|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
7-1429 |
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: 2843.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 7 CSADGSDPFWEWDVSWNTSNPDFTKCFQNTVLVWVPCCYLWLCFPFYFLYLSRHDRGYIQMTYLNKTKTALGFVLWIVCW 86
Cdd:TIGR00957 1 CSADGSDPLWDWNVTWHTSNPDFTKCFQNTVLAWVPCFYLWVCFPCYFLYLSRHDRGYIQMTHLNKTKTALGFLLWIVCW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 87 ADLFYSFWERSWGKILAPVFLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLIALLCALAILRSKIMTALKEDAE 166
Cdd:TIGR00957 81 ADLFYSFWERSHGRAPAPVFLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVALVCALAILRSKILLALKEDAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 167 IDVFRDVTFYIYFSLVLIQLVLSCFSDRPPLFSETIHDLNPCPESSASFLSRVTFWWITGLMVRGYRQPLESTDLWSLNK 246
Cdd:TIGR00957 161 VDPFRDTTFYIYFALVLSQLVLSCFSDKSPLFSETNHDPNPCPESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 247 EDTSEQVVPVLVKNWKKECAKSKRQQRKITYSSKDPAKPKGGSQVDVNEEAEVLIVKTPQKEREPSLFKVLYKTFGPYFL 326
Cdd:TIGR00957 241 EDTSEMVVPVLVENWKKECKKTRKQPVSAVYGKKDPSKPKGSSQLDANEEVEALIVKSPHKPRKPSLFKVLYKTFGPYFL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 327 MSFLFKALHDLMMFAGPEILKLLINFVNDKKAPDWQGYLYTALLFICACLQTLVLHQYFHICFVSGMRIKTAVIGAVYRK 406
Cdd:TIGR00957 321 MSFCFKAIHDLMMFIGPQILSLLIRFVNDPMAPDWQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 407 ALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMILMVPLNAVMAMK 486
Cdd:TIGR00957 401 ALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMK 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 487 TKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTFA 566
Cdd:TIGR00957 481 TKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 567 VYVTVDKNNILDAQKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRPVKDGGGaNSITV 646
Cdd:TIGR00957 561 VYVTVDENNILDAEKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGEG-NSITV 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 647 KNATFTWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGSVAYVPQQAWIQNDSLRENI 726
Cdd:TIGR00957 640 HNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENI 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 727 LFGRQLQERYYKAVIEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVGKHI 806
Cdd:TIGR00957 720 LFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 807 FENVIGPKGMLKNKTRLLVTHSISYLPQVDVIIVMTGGKISEMGSYQELLARDGAFAEFLRTYASGDQEQAEQDDGLTGV 886
Cdd:TIGR00957 800 FEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEQQGHLEDSWTALV 879
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 887 SSPGKEVKQMENGMLVTDVAGKQLQRQLSNSSSYSGDVSRHHTSTAELQKAGPKNEDaWKLVEADKAQTGQVKLSVYWDY 966
Cdd:TIGR00957 880 SGEGKEAKLIENGMLVTDVVGKQLQRQLSASSSDSGDQSRHHGSSAELQKAEAKEET-WKLMEADKAQTGQVELSVYWDY 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 967 MKAIGLFISFLSIFLFLCNHVASLVSNYWLSLWTDDPIVNGTQEHTKIRLSVYGALGISQGITVFGYSMAVSIGGIFASR 1046
Cdd:TIGR00957 959 MKAIGLFITFLSIFLFVCNHVSALASNYWLSLWTDDPMVNGTQNNTSLRLSVYGALGILQGFAVFGYSMAVSIGGIQASR 1038
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1047 RLHVDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFNVIGACIIILLATPIASIIIPPLGLIY 1126
Cdd:TIGR00957 1039 VLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLY 1118
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1127 FFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIVANRWLAVRLECV 1206
Cdd:TIGR00957 1119 FFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECV 1198
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1207 GNCIVLFAALFSVISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQEMAPPST 1286
Cdd:TIGR00957 1199 GNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSG 1278
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1287 WPQVGRVEFRDYGLRYRENLDLVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIGLHDL 1366
Cdd:TIGR00957 1279 WPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL 1358
|
1370 1380 1390 1400 1410 1420
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953392644 1367 RVKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSGLPDKLNQECAEGGEN 1429
Cdd:TIGR00957 1359 RFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGEN 1421
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
102-1429 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 913.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 102 LAPVFLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLIALLCALAILRSKIMTaLKedaeiDVFRDVTFYIYFSL 181
Cdd:PLN03130 107 LPPFEIVSLIVEALTWCSMLVMIGVETKIYIREFRWYVRFAVIYVLVGDAVMLNLVLS-VK-----EYYSSFVLYLYISE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 182 VLIQLVLSCF-----------SDRPPLFSETIHDL---------NPCPESSASFLSRVTFWWITGLMVRGYRQPLESTDL 241
Cdd:PLN03130 181 VAAQVLFGILllvyfpnldpyPGYTPIGSESVDDYeyeelpggeQICPERHANIFSRIFFGWMTPLMQLGYKRPLTEKDV 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 242 WSLNKEDTSEQVVPVLVKNWKKECAKSKrqqrkitysskdpakpkggsqvdvneeaevlivktpqkerePSLFKVLYKTF 321
Cdd:PLN03130 261 WKLDTWDQTETLYRSFQKCWDEELKKPK-----------------------------------------PWLLRALNNSL 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 322 GPYFLMSFLFKALHDLMMFAGPEILKLLINFVNdKKAPDWQGYLYTALLFICACLQTLVLHQYFHICFVSGMRIKTAVIG 401
Cdd:PLN03130 300 GGRFWLGGFFKIGNDLSQFVGPLLLNLLLESMQ-NGEPAWIGYIYAFSIFVGVVLGVLCEAQYFQNVMRVGFRLRSTLVA 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 402 AVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMILMVPLNA 481
Cdd:PLN03130 379 AVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLVLMFPIQT 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 482 VMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLAAVGTFTWVCTPFLVA 561
Cdd:PLN03130 459 FIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSFILNSIPVLVT 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 562 LSTFAVYVTVDKNniLDAQKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEE--LEPDSierrPVKDGG 639
Cdd:PLN03130 539 VVSFGVFTLLGGD--LTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLLAEErvLLPNP----PLEPGL 612
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 640 GAnsITVKNATFTW-ARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVE-GHVAIKGSVAYVPQQAWI 717
Cdd:PLN03130 613 PA--ISIKNGYFSWdSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGTVAYVPQVSWI 690
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 718 QNDSLRENILFGRQLQ-ERYYKAvIEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLS 796
Cdd:PLN03130 691 FNATVRDNILFGSPFDpERYERA-IDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLS 769
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 797 AVDAHVGKHIFENVIgpKGMLKNKTRLLVTHSISYLPQVDVIIVMTGGKISEMGSYQELLArDGAFAEFLRTYASGDQEQ 876
Cdd:PLN03130 770 ALDAHVGRQVFDKCI--KDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSN-NGPLFQKLMENAGKMEEY 846
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 877 AEQDDGltgVSSPGKEVKQMENGMLvtdvagkqlqRQLSNSSSYSGDvsrhhtstaelqkagpKNEDAWKLVEADKAQTG 956
Cdd:PLN03130 847 VEENGE---EEDDQTSSKPVANGNA----------NNLKKDSSSKKK----------------SKEGKSVLIKQEERETG 897
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 957 QVKLSVYWDYMKAIGLFisFLSIFLFLC---NHVASLVSNYWLSLWTDDpivNGTQEHTKI-RLSVYGALGISQGITVFG 1032
Cdd:PLN03130 898 VVSWKVLERYKNALGGA--WVVMILFLCyvlTEVFRVSSSTWLSEWTDQ---GTPKTHGPLfYNLIYALLSFGQVLVTLL 972
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1033 YSMAVSIGGIFASRRLHVDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFNVIGACIIILLAT 1112
Cdd:PLN03130 973 NSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVS 1052
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1113 PIASIIIPPLGLIYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPS 1192
Cdd:PLN03130 1053 TISLWAIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTLVN 1132
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1193 IVANRWLAVRLECVGNCIVLFAALFSVI-----SRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEY 1267
Cdd:PLN03130 1133 MSSNRWLAIRLETLGGLMIWLTASFAVMqngraENQAAFASTMGLLLSYALNITSLLTAVLRLASLAENSLNAVERVGTY 1212
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1268 SETEKEAPWQIQEMAPPSTWPQVGRVEFRDYGLRYRENLDLVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESA 1347
Cdd:PLN03130 1213 IDLPSEAPLVIENNRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELE 1292
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1348 EGEIIIDDINIAKIGLHDLRVKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSGLPDKLNQECAEGG 1427
Cdd:PLN03130 1293 RGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAG 1372
|
..
gi 1953392644 1428 EN 1429
Cdd:PLN03130 1373 EN 1374
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
206-1429 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 847.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 206 NPCPESSASFLSRVTFWWITGLMVRGYRQPLESTDLWSLNKEDTSEQVVpvlvknwkkecaksKRQQRKITYSSKDPakp 285
Cdd:PLN03232 225 NICPERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLI--------------KRFQRCWTEESRRP--- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 286 kggsqvdvneeaevlivktpqkerEPSLFKVLYKTFGPYFLMSFLFKALHDLMMFAGPEILKLLINFVNDKKaPDWQGYL 365
Cdd:PLN03232 288 ------------------------KPWLLRALNNSLGGRFWLGGIFKIGHDLSQFVGPVILSHLLQSMQEGD-PAWVGYV 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 366 YTALLFICACLQTLVLHQYFHICFVSGMRIKTAVIGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIW 445
Cdd:PLN03232 343 YAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLW 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 446 SAPLQVILALYLLWLNLGPSVLAGVAVMILMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFK 525
Cdd:PLN03232 423 SAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 526 DKVLAIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTFAVYVTVDKNniLDAQKAFVSLALFNILRFPLNILPMVISS 605
Cdd:PLN03232 503 SRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLVSFGVFVLLGGD--LTPARAFTSLSLFAVLRSPLNMLPNLLSQ 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 606 IVQASVSLKRLR-IFLSHEELEPDSIERRPvkdggGANSITVKNATFTW-ARSDPPTLSGITFSIPEGSLVAVVGQVGCG 683
Cdd:PLN03232 581 VVNANVSLQRIEeLLLSEERILAQNPPLQP-----GAPAISIKNGYFSWdSKTSKPTLSDINLEIPVGSLVAIVGGTGEG 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 684 KSSLLSALLAEMDKVE-GHVAIKGSVAYVPQQAWIQNDSLRENILFGRQLQ-ERYYKAvIEACALLPDLEILPSGDRTEI 761
Cdd:PLN03232 656 KTSLISAMLGELSHAEtSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFEsERYWRA-IDVTALQHDLDLLPGRDLTEI 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 762 GEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVGKHIFENVIgpKGMLKNKTRLLVTHSISYLPQVDVIIVM 841
Cdd:PLN03232 735 GERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCM--KDELKGKTRVLVTNQLHFLPLMDRIILV 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 842 TGGKISEMGSYQELLARDGAFAeflrtyasgdqeqaeqddgltgvsspgkevKQMENgmlvtdvAGKQLQRQLSNSSSYS 921
Cdd:PLN03232 813 SEGMIKEEGTFAELSKSGSLFK------------------------------KLMEN-------AGKMDATQEVNTNDEN 855
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 922 GDvsrHHTSTAEL----QKAGPKNEDAWK---LVEADKAQTGQVKLSVYWDYMKAIG-LFISFLSIFLFLCNHVASLVSN 993
Cdd:PLN03232 856 IL---KLGPTVTIdvseRNLGSTKQGKRGrsvLVKQEERETGIISWNVLMRYNKAVGgLWVVMILLVCYLTTEVLRVSSS 932
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 994 YWLSLWTDDPIVNGTQEHTKIrlSVYGALGISQGITVFGYSMAVSIGGIFASRRLHVDLLQNVLRSPMSFFERTPSGNLV 1073
Cdd:PLN03232 933 TWLSIWTDQSTPKSYSPGFYI--VVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVI 1010
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1074 NRFSKELDTVDSMIPQVIKMFMGSLFNVIGACIIILLATPIASIIIPPLGLIYFFVQRFYVASSRQLKRLESVSRSPVYS 1153
Cdd:PLN03232 1011 NRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYA 1090
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1154 HFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFSVI-----SRHSLSAG 1228
Cdd:PLN03232 1091 QFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLrngnaENQAGFAS 1170
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1229 LVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQEMAPPSTWPQVGRVEFRDYGLRYRENLDL 1308
Cdd:PLN03232 1171 TMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIENNRPVSGWPSRGSIKFEDVHLRYRPGLPP 1250
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1309 VLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIGLHDLRVKITIIPQDPVLFSGSLRMNL 1388
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI 1330
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|.
gi 1953392644 1389 DPFSQYSDEEVWTSLELAHLKDFVSGLPDKLNQECAEGGEN 1429
Cdd:PLN03232 1331 DPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGEN 1371
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
288-1429 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 661.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 288 GSQVDVNEeaevliVKTPqkeREPSLFKVLYKTFGPYFLMSFLFKALHDLMMFAGPEILKLLINFVNDKKAPDWQGYLYT 367
Cdd:PTZ00243 218 GSVVRPGP------PPTP---KRLSLLRTLFAALPYYVWWQIPFKLLSDVCTLTLPVLLKYFVKFLDADNATWGRGLGLV 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 368 ALLFICACLQTLVLHQYFHICFVSGMRIKTAVIGAVYRKALVITNS--ARKSSTVGEIVNLMSVDAQRFMDLATYINMIW 445
Cdd:PTZ00243 289 LTLFLTQLIQSVCLHRFYYISIRCGLQYRSALNALIFEKCFTISSKslAQPDMNTGRIINMMSTDVERINSFMQYCMYLW 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 446 SAPLQVILALYLLWLNLGPSVLAGVAVMILMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFK 525
Cdd:PTZ00243 369 SSPMVLLLSILLLSRLVGWCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFV 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 526 DKVLAIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTFAVYVTVdkNNILDAQKAFVSLALFNILRFPLNILPMVISS 605
Cdd:PTZ00243 449 ANIEDKRARELRYLRDVQLARVATSFVNNATPTLMIAVVFTVYYLL--GHELTPEVVFPTIALLGVLRMPFFMIPWVFTT 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 606 IVQASVSLKRLRIFLSHE--------ELEPDSIERRPVKDGGGANSI------------------TVKNATFTWA----- 654
Cdd:PTZ00243 527 VLQFLVSIKRISTFLECDnatcstvqDMEEYWREQREHSTACQLAAVlenvdvtafvpvklprapKVKTSLLSRAlrmlc 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 655 --------RSDPPT-------------------------------------------------------LSGITFSIPEG 671
Cdd:PTZ00243 607 ceqcrptkRHPSPSvvvedtdygspssasrhiveggtgggheatptsersaktpkmktddffelepkvlLRDVSVSVPRG 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 672 SLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGSVAYVPQQAWIQNDSLRENILFGRQLQERYYKAVIEACALLPDLE 751
Cdd:PTZ00243 687 KLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLA 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 752 ILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVGKHIFENVIgpKGMLKNKTRLLVTHSISY 831
Cdd:PTZ00243 767 QLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECF--LGALAGKTRVLATHQVHV 844
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 832 LPQVDVIIVMTGGKISEMGSYqellardgafAEFLRT--YASGDQEQAEQDDGLTGVSSPGKEVKQMENGMLVTdvAGKQ 909
Cdd:PTZ00243 845 VPRADYVVALGDGRVEFSGSS----------ADFMRTslYATLAAELKENKDSKEGDADAEVAEVDAAPGGAVD--HEPP 912
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 910 LQRQLSNSSSysGDVSRHHTSTAELqkagpknedawkLVEADKAqTGQVKLSVYWDYMKAIG-LFISFLSIFLFLCNHVA 988
Cdd:PTZ00243 913 VAKQEGNAEG--GDGAALDAAAGRL------------MTREEKA-SGSVPWSTYVAYLRFCGgLHAAGFVLATFAVTELV 977
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 989 SLVSNYWLSLWTddpiVNGTQEHTKIRLSVY------GALGISQGITVFGYSMAVsiggifASRRLHVDLLQNVLRSPMS 1062
Cdd:PTZ00243 978 TVSSGVWLSMWS----TRSFKLSAATYLYVYlgivllGTFSVPLRFFLSYEAMRR------GSRNMHRDLLRSVSRGTMS 1047
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1063 FFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFNVIGACIIILLATPIASIIIPPLGLIYFFVQRFYVASSRQLKR 1142
Cdd:PTZ00243 1048 FFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRR 1127
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1143 LESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFSVI-- 1220
Cdd:PTZ00243 1128 IKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIALIGVIgt 1207
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1221 ----SRHSLsaGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYS-ETEKEAPWQIQE----------MA--- 1282
Cdd:PTZ00243 1208 mlraTSQEI--GLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTdEVPHEDMPELDEevdalerrtgMAadv 1285
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1283 ----------PPSTWP---QVGRVEFRDYGLRYRENLDLVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEG 1349
Cdd:PTZ00243 1286 tgtvviepasPTSAAPhpvQAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGG 1365
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1350 EIIIDDINIAKIGLHDLRVKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSGLPDKLNQECAEGGEN 1429
Cdd:PTZ00243 1366 EIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSN 1445
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
975-1268 |
2.37e-169 |
|
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: 508.17 E-value: 2.37e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 975 SFLSIFLFLCNHVASLVSNYWLSLWTDDPIVNGTQ--EHTKIRLSVYGALGISQGITVFGYSMAVSIGGIFASRRLHVDL 1052
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSDDPALNGTQdtEQRDYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHNKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1053 LQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFNVIGACIIILLATPIASIIIPPLGLIYFFVQRF 1132
Cdd:cd18603 81 LHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1133 YVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVL 1212
Cdd:cd18603 161 YVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLIVL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1953392644 1213 FAALFSVISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYS 1268
Cdd:cd18603 241 FAALFAVLSRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEYS 296
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
328-616 |
8.83e-164 |
|
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: 493.14 E-value: 8.83e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 328 SFLFKALHDLMMFAGPEILKLLINFVNDKKAPDWQGYLYTALLFICACLQTLVLHQYFHICFVSGMRIKTAVIGAVYRKA 407
Cdd:cd18595 2 AALLKLLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 408 LVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMILMVPLNAVMAMKT 487
Cdd:cd18595 82 LRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 488 KTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTFAV 567
Cdd:cd18595 162 KKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFAT 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1953392644 568 YVTVDKNNILDAQKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 616
Cdd:cd18595 242 YVLSDPDNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
209-1427 |
5.69e-139 |
|
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: 464.38 E-value: 5.69e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 209 PESSASFLSRVTFWWITGLMVRGYRQPLESTDLWSLNKEDTSEQVVPVLVKNWKKECAKSKRQqrkitysskdpakpkgg 288
Cdd:TIGR01271 5 PVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELASAKKN----------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 289 sqvdvneeaevlivktpqkerePSLFKVLYKTFGPYFLMSFLFKALHDLMMFAGPEILKLLINFVNDKKAPDWQGYLYTA 368
Cdd:TIGR01271 68 ----------------------PKLLNALRRCFFWRFVFYGILLYFGEATKAVQPLLLGRIIASYDPFNAPEREIAYYLA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 369 ----LLFIcacLQTLVLHQYFHICFVSGMRIKTAVIGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMI 444
Cdd:TIGR01271 126 lglcLLFI---VRTLLLHPAIFGLHHLGMQMRIALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFV 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 445 WSAPLQVILALYLLWLNLGPSVLAGVAVMILMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAF 524
Cdd:TIGR01271 203 WIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAM 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 525 KDKVLAIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTFAVYVTVdKNNILdaQKAFVSLALFNILRFPLN-ILPMVI 603
Cdd:TIGR01271 283 EKIIKNIRQDELKLTRKIAYLRYFYSSAFFFSGFFVVFLSVVPYALI-KGIIL--RRIFTTISYCIVLRMTVTrQFPGAI 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 604 SSIVQASVSLKRLRIFLSHEElepdsieRRPVKDGGGANSITVKNATFTW----------------ARSDP--------- 658
Cdd:TIGR01271 360 QTWYDSLGAITKIQDFLCKEE-------YKTLEYNLTTTEVEMVNVTASWdegigelfekikqnnkARKQPngddglffs 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 659 -------PTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGSVAYVPQQAWIQNDSLRENILFGRQ 731
Cdd:TIGR01271 433 nfslyvtPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFGLS 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 732 LQERYYKAVIEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVGKHIFENVI 811
Cdd:TIGR01271 513 YDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCL 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 812 GPkgMLKNKTRLLVTHSISYLPQVDVIIVMTGGKISEMGSYQELLARDGAFAEFLRTYASGDQEQAEQ------------ 879
Cdd:TIGR01271 593 CK--LMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLLGLEAFDNFSAERrnsiltetlrrv 670
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 880 ---DDGLTGVSS---------PGKEVK-------------------------QMENGMLVTDVAGKQLQRQLS------- 915
Cdd:TIGR01271 671 sidGDSTVFSGPetikqsfkqPPPEFAekrkqsiilnpiasarkfsfvqmgpQKAQATTIEDAVREPSERKFSlvpedeq 750
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 916 ------------------------------NSSSYSGDVSRHHTSTAELQKAGPKNEDAWKL----------------VE 949
Cdd:TIGR01271 751 geeslprgnqyhhglqhqaqrrqsvlqlmtHSNRGENRREQLQTSFRKKSSITQQNELASELdiysrrlskdsvyeisEE 830
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 950 ADKAQTGQ--------VKLSVYWD-YMKAIG-----LFISFLSIFLFLCNHVASLVSnywLSLWTDDPIVNG--TQEHTK 1013
Cdd:TIGR01271 831 INEEDLKEcfaderenVFETTTWNtYLRYITtnrnlVFVLIFCLVIFLAEVAASLLG---LWLITDNPSAPNyvDQQHAN 907
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1014 IR--LSVYGALgISQGITVFGYSMAVSIG------GIF-----------ASRRLHVDLLQNVLRSPMSFFERTPSGNLVN 1074
Cdd:TIGR01271 908 ASspDVQKPVI-ITPTSAYYIFYIYVGTAdsvlalGFFrglplvhtlltVSKRLHEQMLHSVLQAPMAVLNTMKAGRILN 986
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1075 RFSKELDTVDSMIPQVIKMFMGSLFNVIGACIIILLATPIASIIIPPLGLIYFFVQRFYVASSRQLKRLESVSRSPVYSH 1154
Cdd:TIGR01271 987 RFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSH 1066
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1155 FNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIVANRWLAVRLECVgncIVLF--AALFSVISRHSLSAGLVGL 1232
Cdd:TIGR01271 1067 LITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDII---FVFFfiAVTFIAIGTNQDGEGEVGI 1143
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1233 SVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQEMAP--PST------------WPQVGRVEFRDY 1298
Cdd:TIGR01271 1144 ILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEPRPSGGGGKyqLSTvlvienphaqkcWPSGGQMDVQGL 1223
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1299 GLRYRENLDLVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRInESAEGEIIIDDINIAKIGLHDLRVKITIIPQDPV 1378
Cdd:TIGR01271 1224 TAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVF 1302
|
1370 1380 1390 1400
....*....|....*....|....*....|....*....|....*....
