938-1099 |
7.11e-09 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 58.95 E-value: 7.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 938 FTLILVYVLLAVASSFCILIRALLVAMTGFKMATELFTQMHlrifRASMSFFDATPMGRILNRASTD---------QSVA 1008
Cdd:cd18547 49 LLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQ----RLPLSYFDTHSHGDIMSRVTNDvdnisqalsQSLT 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1009 DLrlpgqfayvAIAAINILGIIGVIVQVAWQ---VLIVFIPVVAACAWY-----RQYYISAARELARLAGisrspvvhHF 1080
Cdd:cd18547 125 QL---------ISSILTIVGTLIMMLYISPLltlIVLVTVPLSLLVTKFiakrsQKYFRKQQKALGELNG--------YI 187
|
170
....*....|....*....
gi 30682479 1081 SETLSGITTIRSFDQEPRF 1099
Cdd:cd18547 188 EEMISGQKVVKAFNREEEA 206
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1239-1415 |
7.91e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 60.15 E-value: 7.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1239 LTCTFPGGLKTGIVGRTGCGKSTLiqtlFRIVepaaGEIRIDGINILSIglhDLRSRLSIIPQDPTMFEGTIRSNL---D 1315
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSSL----FRIL----GELWPVYGGRLTK---PAKGKLFYVPQRPYMTLGTLRDQIiypD 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1316 PLEE-----YTDDQIWEALDNCQLGDEVrKKELKLDSPvsengQNW----SVGQRQLVCLGRVLLKRSKLLVLDEATASI 1386
Cdd:TIGR00954 540 SSEDmkrrgLSDKDLEQILDNVQLTHIL-EREGGWSAV-----QDWmdvlSGGEKQRIAMARLFYHKPQFAILDECTSAV 613
|
170 180
....*....|....*....|....*....
gi 30682479 1387 DTATDNLIQETLRHhfADCTVITIAHRIS 1415
Cdd:TIGR00954 614 SVDVEGYMYRLCRE--FGITLFSVSHRKS 640
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1251-1443 |
9.17e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 59.28 E-value: 9.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1251 IVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRS----RLSIIPQDPTMFEGTIrsnldpleeytddqiw 1326
Cdd:PRK10070 59 IMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPHMT---------------- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1327 eALDNCQLGDEV------RKKELKLDSPVSENGQNW--------SVGQRQLVCLGRVLLKRSKLLVLDEATASID----- 1387
Cdd:PRK10070 123 -VLDNTAFGMELaginaeERREKALDALRQVGLENYahsypdelSGGMRQRVGLARALAINPDILLMDEAFSALDplirt 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 30682479 1388 TATDNLIQETLRHHFadcTVITIAHRISSVID-SDMVLLLDQGLIKEHDSPARLLED 1443
Cdd:PRK10070 202 EMQDELVKLQAKHQR---TIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1234-1424 |
9.35e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.68 E-value: 9.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1234 MVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINI--LSIGL-HDLrsRLSIIPQDPTMFEG-T 1309
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCarLTPAKaHQL--GIYLVPQEPLLFPNlS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1310 IRSNL--------DPLEEYTddQIWEALdNCQlgdevrkkeLKLDSPVSengqNWSVGQRQLVCLGRVLLKRSKLLVLDE 1381
Cdd:PRK15439 103 VKENIlfglpkrqASMQKMK--QLLAAL-GCQ---------LDLDSSAG----SLEVADRQIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 30682479 1382 ATASIDTA-TDNL---IQETLR---------HHFADctVITIAHRISSVIDSDMVL 1424
Cdd:PRK15439 167 PTASLTPAeTERLfsrIRELLAqgvgivfisHKLPE--IRQLADRISVMRDGTIAL 220
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
725-811 |
9.74e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 58.27 E-value: 9.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 725 NLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgshlfKEVLLGLLRH------KTVIYVTHQVEFLPEADLILVMK 798
Cdd:PRK13640 143 NLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG-----KEQILKLIRKlkkknnLTVISITHDIDEANMADQVLVLD 217
|
90
....*....|...
gi 30682479 799 DGKITQAGKYHEI 811
Cdd:PRK13640 218 DGKLLAQGSPVEI 230
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1251-1412 |
1.05e-08 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 58.04 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1251 IVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIG---LHDLRS-RLSIIPQD----PTMfegTIRSNLD-PLE--- 1318
Cdd:cd03294 55 IMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRkKISMVFQSfallPHR---TVLENVAfGLEvqg 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1319 ---EYTDDQIWEALDNCQLGDEVRKKELKLdspvsengqnwSVGQRQLVCLGRVLLKRSKLLVLDEATasidTATDNLIQ 1395
Cdd:cd03294 132 vprAEREERAAEALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILLMDEAF----SALDPLIR 196
|
170 180
....*....|....*....|...
gi 30682479 1396 ETLRHHFADC------TVITIAH 1412
Cdd:cd03294 197 REMQDELLRLqaelqkTIVFITH 219
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
726-811 |
1.09e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 58.18 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAhTGShlfKEVL-----LGLLRHKTVIYVTHQVEFLPEADLILVMKDG 800
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDP-SGR---REVVntikeLNKKYGITIILITHYMEEAVEADRIIVMDSG 220
|
90
....*....|.
gi 30682479 801 KITQAGKYHEI 811
Cdd:PRK13633 221 KVVMEGTPKEI 231
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
601-821 |
1.43e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 57.80 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 601 VEISNGTFSWDDSSPIPTLRDMNFKVSQGMNVAICGTVGSGKSSLLSSILGEVPKISGNLKVCGRK-------------A 667
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELltaenvwnlrrkiG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 668 YIAQSPWIQ--SGKVEENILFGkpMEREWYDRvlEACSLNKDLEILPFHDQTVIGERGINLSGGQKQRIQIARALYQDAD 745
Cdd:PRK13642 85 MVFQNPDNQfvGATVEDDVAFG--MENQGIPR--EEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30682479 746 IYLFDDPFSAVDAHTGSHLFKEVL-LGLLRHKTVIYVTHQVEFLPEADLILVMKDGKITQAGKYHEILDSGTDFMEL 821
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHeIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDMVEI 237
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
668-812 |
1.56e-08 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 56.78 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 668 YIAQSPWIQSG-KVEENIL----FGKPMEREWYDRvLEAcsLNKDLEILPFHDQtvigeRGINLSGGQKQRIQIARALYQ 742
Cdd:cd03218 79 YLPQEASIFRKlTVEENILavleIRGLSKKEREEK-LEE--LLEEFHITHLRKS-----KASSLSGGERRRVEIARALAT 150
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30682479 743 DADIYLFDDPFSAVDAHTGSHLFKevLLGLLRHKTV-IYVT-HQV-EFLPEADLILVMKDGKITQAGKYHEIL 812
Cdd:cd03218 151 NPKFLLLDEPFAGVDPIAVQDIQK--IIKILKDRGIgVLITdHNVrETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
897-1099 |
1.70e-08 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 57.87 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 897 GAVIPLILVVqvlF-QLLSIGSNYWMTWVTPvsKDVEPPVSGFTLILVYvlLAVASSFCILIrallvAMTGFKMATELFT 975
Cdd:cd18577 12 GAALPLMTIV---FgDLFDAFTDFGSGESSP--DEFLDDVNKYALYFVY--LGIGSFVLSYI-----QTACWTITGERQA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 976 Q-MHLRIFRA----SMSFFDATPMGRILNRASTD----QSVADLRLPGQFAYVA--IAAInilgIIGVIVQvaWQ---VL 1041
Cdd:cd18577 80 RrIRKRYLKAllrqDIAWFDKNGAGELTSRLTSDtnliQDGIGEKLGLLIQSLStfIAGF----IIAFIYS--WKltlVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30682479 1042 IVFIPVVAACAWYRQYYISAA-----RELARLAGISrspvvhhfSETLSGITTIRSFDQEPRF 1099
Cdd:cd18577 154 LATLPLIAIVGGIMGKLLSKYtkkeqEAYAKAGSIA--------EEALSSIRTVKAFGGEEKE 208
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1250-1443 |
1.75e-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: 59.05 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1250 GIVGRTGCGKSTLIQTLFRIVEPAAGEIRI----DGINILSIGLhDLRSR----LSIIPQDPTMFegTIRSNLDPLEEYT 1321
Cdd:TIGR03269 314 GIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGP-DGRGRakryIGILHQEYDLY--PHRTVLDNLTEAI 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1322 DDQIWEALDNCQ-------LGDEVRKKELKLDSPVSEngqnWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTATDNLI 1394
Cdd:TIGR03269 391 GLELPDELARMKavitlkmVGFDEEKAEEILDKYPDE----LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDV 466
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 30682479 1395 QETLRHHFADC--TVITIAHRISSVID-SDMVLLLDQGLIKEHDSPARLLED 1443
Cdd:TIGR03269 467 THSILKAREEMeqTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1251-1444 |
1.85e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 57.94 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1251 IVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINI-------LSIGLHD---------LRSRLSIIPQDP--TMFEGTIRS 1312
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIgdkknnhELITNPYskkiknfkeLRRRVSMVFQFPeyQLFKDTIEK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1313 NL--DPLeeytddqiweALDncQLGDEVRKK------ELKLDSPVSE-NGQNWSVGQRQLVCLGRVLLKRSKLLVLDEAT 1383
Cdd:PRK13631 137 DImfGPV----------ALG--VKKSEAKKLakfylnKMGLDDSYLErSPFGLSGGQKRRVAIAGILAIQPEILIFDEPT 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30682479 1384 ASIDTATDN-LIQETLRHHFADCTVITIAHRISSVID-SDMVLLLDQGLIKEHDSPARLLEDR 1444
Cdd:PRK13631 205 AGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1219-1436 |
2.17e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 57.89 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHLPMV--LHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRS-R 1295
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1296 LSI--IPQ------DPTMFE---------GT----IRSNLDPLeeytddqiweaLDNCQLGDevrkkelKLDSPVSengq 1354
Cdd:PRK11153 82 RQIgmIFQhfnllsSRTVFDnvalplelaGTpkaeIKARVTEL-----------LELVGLSD-------KADRYPA---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1355 NWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTATDNLIQETLRHHFAD--CTVITIAHRIsSVIDS--DMVLLLDQGL 1430
Cdd:PRK11153 140 QLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRElgLTIVLITHEM-DVVKRicDRVAVIDAGR 218
|
....*.
gi 30682479 1431 IKEHDS 1436
Cdd:PRK11153 219 LVEQGT 224
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
726-802 |
2.60e-08 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 55.13 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgshlfKEVLLGLLRH-----KTVIYVThqvEFLPE----ADLILV 796
Cdd:cd03215 105 LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA-----KAEIYRLIREladagKAVLLIS---SELDEllglCDRILV 176
|
....*.
gi 30682479 797 MKDGKI 802
Cdd:cd03215 177 MYEGRI 182
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
726-806 |
3.26e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 56.18 E-value: 3.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKeVLLGLLR-HKTVIYVTHQVEFLPE-ADLILVMKDGKIT 803
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVS-IIRELAEtGITQVIVTHEVEVARKtASRVVYMENGHIV 220
|
...
gi 30682479 804 QAG 806
Cdd:PRK11124 221 EQG 223
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1251-1387 |
3.98e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 57.15 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1251 IVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINilsiglhdlrsrLSIIP--QDP--TMFEG-------TIRSNLD---- 1315
Cdd:PRK11607 50 LLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD------------LSHVPpyQRPinMMFQSyalfphmTVEQNIAfglk 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30682479 1316 ----PLEEYTDdQIWEALDNCQLGDEVRKKELKLdspvsengqnwSVGQRQLVCLGRVLLKRSKLLVLDEATASID 1387
Cdd:PRK11607 118 qdklPKAEIAS-RVNEMLGLVHMQEFAKRKPHQL-----------SGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
725-814 |
5.70e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 55.62 E-value: 5.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 725 NLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAhTGSHLFKEVLLGLLRHKTVIYVTHQ-VEFLPEADLILVMKDGKIT 803
Cdd:PRK14267 149 NLSGGQRQRLVIARALAMKPKILLMDEPTANIDP-VGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLI 227
|
90
....*....|.
gi 30682479 804 QAGKYHEILDS 814
Cdd:PRK14267 228 EVGPTRKVFEN 238
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1235-1412 |
6.33e-08 |
|
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: 55.13 E-value: 6.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1235 VLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRID----GINILSIG---LHDLRSR--------LSII 1299
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASpreILALRRRtigyvsqfLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1300 PQDPTmfegtirsnLD----PL-EEYTDDQiwEALDncqlgdevRKKEL--KLDSPvsengQN-WSV-------GQRQLV 1364
Cdd:COG4778 106 PRVSA---------LDvvaePLlERGVDRE--EARA--------RARELlaRLNLP-----ERlWDLppatfsgGEQQRV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 30682479 1365 CLGRVLLKRSKLLVLDEATASIDTATDN----LIQETLRhhfADCTVITIAH 1412
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANRAvvveLIEEAKA---RGTAIIGIFH 210
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
726-813 |
6.71e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 54.97 E-value: 6.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDahtgSHLFKEvLLGLL------RHKTVIYVTHQVEflpEADLI----L 795
Cdd:PRK10771 130 LSGGQRQRVALARCLVREQPILLLDEPFSALD----PALRQE-MLTLVsqvcqeRQLTLLMVSHSLE---DAARIaprsL 201
|
90
....*....|....*...