gi 1953392644 1379 LFSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSGLPDKLNQECAEGG 1427
Cdd:TIGR01271 1303 IFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGG 1351
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
327-616 |
2.12e-130 |
|
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: 404.67 E-value: 2.12e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 327 MSFLFKALHDLMMFAGPEILKLLINFVNDKKAPDWQGYLYTALLFICACLQTLVLHQYFHICFVSGMRIKTAVIGAVYRK 406
Cdd:cd18559 1 SFLLIKLVLCNHVFSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 407 ALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMILMVPLNAVMAMK 486
Cdd:cd18559 81 ALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 487 TKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTFA 566
Cdd:cd18559 161 SRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1953392644 567 VYVTVDKNNILDAQKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 616
Cdd:cd18559 241 AYVSRHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
975-1268 |
2.33e-125 |
|
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: 391.19 E-value: 2.33e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 975 SFLSIFLFLCNHVASLVSNYWLSLWTDDPiVNGTQEHTKIRLSVYGALGISQGITVFGYSMAVSIGGIFASRRLHVDLLQ 1054
Cdd:cd18559 1 SFLLIKLVLCNHVFSGPSNLWLLLWFDDP-VNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1055 NVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFNVIGACIIILLATPIASIIIpPLGLIYFFVQRFYV 1134
Cdd:cd18559 80 KALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGI-PLGLLYVPVNRVYA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1135 ASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDeNQKAYYPSIVANRWLAVRLECVGNCIVLFA 1214
Cdd:cd18559 159 ASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRD-NELAYLPSIVYLRALAVRLWCVGPCIVLFA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1953392644 1215 ALFSVISRHSLsAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYS 1268
Cdd:cd18559 238 SFFAYVSRHSL-AGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
644-845 |
2.36e-115 |
|
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: 360.25 E-value: 2.36e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWARSD---PPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGSVAYVPQQAWIQND 720
Cdd:cd03250 1 ISVEDASFTWDSGEqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 721 SLRENILFGRQLQERYYKAVIEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDA 800
Cdd:cd03250 81 TIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1953392644 801 HVGKHIFENVIGPKGMlKNKTRLLVTHSISYLPQVDVIIVMTGGK 845
Cdd:cd03250 161 HVGRHIFENCILGLLL-NNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
975-1268 |
5.11e-114 |
|
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: 360.28 E-value: 5.11e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 975 SFLSIFLFLCNHVASLVSNYWLSLWTDDpIVNGTQEHTKIRLSVYGALGI-SQGITVFGYSMAVSIGGIFASRRLHVDLL 1053
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSD-WSSSPNSSSGYYLGVYAALLVlASVLLVLLRWLLFVLAGLRASRRLHDKLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1054 QNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFNVIGACIIILLATPIASIIIPPLGLIYFFVQRFY 1133
Cdd:cd18580 80 RSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1134 VASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLF 1213
Cdd:cd18580 160 LRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALLALV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1953392644 1214 AALFSVISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYS 1268
Cdd:cd18580 240 VALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
328-616 |
1.37e-113 |
|
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: 359.11 E-value: 1.37e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 328 SFLFKALHDLMMFAGPEILKLLINFVNDKKAPD-WQGYLYTALLFICACLQTLVLHQYFHICFVSGMRIKTAVIGAVYRK 406
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPlSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 407 ALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMILMVPLNAVMAMK 486
Cdd:cd18579 82 ALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 487 TKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTFA 566
Cdd:cd18579 162 ISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1953392644 567 VYVTVDknNILDAQKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 616
Cdd:cd18579 242 TYVLLG--NPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
976-1268 |
6.29e-109 |
|
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: 346.38 E-value: 6.29e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 976 FLSIFLFLCNHVASLVSNYWLSLWTDDpivngtqehtKIRLS------VYGALGISQGITVFGYSMAVSIGGIFASRRLH 1049
Cdd:cd18606 2 PLLLLLLILSQFAQVFTNLWLSFWTED----------FFGLSqgfyigIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1050 VDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFNVIGACIIILLATPIASIIIPPLGLIYFFV 1129
Cdd:cd18606 72 NKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1130 QRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIVANRWLAVRLECVGNC 1209
Cdd:cd18606 152 ANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSL 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1953392644 1210 IVLFAALFSVISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYS 1268
Cdd:cd18606 232 LVLIVALLCVTRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHYA 290
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
976-1268 |
3.76e-91 |
|
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: 297.46 E-value: 3.76e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 976 FLSIFLFLCNHVASLVSNYWLSLWT---DDPIVNGTQEHTKIR-LSVYGALGISQGITVFGYSMAVSIGGIFASRRLHVD 1051
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIWAsayETSSALPPSEVSVLYyLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1052 LLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFNVIGACIIILLATPIASIIIPPLGLIYFFVQR 1131
Cdd:cd18604 82 LLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1132 FYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIV 1211
Cdd:cd18604 162 LYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALFS 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1953392644 1212 LFAALFsVISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYS 1268
Cdd:cd18604 242 FATAAL-LVYGPGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
976-1268 |
1.45e-87 |
|
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: 287.58 E-value: 1.45e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 976 FLSIFLFLCNHVASLVSNYWLSLWTDDPIVNGTQEHTKIR-----------LSVYGALGISQGITVFGYSMAVSIGGIFA 1044
Cdd:cd18602 2 ALVLALALLKQGLRVATDFWLADWTEANHDVASVVFNITSssleddevsyyISVYAGLSLGAVILSLVTNLAGELAGLRA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1045 SRRLHVDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFNVIGACIIILLATPIASIIIPPLGL 1124
Cdd:cd18602 82 ARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIII 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1125 IYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIVANRWLAVRLE 1204
Cdd:cd18602 162 VYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRLD 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953392644 1205 CVGNCIVLFAALFSVISRH--SLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYS 1268
Cdd:cd18602 242 YLGAVIVFLAALSSLTAALagYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEYT 307
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
973-1267 |
6.40e-85 |
|
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: 279.80 E-value: 6.40e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 973 FISFLsIFLFLCnHVASLVSNYWLSLWTD---DPIVNGTQEHTKIRLSVYGALGISQGITVFGYSMAVSIGGIFASRRLH 1049
Cdd:cd18605 1 LILIL-LSLILM-QASRNLIDFWLSYWVShsnNSFFNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1050 VDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFNVIGACIIILLATPIASIIIPPLGLIYFFV 1129
Cdd:cd18605 79 NKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1130 QRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIVANRWLAVRLECVGNC 1209
Cdd:cd18605 159 QRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGVL 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953392644 1210 IVLFAALFSVISRH---SLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEY 1267
Cdd:cd18605 239 IVTFVALTAVVQHFfglSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQY 299
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
307-873 |
1.28e-79 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 274.73 E-value: 1.28e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 307 KEREPSLFKVLYKTFGPY---FLMSFLFKALHDLMMFAGPEILKLLINFVNDKKapDWQG-YLYTALLFICACLQTLVLH 382
Cdd:COG1132 2 SKSPRKLLRRLLRYLRPYrglLILALLLLLLSALLELLLPLLLGRIIDALLAGG--DLSAlLLLLLLLLGLALLRALLSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 383 QYFHICFVSGMRIKTAVIGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMD-LATYINMIWSAPLQVILALYLLWLN 461
Cdd:COG1132 80 LQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQfLAHGLPQLVRSVVTLIGALVVLFVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 462 LGPSVLAGVAVMILMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYA---WELA-FKDKVLAIRQEELK 537
Cdd:COG1132 160 DWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGreeRELErFREANEELRRANLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 538 VLKKSAYLAAVGTFtwvctpfLVALSTFAVYVTVdknnILDAQK------AFVS-LALFNILRFPLNILPMVISSIVQAS 610
Cdd:COG1132 240 AARLSALFFPLMEL-------LGNLGLALVLLVG----GLLVLSgsltvgDLVAfILYLLRLFGPLRQLANVLNQLQRAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 611 VSLKRLRIFLSHEELEPDSIERRPVKDGGGAnsITVKNATFTWArSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSA 690
Cdd:COG1132 309 ASAERIFELLDEPPEIPDPPGAVPLPPVRGE--IEFENVSFSYP-GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 691 LLAEMDKVEGHVAIKG-------------SVAYVPQQAWIQNDSLRENILFGRQ---LQEryykaVIEACA---LLPDLE 751
Cdd:COG1132 386 LLRFYDPTSGRILIDGvdirdltleslrrQIGVVPQDTFLFSGTIRENIRYGRPdatDEE-----VEEAAKaaqAHEFIE 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 752 ILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRLLVTHSISY 831
Cdd:COG1132 461 ALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEAL---ERLMKGRTTIVIAHRLST 537
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1953392644 832 LPQVDVIIVMTGGKISEMGSYQELLARDGAFAEFLRTYASGD 873
Cdd:COG1132 538 IRNADRILVLDDGRIVEQGTHEELLARGGLYARLYRLQFGEE 579
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
329-616 |
5.85e-79 |
|
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: 263.20 E-value: 5.85e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 329 FLFKALHDLMMFAGPEILKLLINFV-NDKKAPDWQGYLYTALLFICACLQTLVLHQYFHICFVSGMRIKTAVIGAVYRKA 407
Cdd:cd18596 3 ALLAVLSSVLSFAPPFFLNRLLRYLeDPGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFEKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 408 LVITNSA-------------------RKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLA 468
Cdd:cd18596 83 LRRRDKSgssksseskkkdkeededeKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSALV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 469 GVAVMILMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLAAV 548
Cdd:cd18596 163 GLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLDLL 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953392644 549 GTFTWVCTPFLVALSTFAVYVTVDKNNiLDAQKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 616
Cdd:cd18596 243 LSLLWFLIPILVTVVTFATYTLVMGQE-LTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
330-616 |
6.65e-78 |
|
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: 259.41 E-value: 6.65e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 330 LFKALHDLMMFAGPEILKLLINFVNDKKAPDWQGYLYTALLFICACLQTLVLHQY-FHICFVSgMRIKTAVIGAVYRKAL 408
Cdd:cd18598 4 LLKLLADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGALLSSHYnFQMNKVS-LKVRAALVTAVYRKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 409 VITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMILMVPLNAVMAMKTK 488
Cdd:cd18598 83 RVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAKRIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 489 TYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTFAVY 568
Cdd:cd18598 163 ALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALCVYFWATTPVLISILTFATY 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1953392644 569 VTVdkNNILDAQKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 616
Cdd:cd18598 243 VLM--GNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
327-616 |
2.62e-76 |
|
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: 255.07 E-value: 2.62e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 327 MSFLFKALHDLMMFAGPEILKLLINFVNDKKA-----PDWQGYLYTALLFICACLQTLVLHQYFHICFVSGMRIKTAVIG 401
Cdd:cd18597 1 LAGLLKLLADVLQVLSPLLLKYLINFVEDAYLggpppSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 402 AVYRKALVITNSARKSSTVGEIVNLMSVDAQRfMDLA-TYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMILMVPLN 480
Cdd:cd18597 81 AIYRKSLRLSGKSRHEFPNGKITNLMSTDLSR-IDFAlGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 481 AVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLAAVGTFTWVCTPFLV 560
Cdd:cd18597 160 GFLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1953392644 561 ALSTFAVYVTVdkNNILDAQKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 616
Cdd:cd18597 240 SMLSFITYYAT--GHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
976-1429 |
1.33e-73 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 257.40 E-value: 1.33e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 976 FLSIFLFLCNHVASLVSNYWLSLWTDDPIVNGTQEHTKIRLSVYGALGISQGITVFGYSMAVSIGGIFASRRLHVDLLQN 1055
Cdd:COG1132 24 ILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEH 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1056 VLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFNVIGACIIILLATPIASIIIPPLGLIYFFVQRFYVA 1135
Cdd:COG1132 104 LLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1136 SSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAA 1215
Cdd:COG1132 184 RLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1216 LFSV--ISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQEMAPPstwPQVGRV 1293
Cdd:COG1132 264 LVGGllVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPDPPGAVPLP---PVRGEI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1294 EFRDYGLRYRENlDLVLKHINITINGGEKVGIVGRTGAGKSSLT---LGLFRINesaEGEIIIDDINIAKIGLHDLRVKI 1370
Cdd:COG1132 341 EFENVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGKSTLVnllLRFYDPT---SGRILIDGVDIRDLTLESLRRQI 416
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953392644 1371 TIIPQDPVLFSGSLRMNL---DPfsQYSDEEVWTSLELAHLKDFVSGLPDKLNQECAEGGEN 1429
Cdd:COG1132 417 GVVPQDTFLFSGTIRENIrygRP--DATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVN 476
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1291-1429 |
7.67e-73 |
|
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: 242.01 E-value: 7.67e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1291 GRVEFRDYGLRYRENLDLVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIGLHDLRVKI 1370
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1953392644 1371 TIIPQDPVLFSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSGLPDKLNQECAEGGEN 1429
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGEN 139
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
971-1268 |
5.81e-72 |
|
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: 243.24 E-value: 5.81e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 971 GLFISFLSIFLFLCNHVASLVSNYWLSLW---TDDPIVNGTQEHTKIRLSVYGALGISQGITVFGYSMAVSI------GG 1041
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWlkqGSGNTTNNVDNSTVDSGNISDNPDLNFYQLVYGGSILVILllslirGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1042 IF------ASRRLHVDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFNVIGACIIILLATPIA 1115
Cdd:cd18599 81 VFvkvtlrASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1116 SIIIPPLGLIYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIVA 1195
Cdd:cd18599 161 LIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953392644 1196 NRWLAVRLECVGNCIVLFAALFSVISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYS 1268
Cdd:cd18599 241 MRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
330-616 |
1.50e-70 |
|
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: 239.06 E-value: 1.50e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 330 LFKALHDLMMFAGPEILKLLINFVNDKKAPDWQ------------------GYLYTALLFICACLQTLVLHQYFHICFVS 391
Cdd:cd18591 4 ILKLLGDLLGFVGPLCISGIVDYVEENTYSSSNstdklsvsyvtveeffsnGYVLAVILFLALLLQATFSQASYHIVIRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 392 GMRIKTAVIGAVYRKALVIT--NSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAG 469
Cdd:cd18591 84 GIRLKTALQAMIYEKALRLSswNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSALIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 470 VAVMILMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLAAVG 549
Cdd:cd18591 164 AALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYWSLM 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953392644 550 TFTWVCTPFLVALSTFAVYVTVDKNNiLDAQKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 616
Cdd:cd18591 244 TFLTQASPILVTLVTFGLYPYLEGEP-LTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
226-867 |
4.87e-67 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 241.66 E-value: 4.87e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 226 GLMVRGYRQPLESTDLWSLnkedtseqvvPVLVKnWKKE--CAKSKRQQRKITYSskDPAKpkGGSQVDVNEEAE----V 299
Cdd:COG2274 60 GLRARGVRLDLEELAELPL----------PAILH-WDGNhfVVLEGVDGDKVTIA--DPAT--GRRKLSLEEFAEswtgV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 300 LIVKTP-----QKEREPSLFKVLYKTFGPY---FLMSFLFKALHDLMMFAGPEILKLLINFVNDKKAPDWqGYLYTALLF 371
Cdd:COG2274 125 ALLLEPtpefdKRGEKPFGLRWFLRLLRRYrrlLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLST-LWVLAIGLL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 372 ICACLQTL--VLHQYF--HIcfvsGMRIKTAVIGAVYRKALVITNSARKSSTVGEIVNlmsvdaqRFMDLATYINMIWSA 447
Cdd:COG2274 204 LALLFEGLlrLLRSYLllRL----GQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLAS-------RFRDVESIREFLTGS 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 448 PLQVILAlyllwlnlGPSVLAGVAVM-----------ILMVPLNAVMA------MKTKTYQVAHMKSKDNRikLMNEILN 510
Cdd:COG2274 273 LLTALLD--------LLFVLIFLIVLffyspplalvvLLLIPLYVLLGllfqprLRRLSREESEASAKRQS--LLVETLR 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 511 GIKVLKLYA--------WELAFKDKVLAirqeELKVLKKSAYLAAVGTFtwvctpfLVALSTFAVYVT----VDKNNI-L 577
Cdd:COG2274 343 GIETIKALGaesrfrrrWENLLAKYLNA----RFKLRRLSNLLSTLSGL-------LQQLATVALLWLgaylVIDGQLtL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 578 DAQKAFVSLalfnILRF--PLNILPMVISSIVQASVSLKRLRIFLSH--EELEPDSIERRPVKDGgganSITVKNATFTW 653
Cdd:COG2274 412 GQLIAFNIL----SGRFlaPVAQLIGLLQRFQDAKIALERLDDILDLppEREEGRSKLSLPRLKG----DIELENVSFRY 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 654 ARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-------------SVAYVPQQAWIQND 720
Cdd:COG2274 484 PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlrqidpaslrrQIGVVLQDVFLFSG 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 721 SLRENILFGRQL--QERyykaVIEAC---ALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPL 795
Cdd:COG2274 564 TIRENITLGDPDatDEE----IIEAArlaGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEAT 639
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953392644 796 SAVDAHVGKHIFENVigpKGMLKNKTRLLVTHSISYLPQVDVIIVMTGGKISEMGSYQELLARDGAFAEFLR 867
Cdd:COG2274 640 SALDAETEAIILENL---RRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
644-844 |
2.66e-64 |
|
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: 217.58 E-value: 2.66e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWArSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHV-----------------AIKG 706
Cdd:cd03290 1 VQVTNGYFSWG-SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 707 SVAYVPQQAWIQNDSLRENILFGRQLQERYYKAVIEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYCDS 786
Cdd:cd03290 80 SVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953392644 787 DIYLFDDPLSAVDAHVGKHIFEnvigpKGMLK-----NKTRLLVTHSISYLPQVDVIIVMTGG 844
Cdd:cd03290 160 NIVFLDDPFSALDIHLSDHLMQ-----EGILKflqddKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
971-1268 |
3.07e-64 |
|
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: 221.04 E-value: 3.07e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 971 GLFISFLSIFLFLCNHVASLVSNYWLSLWTDDPIVNGTQEHT----------------KIRLSVYGALGISQGITVFGYS 1034
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWANLEEKLNDTTDRvqgenstnvdiedldrDFNLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1035 MAVSIGGIFASRRLHVDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFNVIGACIIILLATPI 1114
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1115 ASIIIPPLGLIYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIV 1194
Cdd:cd18601 161 VLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFLA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953392644 1195 ANRWLAVRLECVGNCIVLFAALFSVISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYS 1268
Cdd:cd18601 241 TSRWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEYS 314
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
343-616 |
4.20e-63 |
|
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: 217.12 E-value: 4.20e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 343 PEILKLLIN-FVNDKKAPDWQGYLYTALLFICACLQTLVLHQYFHICFVSGMRIKTAVIGAVYRKALVITNSARKSSTVG 421
Cdd:cd18594 17 PLLLGRLVAyFVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKKTLKLSSSALSKITTG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 422 EIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMILMVPLNAVMAMKTKTYQVAHMKSKDNR 501
Cdd:cd18594 97 HIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFAKYRRKTAGLTDER 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 502 IKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTFAVYVTVdkNNILDAQK 581
Cdd:cd18594 177 VKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPYVLT--GNTLTARK 254
|
250 260 270
....*....|....*....|....*....|....*.
gi 1953392644 582 AFVSLALFNILRFPLNI-LPMVISSIVQASVSLKRL 616
Cdd:cd18594 255 VFTVISLLNALRMTITRfFPESIQTLSESRVSLKRI 290
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
354-616 |
5.37e-59 |
|
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: 205.15 E-value: 5.37e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 354 NDKKAPDWQGYLYTALLFICACLQTLVLHQYFHICFVSGMRIKTAVIGAVYRKALVITNSARKSSTVGEIVNLMSVDAQR 433
Cdd:cd18593 30 NGSSISLTEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLIYRKALRLSQAALGKTTVGQIVNLLSNDVNR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 434 FMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMILMVPLNAVMAmktktYQVAHMKSK-----DNRIKLMNEI 508
Cdd:cd18593 110 FDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFG-----KLFSKLRRKtaartDKRIRIMNEI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 509 LNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLAAV-GTFTWVCTPfLVALSTFAVYVTVDknNILDAQKAFVSLA 587
Cdd:cd18593 185 INGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALnMGLFFVSSK-LILFLTFLAYILLG--NILTAERVFVTMA 261
|
250 260 270
....*....|....*....|....*....|
gi 1953392644 588 LFNILRFPLNI-LPMVISSIVQASVSLKRL 616
Cdd:cd18593 262 LYNAVRLTMTLfFPFAIQFGSELSVSIRRI 291
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
466-867 |
4.83e-57 |
|
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: 208.47 E-value: 4.83e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 466 VLAGVAVMILMVPLNAVMAMKTKTYQVAHMKSkDNRIKLMnEILNGIKVLKLY-AWElAFKDKVLAIRQEELKVLKKSAY 544
Cdd:COG4987 161 LALGLLLAGLLLPLLAARLGRRAGRRLAAARA-ALRARLT-DLLQGAAELAAYgALD-RALARLDAAEARLAAAQRRLAR 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 545 LAAVGTF-TWVCTPFLVALSTFAVYVTVDKNNILDAQKA---FVSLALFNILRfPLnilPMVISSIVQASVSLKRLRIFL 620
Cdd:COG4987 238 LSALAQAlLQLAAGLAVVAVLWLAAPLVAAGALSGPLLAllvLAALALFEALA-PL---PAAAQHLGRVRAAARRLNELL 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 621 SHEELEPDSIERRPVKDGGganSITVKNATFTWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEG 700
Cdd:COG4987 314 DAPPAVTEPAEPAPAPGGP---SLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSG 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 701 HVAIKG-------------SVAYVPQQAWIQNDSLRENILFGR------QLqeryyKAVIEACALLPDLEILPSGDRTEI 761
Cdd:COG4987 391 SITLGGvdlrdldeddlrrRIAVVPQRPHLFDTTLRENLRLARpdatdeEL-----WAALERVGLGDWLAALPDGLDTWL 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 762 GEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVGKHIFENVIGPkgmLKNKTRLLVTHSISYLPQVDVIIVM 841
Cdd:COG4987 466 GEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA---LAGRTVLLITHRLAGLERMDRILVL 542
|
410 420
....*....|....*....|....*.
gi 1953392644 842 TGGKISEMGSYQELLARDGAFAEFLR 867
Cdd:COG4987 543 EDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
619-860 |
1.81e-53 |
|
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: 197.67 E-value: 1.81e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 619 FLSHEELEPDSIERRPVKDGggANSITVKNATFTWArSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKV 698
Cdd:COG4988 314 LLDAPEPAAPAGTAPLPAAG--PPSIELEDVSFSYP-GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPY 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 699 EGHVAIKG-------------SVAYVPQQAWIQNDSLRENILFGR------QLQeryykAVIEACALLPDLEILPSGDRT 759
Cdd:COG4988 391 SGSILINGvdlsdldpaswrrQIAWVPQNPYLFAGTIRENLRLGRpdasdeELE-----AALEAAGLDEFVAALPDGLDT 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 760 EIGEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRLLVTHSISYLPQVDVII 839
Cdd:COG4988 466 PLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQAL---RRLAKGRTVILITHRLALLAQADRIL 542
|
250 260
....*....|....*....|.
gi 1953392644 840 VMTGGKISEMGSYQELLARDG 860
Cdd:COG4988 543 VLDDGRIVEQGTHEELLAKNG 563
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1044-1429 |
8.47e-53 |
|
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: 198.90 E-value: 8.47e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1044 ASRRLHVDLLQNVLRSPMSFFERTPSGNLVNRFSkELDTVDSMIP-QVIKMFMGSLFNVIGACIIILLATPIASI---II 1119
Cdd:COG2274 227 IDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTgSLLTALLDLLFVLIFLIVLFFYSPPLALVvllLI 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1120 PPLGLIYFFVQRFYVASSRQlkrlESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDE----NQKAYYPSIVA 1195
Cdd:COG2274 306 PLYVLLGLLFQPRLRRLSRE----ESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKylnaRFKLRRLSNLL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1196 NRWLAVrLECVGNCIVLFAALFSVISRHsLSAG-LVGlSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYSETEKEA 1274
Cdd:COG2274 382 STLSGL-LQQLATVALLWLGAYLVIDGQ-LTLGqLIA-FNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPER 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1275 PWQIQEMAPPstwPQVGRVEFRDYGLRYRENLDLVLKHINITINGGEKVGIVGRTGAGKSSLT---LGLFRINesaEGEI 1351
Cdd:COG2274 459 EEGRSKLSLP---RLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLkllLGLYEPT---SGRI 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1352 IIDDINIAKIGLHDLRVKITIIPQDPVLFSGSLRMNL---DPfsQYSDEEVWTSLELAHLKDFVSGLPDKLNQECAEGGE 1428
Cdd:COG2274 533 LIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItlgDP--DATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGS 610
|
.
gi 1953392644 1429 N 1429
Cdd:COG2274 611 N 611
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
976-1244 |
2.35e-52 |
|
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: 185.54 E-value: 2.35e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 976 FLSIFLFLCNHVASLVSNYWLSLWTDDPIVNGTQE--HTKIRLSVYGALGISQGITVFGYSMAVSIGGIFASRRLHVDLL 1053
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLGRILDVLLPDGDPEtqALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1054 QNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFNVIGACIIILLATPIASIIIPPLGLIYFFVQRFY 1133
Cdd:pfam00664 82 KKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1134 VASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLF 1213
Cdd:pfam00664 162 AKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYAL 241
|
250 260 270
....*....|....*....|....*....|...
gi 1953392644 1214 AALFSV--ISRHSLSAGLVGLSVSYSLQVTTYL 1244
Cdd:pfam00664 242 ALWFGAylVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
340-616 |
1.68e-51 |
|
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: 183.53 E-value: 1.68e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 340 FAGPEIL-KLLINFVNDKKAPDWQGYLYTALLFICACLQTLVLHQYFHICFVSGMRIKTAVIGAVYRKALVITNSARKSs 418
Cdd:cd18592 14 FIGPTILiRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYKKILRLRSLGDKS- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 419 tVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMILMVPLNAVMAMKTKTYQVAHMKSK 498
Cdd:cd18592 93 -VGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAKLTGKFRRKAIVIT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 499 DNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLAAVGTftwVCTPFLVALS---TFAVYVTVDKNn 575
Cdd:cd18592 172 DKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISI---SLAPIVPVIAsvvTFLAHVALGND- 247
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1953392644 576 iLDAQKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 616
Cdd:cd18592 248 -LTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
659-879 |
1.07e-50 |
|
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: 181.21 E-value: 1.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 659 PTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGSVAYVPQQAWIQNDSLRENILFGRQLQERYYK 738
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 739 AVIEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVGKHIFENVIGPkgMLK 818
Cdd:cd03291 131 SVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCK--LMA 208
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953392644 819 NKTRLLVTHSISYLPQVDVIIVMTGGKISEMGSYQELLARDGAFAEFLRTYASGDQEQAEQ 879
Cdd:cd03291 209 NKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLMGYDTFDQFSAER 269
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1287-1406 |
1.11e-50 |
|
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: 177.99 E-value: 1.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1287 WPQVGRVEFRDYGLRYRENLDLVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIGLHDL 1366
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1953392644 1367 RVKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWTSLELA 1406
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALRVS 120
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
644-864 |
3.91e-48 |
|
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: 172.03 E-value: 3.91e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWarsDP--PTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-------------SV 708
Cdd:cd03253 1 IEFENVTFAY---DPgrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 709 AYVPQQAWIQNDSLRENILFGR--QLQERYYKAViEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYCDS 786
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRYGRpdATDEEVIEAA-KAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953392644 787 DIYLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRLLVTHSISYLPQVDVIIVMTGGKISEMGSYQELLARDGAFAE 864
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAAL---RDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAE 231
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
644-864 |
2.33e-45 |
|
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: 163.94 E-value: 2.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-------------SVAY 710
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlaslrrQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 711 VPQQAWIQNDSLRENILFGRQLQERyyKAVIEAC--ALLPDL-EILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYCDSD 787
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATR--EEVEEAAraANAHEFiMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953392644 788 IYLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRLLVTHSISYLPQVDVIIVMTGGKISEMGSYQELLARDGAFAE 864
Cdd:cd03251 159 ILILDEATSALDTESERLVQAAL---ERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAK 232
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1291-1429 |
2.83e-44 |
|
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: 161.62 E-value: 2.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1291 GRVEFRDYGLRYRENLDLVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIGLHDLRVKI 1370
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1953392644 1371 TIIPQDPVLFSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSGLPDKLNQECAEGGEN 1429
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGEN 156
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
644-845 |
3.12e-43 |
|
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: 155.23 E-value: 3.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-------------SVAY 710
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 711 VPQQAWIQNDSLRENILfgrqlqeryykavieacallpdleilpsgdrteigekgvnlSGGQKQRVSLARAVYCDSDIYL 790
Cdd:cd03228 81 VPQDPFLFSGTIRENIL-----------------------------------------SGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1953392644 791 FDDPLSAVDAHVGKHIFENVigpKGMLKNKTRLLVTHSISYLPQVDVIIVMTGGK 845
Cdd:cd03228 120 LDEATSALDPETEALILEAL---RALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
644-860 |
4.01e-42 |
|
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: 154.31 E-value: 4.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWaRSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-------------SVAY 710
Cdd:cd03254 3 IEFENVNFSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 711 VPQQAWIQNDSLRENILFGRQLQERyyKAVIEACALL-PDLEI--LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYCDSD 787
Cdd:cd03254 82 VLQDTFLFSGTIMENIRLGRPNATD--EEVIEAAKEAgAHDFImkLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953392644 788 IYLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRLLVTHSISYLPQVDVIIVMTGGKISEMGSYQELLARDG 860
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEAL---EKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
644-867 |
5.48e-42 |
|
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: 154.23 E-value: 5.48e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTW-ARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGS-------------VA 709
Cdd:cd03249 1 IEFKNVSFRYpSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrsqIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 710 YVPQQAWIQNDSLRENILFGRQlqERYYKAVIEAC--ALLPD-LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYCDS 786
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKP--DATDEEVEEAAkkANIHDfIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 787 DIYLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRLLVTHSISYLPQVDVIIVMTGGKISEMGSYQELLARDGAFAEFL 866
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEAL---DRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLV 235
|
.