gi 30682479 796 VMKDGKITQAGKYHEILD 813
Cdd:PRK10771 202 VVADGRIAWDGPTDELLS 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1250-1442 |
7.76e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.57 E-value: 7.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1250 GIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDG--INILS--------IGLhdlrsrlsiIPQDPTMFEgtirsNLDPLEe 1319
Cdd:COG3845 35 ALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSprdaialgIGM---------VHQHFMLVP-----NLTVAE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1320 ytddqiwealdNCQLGDE-----------VRKK----------ELKLDSPVSEngqnWSVGQRQLVCLGRVLLKRSKLLV 1378
Cdd:COG3845 100 -----------NIVLGLEptkggrldrkaARARirelseryglDVDPDAKVED----LSVGEQQRVEILKALYRGARILI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30682479 1379 LDEATASI-DTATDNLIqETLRhHFAD--CTVITIAHRISSVID-SDMVLLLDQG-LIKEHD----SPARLLE 1442
Cdd:COG3845 165 LDEPTAVLtPQEADELF-EILR-RLAAegKSIIFITHKLREVMAiADRVTVLRRGkVVGTVDtaetSEEELAE 235
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
658-806 |
8.77e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 55.13 E-value: 8.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 658 GNLKVCGRKAYIAQSPWIQ---------------SGKVEENILFGkPM-----EREWYDRVLEACSL--NKDL-EILPFH 714
Cdd:PRK13647 60 GRVKVMGREVNAENEKWVRskvglvfqdpddqvfSSTVWDDVAFG-PVnmgldKDEVERRVEEALKAvrMWDFrDKPPYH 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 715 dqtvigerginLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAhTGSHLFKEVLLGLLRH-KTVIYVTHQVEFLPE-AD 792
Cdd:PRK13647 139 -----------LSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDP-RGQETLMEILDRLHNQgKTVIVATHDVDLAAEwAD 206
|
170
....*....|....
gi 30682479 793 LILVMKDGKITQAG 806
Cdd:PRK13647 207 QVIVLKEGRVLAEG 220
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1236-1434 |
1.05e-07 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 55.47 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1236 LHGLTCTFPGGLKT-----------------GIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSI---GLHDLRSR 1295
Cdd:COG1135 4 LENLSKTFPTKGGPvtalddvsltiekgeifGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALserELRAARRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1296 LSIIPQDptmFegtirsNLdpLEEYTddqiweALDNCQL--------GDEVRKK--EL--------KLDSPVSEngqnWS 1357
Cdd:COG1135 84 IGMIFQH---F------NL--LSSRT------VAENVALpleiagvpKAEIRKRvaELlelvglsdKADAYPSQ----LS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1358 VGQRQLVCLGRVLLKRSKLLVLDEATASIDTATD----NLIQEtLRHHFaDCTVITIAHRIsSVIDS--DMVLLLDQGLI 1431
Cdd:COG1135 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETTrsilDLLKD-INREL-GLTIVLITHEM-DVVRRicDRVAVLENGRI 219
|
...
gi 30682479 1432 KEH 1434
Cdd:COG1135 220 VEQ 222
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1217-1451 |
1.07e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 55.40 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1217 GEITICNLQVRYGPHLPM---VLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIrIDGINILSIGL---- 1289
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQT-IVGDYAIPANLkkik 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1290 --HDLRSRLSIIPQDP--TMFEGTIRS-------NLDPLEEYTDDQIWEALDNCQLGDEVRKKelkldSPVSENGqnwsv 1358
Cdd:PRK13645 84 evKRLRKEIGLVFQFPeyQLFQETIEKdiafgpvNLGENKQEAYKKVPELLKLVQLPEDYVKR-----SPFELSG----- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1359 GQRQLVCLGRVLLKRSKLLVLDEATASIDTATD----NLIqETLRHHFADcTVITIAHRISSVID-SDMVLLLDQGLIKE 1433
Cdd:PRK13645 154 GQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEedfiNLF-ERLNKEYKK-RIIMVTHNMDQVLRiADEVIVMHEGKVIS 231
|
250
....*....|....*...
gi 30682479 1434 HDSPARLLEDRsSLFSKL 1451
Cdd:PRK13645 232 IGSPFEIFSNQ-ELLTKI 248
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
726-814 |
1.13e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 55.11 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFS-----AVDahtgshLFKEVLLGLLRH-KTVIYVTHQ---VEFLpeADLILV 796
Cdd:COG4152 130 LSKGNQQKVQLIAALLHDPELLILDEPFSgldpvNVE------LLKDVIRELAAKgTTVIFSSHQmelVEEL--CDRIVI 201
|
90
....*....|....*...
gi 30682479 797 MKDGKITQAGKYHEILDS 814
Cdd:COG4152 202 INKGRKVLSGSVDEIRRQ 219
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1218-1436 |
1.26e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 55.09 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1218 EITICNLQVRYGPHLPM---VLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEI-----------RIDGIN 1283
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPTelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1284 ILSIGL-------------HDLRSRLSIIPQ--DPTMFEGTIRSNL--DPLEEYTDDQiwEALdncqlgdEVRKKELKL- 1345
Cdd:PRK13651 82 KVLEKLviqktrfkkikkiKEIRRRVGVVFQfaEYQLFEQTIEKDIifGPVSMGVSKE--EAK-------KRAAKYIELv 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1346 ---DSPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTATDNLIQETLRH-HFADCTVITIAHRISSVID-S 1420
Cdd:PRK13651 153 gldESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNVLEwT 232
|
250
....*....|....*..
gi 30682479 1421 DMVLLLDQG-LIKEHDS 1436
Cdd:PRK13651 233 KRTIFFKDGkIIKDGDT 249
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
658-757 |
1.59e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 54.29 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 658 GNLKVCGRKAYIAQSPWIQSGKVEEniLFGKPMEREWYDRVLEACSLNKDLEilpfhdqtvigeRGI-NLSGGQKQRIQI 736
Cdd:cd03236 85 GDVKVIVKPQYVDLIPKAVKGKVGE--LLKKKDERGKLDELVDQLELRHVLD------------RNIdQLSGGELQRVAI 150
|
90 100
....*....|....*....|.
gi 30682479 737 ARALYQDADIYLFDDPFSAVD 757
Cdd:cd03236 151 AAALARDADFYFFDEPSSYLD 171
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
726-806 |
1.66e-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: 53.35 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgSHLFKEVLLGLLRHKTVIYVTHQVEFLPE-ADLILVMKDGKITQ 804
Cdd:cd03264 131 LSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEE-RIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVF 209
|
..
gi 30682479 805 AG 806
Cdd:cd03264 210 EG 211
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1219-1398 |
1.69e-07 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 53.82 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYgPHLPMvlhGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINilsiglHDL----RS 1294
Cdd:PRK10771 2 LKLTDITWLY-HHLPM---RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD------HTTtppsRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1295 RLSIIPQDPTMFEG-TIRSN----LDPLEEYTDDQiwealdNCQLGDEVRKkeLKLDSPVSENGQNWSVGQRQLVCLGRV 1369
Cdd:PRK10771 72 PVSMLFQENNLFSHlTVAQNiglgLNPGLKLNAAQ------REKLHAIARQ--MGIEDLLARLPGQLSGGQRQRVALARC 143
|
170 180
....*....|....*....|....*....
gi 30682479 1370 LLKRSKLLVLDEATASIDTAtdnLIQETL 1398
Cdd:PRK10771 144 LVREQPILLLDEPFSALDPA---LRQEML 169
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
713-816 |
1.80e-07 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 55.23 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 713 FHDQTVIgergiNLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHtgsHLFKEvlLGLLRH-----KTVIYVTHQVEF 787
Cdd:PRK09536 132 FADRPVT-----SLSGGERQRVLLARALAQATPVLLLDEPTASLDIN---HQVRT--LELVRRlvddgKTAVAAIHDLDL 201
|
90 100 110
....*....|....*....|....*....|
gi 30682479 788 LPE-ADLILVMKDGKITQAGKYHEILDSGT 816
Cdd:PRK09536 202 AARyCDELVLLADGRVRAAGPPADVLTADT 231
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1250-1466 |
1.94e-07 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 53.95 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1250 GIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINIlsiglhdlrsrlSIIPQDPTM-FEGTIRsnlDPLEEYTDDqiweA 1328
Cdd:cd03237 29 GILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV------------SYKPQYIKAdYEGTVR---DLLSSITKD----F 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1329 LDNCQLGDEVrKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTATDNLIQETLRhHFADCTVI 1408
Cdd:cd03237 90 YTHPYFKTEI-AKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIR-RFAENNEK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 30682479 1409 TiahriSSVIDSDMVLlldqglikehdspARLLEDRSSLFSKLVAEYTTSSESKSKRS 1466
Cdd:cd03237 168 T-----AFVVEHDIIM-------------IDYLADRLIVFEGEPSVNGVANPPQSLRS 207
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
721-786 |
2.71e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 53.63 E-value: 2.71e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30682479 721 ERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLfKEVLLGLLRHKTVIYVTHQVE 786
Cdd:PRK14239 144 DSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKI-EETLLGLKDDYTMLLVTRSMQ 208
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
675-811 |
2.74e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 53.65 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 675 IQSGKVEENILFGkpmerewydrvleACSLNKDLEILPFHDQTVIGERGI---------NLSGGQKQRIQIARALYQDAD 745
Cdd:PRK13652 91 IFSPTVEQDIAFG-------------PINLGLDEETVAHRVSSALHMLGLeelrdrvphHLSGGEKKRVAIAGVIAMEPQ 157
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30682479 746 IYLFDDPFSAVDAHTGSHLFKEVLLGLLRHK-TVIYVTHQVEFLPE-ADLILVMKDGKITQAGKYHEI 811
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLPETYGmTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEI 225
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
726-801 |
3.14e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.92 E-value: 3.14e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKevLLGLLRH--KTVIYVTHQVEFLPE-ADLILVMKDGK 801
Cdd:PRK11288 141 LSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFR--VIRELRAegRVILYVSHRMEEIFAlCDAITVFKDGR 217
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
726-814 |
3.22e-07 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 54.69 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGshlfKEVlLGLLR-----HK-TVIYVTHQ---VEFLpeADLILV 796
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQ----AQI-LDLLRdlqreHGlAYLFISHDlavVRAL--AHRVMV 498
|
90
....*....|....*...
gi 30682479 797 MKDGKITQAGKYHEILDS 814
Cdd:COG4172 499 MKDGKVVEQGPTEQVFDA 516
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
932-1381 |
4.34e-07 |
|
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: 54.42 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 932 EPPVSGFTLILVYVLLAVASSFCILIRALLVAMTGFKMATELFTQMHLRIFRASMSFFDATPMGRILNRASTD-QSVAD- 1009
Cdd:COG4615 42 ATGAALARLLLLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDvRTISQa 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1010 -LRLPgqfayvaIAAINILGIIGVIVQVAW---QVLIVFIPVVAACAWYRQYYISAARELARLAGISRSPVVHHFSETLS 1085
Cdd:COG4615 122 fVRLP-------ELLQSVALVLGCLAYLAWlspPLFLLTLVLLGLGVAGYRLLVRRARRHLRRAREAEDRLFKHFRALLE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1086 GITTIRsFDQEPR---FRGDIMRLSDCYSRLKFHsTGAMEWLCFRLELLSTFAFaSSLVILVSAPEGVINPSLAGLAITY 1162
Cdd:COG4615 195 GFKELK-LNRRRRrafFDEDLQPTAERYRDLRIR-ADTIFALANNWGNLLFFAL-IGLILFLLPALGWADPAVLSGFVLV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1163 ALNLNTLQATLIWTLCDLENKMISVERMLQYTNIPSEPPLVIETTRPEKSWPSRGEITICNLQVRYGPHL---PMVLHGL 1239
Cdd:COG4615 272 LLFLRGPLSQLVGALPTLSRANVALRKIEELELALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDgdeGFTLGPI 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1240 TCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSIIPQDPTMFEgtirSNLDPLEE 1319
Cdd:COG4615 352 DLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFD----RLLGLDGE 427
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1320 YTDDQIWEALdncqlgdevrkKELKLDSPVS-ENGQ----NWSVGQRQ---LVClgrVLLKRSKLLVLDE 1381
Cdd:COG4615 428 ADPARARELL-----------ERLELDHKVSvEDGRfsttDLSQGQRKrlaLLV---ALLEDRPILVFDE 483
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1223-1390 |
4.61e-07 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 52.10 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1223 NLQVRYGPHLpmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEP---AAGEIRIDGINILSIGLHdlRSRLSII 1299
Cdd:COG4136 6 NLTITLGGRP--LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE--QRRIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1300 PQDPTMFEG-TIRSNL------DPLEEYTDDQIWEALDNCQLGDEVRKkelkldSPVSENGqnwsvGQRQLVCLGRVLLK 1372
Cdd:COG4136 82 FQDDLLFPHlSVGENLafalppTIGRAQRRARVEQALEEAGLAGFADR------DPATLSG-----GQRARVALLRALLA 150
|
170
....*....|....*...
gi 30682479 1373 RSKLLVLDEATASIDTAT 1390
Cdd:COG4136 151 EPRALLLDEPFSKLDAAL 168
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
680-814 |
4.70e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 53.09 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 680 VEENILFGkPM-----EREWYDRVLEACslnkDLEILPfhdQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFS 754
Cdd:PRK13645 108 IEKDIAFG-PVnlgenKQEAYKKVPELL----KLVQLP---EDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTG 179
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30682479 755 AVDAhTGSHLFKEVLLGLLRH--KTVIYVTHQV-EFLPEADLILVMKDGKITQAGKYHEILDS 814
Cdd:PRK13645 180 GLDP-KGEEDFINLFERLNKEykKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
657-757 |
5.28e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 5.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 657 SGNLKVCGRKAYIAQSPWIQSGKVEEniLFGKPMEREWYDRVLEAcslnkdLEILPFHDQTVIgergiNLSGGQKQRIQI 736
Cdd:PRK13409 157 NGEIKVVHKPQYVDLIPKVFKGKVRE--LLKKVDERGKLDEVVER------LGLENILDRDIS-----ELSGGELQRVAI 223
|
90 100
....*....|....*....|.