gi 1953392644 867 R 867
Cdd:cd03249 236 K 236
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
325-596 |
1.04e-40 |
|
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: 152.03 E-value: 1.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 325 FLMSFLFKALHDLMMFAGPEILKLLINFVNDKKAPDWQ-GYLYTALLFICACLQTLVLHQYFHICFVSGMRIKTAVIGAV 403
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQaLNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 404 YRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSV-LAGVAVMILMVPLNAV 482
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLtLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 483 MAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKV-LKKSAYLAAVGTFTWVCTPFLVA 561
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAgIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....*
gi 1953392644 562 LSTFAVYVTVDKNNiLDAQKAFVSLALFNILRFPL 596
Cdd:pfam00664 241 LALWFGAYLVISGE-LSVGDLVAFLSLFAQLFGPL 274
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
465-841 |
2.51e-39 |
|
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: 154.75 E-value: 2.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 465 SVLAGVaVMILMVPLNAV-MA---MKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAI----RQEEL 536
Cdd:TIGR02857 143 DWISGL-ILLLTAPLIPIfMIligWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSseeyRERTM 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 537 KVLKKSAYLAAVgtftwvcTPFLVALSTFAVYVTVDKNNI---LDAQKAFVSLALFNILRFPLNILPMVISSIVQASVSL 613
Cdd:TIGR02857 222 RVLRIAFLSSAV-------LELFATLSVALVAVYIGFRLLagdLDLATGLFVLLLAPEFYLPLRQLGAQYHARADGVAAA 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 614 KRLRIFLSHEELEpdSIERRPVkDGGGANSITVKNATFTWARSDPpTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLA 693
Cdd:TIGR02857 295 EALFAVLDAAPRP--LAGKAPV-TAAPASSLEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLG 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 694 EMDKVEGHVAIKG-------------SVAYVPQQAWIQNDSLRENILFGR------QLQEryykaVIEACALLPDLEILP 754
Cdd:TIGR02857 371 FVDPTEGSIAVNGvpladadadswrdQIAWVPQHPFLFAGTIAENIRLARpdasdaEIRE-----ALERAGLDEFVAALP 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 755 SGDRTEIGEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRLLVTHSISYLPQ 834
Cdd:TIGR02857 446 QGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEAL---RALAQGRTVLLVTHRLALAAL 522
|
....*..
gi 1953392644 835 VDVIIVM 841
Cdd:TIGR02857 523 ADRIVVL 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
643-846 |
2.82e-39 |
|
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: 145.81 E-value: 2.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 643 SITVKNATFTWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-------------SVA 709
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 710 YVPQQAWIQNDSLRENILFGRQL--QERYYKAViEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYCDSD 787
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGAPLadDERILRAA-ELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1953392644 788 IYLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRLLVTHSISYLPQVDVIIVMTGGKI 846
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERL---RQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1022-1429 |
4.48e-39 |
|
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: 154.87 E-value: 4.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1022 LGISQGITVFGYSMAVSIGGIFASRRLHVDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFNV 1101
Cdd:TIGR02203 63 LAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1102 IGACIIIL-LATPIASIIIPPLGLIYFFVQRFyvasSRQLKRLES---VSRSPVYSHFNETLLGVSVIRAF----EEQER 1173
Cdd:TIGR02203 143 IGLFIVLLyYSWQLTLIVVVMLPVLSILMRRV----SKRLRRISKeiqNSMGQVTTVAEETLQGYRVVKLFggqaYETRR 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1174 F------IRQSDLKVDENQKAYYPSI--VANRWLAVrlecvgnciVLFAALFSVISRHSLSAGLVGLSVSySLQVTTYLN 1245
Cdd:TIGR02203 219 FdavsnrNRRLAMKMTSAGSISSPITqlIASLALAV---------VLFIALFQAQAGSLTAGDFTAFITA-MIALIRPLK 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1246 WLVRMSSEMETNIVAVERLKEYSETEKEApwQIQEMAPPSTwpqVGRVEFRDYGLRYRENLDLVLKHINITINGGEKVGI 1325
Cdd:TIGR02203 289 SLTNVNAPMQRGLAAAESLFTLLDSPPEK--DTGTRAIERA---RGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVAL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1326 VGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIGLHDLRVKITIIPQDPVLFSGSLRMNL---DPfSQYSDEEVWTS 1402
Cdd:TIGR02203 364 VGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRT-EQADRAEIERA 442
|
410 420
....*....|....*....|....*..
gi 1953392644 1403 LELAHLKDFVSGLPDKLNQECAEGGEN 1429
Cdd:TIGR02203 443 LAAAYAQDFVDKLPLGLDTPIGENGVL 469
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
644-867 |
2.49e-36 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 146.70 E-value: 2.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-------------SVAY 710
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrdytlaslrnQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 711 VPQQAWIQNDSLRENILFGRQlqERYYKAVIEACALLPD----LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYCDS 786
Cdd:PRK11176 422 VSQNVHLFNDTIANNIAYART--EQYSREQIEEAARMAYamdfINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 787 DIYLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRLLVTHSISYLPQVDVIIVMTGGKISEMGSYQELLARDGAFAEFL 866
Cdd:PRK11176 500 PILILDEATSALDTESERAIQAAL---DELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLH 576
|
.
gi 1953392644 867 R 867
Cdd:PRK11176 577 K 577
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
619-867 |
5.29e-36 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 145.76 E-value: 5.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 619 FLSHEELEPDSIERRPvkDGGGANSITVKNATFTWArsDPPTLSG-ITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMdK 697
Cdd:PRK11174 327 FLETPLAHPQQGEKEL--ASNDPVTIEAEDLEILSP--DGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-P 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 698 VEGHVAIKG------SVAYVPQQ-AWI-QN-----DSLRENILFGR-QLQERYYKAVIEACALLPDLEILPSGDRTEIGE 763
Cdd:PRK11174 402 YQGSLKINGielrelDPESWRKHlSWVgQNpqlphGTLRDNVLLGNpDASDEQLQQALENAWVSEFLPLLPQGLDTPIGD 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 764 KGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRLLVTHSISYLPQVDVIIVMTG 843
Cdd:PRK11174 482 QAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQAL---NAASRRQTTLMVTHQLEDLAQWDQIWVMQD 558
|
250 260
....*....|....*....|....
gi 1953392644 844 GKISEMGSYQELLARDGAFAEFLR 867
Cdd:PRK11174 559 GQIVQQGDYAELSQAGGLFATLLA 582
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
644-863 |
7.46e-35 |
|
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: 133.77 E-value: 7.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-------------SVAY 710
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 711 VPQQAWIQNDSLRENILFGRQLQERyyKAVIEACALLPDLEI---LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYCDSD 787
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSM--ERVIEAAKLAGAHDFiseLPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953392644 788 IYLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRLLVTHSISYLPQVDVIIVMTGGKISEMGSYQELLARDGAFA 863
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNM---HDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYA 231
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
376-828 |
9.82e-35 |
|
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: 140.96 E-value: 9.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 376 LQTLVLHqyfHICFvsgmRIKTAVIGAVYRKALVITNSARKSSTVGEIVNLMS--VDAQRFMDLATYINMIWSAPLQVIL 453
Cdd:TIGR02868 72 LERLVGH---DAAL----RSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGadVDALQDLYVRVIVPAGVALVVGAAA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 454 ALYLLWLN--LGPSVLAGVAVMILMVPLNAVMAMKTKTYQVAHMKSKDNRiKLMnEILNGIKVLKLYAWELAFKDKVLAI 531
Cdd:TIGR02868 145 VAAIAVLSvpAALILAAGLLLAGFVAPLVSLRAARAAEQALARLRGELAA-QLT-DALDGAAELVASGALPAALAQVEEA 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 532 RQEELKVLKKSAYLAAVGT--FTWVCTpfLVALSTFAVYVTVDKNNILDAQK----AFVSLALFNilrfPLNILPMVISS 605
Cdd:TIGR02868 223 DRELTRAERRAAAATALGAalTLLAAG--LAVLGALWAGGPAVADGRLAPVTlavlVLLPLAAFE----AFAALPAAAQQ 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 606 IVQASVSLKRLRIFLSHEELEPDSIERRPVKDGGGANSITVKNATFTWArSDPPTLSGITFSIPEGSLVAVVGQVGCGKS 685
Cdd:TIGR02868 297 LTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYP-GAPPVLDGVSLDLPPGERVAILGPSGSGKS 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 686 SLLSALLAEMDKVEGHVAIKGS-------------VAYVPQQAWIQNDSLRENILFGR-QLQERYYKAVIEACALLPDLE 751
Cdd:TIGR02868 376 TLLATLAGLLDPLQGEVTLDGVpvssldqdevrrrVSVCAQDAHLFDTTVRENLRLARpDATDEELWAALERVGLADWLR 455
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953392644 752 ILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVGKHIFENVIGPkgmLKNKTRLLVTHS 828
Cdd:TIGR02868 456 ALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAA---LSGRTVVLITHH 529
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1040-1427 |
2.06e-34 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 142.17 E-value: 2.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1040 GGIF------ASRRLHVDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFNVIGACIIILLATP 1113
Cdd:TIGR00958 222 GGSFnytmarINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSP 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1114 IASII----IPPLGLIYFFVQRFYVASSRQLKrlESVSRSPVYSHfnETLLGVSVIRAF--EEQE--RFIRQSDLKVDEN 1185
Cdd:TIGR00958 302 RLTMVtlinLPLVFLAEKVFGKRYQLLSEELQ--EAVAKANQVAE--EALSGMRTVRSFaaEEGEasRFKEALEETLQLN 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1186 QK---AYYPSIVANRWLAVRLECvgncIVLFAALFSVISRHSLSAGLVGLsVSYSLQVTTYLNWLVRMSSEMETNIVAVE 1262
Cdd:TIGR00958 378 KRkalAYAGYLWTTSVLGMLIQV----LVLYYGGQLVLTGKVSSGNLVSF-LLYQEQLGEAVRVLSYVYSGMMQAVGASE 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1263 RLKEYSETEKEAPwQIQEMAPPstwPQVGRVEFRDYGLRY--RENLdLVLKHINITINGGEKVGIVGRTGAGKSSLTLGL 1340
Cdd:TIGR00958 453 KVFEYLDRKPNIP-LTGTLAPL---NLEGLIEFQDVSFSYpnRPDV-PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALL 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1341 FRINESAEGEIIIDDINIAKIGLHDLRVKITIIPQDPVLFSGSLRMNLD-PFSQYSDEEVWTSLELAHLKDFVSGLPDKL 1419
Cdd:TIGR00958 528 QNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAyGLTDTPDEEIMAAAKAANAHDFIMEFPNGY 607
|
....*...
gi 1953392644 1420 NQECAEGG 1427
Cdd:TIGR00958 608 DTEVGEKG 615
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
595-881 |
2.60e-34 |
|
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: 140.73 E-value: 2.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 595 PLNILPMVISSIVQASVSLKRLriF-LSHEELEP-DSIERRPVKDGGGAnsITVKNATFTWarsDP--PTLSGITFSIPE 670
Cdd:COG5265 311 PLNFLGFVYREIRQALADMERM--FdLLDQPPEVaDAPDAPPLVVGGGE--VRFENVSFGY---DPerPILKGVSFEVPA 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 671 GSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-------------SVAYVPQQAWIQNDSLRENILFGR-QLQERY 736
Cdd:COG5265 384 GKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdirdvtqaslraAIGIVPQDTVLFNDTIAYNIAYGRpDASEEE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 737 YKAVIEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVGKHIFENVigpKGM 816
Cdd:COG5265 464 VEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAAL---REV 540
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953392644 817 LKNKTRLLVTHSISYLPQVDVIIVMTGGKISEMGSYQELLARDGAFAEFLRTYASGDQEQAEQDD 881
Cdd:COG5265 541 ARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEAEEALAA 605
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
596-882 |
3.95e-34 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 139.85 E-value: 3.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 596 LNILPMV----ISSIVQ-ASVSLKRLRIFLSHEELEPDSIErrPVKDGGGANSITVKnaTFTWARSDPPTLSGITFSIPE 670
Cdd:PRK10789 265 LMIWPMLalawMFNIVErGSAAYSRIRAMLAEAPVVKDGSE--PVPEGRGELDVNIR--QFTYPQTDHPALENVNFTLKP 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 671 GSLVAVVGQVGCGKSSLLSALLAEMDKVEGHV-------------AIKGSVAYVPQQAWIQNDSLRENILFGR--QLQER 735
Cdd:PRK10789 341 GQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIrfhdipltklqldSWRSRLAVVSQTPFLFSDTVANNIALGRpdATQQE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 736 yykavIEACALLP----DLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVGKHIFENVi 811
Cdd:PRK10789 421 -----IEHVARLAsvhdDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNL- 494
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953392644 812 gpKGMLKNKTRLLVTHSISYLPQVDVIIVMTGGKISEMGSYQELLARDGAFAEFLRtYasgDQEQAEQDDG 882
Cdd:PRK10789 495 --RQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYR-Y---QQLEAALDDA 559
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
582-879 |
4.51e-33 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 136.63 E-value: 4.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 582 AFVSLALFNILRfplniLPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRPVKDGGG-ANSITVKNATFTWARSdPPT 660
Cdd:PRK13657 277 AFVGFATLLIGR-----LDQVVAFINQVFMAAPKLEEFFEVEDAVPDVRDPPGAIDLGRvKGAVEFDDVSFSYDNS-RQG 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-------------SVAYVPQQAWIQNDSLRENIL 727
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdirtvtraslrrNIAVVFQDAGLFNRSIEDNIR 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 728 FGRQ--LQERYYKAViEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVG-- 803
Cdd:PRK13657 431 VGRPdaTDEEMRAAA-ERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEak 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 804 -KHIFENVigpkgmLKNKTRLLVTHSISYLPQVDVIIVMTGGKISEMGSYQELLARDGAFAEFLRtyASG---DQEQAEQ 879
Cdd:PRK13657 510 vKAALDEL------MKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLR--AQGmlqEDERRKQ 581
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
643-867 |
4.52e-33 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 136.49 E-value: 4.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 643 SITVKNATFTWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-------------SVA 709
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGqpiadyseaalrqAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 710 YVPQQAWIQNDSLRENILFGR------QLQERYYKAVIEAcaLLPDLEILpsgdRTEIGEKGVNLSGGQKQRVSLARAVY 783
Cdd:PRK11160 418 VVSQRVHLFSATLRDNLLLAApnasdeALIEVLQQVGLEK--LLEDDKGL----NAWLGEGGRQLSGGEQRRLGIARALL 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 784 CDSDIYLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRLLVTHSISYLPQVDVIIVMTGGKISEMGSYQELLARDGAFA 863
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDAETERQILELL---AEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYY 568
|
....
gi 1953392644 864 EFLR 867
Cdd:PRK11160 569 QLKQ 572
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
643-851 |
3.85e-32 |
|
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: 125.30 E-value: 3.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 643 SITVKNATFTWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-------------SVA 709
Cdd:cd03244 2 DIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 710 YVPQQAWIQNDSLRENI-LFGRQLQERYYKAvIEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYCDSDI 788
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLdPFGEYSDEELWQA-LERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953392644 789 YLFDDPLSAVDAHVGKHIFEnVIgpKGMLKNKTRLLVTHSISYLPQVDVIIVMTGGKISEMGS 851
Cdd:cd03244 161 LVLDEATASVDPETDALIQK-TI--REAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1291-1429 |
5.25e-32 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 125.42 E-value: 5.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1291 GRVEFRDYGLRYRENlDLVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIGLHDLRVKI 1370
Cdd:cd03254 1 GEIEFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1371 TIIPQDPVLFSGSLRMNLDPFSQYSDEEVWT-SLELAHLKDFVSGLPDKLNQECAEGGEN 1429
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIeAAKEAGAHDFIMKLPNGYDTVLGENGGN 139
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
643-864 |
9.27e-32 |
|
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: 134.10 E-value: 9.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 643 SITVKNATFTWARSDPpTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHV-------------AIKGSVA 709
Cdd:TIGR01193 473 DIVINDVSYSYGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEIllngfslkdidrhTLRQFIN 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 710 YVPQQAWIQNDSLRENILFG--RQLQERYYKAVIEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYCDSD 787
Cdd:TIGR01193 552 YLPQEPYIFSGSILENLLLGakENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSK 631
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953392644 788 IYLFDDPLSAVDAHVGKHIFENVIGpkgmLKNKTRLLVTHSISYLPQVDVIIVMTGGKISEMGSYQELLARDGAFAE 864
Cdd:TIGR01193 632 VLILDESTSNLDTITEKKIVNNLLN----LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYAS 704
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
644-869 |
7.47e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 122.51 E-value: 7.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFtwARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG--------SVAYVPQQA 715
Cdd:COG1121 7 IELENLTV--SYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkpprrarrRIGYVPQRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 716 WIQND---SLRENILFGRQ--------LQERYYKAVIEAcalLPDLEILPSGDRTeIGEkgvnLSGGQKQRVSLARAVYC 784
Cdd:COG1121 85 EVDWDfpiTVRDVVLMGRYgrrglfrrPSRADREAVDEA---LERVGLEDLADRP-IGE----LSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 785 DSDIYLFDDPLSAVDAHVGKHIFEnvigpkgMLK-----NKTRLLVTHSISYLPQ-VDVIIVMTGGKISEmGSYQELLAR 858
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYE-------LLRelrreGKTILVVTHDLGAVREyFDRVLLLNRGLVAH-GPPEEVLTP 228
|
250
....*....|.
gi 1953392644 859 DgafaEFLRTY 869
Cdd:COG1121 229 E----NLSRAY 235
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1046-1429 |
2.12e-30 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 128.68 E-value: 2.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1046 RRLHVDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLfNVIGACIIILLATP-----IASIIIP 1120
Cdd:PRK10790 98 QQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSA-ALIGAMLVAMFSLDwrmalVAIMIFP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1121 PLGLIYFFVQRFyvaSSRQLKRLESVsRSPVYSHFNETLLGVSVIRAFEEQERFIRqsdlKVDENQKAYYPSivanRWLA 1200
Cdd:PRK10790 177 AVLVVMVIYQRY---STPIVRRVRAY-LADINDGFNEVINGMSVIQQFRQQARFGE----RMGEASRSHYMA----RMQT 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1201 VRLECVgncivLFAALFSVISRHSL----------SAGLVGLSVSYSlqvttYLNWLVRMS----------SEMETNIVA 1260
Cdd:PRK10790 245 LRLDGF-----LLRPLLSLFSALILcgllmlfgfsASGTIEVGVLYA-----FISYLGRLNeplielttqqSMLQQAVVA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1261 VERLKEYSETEKeapwqiQEMAPPSTWPQVGRVEFRDYGLRYRENlDLVLKHINITINGGEKVGIVGRTGAGKSSLTLGL 1340
Cdd:PRK10790 315 GERVFELMDGPR------QQYGNDDRPLQSGRIDIDNVSFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1341 FRINESAEGEIIIDDINIAKIGLHDLRVKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSGLPDKLN 1420
Cdd:PRK10790 388 MGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLY 467
|
....*....