gi 30682479 737 ARALYQDADIYLFDDPFSAVD 757
Cdd:PRK13409 224 AAALLRDADFYFFDEPTSYLD 244
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
726-812 |
6.47e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 52.22 E-value: 6.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLfKEVLLGLLRHKTVIYVTHqveFLPEA----DLILVMKDGK 801
Cdd:PRK14247 147 LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKI-ESLFLELKKDMTIVLVTH---FPQQAarisDYVAFLYKGQ 222
|
90
....*....|.
gi 30682479 802 ITQAGKYHEIL 812
Cdd:PRK14247 223 IVEWGPTREVF 233
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
657-757 |
7.07e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 53.63 E-value: 7.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 657 SGNLKVCGRKAYIAQSPWIQSGKVEEniLFGKPMEREWYDRVLEAcslnkdLEILPFHDQTVIgergiNLSGGQKQRIQI 736
Cdd:COG1245 157 NGEIKVAHKPQYVDLIPKVFKGTVRE--LLEKVDERGKLDELAEK------LGLENILDRDIS-----ELSGGELQRVAI 223
|
90 100
....*....|....*....|.
gi 30682479 737 ARALYQDADIYLFDDPFSAVD 757
Cdd:COG1245 224 AAALLRDADFYFFDEPSSYLD 244
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1219-1387 |
7.35e-07 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 51.49 E-value: 7.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHLpmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDlRSrLSI 1298
Cdd:cd03301 1 VELENVTKRFGNVT--ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-RD-IAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1299 IPQD----PTMfegTIRSNLD-PLE--EYTDDQIWEaldncqlgdEVRK--KELKLDSPVSENGQNWSVGQRQLVCLGRV 1369
Cdd:cd03301 77 VFQNyalyPHM---TVYDNIAfGLKlrKVPKDEIDE---------RVREvaELLQIEHLLDRKPKQLSGGQRQRVALGRA 144
|
170
....*....|....*...
gi 30682479 1370 LLKRSKLLVLDEATASID 1387
Cdd:cd03301 145 IVREPKVFLMDEPLSNLD 162
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
722-804 |
7.40e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 52.13 E-value: 7.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 722 RGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKevLLGLL--RHKTV-IYVTHQVEFLPEADLILVMK 798
Cdd:PRK11629 142 RPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQ--LLGELnrLQGTAfLVVTHDLQLAKRMSRQLEMR 219
|
....*.
gi 30682479 799 DGKITQ 804
Cdd:PRK11629 220 DGRLTA 225
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1235-1281 |
8.52e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 52.01 E-value: 8.52e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 30682479 1235 VLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDG 1281
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG 87
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
704-806 |
9.77e-07 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 51.21 E-value: 9.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 704 LNKDLEILPFHDQtvigeRGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAhTGSHLFKEVLLGLLRH-KTVIYVT 782
Cdd:cd03266 120 LADRLGMEELLDR-----RVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV-MATRALREFIRQLRALgKCILFST 193
|
90 100
....*....|....*....|....*..
gi 30682479 783 H---QVEFLpeADLILVMKDGKITQAG 806
Cdd:cd03266 194 HimqEVERL--CDRVVVLHRGRVVYEG 218
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
942-1100 |
1.01e-06 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 52.51 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 942 LVYVLLAVASSFCILIRALLVAMTGFKMATELFTQMHLRIFRASMSFFDATPMGRILNRASTD-QSVADLRLPGqFAYVA 1020
Cdd:cd18564 58 AALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDvGAIQDLLVSG-VLPLL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1021 IAAINILGIIGVIVQVAWQ----VLIVFIPVVAACAWYRQYYISAARELAR----LAGISrspvvhhfSETLSGITTIRS 1092
Cdd:cd18564 137 TNLLTLVGMLGVMFWLDWQlaliALAVAPLLLLAARRFSRRIKEASREQRRregaLASVA--------QESLSAIRVVQA 208
|
....*...
gi 30682479 1093 FDQEPRFR 1100
Cdd:cd18564 209 FGREEHEE 216
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
680-810 |
1.06e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 51.94 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 680 VEENILFG----KPMER---EWYDRVLEACSLNKDLEILPFHdqtVIGERGINLSGGQKQRIQIARALYQDADIYLFDDP 752
Cdd:PRK09984 103 VLENVLIGalgsTPFWRtcfSWFTREQKQRALQALTRVGMVH---FAHQRVSTLSGGQQQRVAIARALMQQAKVILADEP 179
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30682479 753 FSAVDAHTgSHLFKEVLLGLLRHK--TVIYVTHQVEF-LPEADLILVMKDGKITQAGKYHE 810
Cdd:PRK09984 180 IASLDPES-ARIVMDTLRDINQNDgiTVVVTLHQVDYaLRYCERIVALRQGHVFYDGSSQQ 239
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1218-1448 |
1.10e-06 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 52.46 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1218 EITICNLQVRYGPHlpMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGinilsiglHDLRSRLS 1297
Cdd:COG1118 2 SIEVRNISKRFGSF--TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG--------RDLFTNLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1298 iiPQD-------------PTMfegTIRSN-------LDPLEEYTDDQIWEALDNCQLGD-EVRK-KELkldspvsengqn 1355
Cdd:COG1118 72 --PRErrvgfvfqhyalfPHM---TVAENiafglrvRPPSKAEIRARVEELLELVQLEGlADRYpSQL------------ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1356 wSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTATDNLIQETLR--HHFADCTVITIAH------RIssvidSDMVLLLD 1427
Cdd:COG1118 135 -SGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRrlHDELGGTTVFVTHdqeealEL-----ADRVVVMN 208
|
250 260
....*....|....*....|.
gi 30682479 1428 QGLIKEHDSPARLLEDRSSLF 1448
Cdd:COG1118 209 QGRIEQVGTPDEVYDRPATPF 229
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1236-1444 |
1.11e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.08 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1236 LHGLTCTFPG-------------GLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLR-SRLSIIPQ 1301
Cdd:PRK10762 7 LKGIDKAFPGvkalsgaalnvypGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQeAGIGIIHQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1302 DPTMF-EGTIRSNLDPLEEYTDdqIWEALDNCQLGDEVRK--KELKL----DSPVSEngqnWSVGQRQLVCLGRVLLKRS 1374
Cdd:PRK10762 87 ELNLIpQLTIAENIFLGREFVN--RFGRIDWKKMYAEADKllARLNLrfssDKLVGE----LSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30682479 1375 KLLVLDEAT-ASIDTATDNL---IQEtLRHHfaDCTVITIAHRISSV--IDSDMVLLLDQGLIKEHDSpARLLEDR 1444
Cdd:PRK10762 161 KVIIMDEPTdALTDTETESLfrvIRE-LKSQ--GRGIVYISHRLKEIfeICDDVTVFRDGQFIAEREV-ADLTEDS 232
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
721-783 |
1.15e-06 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 51.58 E-value: 1.15e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30682479 721 ERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLfkEVLLGLLRHK-TVIYVTH 783
Cdd:COG1117 150 KSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKI--EELILELKKDyTIVIVTH 211
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1239-1429 |
1.18e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 51.47 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1239 LTCTFPGGLKTGIVGRTGCGKSTLiqtLFRI--VEPAAGEIRIDGINILSIGLHDL-RSRLSIIPQDPTMFegtirsnLD 1315
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTL---LARMagLLPGSGSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPF-------AM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1316 PLEEYTD----DQIWEALDNCQLGDEVRKkeLKLDSPVSENGQNWSVGQRQLVCLGRVLLK-------RSKLLVLDEATA 1384
Cdd:PRK03695 85 PVFQYLTlhqpDKTRTEAVASALNEVAEA--LGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMN 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 30682479 1385 SIDTATDNLIqETLRHHFADC--TVITIAHRISSVID-SDMVLLLDQG 1429
Cdd:PRK03695 163 SLDVAQQAAL-DRLLSELCQQgiAVVMSSHDLNHTLRhADRVWLLKQG 209
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1250-1432 |
1.18e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 52.90 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1250 GIVGRTGCGKSTLIQTLFRIVEPA-AGEIRIDG--INILSIgLHDLRSRLSIIPQD-------PTMFEGTiRSNLDPLEE 1319
Cdd:TIGR02633 290 GVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDIRNP-AQAIRAGIAMVPEDrkrhgivPILGVGK-NITLSVLKS 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1320 YTD-DQIWEALDNCQLGDEVRKKELKLDSPVSENGQnWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTATD----NLI 1394
Cdd:TIGR02633 368 FCFkMRIDAAAELQIIGSAIQRLKVKTASPFLPIGR-LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKyeiyKLI 446
|
170 180 190
....*....|....*....|....*....|....*....
gi 30682479 1395 QETLRHHFAdctVITIAHRISSVID-SDMVLLLDQGLIK 1432
Cdd:TIGR02633 447 NQLAQEGVA---IIVVSSELAEVLGlSDRVLVIGEGKLK 482
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1251-1447 |
1.21e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.05 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1251 IVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSIIPQDPTMFEGTirsnLDPLEEYTDDQIWEA-L 1329
Cdd:PRK10522 354 LIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQL----LGPEGKPANPALVEKwL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1330 DNCQLGDEVRKKELKLDSPvsengqNWSVGQRQLVCLGRVLLKRSKLLVLDEATASID--------TATDNLIQETLRhh 1401
Cdd:PRK10522 430 ERLKMAHKLELEDGRISNL------KLSKGQKKRLALLLALAEERDILLLDEWAADQDphfrrefyQVLLPLLQEMGK-- 501
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 30682479 1402 fadcTVITIAHRISSVIDSDMVLLLDQGLIKEHDSPARLLEDRSSL 1447
Cdd:PRK10522 502 ----TIFAISHDDHYFIHADRLLEMRNGQLSELTGEERDAASRDAV 543
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1236-1452 |
1.25e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.99 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1236 LHGLTCTFPG-------------GLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRID---------------GINILSI 1287
Cdd:PRK11288 7 FDGIGKTFPGvkalddisfdcraGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDgqemrfasttaalaaGVAIIYQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1288 GLHdLRSRLSI-----IPQDPTMFeGTIRSNLdpLEEYTDDQIWEaldncqLGDEVRKkelklDSPVSEngqnWSVGQRQ 1362
Cdd:PRK11288 87 ELH-LVPEMTVaenlyLGQLPHKG-GIVNRRL--LNYEAREQLEH------LGVDIDP-----DTPLKY----LSIGQRQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1363 LVCLGRVLLKRSKLLVLDEATASIDT-ATDNL--IQETLRhhfADCTVIT-IAHRISSVID-SDMVLLLDQG-LIKEHDS 1436
Cdd:PRK11288 148 MVEIAKALARNARVIAFDEPTSSLSArEIEQLfrVIRELR---AEGRVILyVSHRMEEIFAlCDAITVFKDGrYVATFDD 224
|
250
....*....|....*.
gi 30682479 1437 PARLleDRSSLFSKLV 1452
Cdd:PRK11288 225 MAQV--DRDQLVQAMV 238
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
938-1100 |
1.27e-06 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 51.87 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 938 FTLILVYVLLAVASsfciLIRALLVAMTGFKMATELFTQMHLRIFRASMSFFDATPMGRILNRASTD----QSVADLRLP 1013
Cdd:cd18780 46 LILLGVVLIGSIAT----FLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDtqvlQNAVTVNLS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1014 GQFAYVAiaaiNILGIIGVIVQVAWQ---VLIVFIPVVAACA-WYRQYyisaARELARL--AGISRSPVVHhfSETLSGI 1087
Cdd:cd18780 122 MLLRYLV----QIIGGLVFMFTTSWKltlVMLSVVPPLSIGAvIYGKY----VRKLSKKfqDALAAASTVA--EESISNI 191
|
170
....*....|...
gi 30682479 1088 TTIRSFDQEPRFR 1100
Cdd:cd18780 192 RTVRSFAKETKEV 204
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1219-1281 |
1.34e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 52.03 E-value: 1.34e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30682479 1219 ITICNLQVRYGPHLpmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDG 1281
Cdd:COG4152 2 LELKGLTKRFGDKT--AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG 62
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
726-815 |
1.36e-06 |
|
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: 50.01 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDAD--IYLFDDPFSAVDAHTGSHLFkEVLLGLLRHK-TVIYVTHQVEFLPEADLILVMKDGki 802
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLL-EVIKGLIDLGnTVILIEHNLDVLSSADWIIDFGPG-- 164
|
90
....*....|....
gi 30682479 803 tqAGKY-HEILDSG 815
Cdd:cd03238 165 --SGKSgGKVVFSG 176
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
721-786 |
1.45e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 51.32 E-value: 1.45e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30682479 721 ERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAhTGSHLFKEVLLGLLRHKTVIYVTHQVE 786
Cdd:PRK14243 147 QSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDP-ISTLRIEELMHELKEQYTIIIVTHNMQ 211
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1235-1440 |
1.48e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 51.73 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1235 VLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHDLRSRLSIIPQDP--TMFEGTIRS 1312
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1313 -------NLDPLEEYTDDQIWEALDncQLGDEvrkkELKLDSPvsengQNWSVGQRQLVCLGRVLLKRSKLLVLDEATAS 1385
Cdd:PRK13652 99 diafgpiNLGLDEETVAHRVSSALH--MLGLE----ELRDRVP-----HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 30682479 1386 ID-TATDNLIQ--ETLRHHFAdCTVITIAHRISSVID-SDMVLLLDQGLIKEHDSPARL 1440
Cdd:PRK13652 168 LDpQGVKELIDflNDLPETYG-MTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
726-801 |
1.55e-06 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 48.98 E-value: 1.55e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgshlfKEVLLGLLR--HKTVIYVTHQVEFLPE-ADLILVMKDGK 801
Cdd:cd03221 71 LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLES-----IEALEEALKeyPGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
680-807 |
1.57e-06 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 50.82 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 680 VEENILF-----GKPmEREWYDRVLEAcsLNKdleilpfhdqtV-IGERG----INLSGGQKQRIQIARALYQDADIYLF 749
Cdd:COG2884 96 VYENVALplrvtGKS-RKEIRRRVREV--LDL-----------VgLSDKAkalpHELSGGEQQRVAIARALVNRPELLLA 161
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30682479 750 DDPFSAVDAHTGS---HLFKEV-LLGllrhKTVIYVTHQVEFLPEADL-ILVMKDGKITQAGK 807
Cdd:COG2884 162 DEPTGNLDPETSWeimELLEEInRRG----TTVLIATHDLELVDRMPKrVLELEDGRLVRDEA 220
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
619-824 |
1.86e-06 |
|
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: 52.99 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 619 LRDMNFKVSQGMNVAICGTVGSGKSSlLSSILGEVPKISGNLKVCG-----------RKAY--IAQSPWIQSGKVEENIl 685
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKST-LLSALLRLLSTEGEIQIDGvswnsvtlqtwRKAFgvIPQKVFIFSGTFRKNL- 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 686 fgKPMEReWYD----RVLEACSLNKDLEILPFHDQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTg 761
Cdd:TIGR01271 1313 --DPYEQ-WSDeeiwKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVT- 1388
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30682479 762 SHLFKEVLLGLLRHKTVIYVTHQVEFLPEADLILVMKDGKITQAGKYHEILDSGTDFMELVGA 824
Cdd:TIGR01271 1389 LQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAMSA 1451
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
619-829 |
2.01e-06 |
|
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: 51.01 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 619 LRDMNFKVSQGMNVAICGTVGSGKSSLLSSILGEVpKISGNLKVCG-----------RKAY--IAQSPWIQSGKVEENI- 684
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGvswnsvplqkwRKAFgvIPQKVFIFSGTFRKNLd 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 685 LFGKPMEREWYdRVLEACSLNKDLEILPFHDQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgSHL 764
Cdd:cd03289 99 PYGKWSDEEIW-KVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPIT-YQV 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30682479 765 FKEVLLGLLRHKTVIYVTHQVEFLPEADLILVMKDGKITQAGKYHEILDSGTDFMELVgAHTEAL 829
Cdd:cd03289 177 IRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAI-SPSDRL 240
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
680-757 |
2.24e-06 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 50.41 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 680 VEENIL----FGKPMEREWYDRvLEacSLNKDLEILPFHDQtvigeRGINLSGGQKQRIQIARALYQDADIYLFDDPFSA 755
Cdd:COG1137 95 VEDNILavleLRKLSKKEREER-LE--ELLEEFGITHLRKS-----KAYSLSGGERRRVEIARALATNPKFILLDEPFAG 166
|
..
gi 30682479 756 VD 757
Cdd:COG1137 167 VD 168
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
722-806 |
2.37e-06 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 49.83 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 722 RGIN--LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAhTGSHLFKEVLLGLLR-HKTVIYVTHQVEFL--PEADLILV 796
Cdd:cd03217 99 RYVNegFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI-DALRLVAEVINKLREeGKSVLIITHYQRLLdyIKPDRVHV 177
|
90
....*....|
gi 30682479 797 MKDGKITQAG 806
Cdd:cd03217 178 LYDGRIVKSG 187
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
599-823 |
2.91e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 50.82 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 599 MAVEISNGTFSWDDSSPIPT--LRDMNFKVSQGMNVAICGTVGSGKSSLLSSILGEVPKISGNLKVCG------------ 664
Cdd:PRK13637 1 MSIKIENLTHIYMEGTPFEKkaLDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 665 -RK--AYIAQSPWIQ--SGKVEENILFGkPM-----EREWYDRVLEACSLNK-DLEIL----PFhdqtvigergiNLSGG 729
Cdd:PRK13637 81 iRKkvGLVFQYPEYQlfEETIEKDIAFG-PInlglsEEEIENRVKRAMNIVGlDYEDYkdksPF-----------ELSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 730 QKQRIQIARALYQDADIYLFDDPFSAVDAHTgshlfKEVLLGLLR--HK----TVIYVTHQVEFLPE-ADLILVMKDGKI 802
Cdd:PRK13637 149 QKRRVAIAGVVAMEPKILILDEPTAGLDPKG-----RDEILNKIKelHKeynmTIILVSHSMEDVAKlADRIIVMNKGKC 223
|
250 260
....*....|....*....|.
gi 30682479 803 TQAGKYHEILDSgTDFMELVG 823
Cdd:PRK13637 224 ELQGTPREVFKE-VETLESIG 243
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
940-1097 |
2.92e-06 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 50.89 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 940 LILVYVLLAVASSFCILIRALLVAMTGFKMATELFTQMHLRIFRASMSFFDATPMGRILNRASTDqsVADLR--LPGQFA 1017
Cdd:cd18542 41 LALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSD--VDTIRrfLAFGLV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1018 YVAIAAINILGIIGVIVQVAWQ---VLIVFIPVVAACAWY-----RQYYISAARELARLagisrSPVVhhfSETLSGITT 1089
Cdd:cd18542 119 ELVRAVLLFIGALIIMFSINWKltlISLAIIPFIALFSYVffkkvRPAFEEIREQEGEL-----NTVL---QENLTGVRV 190
|
....*...
gi 30682479 1090 IRSFDQEP 1097
Cdd:cd18542 191 VKAFARED 198
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1223-1448 |
2.97e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 51.26 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1223 NLQVRYGPHlpMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINIL--SIGLHDLrsrlSIIP 1300
Cdd:PRK11432 11 NITKRFGSN--TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVThrSIQQRDI----CMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1301 QDPTMF-EGTIRSNLD--------PLEEyTDDQIWEALDNCQL-GDEVRKKElkldspvsengqNWSVGQRQLVCLGRVL 1370
Cdd:PRK11432 85 QSYALFpHMSLGENVGyglkmlgvPKEE-RKQRVKEALELVDLaGFEDRYVD------------QISGGQQQRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1371 LKRSKLLVLDEATASIDTATDNLIQETLR---HHFaDCTVITIAHRISSVID-SDMVLLLDQGLIKEHDSPARLLEDRSS 1446
Cdd:PRK11432 152 ILKPKVLLFDEPLSNLDANLRRSMREKIRelqQQF-NITSLYVTHDQSEAFAvSDTVIVMNKGKIMQIGSPQELYRQPAS 230
|
..
gi 30682479 1447 LF 1448
Cdd:PRK11432 231 RF 232
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
692-813 |
3.02e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 51.97 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 692 REWYDRVLEACSLNKdleilpfHDQTVIGERGI--NLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKeVL 769
Cdd:TIGR00955 138 RERVDEVLQALGLRK-------CANTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQ-VL 209
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 30682479 770 LGL-LRHKTVIYVTHQveflPEADL------ILVMKDGKITQAGKYHEILD 813
Cdd:TIGR00955 210 KGLaQKGKTIICTIHQ----PSSELfelfdkIILMAEGRVAYLGSPDQAVP 256
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
937-1148 |
3.38e-06 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 50.49 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 937 GFTLILVYVLLAVAssfCILIRALLVA---MTGFKMA----TELFTQMHLRIFRASMSFFDATPMGRILNRAsTDQsVAD 1009
Cdd:cd18584 32 GLAALLPLLLLLLA---ALLLRALLAWaqeRLAARAAarvkAELRRRLLARLLALGPALLRRQSSGELATLL-TEG-VDA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1010 LR------LPGQFAyvaiAAINILGIIGVIVQVAWQV-LIV-----FIPV-------VAACAWYRQYyisaaRELARLAG 1070
Cdd:cd18584 107 LDgyfaryLPQLVL----AAIVPLLILVAVFPLDWVSaLILlvtapLIPLfmiligkAAQAASRRQW-----AALSRLSG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1071 isrspvvhHFSETLSGITTIRSFDQEPRFRGDIMRLSDCYS-------RLKFHSTGAMEWLC------------FRLeLL 1131
Cdd:cd18584 178 --------HFLDRLRGLPTLKLFGRARAQAARIARASEDYRrrtmkvlRVAFLSSAVLEFFAtlsialvavyigFRL-LG 248
|
250
....*....|....*..
gi 30682479 1132 STFAFASSLVILVSAPE 1148
Cdd:cd18584 249 GSLTLFTALFVLLLAPE 265
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
726-814 |
3.49e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 50.05 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAhTGSHLFKEVLLGLLRHKTVIYVTHQVEFLPE-ADLILVMKDGKITQ 804
Cdd:PRK14246 154 LSGGQQQRLTIARALALKPKVLLMDEPTSMIDI-VNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVE 232
|
90
....*....|
gi 30682479 805 AGKYHEILDS 814
Cdd:PRK14246 233 WGSSNEIFTS 242
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1219-1412 |
3.60e-06 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 48.21 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHLpmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGinilsiglhdlRSRLSI 1298
Cdd:cd03221 1 IELENLSKTYGGKL--LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1299 IPQdptmfegtirsnLdpleeytddqiwealdncqlgdevrkkelkldspvsengqnwSVGQRQLVCLGRVLLKRSKLLV 1378
Cdd:cd03221 68 FEQ------------L------------------------------------------SGGEKMRLALAKLLLENPNLLL 93
|
170 180 190
....*....|....*....|....*....|....
gi 30682479 1379 LDEATASIDTATDNLIQETLRHHfaDCTVITIAH 1412
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEY--PGTVILVSH 125
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
726-805 |
3.79e-06 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 49.74 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGshlfkEVLLGLL------RHKTVIYVTHQVEFLPEADLILVMKD 799
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPTGNLDAATG-----EQIIDLLfelnreRGTTLVLVTHDPALAARCDRVLRLRA 221
|
....*.
gi 30682479 800 GKITQA 805
Cdd:COG4181 222 GRLVED 227
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
941-1096 |
3.94e-06 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 50.39 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 941 ILVYVLLAVASSFCILIRALLVAMTGFKMATELFTQMHLRIFRASMSFFDATPMGRILNRASTDQSVADLRLPGQFAYVA 1020
Cdd:cd18784 39 IIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1021 IAAINILGIIGVIVQVAWQV-LIVFI--PVVAACA-WYRQYYISAARE----LARLAGISrspvvhhfSETLSGITTIRS 1092
Cdd:cd18784 119 RSLVKAIGVIVFMFKLSWQLsLVTLIglPLIAIVSkVYGDYYKKLSKAvqdsLAKANEVA--------EETISSIRTVRS 190
|
....
gi 30682479 1093 FDQE 1096
Cdd:cd18784 191 FANE 194
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1239-1429 |
4.03e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 51.94 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1239 LTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINIlSIGLHDLRSRLSIIPQDPTMFEGTIRSNLDPLE 1318
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHLTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1319 EYTDDQIWEaldNCQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTATDNLIQETL 1398
Cdd:TIGR01257 1028 AQLKGRSWE---EAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170 180 190
....*....|....*....|....*....|..
gi 30682479 1399 RHHFADCTVITIAHRISSV-IDSDMVLLLDQG 1429
Cdd:TIGR01257 1105 LKYRSGRTIIMSTHHMDEAdLLGDRIAIISQG 1136
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
939-1106 |
4.14e-06 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 50.17 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 939 TLILVYVLlaVASSFCILIRALLVAMTGFKMATELFTQMHLRIFRASMSFFDATPMGRILNRASTDqsVADLR--LPGQF 1016
Cdd:cd18576 39 ALLLLGLF--LLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSND--VTQIQdtLTTTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1017 AYVAIAAINILGIIGVIVQVAWQ----VLIVFIPVVAACAWY----RQYYISAARELARLAGISrspvvhhfSETLSGIT 1088
Cdd:cd18576 115 AEFLRQILTLIGGVVLLFFISWKltllMLATVPVVVLVAVLFgrriRKLSKKVQDELAEANTIV--------EETLQGIR 186
|
170 180
....*....|....*....|..
gi 30682479 1089 TIRSFDQEP----RFRGDIMRL 1106
Cdd:cd18576 187 VVKAFTREDyeieRYRKALERV 208
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
667-806 |
4.27e-06 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 49.58 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 667 AYIAQSP-WIQSGKVEENILFGKPM-----EREWYDRVLEACSLNKDLeilpfHDQTVIGERGINLSGGQKQRIQIARAL 740
Cdd:cd03234 84 AYVRQDDiLLPGLTVRETLTYTAILrlprkSSDAIRKKRVEDVLLRDL-----ALTRIGGNLVKGISGGERRRVSIAVQL 158
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30682479 741 YQDADIYLFDDPFSAVDAHTGSHLFKevllgLLRH-----KTVIYVTHQ--VEFLPEADLILVMKDGKITQAG 806
Cdd:cd03234 159 LWDPKVLILDEPTSGLDSFTALNLVS-----TLSQlarrnRIVILTIHQprSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
614-813 |
4.40e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.21 E-value: 4.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 614 SPIPTLRDMNFKVSQGMNVAICGTVGSGKSSLLSSILGEVPKISGNLKVCGR--------KAY------IAQSPWI---Q 676
Cdd:PRK15439 22 SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpaKAHqlgiylVPQEPLLfpnL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 677 SgkVEENILFGKPMEREWYDRVLE-----ACSLNKD-----LEILpfhDQtvigerginlsggqkQRIQIARALYQDADI 746
Cdd:PRK15439 102 S--VKENILFGLPKRQASMQKMKQllaalGCQLDLDssagsLEVA---DR---------------QIVEILRGLMRDSRI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30682479 747 YLFDDPFSAVDAHTGSHLFKEVLLGLLRHKTVIYVTHQvefLPE----ADLILVMKDGKITQAGKYHEILD 813
Cdd:PRK15439 162 LILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHK---LPEirqlADRISVMRDGTIALSGKTADLST 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
725-803 |
5.26e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 50.79 E-value: 5.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 725 NLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAhtGShlfKEVLLGLLRH-----KTVIYVTHQvefLPE----ADLIL 795
Cdd:COG1129 394 NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDV--GA---KAEIYRLIRElaaegKAVIVISSE---LPEllglSDRIL 465
|
....*...