gi 1953392644 1421 QECAEGGEN 1429
Cdd:PRK10790 468 TPLGEQGNN 476
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1021-1427 |
8.49e-30 |
|
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: 125.94 E-value: 8.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1021 ALGISQGitVFGY-SMAVSIGGIFAS-RRLHVDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIkmfmgsl 1098
Cdd:TIGR02868 61 AFGIGRA--VFRYlERLVGHDAALRSlGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVI------- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1099 FNVIGACIIILLATPIASIIIPPLGLI--------YFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEE 1170
Cdd:TIGR02868 132 VPAGVALVVGAAAVAAIAVLSVPAALIlaaglllaGFVAPLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1171 QERFIRQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFSV--ISRHSLSAGLVGLSVSYSLQVTTYLNWLV 1248
Cdd:TIGR02868 212 LPAALAQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGGpaVADGRLAPVTLAVLVLLPLAAFEAFAALP 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1249 RMSSEMETNIVAVERLKEYSETEKEAPWQIQEMAPPSTwPQVGRVEFRDYGLRYRENlDLVLKHINITINGGEKVGIVGR 1328
Cdd:TIGR02868 292 AAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVG-LGKPTLELRDLSAGYPGA-PPVLDGVSLDLPPGERVAILGP 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1329 TGAGKSSLTLGLFRINESAEGEIIIDDINIAKIGLHDLRVKITIIPQDPVLFSGSLRMNL---DPfsQYSDEEVWTSLEL 1405
Cdd:TIGR02868 370 SGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLrlaRP--DATDEELWAALER 447
|
410 420
....*....|....*....|..
gi 1953392644 1406 AHLKDFVSGLPDKLNQECAEGG 1427
Cdd:TIGR02868 448 VGLADWLRALPDGLDTVLGEGG 469
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
605-858 |
2.02e-29 |
|
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: 125.25 E-value: 2.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 605 SIVQASVSLKRLRIFLSHEELEPDSIER-RPvkdgggANSITVKNATFTWARSDPPTLSGITFSIPEGSLVAVVGQVGCG 683
Cdd:COG4618 297 QFVSARQAYRRLNELLAAVPAEPERMPLpRP------KGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSG 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 684 KSSLLSALLAEMDKVEGHVAIKG-------------SVAYVPQQAWIQNDSLRENIlfgrqlqERYYKA----VIEACAL 746
Cdd:COG4618 371 KSTLARLLVGVWPPTAGSVRLDGadlsqwdreelgrHIGYLPQDVELFDGTIAENI-------ARFGDAdpekVVAAAKL 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 747 --LPDLeI--LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAhVGKHIFENVIgpkGMLK--NK 820
Cdd:COG4618 444 agVHEM-IlrLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD-EGEAALAAAI---RALKarGA 518
|
250 260 270
....*....|....*....|....*....|....*...
gi 1953392644 821 TRLLVTHSISYLPQVDVIIVMTGGKISEMGSYQELLAR 858
Cdd:COG4618 519 TVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1293-1388 |
2.25e-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: 115.56 E-value: 2.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1293 VEFRDYGLRYRENLDLVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIGLHDLRVKITI 1372
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90
....*....|....*.
gi 1953392644 1373 IPQDPVLFSGSLRMNL 1388
Cdd:cd03228 81 VPQDPFLFSGTIRENI 96
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
646-846 |
2.95e-29 |
|
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: 116.86 E-value: 2.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 646 VKNATFTWarSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG--------SVAYVPQQAWI 717
Cdd:cd03235 2 VEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 718 QND---SLRENIL--------FGRQLQERYYKAVIEAcalLPDLEILPSGDRTeIGEkgvnLSGGQKQRVSLARAVYCDS 786
Cdd:cd03235 80 DRDfpiSVRDVVLmglyghkgLFRRLSKADKAKVDEA---LERVGLSELADRQ-IGE----LSGGQQQRVLLARALVQDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953392644 787 DIYLFDDPLSAVDAHVGKHIFENVIGPKGmlKNKTRLLVTHSI-SYLPQVDVIIVMTGGKI 846
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLRELRR--EGMTILVVTHDLgLVLEYFDRVLLLNRTVV 210
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1291-1429 |
1.71e-28 |
|
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: 114.99 E-value: 1.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1291 GRVEFRDYGLRYRENLDLVLKHINITINGGEKVGIVGRTGAGKSSLT---LGLFRineSAEGEIIIDDINIAKIGLHDLR 1367
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLkllAGLYK---PTSGSVLLDGTDIRQLDPADLR 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953392644 1368 VKITIIPQDPVLFSGSLRMNLDPFSQY-SDEEVWTSLELAHLKDFVSGLPDKLNQECAEGGEN 1429
Cdd:cd03245 78 RNIGYVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRG 140
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
644-863 |
3.52e-28 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 122.52 E-value: 3.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTW-ARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-------------SVA 709
Cdd:TIGR00958 479 IEFQDVSFSYpNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqydhhylhrQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 710 YVPQQAWIQNDSLRENILFG-RQLQERYYKAVIEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYCDSDI 788
Cdd:TIGR00958 559 LVGQEPVLFSGSVRENIAYGlTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRV 638
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953392644 789 YLFDDPLSAVDAHVgkhifENVIGPKGMLKNKTRLLVTHSISYLPQVDVIIVMTGGKISEMGSYQELLARDGAFA 863
Cdd:TIGR00958 639 LILDEATSALDAEC-----EQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYK 708
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
644-846 |
3.54e-28 |
|
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: 112.31 E-value: 3.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGS-------------VAY 710
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdpnelgdhVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 711 VPQQAWIQNDSLRENIlfgrqlqeryykavieacallpdleilpsgdrteigekgvnLSGGQKQRVSLARAVYCDSDIYL 790
Cdd:cd03246 81 LPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1953392644 791 FDDPLSAVDAHVGKHIFENVIGPKgmLKNKTRLLVTHSISYLPQVDVIIVMTGGKI 846
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALK--AAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1291-1427 |
6.14e-28 |
|
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: 114.95 E-value: 6.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1291 GRVEFRDYGLRYRENLDLVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRInESAEGEIIIDDINIAKIGLHDLRVKI 1370
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1953392644 1371 TIIPQDPVLFSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSGLPDKLNQECAEGG 1427
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGG 136
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
646-845 |
6.30e-28 |
|
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: 112.95 E-value: 6.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 646 VKNATFTWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-------------SVAYVP 712
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltklslkelrrKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 713 QQAWIQ--NDSLRENILFG-RQL---QERYYKAVIEACALLpDLEILPsgDRtEIGEkgvnLSGGQKQRVSLARAVYCDS 786
Cdd:cd03225 82 QNPDDQffGPTVEEEVAFGlENLglpEEEIEERVEEALELV-GLEGLR--DR-SPFT----LSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953392644 787 DIYLFDDPLSAVDAHVGKHIFEnvigpkgMLK-----NKTRLLVTHSISYLPQV-DVIIVMTGGK 845
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLE-------LLKklkaeGKTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
644-848 |
6.36e-28 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 114.42 E-value: 6.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWARSDPPT--LSGITFSIPEGSLVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVAIKG--------SVAYVP 712
Cdd:COG1116 8 LELRGVSKRFPTGGGGVtaLDDVSLTVAAGEFVALVGPSGCGKSTLLR-LIAGLEKPtSGEVLVDGkpvtgpgpDRGVVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 713 QQawiqnDSL------RENILFGRQLQ-----ERYYKA--VIEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLA 779
Cdd:COG1116 87 QE-----PALlpwltvLDNVALGLELRgvpkaERRERAreLLELVGLAGFEDAYPH-----------QLSGGMRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 780 RAVYCDSDIYLFDDPLSAVDAHVgkhifenvigpKGML----------KNKTRLLVTHSIS---YLpqVDVIIVMTG--G 844
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALT-----------RERLqdellrlwqeTGKTVLFVTHDVDeavFL--ADRVVVLSArpG 217
|
....
gi 1953392644 845 KISE 848
Cdd:COG1116 218 RIVE 221
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
661-796 |
6.79e-28 |
|
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: 110.82 E-value: 6.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-------------SVAYVPQQAWIQND-SLRENI 726
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderkslrkEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953392644 727 LFGRQLQERYYKAV-IEACALLPDLEILPSGDRTeIGEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLS 796
Cdd:pfam00005 81 RLGLLLKGLSKREKdARAEEALEKLGLGDLADRP-VGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1293-1427 |
1.16e-26 |
|
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: 110.01 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1293 VEFRDYGLRYRENLDLVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIGLHDLRVKITI 1372
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1373 IPQDPVLFSGSLRMNLdpfsQY-----SDEEVWTSLELAHLKDFVSGLPDKLNQECAEGG 1427
Cdd:cd03251 81 VSQDVFLFNDTVAENI----AYgrpgaTREEVEEAARAANAHEFIMELPEGYDTVIGERG 136
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
644-846 |
1.28e-26 |
|
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: 109.50 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWARSDPPT--LSGITFSIPEGSLVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVAIKG-------------- 706
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVRVDGtdisklsekelaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 707 ---SVAYVPQQ-AWIQNDSLRENILFGRQLQERYYKAVIEACALLpdLEILPSGDRteIGEKGVNLSGGQKQRVSLARAV 782
Cdd:cd03255 80 rrrHIGFVFQSfNLLPDLTALENVELPLLLAGVPKKERRERAEEL--LERVGLGDR--LNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 783 YCDSDIYLFDDPLSAVDAHVGKHIFEnvigpkgMLK------NKTRLLVTHSISYLPQVDVIIVMTGGKI 846
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVME-------LLRelnkeaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
644-846 |
2.09e-26 |
|
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: 108.71 E-value: 2.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWARSDPPT--LSGITFSIPEGSLVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVAIKG--------SVAYVP 712
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtaLEDISLSVEEGEFVALVGPSGCGKSTLLR-IIAGLERPtSGEVLVDGepvtgpgpDRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 713 QQA----WIqndSLRENILFGRQLQERYYKAVIE-ACALLpdleilpsgdrTEIGEKGV------NLSGGQKQRVSLARA 781
Cdd:cd03293 80 QQDallpWL---TVLDNVALGLELQGVPKAEARErAEELL-----------ELVGLSGFenayphQLSGGMRQRVALARA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953392644 782 VYCDSDIYLFDDPLSAVDAHVGKHIFENVIgpkGMLK--NKTRLLVTHSIS---YLPqvDVIIVMTG--GKI 846
Cdd:cd03293 146 LAVDPDVLLLDEPFSALDALTREQLQEELL---DIWRetGKTVLLVTHDIDeavFLA--DRVVVLSArpGRI 212
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
633-860 |
2.80e-26 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 115.97 E-value: 2.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 633 RPVKDGgganSITVKNATFTWaRSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEG------------ 700
Cdd:PRK10790 334 RPLQSG----RIDIDNVSFAY-RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGeirldgrplssl 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 701 -HVAIKGSVAYVPQQAWIQNDSLRENILFGRQLQERYYKAVIEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLA 779
Cdd:PRK10790 409 sHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALA 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 780 RAVYCDSDIYLFDDPLSAVDAHVGKHIFENVigpkGMLKNKTRLLV-THSISYLPQVDVIIVMTGGKISEMGSYQELLAR 858
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDSGTEQAIQQAL----AAVREHTTLVViAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAA 564
|
..
gi 1953392644 859 DG 860
Cdd:PRK10790 565 QG 566
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
644-882 |
5.52e-26 |
|
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: 114.23 E-value: 5.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSA---LLAEMDKVEGHVAIKG-------------S 707
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALAlmgLLPHGGRISGEVLLDGrdllelsealrgrR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 708 VAYVPQQAWIQNDSLR--ENILFGRQLQERYYKAVIEACALLPDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYCD 785
Cdd:COG1123 85 IGMVFQDPMTQLNPVTvgDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQ----LSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 786 SDIYLFDDPLSAVDAHVGKHIFEnVIGPKGMLKNKTRLLVTHSISYLPQV-DVIIVMTGGKISEMGSYQELLARDGAFAE 864
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILD-LLRELQRERGTTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEEILAAPQALAA 239
|
250
....*....|....*...
gi 1953392644 865 FLRTYASGDQEQAEQDDG 882
Cdd:COG1123 240 VPRLGAARGRAAPAAAAA 257
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
651-850 |
1.72e-25 |
|
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: 106.06 E-value: 1.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 651 FTWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVAIKG-----------SVAYVPQQ-AWI 717
Cdd:cd03259 6 LSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLR-LIAGLERPdSGEILIDGrdvtgvpperrNIGMVFQDyALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 718 QNDSLRENILFG--------RQLQERYyKAVIEACALLPDLEILPSGdrteigekgvnLSGGQKQRVSLARAVYCDSDIY 789
Cdd:cd03259 85 PHLTVAENIAFGlklrgvpkAEIRARV-RELLELVGLEGLLNRYPHE-----------LSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953392644 790 LFDDPLSAVDAHVGKHIFENVigpKGMLKN--KTRLLVTHSIS-YLPQVDVIIVMTGGKISEMG 850
Cdd:cd03259 153 LLDEPLSALDAKLREELREEL---KELQRElgITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
972-1264 |
1.74e-25 |
|
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350044 [Multi-domain] Cd Length: 324 Bit Score: 109.12 E-value: 1.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 972 LFISFLSIFLFLCNHVASLVsnyWLSLWTDDPIVNGTQE-------------HTKIRLSVYGALGISQGITVFGYSMAVS 1038
Cdd:cd18600 17 IFVLILCLVIFAIEVAASLV---GLWLLRSQADRVNTTRpesssntyavivtFTSSYYVFYIYVGVADSLLAMGFFRGLP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1039 I--GGIFASRRLHVDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFNVIGACIIILLATPIAS 1116
Cdd:cd18600 94 LvhTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIGAITVVSILQPYIF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1117 IIIPPLGLIYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIVAN 1196
Cdd:cd18600 174 LATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTL 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1197 RWLAVRLECVgncIVLF--AALFSVISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERL 1264
Cdd:cd18600 254 RWFQMRIEMI---FVIFftAVTFISIGTTGDGEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSRI 320
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1045-1429 |
2.36e-25 |
|
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: 113.68 E-value: 2.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1045 SRRLHVDLLQN----VLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMF-------MGSLFNV---IGACIIILL 1110
Cdd:TIGR01193 224 GQRLSIDIILSyikhLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFldmwilvIVGLFLVrqnMLLFLLSLL 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1111 ATPIASIIIpplgliYFFVQRFYVASSRQLKrlesvSRSPVYSHFNETLLGVSVIRAF-EEQERFIRQSDLKVDENQKA- 1188
Cdd:TIGR01193 304 SIPVYAVII------ILFKRTFNKLNHDAMQ-----ANAVLNSSIIEDLNGIETIKSLtSEAERYSKIDSEFGDYLNKSf 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1189 -YYPSIVANRWLAVRLECVGNCIVLFAALFSVIsRHSLSAGLVglsVSYSLQVTTYLNWL---VRMSSEMETNIVAVERL 1264
Cdd:TIGR01193 373 kYQKADQGQQAIKAVTKLILNVVILWTGAYLVM-RGKLTLGQL---ITFNALLSYFLTPLeniINLQPKLQAARVANNRL 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1265 KE--YSETEKEAPWQIQEMAPPSTWPQVGRVEFRdYGLRyrenlDLVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFR 1342
Cdd:TIGR01193 449 NEvyLVDSEFINKKKRTELNNLNGDIVINDVSYS-YGYG-----SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVG 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1343 INESAEGEIIIDDINIAKIGLHDLRVKITIIPQDPVLFSGSLRMNLDPFSQ--YSDEEVWTSLELAHLKDFVSGLPDKLN 1420
Cdd:TIGR01193 523 FFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKenVSQDEIWAACEIAEIKDDIENMPLGYQ 602
|
....*....
gi 1953392644 1421 QECAEGGEN 1429
Cdd:TIGR01193 603 TELSEEGSS 611
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1293-1428 |
3.41e-25 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 105.78 E-value: 3.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1293 VEFRDYGLRYRENLDlVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIGLHDLRVKITI 1372
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953392644 1373 IPQDPVLFSGSLRMNLdpfsQY-----SDEEVWTSLELAHLKDFVSGLPDKLNQECAE------GGE 1428
Cdd:cd03253 80 VPQDTVLFNDTIGYNI----RYgrpdaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGErglklsGGE 142
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
647-846 |
4.41e-25 |
|
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: 105.25 E-value: 4.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 647 KNATFTW-ARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGS-------------VAYVP 712
Cdd:cd03248 15 QNVTFAYpTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkylhskVSLVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 713 QQAWIQNDSLRENILFGrqLQERYYKAVIEACALL---PDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYCDSDIY 789
Cdd:cd03248 95 QEPVLFARSLQDNIAYG--LQSCSFECVKEAAQKAhahSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1953392644 790 LFDDPLSAVDAHvGKHIFENVIgpKGMLKNKTRLLVTHSISYLPQVDVIIVMTGGKI 846
Cdd:cd03248 173 ILDEATSALDAE-SEQQVQQAL--YDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
644-864 |
7.92e-25 |
|
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: 104.34 E-value: 7.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWaRSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSL---LSALLAEMdkvEGHVAIKG-------------S 707
Cdd:COG1122 1 IELENLSFSY-PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLlrlLNGLLKPT---SGEVLVDGkditkknlrelrrK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 708 VAYVPQQAWIQ--NDSLRENILFG-RQL---QERYYKAVIEACALLpDLEilpsgdrtEIGEKGV-NLSGGQKQRVSLAR 780
Cdd:COG1122 77 VGLVFQNPDDQlfAPTVEEDVAFGpENLglpREEIRERVEEALELV-GLE--------HLADRPPhELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 781 AVYCDSDIYLFDDPLSAVDAHVGKHIFEnvigpkgMLK-----NKTRLLVTHSISYLPQV-DVIIVMTGGKISEMGSYQE 854
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLE-------LLKrlnkeGKTVIIVTHDLDLVAELaDRVIVLDDGRIVADGTPRE 220
|
250
....*....|
gi 1953392644 855 LLARDGAFAE 864
Cdd:COG1122 221 VFSDYELLEE 230
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1220-1428 |
1.10e-24 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 111.07 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1220 ISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYSETEKEapwqIQEM--APPSTwPQVGRVEFRD 1297
Cdd:COG5265 288 VVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPE----VADApdAPPLV-VGGGEVRFEN 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1298 YGLRY---REnldlVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIGLHDLRVKITIIP 1374
Cdd:COG5265 363 VSFGYdpeRP----ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVP 438
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953392644 1375 QDPVLFSGSLRMNLdpfsQY-----SDEEVWTSLELAHLKDFVSGLPDKLNQECAE------GGE 1428
Cdd:COG5265 439 QDTVLFNDTIAYNI----AYgrpdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGErglklsGGE 499
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
651-846 |
1.26e-24 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 103.36 E-value: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 651 FTWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-------------SVAYVPQQAWI 717
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplsampppewrrQVAYVPQEPAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 718 QNDSLRENILFGRQLQERYYKAViEACALLPDLEiLPsgdrTEIGEKGV-NLSGGQKQRVSLARAVYCDSDIYLFDDPLS 796
Cdd:COG4619 86 WGGTVRDNLPFPFQLRERKFDRE-RALELLERLG-LP----PDILDKPVeRLSGGERQRLALIRALLLQPDVLLLDEPTS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1953392644 797 AVDAHvGKHIFENVIgpKGMLKNKTR--LLVTHSISYLPQV-DVIIVMTGGKI 846
Cdd:COG4619 160 ALDPE-NTRRVEELL--REYLAEEGRavLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
644-850 |
2.15e-24 |
|
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: 101.62 E-value: 2.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGS------------VAYV 711
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdlekalsslISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 712 PQQAWIQNDSLRENIlfGRQLqeryykavieacallpdleilpsgdrteigekgvnlSGGQKQRVSLARAVYCDSDIYLF 791
Cdd:cd03247 81 NQRPYLFDTTLRNNL--GRRF------------------------------------SGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1953392644 792 DDPLSAVDAHVGKHIFENVIgpkGMLKNKTRLLVTHSISYLPQVDVIIVMTGGKISEMG 850
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIF---EVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
643-858 |
4.57e-24 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 105.54 E-value: 4.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 643 SITVKNATFTWarSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVAIKG-----------SVAY 710
Cdd:COG3839 3 SLELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLR-MIAGLEDPtSGEILIGGrdvtdlppkdrNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 711 VPQQ-AWIQNDSLRENILFGRQLQeRYYKAVI-----EACALLpdlEILPSGDRteigeKGVNLSGGQKQRVSLARAVYC 784
Cdd:COG3839 80 VFQSyALYPHMTVYENIAFPLKLR-KVPKAEIdrrvrEAAELL---GLEDLLDR-----KPKQLSGGQRQRVALGRALVR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 785 DSDIYLFDDPLSAVDAHvgkhifenvigpkgmLKNKTR--------------LLVTHSisylpQV------DVIIVMTGG 844
Cdd:COG3839 151 EPKVFLLDEPLSNLDAK---------------LRVEMRaeikrlhrrlgtttIYVTHD-----QVeamtlaDRIAVMNDG 210
|
250
....*....|....
gi 1953392644 845 KISEMGSYQELLAR 858
Cdd:COG3839 211 RIQQVGTPEELYDR 224
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1293-1427 |
4.61e-24 |
|
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: 102.62 E-value: 4.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1293 VEFRDYGLRYRENLD-LVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIGLHDLRVKIT 1371
Cdd:cd03249 1 IEFKNVSFRYPSRPDvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953392644 1372 IIPQDPVLFSGSLRMNL-----DPfsqySDEEVWTSLELAHLKDFVSGLPDKLNQECAEGG 1427
Cdd:cd03249 81 LVSQEPVLFDGTIAENIrygkpDA----TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERG 137
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
644-848 |
7.80e-24 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 101.66 E-value: 7.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWARSDPPT--LSGITFSIPEGSLVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVAIKG-------------- 706
Cdd:COG1136 5 LELRNLTKSYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVLIDGqdisslserelarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 707 ---SVAYVPQQA-WIQNDSLRENILFGRQLQERYYKAVIE-ACALLPDLEIlpsGDRTE--IGEkgvnLSGGQKQRVSLA 779
Cdd:COG1136 84 rrrHIGFVFQFFnLLPELTALENVALPLLLAGVSRKERRErARELLERVGL---GDRLDhrPSQ----LSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953392644 780 RAVYCDSDIYLFDDPLSAVDAHVGKHIFEnvigpkgMLK------NKTRLLVTHSISYLPQVDVIIVMTGGKISE 848
Cdd:COG1136 157 RALVNRPKLILADEPTGNLDSKTGEEVLE-------LLRelnrelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1021-1427 |
1.83e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 107.03 E-value: 1.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1021 ALGISQGITVF--GYSMA-VSIGGIFASRRlhvDLLQNVLRSPMSFFERTPSGNLVNRFskeldTVDSmiPQVIKMFMGS 1097
Cdd:PRK11176 73 GLMILRGITSFisSYCISwVSGKVVMTMRR---RLFGHMMGMPVSFFDKQSTGTLLSRI-----TYDS--EQVASSSSGA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1098 LFNVI--GACIIILLATPIA-----SIIIPPLGLIYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAF-- 1168
Cdd:PRK11176 143 LITVVreGASIIGLFIMMFYyswqlSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFgg 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1169 --EEQERF------IRQSDLKVDENQKAYYPSI--VANRWLAVrlecvgnciVLFAALFSVIsRHSLSAGLVGLSVSYSL 1238
Cdd:PRK11176 223 qeVETKRFdkvsnrMRQQGMKMVSASSISDPIIqlIASLALAF---------VLYAASFPSV-MDTLTAGTITVVFSSMI 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1239 QVTTYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQEMAPPStwpqvGRVEFRDYGLRYRENLDLVLKHINITIN 1318
Cdd:PRK11176 293 ALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQEKDEGKRVIERAK-----GDIEFRNVTFTYPGKEVPALRNINFKIP 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1319 GGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIGLHDLRVKITIIPQDPVLFSGSLRMNLDPFS--QYSD 1396
Cdd:PRK11176 368 AGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARteQYSR 447
|
410 420 430
....*....|....*....|....*....|.
gi 1953392644 1397 EEVWTSLELAHLKDFVSGLPDKLNQECAEGG 1427
Cdd:PRK11176 448 EQIEEAARMAYAMDFINKMDNGLDTVIGENG 478
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
644-860 |
2.46e-23 |
|
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: 100.70 E-value: 2.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWarSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG------------SVAYV 711
Cdd:COG4555 2 IEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearrQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 712 PQQAWI-QNDSLRENILF---GRQLQERYYKAVIEAcaLLPDLEILPSGDRteigeKGVNLSGGQKQRVSLARAVYCDSD 787
Cdd:COG4555 80 PDERGLyDRLTVRENIRYfaeLYGLFDEELKKRIEE--LIELLGLEEFLDR-----RVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953392644 788 IYLFDDPLSAVDAhVGKHIFENVIgpKGMLK-NKTRLLVTHSISYLPQV-DVIIVMTGGKISEMGSYQELLARDG 860
Cdd:COG4555 153 VLLLDEPTNGLDV-MARRLLREIL--RALKKeGKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
643-851 |
2.61e-23 |
|
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: 99.41 E-value: 2.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 643 SITVKNATFTWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-------------SVA 709
Cdd:cd03369 6 EIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 710 YVPQQAWIQNDSLRENI-LFGRQLQERYYKAVieacallpdleilpsgdrtEIGEKGVNLSGGQKQRVSLARAVYCDSDI 788
Cdd:cd03369 86 IIPQDPTLFSGTIRSNLdPFDEYSDEEIYGAL-------------------RVSEGGLNLSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953392644 789 YLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRLLVTHSISYLPQVDVIIVMTGGKISEMGS 851
Cdd:cd03369 147 LVLDEATASIDYATDALIQKTI---REEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
645-845 |
5.89e-23 |
|
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: 96.93 E-value: 5.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 645 TVKNATFTWArsDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGSVAyvpqqAWIQNDSLRE 724
Cdd:cd00267 1 EIENLSFRYG--GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI-----AKLPLEELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 725 NILFGRQLqeryykavieacallpdleilpsgdrteigekgvnlSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHvGK 804
Cdd:cd00267 74 RIGYVPQL------------------------------------SGGQRQRVALARALLLNPDLLLLDEPTSGLDPA-SR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1953392644 805 HIFENVIgpKGML-KNKTRLLVTHSISYLPQV-DVIIVMTGGK 845
Cdd:cd00267 117 ERLLELL--RELAeEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
644-850 |
9.41e-23 |
|
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: 98.35 E-value: 9.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKN--ATFTWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG--------------- 706
Cdd:cd03257 2 LEVKNlsVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 707 -SVAYVPQQAW--------IQnDSLRENILFGRQL--QERYYKAVIEA-CALLPDLEILpsgDR--TEigekgvnLSGGQ 772
Cdd:cd03257 82 kEIQMVFQDPMsslnprmtIG-EQIAEPLRIHGKLskKEARKEAVLLLlVGVGLPEEVL---NRypHE-------LSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 773 KQRVSLARAVYCDSDIYLFDDPLSAVDAHVGKHIFEnvigpkgMLK------NKTRLLVTHSISYLPQV-DVIIVMTGGK 845
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILD-------LLKklqeelGLTLLFITHDLGVVAKIaDRVAVMYAGK 223
|
....*
gi 1953392644 846 ISEMG 850
Cdd:cd03257 224 IVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
644-858 |
1.51e-22 |
|
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: 98.34 E-value: 1.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKN--ATFTWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGS-------------V 708
Cdd:COG1124 2 LEVRNlsVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRpvtrrrrkafrrrV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 709 AYVPQQA-------WIQNDSLRE--NILFGRQLQERyykavieACALLPDLEiLPSGDRTEIGEKgvnLSGGQKQRVSLA 779
Cdd:COG1124 82 QMVFQDPyaslhprHTVDRILAEplRIHGLPDREER-------IAELLEQVG-LPPSFLDRYPHQ---LSGGQRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 780 RAVYCDSDIYLFDDPLSAVDAHVGKHIFEnvigpkgMLK------NKTRLLVTHS---ISYLpqVDVIIVMTGGKISEMG 850
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILN-------LLKdlreerGLTYLFVSHDlavVAHL--CDRVAVMQNGRIVEEL 221
|
....*...
gi 1953392644 851 SYQELLAR 858
Cdd:COG1124 222 TVADLLAG 229
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
641-858 |
1.52e-22 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 100.94 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 641 ANSITVKNATFTWArsDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVAIKG-----------SV 708
Cdd:COG3842 3 MPALELENVSKRYG--DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLR-MIAGFETPdSGRILLDGrdvtglppekrNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 709 AYVPQqawiqNDSL------RENILFGrqLQER-YYKAVIEACALlpdlEILpsgDRTEIGEKG----VNLSGGQKQRVS 777
Cdd:COG3842 80 GMVFQ-----DYALfphltvAENVAFG--LRMRgVPKAEIRARVA----ELL---ELVGLEGLAdrypHQLSGGQQQRVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 778 LARAVYCDSDIYLFDDPLSAVDAHVGKHIFENVigpKGMLK--NKTRLLVTH------SISylpqvDVIIVMTGGKISEM 849
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDAKLREEMREEL---RRLQRelGITFIYVTHdqeealALA-----DRIAVMNDGRIEQV 217
|
....*....
gi 1953392644 850 GSYQELLAR 858
Cdd:COG3842 218 GTPEEIYER 226
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
661-858 |
1.63e-22 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 97.83 E-value: 1.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLL------------SALLAEMDKVEGHVAIKGSVAYVPQQAWIQND-SLRENIL 727
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIrmllgllrptsgEVRVLGEDVARDPAEVRRRIGYVPQEPALYPDlTVRENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 728 F--------GRQLQERYYKaVIEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVD 799
Cdd:COG1131 96 FfarlyglpRKEARERIDE-LLELFGLTDAADRKVG-----------TLSGGMKQRLGLALALLHDPELLILDEPTSGLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953392644 800 AhVGKHIFENVIgpKGMLK-NKTRLLVTHsisYLPQV----DVIIVMTGGKISEMGSYQELLAR 858
Cdd:COG1131 164 P-EARRELWELL--RELAAeGKTVLLSTH---YLEEAerlcDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
644-876 |
4.86e-22 |
|
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: 96.99 E-value: 4.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWaRSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSAL--LAEMDkvEGHVAIKG-------------SV 708
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMInrLIEPT--SGEIFIDGedireqdpvelrrKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 709 AYVPQQAWI-QNDSLRENILFGRQL----QERYYKAVIEACALLpDLEILPSGDRTEiGEkgvnLSGGQKQRVSLARAVY 783
Cdd:cd03295 78 GYVIQQIGLfPHMTVEENIALVPKLlkwpKEKIRERADELLALV-GLDPAEFADRYP-HE----LSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 784 CDSDIYLFDDPLSAVDAHVGKHIFENVIGPKGMLkNKTRLLVTHSI-SYLPQVDVIIVMTGGKISEMGSYQELLARDGaf 862
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQEL-GKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRSPA-- 228
|
250
....*....|....
gi 1953392644 863 AEFLRTYASGDQEQ 876
Cdd:cd03295 229 NDFVAEFVGADRLL 242
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
661-855 |
5.48e-22 |
|
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: 96.10 E-value: 5.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSAL-----LAEMDKVEGHVAIKGS---------------VAYVPQQAWIQND 720
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKdiydldvdvlelrrrVGMVFQKPNPFPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 721 SLRENILFGRQLQ----ERYYKAVIEAC---ALLPDLEilpsGDRTeigeKGVNLSGGQKQRVSLARAVYCDSDIYLFDD 793
Cdd:cd03260 96 SIYDNVAYGLRLHgiklKEELDERVEEAlrkAALWDEV----KDRL----HALGLSGGQQQRLCLARALANEPEVLLLDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953392644 794 PLSAVDAhVGKHIFENVIgpKGMLKNKTRLLVTHSisyLPQV----DVIIVMTGGKISEMGSYQEL 855
Cdd:cd03260 168 PTSALDP-ISTAKIEELI--AELKKEYTIVIVTHN---MQQAarvaDRTAFLLNGRLVEFGPTEQI 227
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
394-878 |
7.94e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 103.13 E-value: 7.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 394 RIKTAVIGAVYRKALVITNSarksSTVGEIVNLMSVDAQRF-MDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAV 472
Cdd:PLN03232 984 RLHDAMLNSILRAPMLFFHT----NPTGRVINRFSKDIGDIdRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPL 1059
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 473 MILMvpLNAVMAMKTKTYQVAHMKS--KDNRIKLMNEILNG---IKVLKLYAW-----------ELAF------KDKVLA 530
Cdd:PLN03232 1060 LILF--YAAYLYYQSTSREVRRLDSvtRSPIYAQFGEALNGlssIRAYKAYDRmakingksmdnNIRFtlantsSNRWLT 1137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 531 IRQEELKvlkksaylaavGTFTWVctpflvaLSTFAVYVTVDKNNildaQKAFVSLALFnILRFPLNILPMVISSIVQAS 610
Cdd:PLN03232 1138 IRLETLG-----------GVMIWL-------TATFAVLRNGNAEN----QAGFASTMGL-LLSYTLNITTLLSGVLRQAS 1194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 611 V------SLKRLRIFLSHEELEPDSIER-RPVKDGGGANSITVKNATFTWARSDPPTLSGITFSIPEGSLVAVVGQVGCG 683
Cdd:PLN03232 1195 KaenslnSVERVGNYIDLPSEATAIIENnRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAG 1274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 684 KSSLLSALLAEMDKVEGHVAIKG-------------SVAYVPQQAWIQNDSLRENI-LFGRQLQERYYKAvIEACALLPD 749
Cdd:PLN03232 1275 KSSMLNALFRIVELEKGRIMIDDcdvakfgltdlrrVLSIIPQSPVLFSGTVRFNIdPFSEHNDADLWEA-LERAHIKDV 1353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 750 LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRLLVTHSI 829
Cdd:PLN03232 1354 IDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTI---REEFKSCTMLVIAHRL 1430
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1953392644 830 SYLPQVDVIIVMTGGKISEMGSYQELLARDGafAEFLRTYASGDQEQAE 878
Cdd:PLN03232 1431 NTIIDCDKILVLSSGQVLEYDSPQELLSRDT--SAFFRMVHSTGPANAQ 1477
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
643-858 |
1.19e-21 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 98.30 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 643 SITVKNATFTWArsDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSAL--LAEMDkvEGHVAIKGSVAYV---PQQAWI 717
Cdd:COG1118 2 SIEVRNISKRFG--SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIagLETPD--SGRIVLNGRDLFTnlpPRERRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 718 ----QNDSL------RENILFGrqLQERYY-KAVIEACAL-------LPDLE-ILPSgdrteigekgvNLSGGQKQRVSL 778
Cdd:COG1118 78 gfvfQHYALfphmtvAENIAFG--LRVRPPsKAEIRARVEellelvqLEGLAdRYPS-----------QLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 779 ARAVYCDSDIYLFDDPLSAVDAHVGK-------HIFENVigpkgmlkNKTRLLVTHSisylpQVDV------IIVMTGGK 845
Cdd:COG1118 145 ARALAVEPEVLLLDEPFGALDAKVRKelrrwlrRLHDEL--------GGTTVFVTHD-----QEEAleladrVVVMNQGR 211
|
250
....*....|...
gi 1953392644 846 ISEMGSYQELLAR 858
Cdd:COG1118 212 IEQVGTPDEVYDR 224
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
644-856 |
1.56e-21 |
|
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: 95.50 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFtwARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-------------SVAY 710
Cdd:COG1120 2 LEAENLSV--GYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelarRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 711 VPQQAwIQNDSL--RENILFGR--------QLQERYYKAVIEACALLpdlEILPSGDRTeIGEkgvnLSGGQKQRVSLAR 780
Cdd:COG1120 80 VPQEP-PAPFGLtvRELVALGRyphlglfgRPSAEDREAVEEALERT---GLEHLADRP-VDE----LSGGERQRVLIAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 781 AVYCDSDIYLFDDPLSAVDAHvgkHIFEnvigpkgML---------KNKTRLLVTHsisYLPQV----DVIIVMTGGKIS 847
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLA---HQLE-------VLellrrlareRGRTVVMVLH---DLNLAaryaDRLVLLKDGRIV 217
|
....*....