gi 30682479 796 VMKDGKIT 803
Cdd:COG1129 466 VMREGRIV 473
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
726-806 |
6.04e-06 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 49.38 E-value: 6.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADI-----YLF-DDPFSAVD-AHtgshlfKEVLLGLLRHKT------VIYVTHQVE----Fl 788
Cdd:PRK13548 135 LSGGEQQRVQLARVLAQLWEPdgpprWLLlDEPTSALDlAH------QHHVLRLARQLAherglaVIVVLHDLNlaarY- 207
|
90
....*....|....*...
gi 30682479 789 peADLILVMKDGKITQAG 806
Cdd:PRK13548 208 --ADRIVLLHQGRLVADG 223
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
619-794 |
6.26e-06 |
|
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: 48.63 E-value: 6.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 619 LRDMNFKVSQGMNVAICG-------TvgsgkssLLSSILGEVPKISGNLKVCGRK------------AYIAQSPWIQSG- 678
Cdd:COG4133 18 FSGLSFTLAAGEALALTGpngsgktT-------LLRILAGLLPPSAGEVLWNGEPirdaredyrrrlAYLGHADGLKPEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 679 KVEENILF-----GKPMEREWYDRVLEACSLnKDLEILPFHdqtvigergiNLSGGQKQRIQIARALYQDADIYLFDDPF 753
Cdd:COG4133 91 TVRENLRFwaalyGLRADREAIDEALEAVGL-AGLADLPVR----------QLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 30682479 754 SAVDAHTgshlfKEVLLGLLRH-----KTVIYVTHQVEFLPEADLI 794
Cdd:COG4133 160 TALDAAG-----VALLAELIAAhlargGAVLLTTHQPLELAAARVL 200
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
727-813 |
7.18e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 49.15 E-value: 7.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 727 SGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHlfkevLLGLLRHKT------VIYVTHQ---VEFLpeADLILVM 797
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQAR-----LLDLLRGLVrelglaVVIVTHDlavARLL--AHRLLVM 225
|
90
....*....|....*.
gi 30682479 798 KDGKITQAGKYHEILD 813
Cdd:PRK11701 226 KQGRVVESGLTDQVLD 241
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1235-1412 |
7.24e-06 |
|
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: 50.32 E-value: 7.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1235 VLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRI-DGINIlsiglhdlrsrlSIIPQDP------TMFE 1307
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGIKV------------GYLPQEPqldptkTVRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1308 ------GTIRSNLDPLEE----YTDDQ------------IWEALDNCQLGDEVRKKE-----LKL---DSPVSengqNWS 1357
Cdd:TIGR03719 88 nveegvAEIKDALDRFNEisakYAEPDadfdklaaeqaeLQEIIDAADAWDLDSQLEiamdaLRCppwDADVT----KLS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1358 VGQRQLVCLGRVLLKRSKLLVLDEATASIDTatdnliqET---LRHHFADC--TVITIAH 1412
Cdd:TIGR03719 164 GGERRRVALCRLLLSKPDMLLLDEPTNHLDA-------ESvawLERHLQEYpgTVVAVTH 216
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
724-823 |
8.88e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 47.95 E-value: 8.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 724 INLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKeVLLGLLRH--KTVIYVTHQVEFLPE-ADLILVM--K 798
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAAR-AIRRLSEEgkKTALVVEHDLAVLDYlSDRIHVFegE 148
|
90 100
....*....|....*....|....*
gi 30682479 799 DGKITQAGKYHEILDSGTDFMELVG 823
Cdd:cd03222 149 PGVYGIASQPKGTREGINRFLRGYL 173
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1250-1441 |
9.12e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.91 E-value: 9.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1250 GIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDG--INILSIGlHDLRSRLSIIPQDpTMFEG-----TIRSNLD------- 1315
Cdd:PRK11288 283 GLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPR-DAIRAGIMLCPED-RKAEGiipvhSVADNINisarrhh 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1316 -PLEEYTDDQiWEAldncQLGDEVRKKeLKLDSPvseNGQ----NWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTAT 1390
Cdd:PRK11288 361 lRAGCLINNR-WEA----ENADRFIRS-LNIKTP---SREqlimNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGA 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 30682479 1391 DNLIQETLrHHFAD--CTVITIAHRISSVID-SDMVLLLDQGLI-----KEHDSPARLL 1441
Cdd:PRK11288 432 KHEIYNVI-YELAAqgVAVLFVSSDLPEVLGvADRIVVMREGRIagelaREQATERQAL 489
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
726-802 |
1.10e-05 |
|
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: 47.93 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHlfkevLLGLLR-----HKTVIYVTHQV--EFLPEADLILVMK 798
Cdd:cd03213 112 LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ-----VMSLLRrladtGRTIICSIHQPssEIFELFDKLLLLS 186
|
....
gi 30682479 799 DGKI 802
Cdd:cd03213 187 QGRV 190
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
938-1098 |
1.18e-05 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 48.97 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 938 FTLILVYVLLAVASSFCILIRALLVAMTGFKMATELFTQMHLRIFRASMSFFDATPMGRILNRASTDQSVadLR--LPGQ 1015
Cdd:cd18551 36 GGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTL--LRelITSG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1016 FAYVAIAAINILGIIGVIVQVAWQ---VLIVFIPVVAACAWY-----RQYYISAARELARLAGisrspvvhHFSETLSGI 1087
Cdd:cd18551 114 LPQLVTGVLTVVGAVVLMFLLDWVltlVTLAVVPLAFLIILPlgrriRKASKRAQDALGELSA--------ALERALSAI 185
|
170
....*....|.
gi 30682479 1088 TTIRSFDQEPR 1098
Cdd:cd18551 186 RTVKASNAEER 196
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
680-791 |
1.21e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 47.95 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 680 VEENILF-----GKPMEREwyDRVLEACSLNkDLEILPFHdqtvigergiNLSGGQKQRIQIARALYQDADIYLFDDPFS 754
Cdd:PRK13539 90 VAENLEFwaaflGGEELDI--AAALEAVGLA-PLAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 30682479 755 AVDAHTgshlfKEVLLGLLRHK-----TVIYVTHQVEFLPEA 791
Cdd:PRK13539 157 ALDAAA-----VALFAELIRAHlaqggIVIAATHIPLGLPGA 193
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
725-812 |
1.33e-05 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 48.20 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 725 NLSGGQKQRIQIARALYQDADIYLFDDPFSAVdahtgSHLFKEVLLGLLR-----HKTVIYVTHQVEFLPE-ADLILVMK 798
Cdd:cd03219 143 ELSYGQQRRLEIARALATDPKLLLLDEPAAGL-----NPEETEELAELIRelrerGITVLLVEHDMDVVMSlADRVTVLD 217
|
90
....*....|....
gi 30682479 799 DGKITQAGKYHEIL 812
Cdd:cd03219 218 QGRVIAEGTPDEVR 231
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
726-816 |
1.57e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 48.62 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSH---LFKEvlLGLLRHKTVIYVTHQV-EFLPEADLILVMKDGK 801
Cdd:PRK13646 146 MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQvmrLLKS--LQTDENKTIILVSHDMnEVARYADEVIVMKEGS 223
|
90
....*....|....*
gi 30682479 802 ITQAGKYHEILDSGT 816
Cdd:PRK13646 224 IVSQTSPKELFKDKK 238
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
680-801 |
1.77e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.16 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 680 VEENILFGkpmeREW-------YDRV-LEACSLNKDLEIlpfhDQTViGERGINLSGGQKQRIQIARALYQDADIYLFDD 751
Cdd:PRK13549 99 VLENIFLG----NEItpggimdYDAMyLRAQKLLAQLKL----DINP-ATPVGNLGLGQQQLVEIAKALNKQARLLILDE 169
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 30682479 752 PFSAVDAHTGSHLFKevLLGLLRHKTV--IYVTHQVEFLPE-ADLILVMKDGK 801
Cdd:PRK13549 170 PTASLTESETAVLLD--IIRDLKAHGIacIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1235-1427 |
1.78e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.17 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1235 VLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGL-------HDLRSRLsiipqdptmfE 1307
Cdd:PRK13541 15 NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKpyctyigHNLGLKL----------E 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1308 GTIRSNLDPLEEYTD--DQIWEALDNCQLGDEVRKKELKLDSpvsengqnwsvGQRQLVCLGRVLLKRSKLLVLDEATAS 1385
Cdd:PRK13541 85 MTVFENLKFWSEIYNsaETLYAAIHYFKLHDLLDEKCYSLSS-----------GMQKIVAIARLIACQSDLWLLDEVETN 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 30682479 1386 IDTATDNLIQETLRHHFADCTVITIAHRISSVIDSDMVLLLD 1427
Cdd:PRK13541 154 LSKENRDLLNNLIVMKANSGGIVLLSSHLESSIKSAQILQLD 195
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
680-806 |
2.36e-05 |
|
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: 49.24 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 680 VEENILFGKPME-REWYDRVLEACSLnkdLEILPFHDQTviGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDA 758
Cdd:TIGR01257 1020 VAEHILFYAQLKgRSWEEAQLEMEAM---LEDTGLHHKR--NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP 1094
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 30682479 759 HTGSHLFkEVLLGLLRHKTVIYVTHQVEflpEADL----ILVMKDGKITQAG 806
Cdd:TIGR01257 1095 YSRRSIW-DLLLKYRSGRTIIMSTHHMD---EADLlgdrIAIISQGRLYCSG 1142
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
685-806 |
2.49e-05 |
|
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: 46.98 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 685 LFGKPmEREWYDRVLEACSLnkdLEILPFHDQTVIgergiNLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHL 764
Cdd:cd03265 100 LYGVP-GAERRERIDELLDF---VGLLEAADRLVK-----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHV 170
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 30682479 765 FkEVLLGLLRHK--TVIYVTHQVEflpEADL----ILVMKDGKITQAG 806
Cdd:cd03265 171 W-EYIEKLKEEFgmTILLTTHYME---EAEQlcdrVAIIDHGRIIAEG 214
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
698-802 |
2.52e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 47.08 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 698 VLEACSLNKDLEILPfhdqtvigergINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLfKEVLLGLLRH-- 775
Cdd:PRK10584 130 LLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI-ADLLFSLNREhg 197
|
90 100
....*....|....*....|....*..
gi 30682479 776 KTVIYVTHQVEFLPEADLILVMKDGKI 802
Cdd:PRK10584 198 TTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
706-823 |
2.55e-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: 47.40 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 706 KDLEILPFHDQTVIgergiNLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEVLLGLLRH-KTVIYVTHQ 784
Cdd:cd03237 101 KPLQIEQILDREVP-----ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNeKTAFVVEHD 175
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 30682479 785 VEFLPE-ADLILVM--KDGKITQAGKYHEILDSGTDFMELVG 823
Cdd:cd03237 176 IIMIDYlADRLIVFegEPSVNGVANPPQSLRSGMNRFLKNLD 217
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
726-811 |
2.61e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 48.20 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFkEVLLGLLRHK--TVIYVTHQVEFLPE-ADLILVMKDGKI 802
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQII-ELLLELQQKEnmALVLITHDLALVAEaAHKIIVMYAGQV 232
|
....*....
gi 30682479 803 TQAGKYHEI 811
Cdd:PRK11022 233 VETGKAHDI 241
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
725-800 |
2.74e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.63 E-value: 2.74e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30682479 725 NLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFkeVLLGLLRH--KTVIYVTHQV-EFLPEADLILVMKDG 800
Cdd:PRK09700 145 NLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLF--LIMNQLRKegTAIVYISHKLaEIRRICDRYTVMKDG 221
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1246-1427 |
2.95e-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: 45.83 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1246 GLKTGIVGRTGCGKSTLIQTLfrivepaAGEIRIDGINILSIglhdlrsrlsiipqdptmfegtirsNLDPLEEYTDDQI 1325
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARAL-------ARELGPPGGGVIYI-------------------------DGEDILEEVLDQL 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1326 WEALDNCQLGDEVRKKElkldspvsengqnwsvgQRQLvcLGRVLLKRSKLLVLDEATASIDTATDNLIQETLR------ 1399
Cdd:smart00382 50 LLIIVGGKKASGSGELR-----------------LRLA--LALARKLKPDVLILDEITSLLDAEQEALLLLLEElrllll 110
|
170 180
....*....|....*....|....*....
gi 30682479 1400 -HHFADCTVITIAHRISSVIDSDMVLLLD 1427
Cdd:smart00382 111 lKSEKNLTVILTTNDEKDLGPALLRRRFD 139
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1219-1321 |
3.10e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 47.45 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1219 ITICNLQVRYGPHLpmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSI---GLHDLRSR 1295
Cdd:PRK11831 8 VDMRGVSFTRGNRC--IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMsrsRLYTVRKR 85
|
90 100
....*....|....*....|....*...
gi 30682479 1296 LSIIPQDPTMF-EGTIRSNLD-PLEEYT 1321
Cdd:PRK11831 86 MSMLFQSGALFtDMNVFDNVAyPLREHT 113
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1251-1429 |
3.32e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 46.88 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1251 IVGRTGCGKSTLIQTLFRIVEPAAGEIRIDginilsiglhdlrsrlsiIPQDPTMFEGTIRSNLDPLEEyTDDQIwEALD 1330
Cdd:COG2401 61 IVGASGSGKSTLLRLLAGALKGTPVAGCVD------------------VPDNQFGREASLIDAIGRKGD-FKDAV-ELLN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1331 NCQLGDEV----RKKELkldspvsengqnwSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTATDNL----IQETLRHHF 1402
Cdd:COG2401 121 AVGLSDAVlwlrRFKEL-------------STGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRvarnLQKLARRAG 187
|
170 180
....*....|....*....|....*....