gi 1953392644 848 EMGSYQELL 856
Cdd:COG1120 218 AQGPPEEVL 226
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
643-855 |
5.27e-21 |
|
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: 93.56 E-value: 5.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 643 SITVKNATFTWARSdpPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVAIKG-----------SVAY 710
Cdd:cd03296 2 SIEVRNVSKRFGDF--VALDDVSLDIPSGELVALLGPSGSGKTTLLR-LIAGLERPdSGTILFGGedatdvpvqerNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 711 VPQQ-AWIQNDSLRENILFG---RQLQERYYKAVIEA--CALLPDLEILPSGDRTEigekgVNLSGGQKQRVSLARAVYC 784
Cdd:cd03296 79 VFQHyALFRHMTVFDNVAFGlrvKPRSERPPEAEIRAkvHELLKLVQLDWLADRYP-----AQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953392644 785 DSDIYLFDDPLSAVDAHVGKHIfenvigpKGMLK------NKTRLLVTHSISYLPQV-DVIIVMTGGKISEMGSYQEL 855
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKEL-------RRWLRrlhdelHVTTVFVTHDQEEALEVaDRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
645-846 |
1.26e-20 |
|
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: 90.96 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 645 TVKNATFtwARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVaikgsvayvpqqawiqndslre 724
Cdd:cd03214 1 EVENLSV--GYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI---------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 725 nILFGRQLQERYYKAVIEACALLPD-LEILpsgDRTEIGEKGVN-LSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHV 802
Cdd:cd03214 57 -LLDGKDLASLSPKELARKIAYVPQaLELL---GLAHLADRPFNeLSGGERQRVLLARALAQEPPILLLDEPTSHLDIAH 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1953392644 803 GKHIFENVIGPKGMlKNKTRLLVTHSISYLPQV-DVIIVMTGGKI 846
Cdd:cd03214 133 QIELLELLRRLARE-RGKTVVMVLHDLNLAARYaDRVILLKDGRI 176
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
644-859 |
1.34e-20 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 92.56 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFtwARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGS---------------- 707
Cdd:cd03261 1 IELRGLTK--SFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlrrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 708 VAYVPQQAWIQND-SLRENILFG----RQLQERYYKAV----IEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSL 778
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVAFPlrehTRLSEEEIREIvlekLEAVGLRGAEDLYPA-----------ELSGGMKKRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 779 ARAVYCDSDIYLFDDPLSAVDAhVGKHIFENVIGPKGMLKNKTRLLVTHSISYLPQV-DVIIVMTGGKISEMGSYQELLA 857
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDP-IASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPEELRA 226
|
..
gi 1953392644 858 RD 859
Cdd:cd03261 227 SD 228
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
325-616 |
1.62e-20 |
|
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: 93.77 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 325 FLMSFLFKALHDLMMFAGPEILKLLINFVndKKAPDWQGYLYTALLFICAC-LQTLVLHQYFHICFVSGMRIKTAVIGAV 403
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDV--IPAGDLSLLLWIALLLLLLAlLRALLSYLRRYLAARLGQRVVFDLRRDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 404 YRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATY-INMIWSAPLQVILALYLLWLNLGPSVLAGVAVMILMVPLNAV 482
Cdd:cd07346 79 FRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSgLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 483 MAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWE----LAFKDKVLAIRQEELKVLKKSAYLAAVGTFTWVCTPF 558
Cdd:cd07346 159 FRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEereiERFREANRDLRDANLRAARLSALFSPLIGLLTALGTA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1953392644 559 LVALstFAVYVTVdkNNILDAQKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 616
Cdd:cd07346 239 LVLL--YGGYLVL--QGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
976-1264 |
2.25e-20 |
|
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: 93.38 E-value: 2.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 976 FLSIFLFLCNHVASLVSNYWLSLWTDDPIVNGTQEHTKIRLSVYGALGISQGITVFGYSMAVSIGGIFASRRLHVDLLQN 1055
Cdd:cd07346 2 LLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1056 VLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFNVIGACIIILLATP----IASIIIPPLGLIYFFVQR 1131
Cdd:cd07346 82 LQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWkltlVALLLLPLYVLILRYFRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1132 FYVASSRQLKrlESVSRspVYSHFNETLLGVSVIRAF----EEQERFIRQSDLKVDENQKAYYPSIVANRWLAVrLECVG 1207
Cdd:cd07346 162 RIRKASREVR--ESLAE--LSAFLQESLSGIRVVKAFaaeeREIERFREANRDLRDANLRAARLSALFSPLIGL-LTALG 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1953392644 1208 NCIVLFAALFSVIsRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERL 1264
Cdd:cd07346 237 TALVLLYGGYLVL-QGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
618-858 |
2.60e-20 |
|
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: 96.51 E-value: 2.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 618 IFLSHEELE--PDSIERRPVKDGGGANS---ITVKNATFTWARSDPPT---LSGITFSIPEGSLVAVVGQVGCGKSSLLS 689
Cdd:COG1123 230 ILAAPQALAavPRLGAARGRAAPAAAAAeplLEVRNLSKRYPVRGKGGvraVDDVSLTLRRGETLGLVGESGSGKSTLAR 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 690 ALLAEMDKVEGHVAIKG----------------SVAYVPQQAwiqNDSL------RENILFGRQLQERYYKA-------- 739
Cdd:COG1123 310 LLLGLLRPTSGSILFDGkdltklsrrslrelrrRVQMVFQDP---YSSLnprmtvGDIIAEPLRLHGLLSRAerrervae 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 740 VIEACALLPD-LEILPSGdrteigekgvnLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVGKHIFEnvigpkgMLK 818
Cdd:COG1123 387 LLERVGLPPDlADRYPHE-----------LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILN-------LLR 448
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1953392644 819 ------NKTRLLVTHSISYLPQV-DVIIVMTGGKISEMGSYQELLAR 858
Cdd:COG1123 449 dlqrelGLTYLFISHDLAVVRYIaDRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
976-1196 |
1.10e-19 |
|
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: 91.30 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 976 FLSIFLFLCNHVASLVSNYWLSLWTDDPIVNGTQEHTKIRL--SVYGALGISQGITVFGYSMAVSIGGIFASRRLHVDLL 1053
Cdd:cd18544 2 ILALLLLLLATALELLGPLLIKRAIDDYIVPGQGDLQGLLLlaLLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1054 QNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFNVIGACIIIL-----LATpIASIIIPPLGLIYFF 1128
Cdd:cd18544 82 SHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFllnwrLAL-ISLLVLPLLLLATYL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953392644 1129 VQRFYVASSRQLKrlESVSRspVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIVAN 1196
Cdd:cd18544 161 FRKKSRKAYREVR--EKLSR--LNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLF 224
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
644-811 |
1.41e-19 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 88.69 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFtwARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG------------SVAYV 711
Cdd:COG4133 3 LEAENLSC--RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaredyrrRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 712 PQQ-AWIQNDSLRENILF-----GRQLQERYYKAVIEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYCD 785
Cdd:COG4133 81 GHAdGLKPELTVRENLRFwaalyGLRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLLSP 149
|
170 180
....*....|....*....|....*.
gi 1953392644 786 SDIYLFDDPLSAVDAHvGKHIFENVI 811
Cdd:COG4133 150 APLWLLDEPFTALDAA-GVALLAELI 174
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
644-855 |
2.33e-19 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 88.33 E-value: 2.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSAL------------LAEMDKVEGHVAIKGSVAYV 711
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLtgelrptsgtayINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 712 PQqawiqNDSL------RENILFGRQLQ---ERYYKAVIEAcaLLPDLEILPSGDRteigeKGVNLSGGQKQRVSLARAV 782
Cdd:cd03263 81 PQ-----FDALfdeltvREHLRFYARLKglpKSEIKEEVEL--LLRVLGLTDKANK-----RARTLSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953392644 783 YCDSDIYLFDDPLSAVDaHVGKHIFENVIgpKGMLKNKTRLLVTHS---ISYLpqVDVIIVMTGGKISEMGSYQEL 855
Cdd:cd03263 149 IGGPSVLLLDEPTSGLD-PASRRAIWDLI--LEVRKGRSIILTTHSmdeAEAL--CDRIAIMSDGKLRCIGSPQEL 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
666-890 |
2.85e-19 |
|
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: 91.32 E-value: 2.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 666 FSIPEGSLVAVVGQVGCGKSSLLSAL--LAEMDkvEGHVAIKGSV-----------------AYVPQQAwiqndSL---- 722
Cdd:COG4148 20 FTLPGRGVTALFGPSGSGKTTLLRAIagLERPD--SGRIRLGGEVlqdsargiflpphrrriGYVFQEA-----RLfphl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 723 --RENILFGRQ---LQERYYK--AVIEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYCDSDIYLFDDPL 795
Cdd:COG4148 93 svRGNLLYGRKrapRAERRISfdEVVELLGIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 796 SAVDAHVGKHI---FENvigpkgmLKNKTR---LLVTHSisyLPQV----DVIIVMTGGKISEMGSYQELLARDGafaef 865
Cdd:COG4148 162 AALDLARKAEIlpyLER-------LRDELDipiLYVSHS---LDEVarlaDHVVLLEQGRVVASGPLAEVLSRPD----- 226
|
250 260 270
....*....|....*....|....*....|....
gi 1953392644 866 LRTYASGDQ---------EQAEQDDGLTGVSSPG 890
Cdd:COG4148 227 LLPLAGGEEagsvleatvAAHDPDYGLTRLALGG 260
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
648-829 |
4.11e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 88.77 E-value: 4.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 648 NATFTWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGSV--------AYVpqqawIQN 719
Cdd:COG4525 10 SVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgadrGVV-----FQK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 720 DSL------RENILFGRQLQ-----ERYYKAvieacallpdLEILPSGDRTEIGEKGV-NLSGGQKQRVSLARAVYCDSD 787
Cdd:COG4525 85 DALlpwlnvLDNVAFGLRLRgvpkaERRARA----------EELLALVGLADFARRRIwQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1953392644 788 IYLFDDPLSAVDAHVGKHIFENVigpkgmLK-----NKTRLLVTHSI 829
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQELL------LDvwqrtGKGVFLITHSV 195
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
664-855 |
4.18e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 90.55 E-value: 4.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 664 ITFSIPEGSLVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVAIKGSvaYVPQQAWIQND--------------SLRENILF 728
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLR-LVAGLEKpTEGQIFIDGE--DVTHRSIQQRDicmvfqsyalfphmSLGENVGY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 729 GRQLQ----ERYYKAVIEACALLpDLEILpsGDRTeigekgVN-LSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVG 803
Cdd:PRK11432 102 GLKMLgvpkEERKQRVKEALELV-DLAGF--EDRY------VDqISGGQQQRVALARALILKPKVLLFDEPLSNLDANLR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1953392644 804 KHIFENVIGPKGMLkNKTRLLVTHSISYLPQV-DVIIVMTGGKISEMGSYQEL 855
Cdd:PRK11432 173 RSMREKIRELQQQF-NITSLYVTHDQSEAFAVsDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
641-881 |
4.94e-19 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 88.79 E-value: 4.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 641 ANSITVKNATFTWaRSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGS----------VAY 710
Cdd:PRK15056 4 QAGIVVNDVTVTW-RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 711 VPQQA---WIQNDSLRENILFGR--------QLQERYYKAVIEACALLPDLEIlpsgDRTEIGEkgvnLSGGQKQRVSLA 779
Cdd:PRK15056 83 VPQSEevdWSFPVLVEDVVMMGRyghmgwlrRAKKRDRQIVTAALARVDMVEF----RHRQIGE----LSGGQKKRVFLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 780 RAVYCDSDIYLFDDPLSAVDAHVGKHIfenvIGPKGMLKN--KTRLLVTHSISYLPQVDVIIVMTGGKISEMGSYQELLA 857
Cdd:PRK15056 155 RAIAQQGQVILLDEPFTGVDVKTEARI----ISLLRELRDegKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFT 230
|
250 260
....*....|....*....|....*...
gi 1953392644 858 RDG---AFAEFLRTYA-SGDQEQAEQDD 881
Cdd:PRK15056 231 AENlelAFSGVLRHVAlNGSEESIITDD 258
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1044-1428 |
5.89e-19 |
|
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: 92.35 E-value: 5.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1044 ASRRLHVDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDS----MIPQVIKMFMGSLfnVIGAciIILLATPIASIII 1119
Cdd:TIGR02857 75 VKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGyfarYLPQLVLAVIVPL--AILA--AVFPQDWISGLIL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1120 ---PPLgLIYFFVQRFYVASSRQLKRLESVSRspVYSHFNETLLGVSVIRAF----EEQERFIRQSD---------LKVd 1183
Cdd:TIGR02857 151 lltAPL-IPIFMILIGWAAQAAARKQWAALSR--LSGHFLDRLRGLPTLKLFgrakAQAAAIRRSSEeyrertmrvLRI- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1184 enqkAYYPSIVanrwlavrLEcvgncivLFAALfSVisrhSLSAGLVGLSVSYSlQVTTYLNWLV------------RMS 1251
Cdd:TIGR02857 227 ----AFLSSAV--------LE-------LFATL-SV----ALVAVYIGFRLLAG-DLDLATGLFVlllapefylplrQLG 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1252 SEMETNIVAVERLKEYSETEKEAPWQIQEMAPpSTWPQVGRVEFRDYGLRYrENLDLVLKHINITINGGEKVGIVGRTGA 1331
Cdd:TIGR02857 282 AQYHARADGVAAAEALFAVLDAAPRPLAGKAP-VTAAPASSLEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVGPSGA 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1332 GKSSLTLGLFRINESAEGEIIIDDINIAKIGLHDLRVKITIIPQDPVLFSGSLRMNL---DPFSqySDEEVWTSLELAHL 1408
Cdd:TIGR02857 360 GKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIrlaRPDA--SDAEIREALERAGL 437
|
410 420
....*....|....*....|
gi 1953392644 1409 KDFVSGLPDKLNQECAEGGE 1428
Cdd:TIGR02857 438 DEFVAALPQGLDTPIGEGGA 457
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
661-846 |
5.90e-19 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 85.91 E-value: 5.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGsvayvpQQAWIQNDSLRENILFgrqlqeryykaV 740
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG------KDIKKEPEEVKRRIGY-----------L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 741 IEACALLPDL---EILpsgdrteigekgvNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAhVGKHIFENVIgpKGML 817
Cdd:cd03230 79 PEEPSLYENLtvrENL-------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDP-ESRREFWELL--RELK 142
|
170 180 190
....*....|....*....|....*....|.
gi 1953392644 818 K-NKTRLLVTHSISYLPQV-DVIIVMTGGKI 846
Cdd:cd03230 143 KeGKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
644-858 |
1.40e-18 |
|
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: 86.48 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNAT--FTWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVAIKG-------------- 706
Cdd:cd03258 2 IELKNVSkvFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIR-CINGLERpTSGSVLVDGtdltllsgkelrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 707 --SVAYVPQQ-AWIQNDSLRENILFGRQLqERYYKAVIEAcALLPDLEILPSGDRTEIGEKgvNLSGGQKQRVSLARAVY 783
Cdd:cd03258 81 rrRIGMIFQHfNLLSSRTVFENVALPLEI-AGVPKAEIEE-RVLELLELVGLEDKADAYPA--QLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 784 CDSDIYLFDDPLSAVDAHVGKHIFEnvigpkgMLK--NK----TRLLVTHSISYLPQV-DVIIVMTGGKISEMGSYQELL 856
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILA-------LLRdiNRelglTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEEVF 229
|
..
gi 1953392644 857 AR 858
Cdd:cd03258 230 AN 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
563-875 |
1.69e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 92.49 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 563 STFAVYvtvdKNNILDAQKAFVS-LALfnILRFPLNILPMVISSIVQASV------SLKRLRIFLSHEELEPDSIE-RRP 634
Cdd:PLN03130 1155 ASFAVM----QNGRAENQAAFAStMGL--LLSYALNITSLLTAVLRLASLaenslnAVERVGTYIDLPSEAPLVIEnNRP 1228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 635 VKDGGGANSITVKNATFTWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-------- 706
Cdd:PLN03130 1229 PPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGcdiskfgl 1308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 707 -----SVAYVPQQAWIQNDSLRENI-LFGRQ--------LQERYYKAVIEACALlpdleilpsGDRTEIGEKGVNLSGGQ 772
Cdd:PLN03130 1309 mdlrkVLGIIPQAPVLFSGTVRFNLdPFNEHndadlwesLERAHLKDVIRRNSL---------GLDAEVSEAGENFSVGQ 1379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 773 KQRVSLARAVYCDSDIYLFDDPLSAV----DAHVGKHIFENvigpkgmLKNKTRLLVTHSISYLPQVDVIIVMTGGKISE 848
Cdd:PLN03130 1380 RQLLSLARALLRRSKILVLDEATAAVdvrtDALIQKTIREE-------FKSCTMLIIAHRLNTIIDCDRILVLDAGRVVE 1452
|
330 340 350
....*....|....*....|....*....|....*....