gi 30682479 1403 AdcTVITIAHR--ISSVIDSDMVLLLDQG 1429
Cdd:COG2401 188 I--TLVVATHHydVIDDLQPDLLIFVGYG 214
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1223-1443 |
4.05e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 46.99 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1223 NLQVRYgPHLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDG--INILSIGLHDLRSRLSIIP 1300
Cdd:PRK13639 6 DLKYSY-PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTVGIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1301 QDPtmfegtirsnldpleeytDDQIWE-------ALDNCQLG---DEVRKKELKLDSPVSENG------QNWSVGQRQLV 1364
Cdd:PRK13639 85 QNP------------------DDQLFAptveedvAFGPLNLGlskEEVEKRVKEALKAVGMEGfenkppHHLSGGQKKRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1365 CLGRVLLKRSKLLVLDEATASID----TATDNLIQETLRHHFadcTVITIAHRISSV-IDSDMVLLLDQGLIKEHDSPAR 1439
Cdd:PRK13639 147 AIAGILAMKPEIIVLDEPTSGLDpmgaSQIMKLLYDLNKEGI---TIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKE 223
|
....
gi 30682479 1440 LLED 1443
Cdd:PRK13639 224 VFSD 227
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
721-801 |
4.10e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.80 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 721 ERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKevLLGLLRHK--TVIYVTHQVEFLPE-ADLILVM 797
Cdd:PRK10982 130 AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFT--IIRKLKERgcGIVYISHKMEEIFQlCDEITIL 207
|
....
gi 30682479 798 KDGK 801
Cdd:PRK10982 208 RDGQ 211
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
726-806 |
4.24e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 47.07 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKevLLGLLRHK---TVIYVTHQV-EFLPEADLILVMKDGK 801
Cdd:PRK11831 144 LSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVK--LISELNSAlgvTCVVVSHDVpEVLSIADHAYIVADKK 221
|
....*
gi 30682479 802 ITQAG 806
Cdd:PRK11831 222 IVAHG 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1223-1395 |
4.40e-05 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 47.76 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1223 NLQVRYGPHLPM--VLHGLTCTFPGGLKTGIVGRTGCGKS----TLIQTLFRIVEPAAGEIRIDGINILSIGLHDLR--- 1293
Cdd:COG4172 11 DLSVAFGQGGGTveAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRrir 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1294 -SRLSIIPQDPtMfegtirSNLDPLeeYT-DDQIWEALdncQL-----GDEVRKKELKL------DSPvsENGQNW---- 1356
Cdd:COG4172 91 gNRIAMIFQEP-M------TSLNPL--HTiGKQIAEVL---RLhrglsGAAARARALELlervgiPDP--ERRLDAyphq 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 30682479 1357 -SVGQRQLVCLGRVLLKRSKLLVLDEATasidTATDNLIQ 1395
Cdd:COG4172 157 lSGGQRQRVMIAMALANEPDLLIADEPT----TALDVTVQ 192
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
724-803 |
4.50e-05 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 47.87 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 724 INLSGGQKQRIQIARALYQDADIYLFD------DP-FSavdahtgsHLFKEVLLGLLRH--KTVIYVTHQVEFLPEADLI 794
Cdd:COG4615 456 TDLSQGQRKRLALLVALLEDRPILVFDewaadqDPeFR--------RVFYTELLPELKArgKTVIAISHDDRYFDLADRV 527
|
....*....
gi 30682479 795 LVMKDGKIT 803
Cdd:COG4615 528 LKMDYGKLV 536
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
938-1108 |
4.53e-05 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 47.02 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 938 FTLILVYVLLAVASSFCILIRALLVAMTGFKMATELFTQMHLRIFRASMSFFDATPMGRILNRASTD-QSVADLRLPGqF 1016
Cdd:cd18541 40 LRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDlNAVRMALGPG-I 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1017 AYVAIAAINILGIIGVIVQVAWQV-LIVFIP--VVAACAWY-----RQYYISAARELARLAGISRspvvhhfsETLSGIT 1088
Cdd:cd18541 119 LYLVDALFLGVLVLVMMFTISPKLtLIALLPlpLLALLVYRlgkkiHKRFRKVQEAFSDLSDRVQ--------ESFSGIR 190
|
170 180
....*....|....*....|
gi 30682479 1089 TIRSFDQEPRFRGDIMRLSD 1108
Cdd:cd18541 191 VIKAFVQEEAEIERFDKLNE 210
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
727-757 |
5.28e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 47.27 E-value: 5.28e-05
10 20 30
....*....|....*....|....*....|.
gi 30682479 727 SGGQKQRIQIARALYQDADIYLFDDPFSAVD 757
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
716-811 |
5.68e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.54 E-value: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 716 QTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKevLLGLLRHKT---VIYVTHQVEFLPE-A 791
Cdd:PRK10261 159 QTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQ--LIKVLQKEMsmgVIFITHDMGVVAEiA 236
|
90 100
....*....|....*....|
gi 30682479 792 DLILVMKDGKITQAGKYHEI 811
Cdd:PRK10261 237 DRVLVMYQGEAVETGSVEQI 256
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
725-755 |
7.29e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.09 E-value: 7.29e-05
10 20 30
....*....|....*....|....*....|.
gi 30682479 725 NLSGGQKQRIQIARALYQDADIYLFDDPfSA 755
Cdd:COG1245 455 DLSGGELQRVAIAACLSRDADLYLLDEP-SA 484
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1236-1389 |
7.32e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 45.64 E-value: 7.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1236 LHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHD---LRSRLSIIPQD-PTMFEGTIR 1311
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDhHLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1312 SNLD-PL------EEYTDDQIWEALDNCQLGDEVRKKELKLdspvsengqnwSVGQRQLVCLGRVLLKRSKLLVLDEATA 1384
Cdd:PRK10908 98 DNVAiPLiiagasGDDIRRRVSAALDKVGLLDKAKNFPIQL-----------SGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
....*
gi 30682479 1385 SIDTA 1389
Cdd:PRK10908 167 NLDDA 171
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
725-755 |
8.28e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.11 E-value: 8.28e-05
10 20 30
....*....|....*....|....*....|.
gi 30682479 725 NLSGGQKQRIQIARALYQDADIYLFDDPfSA 755
Cdd:PRK13409 453 DLSGGELQRVAIAACLSRDADLYLLDEP-SA 482
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
938-1099 |
8.36e-05 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 46.28 E-value: 8.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 938 FTLILVYVLLAVASSFCILIRALLVAMTGFKMATELFTQMHLRIFRASMSFFDATPMGRILNR---ASTDQSVadlrlpg 1014
Cdd:cd18570 42 NIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRfndANKIREA------- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1015 qFAYVAI-AAINILGIIGVIVQVAWQ------VLIVFIPVVAACAW-YRQYYISAARELARLAGISRSpvvhHFSETLSG 1086
Cdd:cd18570 115 -ISSTTIsLFLDLLMVIISGIILFFYnwklflITLLIIPLYILIILlFNKPFKKKNREVMESNAELNS----YLIESLKG 189
|
170
....*....|...
gi 30682479 1087 ITTIRSFDQEPRF 1099
Cdd:cd18570 190 IETIKSLNAEEQF 202
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
725-822 |
8.42e-05 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 47.10 E-value: 8.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 725 NLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgSHLFKEVLLGLLRHK--TVIYVTHQVEFLPE-ADLILVMKDGK 801
Cdd:TIGR03269 168 DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQT-AKLVHNALEEAVKASgiSMVLTSHWPEVIEDlSDKAIWLENGE 246
|
90 100
....*....|....*....|.
gi 30682479 802 ITQAGKYHEILDSgtdFMELV 822
Cdd:TIGR03269 247 IKEEGTPDEVVAV---FMEGV 264
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
726-814 |
8.77e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 46.24 E-value: 8.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLfKEVLLGLLRHKTVIYVTHQVEFLPE-ADLILVMKDGKITQ 804
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKI-EEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVE 242
|
90
....*....|
gi 30682479 805 AGKYHEILDS 814
Cdd:PRK14271 243 EGPTEQLFSS 252
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
727-813 |
9.74e-05 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 46.24 E-value: 9.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 727 SGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGS---HLFKEVL--LGLlrhkTVIYVTHQVEFLPE-ADLILVMKDG 800
Cdd:PRK15079 163 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAqvvNLLQQLQreMGL----SLIFIAHDLAVVKHiSDRVLVMYLG 238
|
90
....*....|...
gi 30682479 801 KITQAGKYHEILD 813
Cdd:PRK15079 239 HAVELGTYDEVYH 251
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
726-814 |
1.01e-04 |
|
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: 46.20 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAhtgS------HLFKEvllglLRHK---TVIYVTH------QVeflpe 790
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDV---TiqaqilNLLKD-----LQRElglAILFITHdlgvvaEI----- 217
|
90 100
....*....|....*....|....
gi 30682479 791 ADLILVMKDGKITQAGKYHEILDS 814
Cdd:COG0444 218 ADRVAVMYAGRIVEEGPVEELFEN 241
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1235-1431 |
1.02e-04 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 44.83 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1235 VLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTL--FRIVEPAAGEIRIDGINILSIGLHDlRSRLSII--PQDPTMFEGTi 1310
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEE-RARLGIFlaFQYPPEIPGV- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1311 rsnldpleeytddqiwealdncQLGDEVRkkelkldsPVSEngqNWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTAT 1390
Cdd:cd03217 93 ----------------------KNADFLR--------YVNE---GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 30682479 1391 DNLIQETLRH-HFADCTVITIAH--RISSVIDSDMVLLLDQGLI 1431
Cdd:cd03217 140 LRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRI 183
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
726-820 |
1.02e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 45.89 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHL---FKEVllgllrHK---TVIYVTHQVEFLPE-ADLILVMK 798
Cdd:PRK13649 146 LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELmtlFKKL------HQsgmTIVLVTHLMDDVANyADFVYVLE 219
|
90 100
....*....|....*....|..
gi 30682479 799 DGKITQAGKYHEILDSgTDFME 820
Cdd:PRK13649 220 KGKLVLSGKPKDIFQD-VDFLE 240
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
726-800 |
1.33e-04 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 46.34 E-value: 1.33e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKeVLLGLLRHKTVIYVTHQVEFLPEADLILVMKDG 800
Cdd:COG4178 486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQ-LLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
727-788 |
1.52e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 1.52e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30682479 727 SGGQKQRIQIARALYQDADIYLFDDPFSAVDAHtgSHLFKEVLLgLLRHKTVIYVTHQVEFL 788
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLH--AVLWLETYL-LKWPKTFIVVSHAREFL 404
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
726-798 |
1.65e-04 |
|
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: 43.89 E-value: 1.65e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30682479 726 LSGGQKQRIQIARAL----YQDADIYLFDDPFSAVDAHTGSHLFKEVLLGLLRHKTVIYVTHQVEFLPEADLILVMK 798
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIK 154
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
687-811 |
1.76e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 45.08 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 687 GKPMEREWYDRVLEACSLNKDLEIL---PFHdqtvigerginLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSH 763
Cdd:PRK10418 110 GKPADDATLTAALEAVGLENAARVLklyPFE-----------MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQAR 178
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 30682479 764 LFkEVLLGLLRHKT--VIYVTHQVEFLPE-ADLILVMKDGKITQAGKYHEI 811
Cdd:PRK10418 179 IL-DLLESIVQKRAlgMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETL 228
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
667-792 |
1.78e-04 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 44.70 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 667 AYIAQSPWIQSGKVEENILFGKPMEREWYDRVleacSLNKDLEI--LPFHdqtvIGERGIN-LSGGQKQRIQIARALYQD 743
Cdd:PRK10247 84 SYCAQTPTLFGDTVYDNLIFPWQIRNQQPDPA----IFLDDLERfaLPDT----ILTKNIAeLSGGEKQRISLIRNLQFM 155
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 30682479 744 ADIYLFDDPFSAVDAHTgSHLFKEVLLGLLRHK--TVIYVTHQVEFLPEAD 792
Cdd:PRK10247 156 PKVLLLDEITSALDESN-KHNVNEIIHRYVREQniAVLWVTHDKDEINHAD 205
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
727-800 |
1.84e-04 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 44.73 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 727 SGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgshlfKEVLLGLLRHK-----TVIYVTHQVEFLPE-ADLILVMKDG 800
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAAN-----RAVVVELIEEAkargtAIIGIFHDEEVREAvADRVVDVTPF 228
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
939-1100 |
2.11e-04 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 44.89 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 939 TLILVYVLLAVASSFCILIRALLVAMTGFKMATELFTQMHLRIFRASMSFFDATPMGRILNRASTDQSVADLrLPGQFAY 1018
Cdd:cd18782 43 VIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRISELDTIRGF-LTGTALT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1019 VAIAAINILGIIGVIVQVAWQ---VLIVFIPVVAACAWY------RQYyisaaRELARLAGISRSPVVhhfsETLSGITT 1089
Cdd:cd18782 122 TLLDVLFSVIYIAVLFSYSPLltlVVLATVPLQLLLTFLfgpilrRQI-----RRRAEASAKTQSYLV----ESLTGIQT 192
|
170
....*....|.
gi 30682479 1090 IRSFDQEPRFR 1100
Cdd:cd18782 193 VKAQNAELKAR 203
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1225-1440 |
2.19e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 44.69 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1225 QVRYGPHLPMVlHGLTCTFPGGLKTGIVGRTGCGKS----TLIQTLFRIVEPAAGEIRIDGInilSIGLHDLRSRL-SII 1299
Cdd:PRK10418 9 NIALQAAQPLV-HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGK---PVAPCALRGRKiATI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1300 PQDPtmfegtiRSNLDPLE---------------EYTDDQIWEALDNCQLGDEVRKKELkldSPVSENGqnwSVGQRQLV 1364
Cdd:PRK10418 85 MQNP-------RSAFNPLHtmhtharetclalgkPADDATLTAALEAVGLENAARVLKL---YPFEMSG---GMLQRMMI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1365 CLGrvLLKRSKLLVLDEATASIDTATD----NLIQETLRHHfaDCTVITIAHRISSVID-SDMVLLLDQGLIKEHDSPAR 1439
Cdd:PRK10418 152 ALA--LLCEAPFIIADEPTTDLDVVAQarilDLLESIVQKR--ALGMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVET 227
|
.
gi 30682479 1440 L 1440
Cdd:PRK10418 228 L 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
715-811 |
2.24e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 44.82 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 715 DQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEVLLGLLRHKTVIYVTHQVEFLPE-ADL 793
Cdd:PRK13641 135 SEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADD 214
|
90
....*....|....*...
gi 30682479 794 ILVMKDGKITQAGKYHEI 811
Cdd:PRK13641 215 VLVLEHGKLIKHASPKEI 232
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
724-804 |
2.61e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 45.35 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 724 INLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgSHLFKEVLLGLLRH--KTVIYVTHQVEFLPEADLILVMKDGK 801
Cdd:PRK10522 448 LKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHF-RREFYQVLLPLLQEmgKTIFAISHDDHYFIHADRLLEMRNGQ 526
|
...
gi 30682479 802 ITQ 804
Cdd:PRK10522 527 LSE 529
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
719-815 |
2.73e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.59 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 719 IGERGINLSGGQKQRIQIARALY---QDADIYLFDDPFSAVDAHTGSHLFKEVLLGLLRHKTVIYVTHQVEFLPEADLIL 795
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQADYLI 1772
|
90 100
....*....|....*....|
gi 30682479 796 VMKDGKITQAGKyheILDSG 815
Cdd:PRK00635 1773 EMGPGSGKTGGK---ILFSG 1789
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
695-757 |
2.74e-04 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 44.11 E-value: 2.74e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30682479 695 YDRVLEACSLNKDL----------EILP-FHDQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVD 757
Cdd:PRK10895 96 YDNLMAVLQIRDDLsaeqredranELMEeFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
726-812 |
2.76e-04 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 44.59 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFkEVLLGLLRHK--TVIYVTHQV-EFLPEADLILVMKDGKI 802
Cdd:PRK10253 144 LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLL-ELLSELNREKgyTLAAVLHDLnQACRYASHLIALREGKI 222
|
90
....*....|
gi 30682479 803 TQAGKYHEIL 812
Cdd:PRK10253 223 VAQGAPKEIV 232
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
938-1101 |
3.53e-04 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 44.40 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 938 FTLILVYVLLAVASSFciliRALLVAMTGFKMATELFTQMHLRIFRASMSFFDATPMGRILNRASTD----QSVADlrlp 1013
Cdd:cd18575 40 LLLLAVALVLALASAL----RFYLVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDttliQTVVG---- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1014 gqfAYVAIAAINILGIIGVIVQVAWQ-----------VLIVFIPVVAACAWYRQYyisaARE-LARLAGISrspvvHHFS 1081
Cdd:cd18575 112 ---SSLSIALRNLLLLIGGLVMLFITspkltllvllvIPLVVLPIILFGRRVRRL----SRAsQDRLADLS-----AFAE 179
|
170 180
....*....|....*....|
gi 30682479 1082 ETLSGITTIRSFDQEPRFRG 1101
Cdd:cd18575 180 ETLSAIKTVQAFTREDAERQ 199
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
903-1142 |
3.64e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 44.37 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 903 ILVVQVLFQLLSIGSNYWMTWVT---PVSKDVEppvSGFTLILVYVLLAVASSFCILIRALLV----AMTGFKMATELFT 975
Cdd:cd18567 7 ILLLSLALELFALASPLYLQLVIdevIVSGDRD---LLTVLAIGFGLLLLLQALLSALRSWLVlylsTSLNLQWTSNLFR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 976 qmHLriFRASMSFFDATPMGRILNRASTDQSVADLrLPGQFAYVAIAAINILGIIGVI----VQVAWQVLI-VFIPVVAA 1050
Cdd:cd18567 84 --HL--LRLPLSYFEKRHLGDIVSRFGSLDEIQQT-LTTGFVEALLDGLMAILTLVMMflysPKLALIVLAaVALYALLR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1051 CAWYRqYYISAARELARLAGISRSpvvhHFSETLSGITTIRSFDQEPRFRGDIM-RLSDC------YSRLKFHSTGAMEW 1123
Cdd:cd18567 159 LALYP-PLRRATEEQIVASAKEQS----HFLETIRGIQTIKLFGREAEREARWLnLLVDAinadirLQRLQILFSAANGL 233
|
250
....*....|....*....
gi 30682479 1124 LcFRLELLSTFAFASSLVI 1142
Cdd:cd18567 234 L-FGLENILVIYLGALLVL 251
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
725-820 |
3.83e-04 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 44.67 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 725 NLSGGQKQRIQIARALYQDADIYLFDDPfsavdahTgSHL-------FKEVLLGllRHKTVIYVTHQVEFLPE-ADLILV 796
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEP-------T-NHLdlesiewLEEFLKN--YPGTVLVVSHDRYFLDRvATRILE 221
|
90 100
....*....|....*....|....*
gi 30682479 797 MKDGKITQ-AGKYheildsgTDFME 820
Cdd:COG0488 222 LDRGKLTLyPGNY-------SAYLE 239
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
892-1096 |
4.66e-04 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, 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. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 44.07 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 892 ALAYGGAVIPLIL--VVQVLFQLLS-IGSNYWMTWVTPVSKdveppvsgftLILVYVLLAVASSFCILiralLVAMTGFK 968
Cdd:cd18574 7 AAALVNIQIPLLLgdLVNVISRSLKeTNGDFIEDLKKPALK----------LLGLYLLQSLLTFAYIS----LLSVVGER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 969 MATELFTQMHLRIFRASMSFFDATPMGRILNRASTDqsVADLRLPGQFAyVAIAAINILGIIGVIVQVAW------QVLI 1042
Cdd:cd18574 73 VAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTAD--VQEFKSSFKQC-VSQGLRSVTQTVGCVVSLYLispkltLLLL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 30682479 1043 VFIPVVAACAWY-----RQYYISAARELARLAGISrspvvhhfSETLSGITTIRSFDQE 1096
Cdd:cd18574 150 VIVPVVVLVGTLygsflRKLSRRAQAQVAKATGVA--------DEALGNIRTVRAFAME 200
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
726-814 |
4.78e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 43.62 E-value: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKevLLGLLRHK---TVIYVTHQVEFLPE-ADLILVMKDGK 801
Cdd:PRK15112 150 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLIN--LMLELQEKqgiSYIYVTQHLGMMKHiSDQVLVMHQGE 227
|
90
....*....|...
gi 30682479 802 ITQAGKYHEILDS 814
Cdd:PRK15112 228 VVERGSTADVLAS 240
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
724-803 |
4.79e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.52 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 724 INLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFkEVLLGLL-RHKTVIYVTHQvefLPE----ADLILVMK 798
Cdd:PRK11288 395 MNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIY-NVIYELAaQGVAVLFVSSD---LPEvlgvADRIVVMR 470
|
....*
gi 30682479 799 DGKIT 803
Cdd:PRK11288 471 EGRIA 475
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
726-823 |
4.98e-04 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 43.84 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEVLLGLLRHKTVIYVTHQVEFLPE-ADLILVMKDGKITQ 804
Cdd:PRK13638 137 LSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILT 216
|
90
....*....|....*....
gi 30682479 805 AGKYHEILdSGTDFMELVG 823
Cdd:PRK13638 217 HGAPGEVF-ACTEAMEQAG 234
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1250-1432 |
5.14e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 44.53 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1250 GIVGRTGCGKSTLIQTLFRiVEPAA--GEIRIDG--INILSIgLHDLRSRLSIIPQD-------PTMFEGTiRSNLDPLE 1318
Cdd:PRK13549 292 GIAGLVGAGRTELVQCLFG-AYPGRweGEIFIDGkpVKIRNP-QQAIAQGIAMVPEDrkrdgivPVMGVGK-NITLAALD 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1319 EYTD-DQIWEALDNCQLGDEVRKKELKLDSPVSENGqNWSVGQRQLVCLGRVLLKRSKLLVLDEATASIDTATD----NL 1393
Cdd:PRK13549 369 RFTGgSRIDDAAELKTILESIQRLKVKTASPELAIA-RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKyeiyKL 447
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 30682479 1394 IQETLRHHFAdctVITIAHRISSVID-SDMVLLLDQGLIK 1432
Cdd:PRK13549 448 INQLVQQGVA---IIVISSELPEVLGlSDRVLVMHEGKLK 484
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
680-801 |
5.16e-04 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 44.43 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 680 VEENILFGK----PMEREWYDR-VLEACSLNKDLEILPFHDQTVIGERGinlsGGQKQRIQIARALYQDADIYLFDDPFS 754
Cdd:TIGR02633 95 VAENIFLGNeitlPGGRMAYNAmYLRAKNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEPSS 170
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 30682479 755 AVDAHTgshlfKEVLLGLLR---HKTV--IYVTHQV-EFLPEADLILVMKDGK 801
Cdd:TIGR02633 171 SLTEKE-----TEILLDIIRdlkAHGVacVYISHKLnEVKAVCDTICVIRDGQ 218
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
906-1174 |
5.58e-04 |
|
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: 43.63 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 906 VQVLFQLLSIGSNYwmtwVTPV----------SKDVEPPVSGFTLILVYVLLAVASSFCILIRALLVAMTGFKMATELFT 975
Cdd:cd18579 1 LAGLLKLLEDLLSL----AQPLllgllisylsSYPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 976 QMHLRIFRASMSFFDATPMGRILNRASTD-QSVADlrLPGQFAYVAIAAINILGIIGVIV-QVAWQ------VLIVFIPV 1047
Cdd:cd18579 77 LIYRKALRLSSSARQETSTGEIVNLMSVDvQRIED--FFLFLHYLWSAPLQIIVALYLLYrLLGWAalaglgVLLLLIPL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1048 VAACAwyrqYYISAARELARLAGISRspvVHHFSETLSGITTIRSFDQEPRFRGDIMRLsdcysRLKfhstgamEwlcfr 1127
Cdd:cd18579 155 QAFLA----KLISKLRKKLMKATDER---VKLTNEILSGIKVIKLYAWEKPFLKRIEEL-----RKK-------E----- 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 30682479 1128 LELLSTFAFASSLVILVSapegVINPSLAGLA--ITYALNLNTLQATLI 1174
Cdd:cd18579 211 LKALRKFGYLRALNSFLF----FSTPVLVSLAtfATYVLLGNPLTAAKV 255
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
667-784 |
7.93e-04 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 42.48 E-value: 7.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 667 AYIAQSPWIQSG-KVEENILFGKPM-EREWYDRVLEACSLNKdLEILPFHdqtvigergiNLSGGQKQRIQIARALYQDA 744
Cdd:cd03231 76 LYLGHAPGIKTTlSVLENLRFWHADhSDEQVEEALARVGLNG-FEDRPVA----------QLSAGQQRRVALARLLLSGR 144
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 30682479 745 DIYLFDDPFSAVDAhTGSHLFKEVLLG-LLRHKTVIYVTHQ 784
Cdd:cd03231 145 PLWILDEPTTALDK-AGVARFAEAMAGhCARGGMVVLTTHQ 184
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
719-804 |
8.32e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 43.10 E-value: 8.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 719 IGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTG---SHLFKEvlLGLLRHKTVIYVTH---QVEFLPEAD 792
Cdd:PRK14258 144 IHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASmkvESLIQS--LRLRSELTMVIVSHnlhQVSRLSDFT 221
|
90
....*....|..
gi 30682479 793 LILVMKDGKITQ 804
Cdd:PRK14258 222 AFFKGNENRIGQ 233
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
725-816 |
1.01e-03 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 42.85 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 725 NLSGGQKQRIQIARALYQDADIYLFDDPFSAVD-AHTgshlfKEVL-----LGLLRHKTVIYVTHQVEFLPE-ADLILVM 797
Cdd:PRK10575 147 SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiAHQ-----VDVLalvhrLSQERGLTVIAVLHDINMAARyCDYLVAL 221
|
90
....*....|....*....
gi 30682479 798 KDGKITQAGKYHEILDSGT 816
Cdd:PRK10575 222 RGGEMIAQGTPAELMRGET 240
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
619-821 |
1.04e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 42.70 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 619 LRDMNFKVSQGMNVAICGTVGSGKSSLLSSILGEVPKISG----------------NLKVCGRKAYIA-QSPWIQ--SGK 679
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGtvtigervitagkknkKLKPLRKKVGIVfQFPEHQlfEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 680 VEENILFGkPME--------REWYDRVLEACSLNKD-LEILPFhdqtvigergiNLSGGQKQRIQIARALYQDADIYLFD 750
Cdd:PRK13634 103 VEKDICFG-PMNfgvseedaKQKAREMIELVGLPEElLARSPF-----------ELSGGQMRRVAIAGVLAMEPEVLVLD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30682479 751 DPFSAVDAHtGSHLFKEVLLGLLRHK--TVIYVTHQVEFLPE-ADLILVMKDGKITQAGKYHEILDSGTDFMEL 821
Cdd:PRK13634 171 EPTAGLDPK-GRKEMMEMFYKLHKEKglTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFADPDELEAI 243
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
726-812 |
1.13e-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: 43.25 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEVLLGLLR-HKTVIYVTHQVEFLPE-ADLILVMKDGKIT 803
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDvCDRAALMRDGKIV 507
|
....*....
gi 30682479 804 QAGKYHEIL 812
Cdd:TIGR03269 508 KIGDPEEIV 516
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
726-804 |
1.17e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 43.23 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKevllgLLRH-----KTVIYVTHQV-EFLPEADLILVMKD 799
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYK-----VMRQladdgKVILMVSSELpEIITVCDRIAVFCE 484
|
....*
gi 30682479 800 GKITQ 804
Cdd:PRK09700 485 GRLTQ 489
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1235-1381 |
1.18e-03 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 42.17 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1235 VLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLFRIVEPAAGEIRIDGINILSIGLHD-LRSRLSIIPQDPTMFEG-TIRS 1312
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAIVPEGRRVFSRmTVEE 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30682479 1313 NLDPLEEYTDDQIWEaldncQLGDEVRKKELKLDSPVSENGQNWSVGQRQLVCLGRVLLKRSKLLVLDE 1381
Cdd:PRK11614 100 NLAMGGFFAERDQFQ-----ERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
726-757 |
1.91e-03 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 42.03 E-value: 1.91e-03
10 20 30
....*....|....*....|....*....|..
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVD 757
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
726-802 |
2.39e-03 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 41.60 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKevLLGLLRHKT---VIYVTHQVEFLPE-ADLILVMKDGK 801
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIR--LLKKLQQQFgtaCLFITHDLRLVERfCQRVMVMDNGQ 229
|
.
gi 30682479 802 I 802
Cdd:PRK10419 230 I 230
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
726-784 |
2.48e-03 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 40.94 E-value: 2.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHtGShlfkEVLLGLLRHKT-----VIYVTHQ 784
Cdd:PRK13538 130 LSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ-GV----ARLEALLAQHAeqggmVILTTHQ 188
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
938-1096 |
2.57e-03 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 41.67 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 938 FTLILVYVLLAVASSFCILIRALLVAMTGFKMAT----ELFTQMHlrifRASMSFFDATPMGRILNRASTDqsvadLRLP 1013
Cdd:cd18549 42 LIIGAILLALYILRTLLNYFVTYWGHVMGARIETdmrrDLFEHLQ----KLSFSFFDNNKTGQLMSRITND-----LFDI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1014 GQFAY-----VAIAAINILGIIGVIVQVAWQ---VLIVFIPVVAACAWYRQYYISAARELAR--LAGISrspvvHHFSET 1083
Cdd:cd18549 113 SELAHhgpedLFISIITIIGSFIILLTINVPltlIVFALLPLMIIFTIYFNKKMKKAFRRVRekIGEIN-----AQLEDS 187
|
170
....*....|...
gi 30682479 1084 LSGITTIRSFDQE 1096
Cdd:cd18549 188 LSGIRVVKAFANE 200
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
726-813 |
2.63e-03 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 41.97 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTgshlfKEVLLGLLRH--KTVIYVTHQVEFLPE-ADLILVMKDGKI 802
Cdd:COG0488 433 LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET-----LEALEEALDDfpGTVLLVSHDRYFLDRvATRILEFEDGGV 507
|
90
....*....|..
gi 30682479 803 TQ-AGKYHEILD 813
Cdd:COG0488 508 REyPGGYDDYLE 519
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
725-788 |
2.66e-03 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 42.23 E-value: 2.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30682479 725 NLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEvllgLLRHK-TVIYVTHQVEFL 788
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERH----LQEYPgTVVAVTHDRYFL 221
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1219-1281 |
2.85e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 41.75 E-value: 2.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30682479 1219 ITICNLQVRYGPHLPmVLHGLTCTFPGGLKTGIVGRTGCGKSTLIqtlfRIV----EPAAGEIRIDG 1281
Cdd:PRK11650 4 LKLQAVRKSYDGKTQ-VIKGIDLDVADGEFIVLVGPSGCGKSTLL----RMVagleRITSGEIWIGG 65
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1250-1387 |
2.93e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.10 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1250 GIVGRTGCGKSTLIQTLFRIVEPAAGEIridginilsiglhDLRSRLSIIPQ----DptmFEGTIRSNLdpleeytdDQI 1325
Cdd:PRK13409 369 GIVGPNGIGKTTFAKLLAGVLKPDEGEV-------------DPELKISYKPQyikpD---YDGTVEDLL--------RSI 424
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30682479 1326 WEALDNCQLGDEVRKKeLKL----DSPVSEngqnWSVGQRQLVCLGRVLLKRSKLLVLDEATASID 1387
Cdd:PRK13409 425 TDDLGSSYYKSEIIKP-LQLerllDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
680-806 |
2.93e-03 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 40.97 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 680 VEENILFG----KPMEREWYDRVLEACSLNKDLeilpfhdqtvIGERGINLSGGQKQRIQIARALYQDADIYLFDDPF-- 753
Cdd:TIGR03410 92 VEENLLTGlaalPRRSRKIPDEIYELFPVLKEM----------LGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTeg 161
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30682479 754 ---SAVdahtgshlfKEV--LLGLLRHK---TVIYVTHQVEFLPE-ADLILVMKDGKITQAG 806
Cdd:TIGR03410 162 iqpSII---------KDIgrVIRRLRAEggmAILLVEQYLDFARElADRYYVMERGRVVASG 214
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
687-804 |
2.99e-03 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 41.33 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 687 GKPMERewYDRVLEACSLNKDLEILPFHD--QTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHL 764
Cdd:TIGR02769 112 GEPLRH--LTSLDESEQKARIAELLDMVGlrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVI 189
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 30682479 765 FKevLLGLLRHK---TVIYVTHQVEFLPE-ADLILVMKDGKITQ 804
Cdd:TIGR02769 190 LE--LLRKLQQAfgtAYLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1357-1429 |
3.02e-03 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 41.15 E-value: 3.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30682479 1357 SVGQRQLVCLGRVLLKRSKLLVLDEATASIDTATDNLIQETLR--HHFADCTVITIAHRISSVID-SDMVLLLDQG 1429
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDYALRyCERIVALRQG 229
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1358-1424 |
3.07e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.08 E-value: 3.07e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30682479 1358 VGQRQLVCLGRVLLKRSKLLVLDEATASI-DTATDNLIQ--ETLRHHfaDCTVITIAHR---ISSVIDSDMVL 1424
Cdd:NF040905 142 VGKQQLVEIAKALSKDVKLLILDEPTAALnEEDSAALLDllLELKAQ--GITSIIISHKlneIRRVADSITVL 212
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
725-813 |
3.09e-03 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 40.84 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 725 NLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHtgshlFKEVLLGLLR-----HKTVIYVTHQVEFLPE-ADLILVMK 798
Cdd:COG1134 146 TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAA-----FQKKCLARIRelresGRTVIFVSHSMGAVRRlCDRAIWLE 220
|
90
....*....|....*
gi 30682479 799 DGKITQAGKYHEILD 813
Cdd:COG1134 221 KGRLVMDGDPEEVIA 235
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
726-814 |
3.82e-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: 41.59 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 726 LSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGshlfKEV--LLGLLRHKT---VIYVTHQV----EFlpeADLILV 796
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQ----AQIldLLKDLQRELgmaLLLITHDLgvvrRF---ADRVAV 229
|
90
....*....|....*...
gi 30682479 797 MKDGKITQAGKYHEILDS 814
Cdd:COG4172 230 MRQGEIVEQGPTAELFAA 247
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
983-1110 |
3.91e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 41.01 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 983 RASMSFFDATPMGRILNRASTDqsVADLRlpgQFAYVAIAAI-----NILGIIGVIVQVAWQ---VLIVFIPVVAACAWY 1054
Cdd:cd18565 99 RLDMAFFEDRQTGDLMSVLNND--VNQLE---RFLDDGANSIirvvvTVLGIGAILFYLNWQlalVALLPVPLIIAGTYW 173
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 30682479 1055 RQyyisaaRELARLAGISRSPV---VHHFSETLSGITTIRSFDQEPRFRGDIMRLSDCY 1110
Cdd:cd18565 174 FQ------RRIEPRYRAVREAVgdlNARLENNLSGIAVIKAFTAEDFERERVADASEEY 226
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
616-803 |
4.01e-03 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 40.78 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 616 IPTLRDMNFKVSQGMNVAICGTVGSGKSSLLSSILGEVPKISGNLKVCGRKayiaqsPWIQSGKVEENI--LFGKPMERE 693
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV------PWKRRKKFLRRIgvVFGQKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 694 WYDRVLEACSLNKD-------------------LEILPFHDQTVigeRgiNLSGGQKQRIQIARALYQDADIYLFDDPFS 754
Cdd:cd03267 108 WDLPVIDSFYLLAAiydlpparfkkrldelselLDLEELLDTPV---R--QLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 30682479 755 AVDAHTgshlfKEVLLGLLR-----HKTVIYVT----HQVEFLpeADLILVMKDGKIT 803
Cdd:cd03267 183 GLDVVA-----QENIRNFLKeynreRGTTVLLTshymKDIEAL--ARRVLVIDKGRLL 233
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
715-810 |
5.32e-03 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 41.40 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 715 DQTVIGE---RGInlSGGQKQRIQIARALYQDADIYLFDDPFSAVDAhTGSHLFKEVLLGLL-RHKTVIYVTHQveflPE 790
Cdd:PLN03211 195 ENTIIGNsfiRGI--SGGERKRVSIAHEMLINPSLLILDEPTSGLDA-TAAYRLVLTLGSLAqKGKTIVTSMHQ----PS 267
|
90 100
....*....|....*....|....*.
gi 30682479 791 A------DLILVMKDGKITQAGKYHE 810
Cdd:PLN03211 268 SrvyqmfDSVLVLSEGRCLFFGKGSD 293
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
555-756 |
5.49e-03 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 41.27 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 555 IYKLPETISMIVQTKVSLNRIASFL--------CLDDLQQD-----VVGRLPSGSSE----MAVEISnGTFSWDDSS--- 614
Cdd:TIGR00954 376 LLKAADALGRLMLAGRDMTRLAGFTarvdtllqVLDDVKSGnfkrpRVEEIESGREGgrnsNLVPGR-GIVEYQDNGikf 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 615 ---PIPT------LRDMNFKVSQGMNVAICGTVGSGKSSLLSSILGEVPKISGNLKVC--GRKAYIAQSPWIQSGKVEEN 683
Cdd:TIGR00954 455 eniPLVTpngdvlIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPakGKLFYVPQRPYMTLGTLRDQ 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 684 ILFgkPMERE-WYDRVLEACSLNKDLEILPFHDqtvIGERGIN----------LSGGQKQRIQIARALYQDADIYLFDDP 752
Cdd:TIGR00954 535 IIY--PDSSEdMKRRGLSDKDLEQILDNVQLTH---ILEREGGwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDEC 609
|
....
gi 30682479 753 FSAV 756
Cdd:TIGR00954 610 TSAV 613
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1219-1281 |
6.08e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.92 E-value: 6.08e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30682479 1219 ITICNLQVRYGphLPMVLHGLTCTFPGGLKTGIVGRTGCGKSTLIQTLfrivepaAGEIRIDG 1281
Cdd:PRK10636 2 IVFSSLQIRRG--VRVLLDNATATINPGQKVGLVGKNGCGKSTLLALL-------KNEISADG 55
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1236-1451 |
6.49e-03 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 40.80 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1236 LHGLTctfpGGLKTG----IVGRTGCGKSTLIQTL-FRIvepaAGEIRIDG---INILSIGLHDLRSRLSIIPQD----P 1303
Cdd:TIGR00955 41 LKNVS----GVAKPGellaVMGSSGAGKTTLMNALaFRS----PKGVKGSGsvlLNGMPIDAKEMRAISAYVQQDdlfiP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1304 TMfegTIRSNLD-------PLEEYTD------DQIWEA--LDNCQ---LGDEVRKKELkldspvsengqnwSVGQRQLVC 1365
Cdd:TIGR00955 113 TL---TVREHLMfqahlrmPRRVTKKekrervDEVLQAlgLRKCAntrIGVPGRVKGL-------------SGGERKRLA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1366 LGRVLLKRSKLLVLDEATASIDTATDNLIQETLRhHFAD--CTVITIAHRISSVIDS--DMVLLLDQGLIKEHDSPARLL 1441
Cdd:TIGR00955 177 FASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLK-GLAQkgKTIICTIHQPSSELFElfDKIILMAEGRVAYLGSPDQAV 255
|
250
....*....|
gi 30682479 1442 EdrssLFSKL 1451
Cdd:TIGR00955 256 P----FFSDL 261
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
936-1111 |
6.85e-03 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 40.15 E-value: 6.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 936 SGFT-LILVYVLLAVASSFCILIRALLVAMTGFKMATELFTQMHLRIFRASMSFFDATPMGRILNRASTDQSVADLRLPG 1014
Cdd:cd18589 33 EAFTaAITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1015 QFAYVAIAAINILGIIGVIVQVAWQVLIVFI---PVVAACA-----WYRQYYISAARELARLAGISrspvvhhfSETLSG 1086
Cdd:cd18589 113 NLSLLMWYLARGLFLFIFMLWLSPKLALLTAlglPLLLLVPkfvgkFQQSLAVQVQKSLARANQVA--------VETFSA 184
|
170 180
....*....|....*....|....*....
gi 30682479 1087 ITTIRSFDQE----PRFRGdimRLSDCYS 1111
Cdd:cd18589 185 MKTVRSFANEegeaQRYRQ---RLQKTYR 210
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1250-1387 |
8.29e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 40.54 E-value: 8.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 1250 GIVGRTGCGKSTLIQTLFRIVEPAAGEIridginilsiglhDLRSRLSIIPQ----DptmFEGTIRSNL-DPLEEYTDDQ 1324
Cdd:COG1245 370 GIVGPNGIGKTTFAKILAGVLKPDEGEV-------------DEDLKISYKPQyispD---YDGTVEEFLrSANTDDFGSS 433
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30682479 1325 IWEAldncQLGDEVRKKELkLDSPVSEngqnWSVGQRQLVCLGRVLLKRSKLLVLDEATASID 1387
Cdd:COG1245 434 YYKT----EIIKPLGLEKL-LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
712-803 |
8.69e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.48 E-value: 8.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30682479 712 PFHdQTVIGergiNLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEVLLGLLRHKTVIYVTHQV-EFLPE 790
Cdd:PRK10982 383 PGH-RTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMpELLGI 457
|
90
....*....|...
gi 30682479 791 ADLILVMKDGKIT 803
Cdd:PRK10982 458 TDRILVMSNGLVA 470
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
727-757 |
9.93e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 40.46 E-value: 9.93e-03
10 20 30
....*....|....*....|....*....|.
gi 30682479 727 SGGQKQRIQIARALYQDADIYLFDDPFSAVD 757
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
|
| |