gi 1953392644 849 MGSYQELLARDG------------AFAEFLRTYASGDQE 875
Cdd:PLN03130 1453 FDTPENLLSNEGsafskmvqstgaANAQYLRSLVFGGDE 1491
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
645-846 |
2.35e-18 |
|
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: 85.00 E-value: 2.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 645 TVKNATFTWARSdPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG----------SVAYVPQQ 714
Cdd:cd03226 1 RIENISFSYKKG-TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakerrkSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 715 AWIQ--NDSLRENILFGrqlQERYYKAVIEACALLPDLEILPSGDRTEIgekgvNLSGGQKQRVSLARAVYCDSDIYLFD 792
Cdd:cd03226 80 VDYQlfTDSVREELLLG---LKELDAGNEQAETVLKDLDLYALKERHPL-----SLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1953392644 793 DPLSAVDAH----VGKHIFEnvIGPKGmlknKTRLLVTHSISYLPQV-DVIIVMTGGKI 846
Cdd:cd03226 152 EPTSGLDYKnmerVGELIRE--LAAQG----KAVIVITHDYEFLAKVcDRVLLLANGAI 204
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
644-845 |
4.84e-18 |
|
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: 83.39 E-value: 4.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTwaRSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG---------------SV 708
Cdd:cd03229 1 LELKNVSKR--YGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltdledelpplrrRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 709 AYVPQQ-AWIQNDSLRENILFGrqlqeryykavieacallpdleilpsgdrteigekgvnLSGGQKQRVSLARAVYCDSD 787
Cdd:cd03229 79 GMVFQDfALFPHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1953392644 788 IYLFDDPLSAVDAHVGKHIFENVIGPKGMLKnKTRLLVTHSISYLPQV-DVIIVMTGGK 845
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQLG-ITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1293-1427 |
5.87e-18 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 84.85 E-value: 5.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1293 VEFRDYGLRYRENLDLVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIGLHDLRVKITI 1372
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1953392644 1373 IPQDPVLFSGSLRMNL---DPfsQYSDEEVWTSLELAHLKDFVSGLPDKLNQECAEGG 1427
Cdd:cd03252 81 VLQENVLFNRSIRDNIalaDP--GMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQG 136
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
660-850 |
1.04e-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: 83.46 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 660 TLSGITFSIPEGSLVAVVGQVGCGKSSLLS--ALLAEMDKveGHVAIKG-----------SVAYVPQQ-AWIQNDSLREN 725
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRmiAGLEEPTS--GRIYIGGrdvtdlppkdrDIAMVFQNyALYPHMTVYDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 726 ILFGRQLQeRYYKAVI-----EACALLPDLEILpsgDRteigeKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDA 800
Cdd:cd03301 93 IAFGLKLR-KVPKDEIdervrEVAELLQIEHLL---DR-----KPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1953392644 801 HVGkhiFENVIGPKGMLKN--KTRLLVTHS-ISYLPQVDVIIVMTGGKISEMG 850
Cdd:cd03301 164 KLR---VQMRAELKRLQQRlgTTTIYVTHDqVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
644-867 |
1.12e-17 |
|
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: 84.79 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSL---LSALL-AEmdkvEGHVAIKGSVAYVPQQAW--- 716
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLaklLNGLLlPT----SGKVTVDGLDTLDEENLWeir 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 717 ------IQN-D------SLRENILFG--------RQLQERYYKAvIEACALLPDLEILPSgdrteigekgvNLSGGQKQR 775
Cdd:TIGR04520 77 kkvgmvFQNpDnqfvgaTVEDDVAFGlenlgvprEEMRKRVDEA-LKLVGMEDFRDREPH-----------LLSGGQKQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 776 VSLARAVYCDSDIYLFDDPLSAVDahvgkhifenvigPKG-------MLK-----NKTRLLVTHSISYLPQVDVIIVMTG 843
Cdd:TIGR04520 145 VAIAGVLAMRPDIIILDEATSMLD-------------PKGrkevletIRKlnkeeGITVISITHDMEEAVLADRVIVMNK 211
|
250 260
....*....|....*....|....
gi 1953392644 844 GKISEMGSYQELLARdgafAEFLR 867
Cdd:TIGR04520 212 GKIVAEGTPREIFSQ----VELLK 231
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
464-858 |
1.24e-17 |
|
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: 88.32 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 464 PSVLAGVAVMI-LMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKL-YAWELAFKDKVLAIRQEELKVLKK 541
Cdd:COG4615 147 PPLFLLTLVLLgLGVAGYRLLVRRARRHLRRAREAEDRLFKHFRALLEGFKELKLnRRRRRAFFDEDLQPTAERYRDLRI 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 542 SAYLAAVGTFTWVCTPFLVALST----FAVYVTVDKNNIldaqKAFVSLALFniLRFPLNILPMVISSIVQASVSLKRL- 616
Cdd:COG4615 227 RADTIFALANNWGNLLFFALIGLilflLPALGWADPAVL----SGFVLVLLF--LRGPLSQLVGALPTLSRANVALRKIe 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 617 RIFLSHEELEPDSIERRPVKDGGGANSITVKNATFTWARSDPP---TLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLA 693
Cdd:COG4615 301 ELELALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGDegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTG 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 694 EMDKVEGHVAIKGSVayVPQQAWiqnDSLRENI--------LFGRQLQERYYKAVIEACALLPDLEIlpsGDRTEIgEKG 765
Cdd:COG4615 381 LYRPESGEILLDGQP--VTADNR---EAYRQLFsavfsdfhLFDRLLGLDGEADPARARELLERLEL---DHKVSV-EDG 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 766 ----VNLSGGQKQRVSLARAVYCDSDIYLFD------DPlsavdahVGKHIFENVIGPkgMLK--NKTRLLVTHSISYLP 833
Cdd:COG4615 452 rfstTDLSQGQRKRLALLVALLEDRPILVFDewaadqDP-------EFRRVFYTELLP--ELKarGKTVIAISHDDRYFD 522
|
410 420
....*....|....*....|....*
gi 1953392644 834 QVDVIIVMTGGKISEMGSYQELLAR 858
Cdd:COG4615 523 LADRVLKMDYGKLVELTGPAALAAS 547
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
644-856 |
1.29e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 84.66 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG------SVAYVPQQAWI 717
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiskeNLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 718 --QND-------SLRENILFG---RQLQERYYKAVIEACALLPDLEILpsgdrteIGEKGVNLSGGQKQRVSLARAVYCD 785
Cdd:PRK13632 88 ifQNPdnqfigaTVEDDIAFGlenKKVPPKKMKDIIDDLAKKVGMEDY-------LDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953392644 786 SDIYLFDDPLSAVDAHvGKHIFENVIGPKGMLKNKTRLLVTHSISYLPQVDVIIVMTGGKISEMGSYQELL 856
Cdd:PRK13632 161 PEIIIFDESTSMLDPK-GKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
644-846 |
1.88e-17 |
|
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: 83.39 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWARSDPpTLSGITFSIPEGSLVAVVGQVGCGKSSLLSAL--LAEMDKVEGHV--------------AIKGS 707
Cdd:cd03256 1 IEVENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLngLVEPTSGSVLIdgtdinklkgkalrQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 708 VAYVPQQ-AWIQNDSLRENILFGR--------QLQERYYKAVIE-ACALLPDLEILPSGDRteigeKGVNLSGGQKQRVS 777
Cdd:cd03256 80 IGMIFQQfNLIERLSVLENVLSGRlgrrstwrSLFGLFPKEEKQrALAALERVGLLDKAYQ-----RADQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953392644 778 LARAVYCDSDIYLFDDPLSAVD---AHVGKHIFENvigpKGMLKNKTRLLVTHSISY-LPQVDVIIVMTGGKI 846
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDpasSRQVMDLLKR----INREEGITVIVSLHQVDLaREYADRIVGLKDGRI 223
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1046-1428 |
3.41e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 86.94 E-value: 3.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1046 RRLHV--DLLQNVLRSPMSFFERTPSGNLVNRFskeLDTVDSMIpQVIKMFMGSLFNVIGAcIIILLATPIA-----SII 1118
Cdd:PRK13657 87 RRLAVltEYFERIIQLPLAWHSQRGSGRALHTL---LRGTDALF-GLWLEFMREHLATLVA-LVVLLPLALFmnwrlSLV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1119 IPPLGLIYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAF---EEQERFIRQSdlkVDENQKAYYPsiVA 1195
Cdd:PRK13657 162 LVVLGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYnriEAETQALRDI---ADNLLAAQMP--VL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1196 NRWlavrlecvgncivlfaALFSVISRHS--------LSAGL---------VGLSVSYSLQVTTYLNWLVRMSSEMETNI 1258
Cdd:PRK13657 237 SWW----------------ALASVLNRAAstitmlaiLVLGAalvqkgqlrVGEVVAFVGFATLLIGRLDQVVAFINQVF 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1259 VAVERLKEYSETEKEAPwQIQEMAPPSTWPQV-GRVEFRDYGLRYrENLDLVLKHINITINGGEKVGIVGRTGAGKSSLT 1337
Cdd:PRK13657 301 MAAPKLEEFFEVEDAVP-DVRDPPGAIDLGRVkGAVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLI 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1338 LGLFRINESAEGEIIIDDINIAKIGLHDLRVKITIIPQDPVLFSGSLRMNL-----DPfsqySDEEVWTSLELAHLKDFV 1412
Cdd:PRK13657 379 NLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIrvgrpDA----TDEEMRAAAERAQAHDFI 454
|
410 420
....*....|....*....|..
gi 1953392644 1413 SGLPDKLNQECAE------GGE 1428
Cdd:PRK13657 455 ERKPDGYDTVVGErgrqlsGGE 476
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
506-862 |
7.40e-17 |
|
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: 86.92 E-value: 7.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 506 NEILNGIKVLKlyawelAFKDKVLAIRQEELKV-LKKSAYLAAVGTFTWV-----CTPFLVALstFAVYVTVDKNNILDA 579
Cdd:TIGR00957 1148 NETLLGVSVIR------AFEEQERFIHQSDLKVdENQKAYYPSIVANRWLavrleCVGNCIVL--FAALFAVISRHSLSA 1219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 580 QKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSI-ERRPVKDGGGANSITVKNATFTWARSDP 658
Cdd:TIGR00957 1220 GLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIqETAPPSGWPPRGRVEFRNYCLRYREDLD 1299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 659 PTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-------------SVAYVPQQAWIQNDSLREN 725
Cdd:TIGR00957 1300 LVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlniakiglhdlrfKITIIPQDPVLFSGSLRMN 1379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 726 I-LFGRQLQERYYKAvIEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVGK 804
Cdd:TIGR00957 1380 LdPFSQYSDEEVWWA-LELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDN 1458
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1953392644 805 HIFENVigpKGMLKNKTRLLVTHSISYLPQVDVIIVMTGGKISEMGSYQELLARDGAF 862
Cdd:TIGR00957 1459 LIQSTI---RTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1258-1427 |
7.97e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 85.65 E-value: 7.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1258 IVAVERLKEYSETEKEAPWQIQEMAPPSTwpqvGRVEFRDYGLRYRENLDLVLKHINITINGGEKVGIVGRTGAGKSSLT 1337
Cdd:PRK11160 308 IASARRINEITEQKPEVTFPTTSTAAADQ----VSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1338 LGLFRINESAEGEIIIDDINIAKIGLHDLRVKITIIPQDPVLFSGSLRMNL---DPfsQYSDEEVWTSLELAHLKDFVSG 1414
Cdd:PRK11160 384 QLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGLEKLLED 461
|
170
....*....|...
gi 1953392644 1415 lPDKLNQECAEGG 1427
Cdd:PRK11160 462 -DKGLNAWLGEGG 473
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
644-846 |
9.89e-17 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 81.64 E-value: 9.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWArSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG----------------S 707
Cdd:COG3638 3 LELRNLSKRYP-GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGqdvtalrgralrrlrrR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 708 VAYVPQQ-AWIQNDSLRENILFGRQ--------LQERYYKAVIE-ACALLPDLEILP-SGDRTEigekgvNLSGGQKQRV 776
Cdd:COG3638 82 IGMIFQQfNLVPRLSVLTNVLAGRLgrtstwrsLLGLFPPEDRErALEALERVGLADkAYQRAD------QLSGGQQQRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 777 SLARAVYCDSDIYLFDDPLSAVDAHVGKHIFEnvigpkgMLK------NKTRLLVTHsisylpQVDV-------IIVMTG 843
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTARQVMD-------LLRriaredGITVVVNLH------QVDLarryadrIIGLRD 222
|
...
gi 1953392644 844 GKI 846
Cdd:COG3638 223 GRV 225
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
620-867 |
1.09e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 86.24 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 620 LSHEELEPDSIERR--PVKDGGG---ANS------ITVKNATFTW-ARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSL 687
Cdd:PTZ00265 1131 LSFEKYYPLIIRKSniDVRDNGGiriKNKndikgkIEIMDVNFRYiSRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTV 1210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 688 LSALLAEMD-KVEGHVAIKGS----------------------------------------------------------- 707
Cdd:PTZ00265 1211 MSLLMRFYDlKNDHHIVFKNEhtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfknsgkilldgvdicdyn 1290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 708 -------VAYVPQQAWIQNDSLRENILFGRQLQERY-YKAVIEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLA 779
Cdd:PTZ00265 1291 lkdlrnlFSIVSQEPMLFNMSIYENIKFGKEDATREdVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIA 1370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 780 RAVYCDSDIYLFDDPLSAVDAHVGKHIFENVIGPKGMlKNKTRLLVTHSISYLPQVDVIIVM-----TGGKISEMGSYQE 854
Cdd:PTZ00265 1371 RALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDK-ADKTIITIAHRIASIKRSDKIVVFnnpdrTGSFVQAHGTHEE 1449
|
330
....*....|....
gi 1953392644 855 LL-ARDGAFAEFLR 867
Cdd:PTZ00265 1450 LLsVQDGVYKKYVK 1463
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1293-1392 |
1.47e-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: 78.89 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1293 VEFRDYGLRYRENLDLVLKHINITINGGEKVGIVGRTGAGKSSLtLGLFRINESA-EGEIIIDDINIAKIGlHDLRVKIT 1371
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTL-LQLLTGDLKPqQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100
....*....|....*....|..
gi 1953392644 1372 IIPQDPVLFSGSLRMNL-DPFS 1392
Cdd:cd03247 79 VLNQRPYLFDTTLRNNLgRRFS 100
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
661-858 |
1.83e-16 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 80.42 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSAL--LAEMDkvEGHVAIKGSVAYVPQQAWIQndsLRENI--------LF-- 728
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCInlLEEPD--SGTITVDGEDLTDSKKDINK---LRRKVgmvfqqfnLFph 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 729 ---------------GRQLQEryykAVIEACALLpdleilpsgDRTEIGEKG----VNLSGGQKQRVSLARAVYCDSDIY 789
Cdd:COG1126 92 ltvlenvtlapikvkKMSKAE----AEERAMELL---------ERVGLADKAdaypAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953392644 790 LFDDPLSAVD----AHVgkhifENVIgpK-----GMlknkTRLLVTHSISYLPQV-DVIIVMTGGKISEMGSYQELLAR 858
Cdd:COG1126 159 LFDEPTSALDpelvGEV-----LDVM--RdlakeGM----TMVVVTHEMGFAREVaDRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
979-1264 |
2.13e-16 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 81.45 E-value: 2.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 979 IFLFLCNhVASLVSNYWLSLWTDDPIVNGTQEHTKIRLSVYGALGISQGITVFGYSMAVSIGGIFASRRLHVDLLQNVLR 1058
Cdd:cd18557 3 LFLLISS-AAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1059 SPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFNVIGaCIIILLA-----TPIASIIIPPLGLIYFFVQRFY 1133
Cdd:cd18557 82 QEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIG-GLIILFIlswklTLVLLLVIPLLLIASKIYGRYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1134 VASSRQLkrLESVSRSPvySHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIVAN---RWLAVRLECVGNCI 1210
Cdd:cd18557 161 RKLSKEV--QDALAKAG--QVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANalfQGITSLLIYLSLLL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1953392644 1211 VLFAALFSVISRHsLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERL 1264
Cdd:cd18557 237 VLWYGGYLVLSGQ-LTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
661-846 |
2.61e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 80.49 E-value: 2.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSaLLAEMDKVEGHVAIKGSVAYvpqqAWIQNDSlreNILF--GRQLQeryYK 738
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLR-LLAGLETPSAGELLAGTAPL----AEAREDT---RLMFqdARLLP---WK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 739 AVIEACAL----------LPDLEILPSGDRTeiGEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVG---KH 805
Cdd:PRK11247 97 KVIDNVGLglkgqwrdaaLQALAAVGLADRA--NEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRiemQD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1953392644 806 IFENVIGPKGMlknkTRLLVTHSISYLPQV-DVIIVMTGGKI 846
Cdd:PRK11247 175 LIESLWQQHGF----TVLLVTHDVSEAVAMaDRVLLIEEGKI 212
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
664-867 |
3.21e-16 |
|
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: 80.38 E-value: 3.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 664 ITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-----------------SVAYVPQQ-AWIQNDSLREN 725
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaamsrkelrelrrkKISMVFQSfALLPHRTVLEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 726 ILFGRQLQ-----ERYYKA--VIEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAV 798
Cdd:cd03294 123 VAFGLEVQgvpraEREERAaeALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953392644 799 DAHVGKHIFENVIGPKGMLKnKTRLLVTHSISYLPQV-DVIIVMTGGKISEMGSYQELLAR--DGAFAEFLR 867
Cdd:cd03294 192 DPLIRREMQDELLRLQAELQ-KTIVFITHDLDEALRLgDRIAIMKDGRLVQVGTPEEILTNpaNDYVREFFR 262
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
661-846 |
3.46e-16 |
|
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: 79.11 E-value: 3.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSAL--LAEMDkvEGHVAIKGSVAYVPQQAWIQndsLRENI--------LFGR 730
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCInlLEEPD--SGTIIIDGLKLTDDKKNINE---LRQKVgmvfqqfnLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 731 qlqeryyKAVIEACALLP--------------DLEILpsgDRTEIGEKG----VNLSGGQKQRVSLARAVYCDSDIYLFD 792
Cdd:cd03262 91 -------LTVLENITLAPikvkgmskaeaeerALELL---EKVGLADKAdaypAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1953392644 793 DPLSAVDAHVGKHIFENV--IGPKGMlknkTRLLVTHSISYLPQV-DVIIVMTGGKI 846
Cdd:cd03262 161 EPTSALDPELVGEVLDVMkdLAEEGM----TMVVVTHEMGFAREVaDRVIFMDDGRI 213
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
643-855 |
5.18e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 81.28 E-value: 5.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 643 SITVKNATFTWARSDppTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGS-----------VAYV 711
Cdd:PRK10851 2 SIEIANIKKSFGRTQ--VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 712 PQQ-AWIQNDSLRENILFGRQL---QERYYKAVI--EACALLPDLEILPSGDRTEigekgVNLSGGQKQRVSLARAVYCD 785
Cdd:PRK10851 80 FQHyALFRHMTVFDNIAFGLTVlprRERPNAAAIkaKVTQLLEMVQLAHLADRYP-----AQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953392644 786 SDIYLFDDPLSAVDAHVGKHIFENVIGPKGMLKNkTRLLVTHSISYLPQV-DVIIVMTGGKISEMGSYQEL 855
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKF-TSVFVTHDQEEAMEVaDRVVVMSQGNIEQAGTPDQV 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
644-857 |
6.17e-16 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 79.02 E-value: 6.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWarSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSA--LLAEMD----KVeGHVAIKGSVAYVPQQAWI 717
Cdd:PRK11264 4 IEVKNLVKKF--HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCinLLEQPEagtiRV-GDITIDTARSLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 718 -----------QNDSL------RENILFGRQL--QERYYKAVIEACALLPDLEIlpSGDRTEIGEKgvnLSGGQKQRVSL 778
Cdd:PRK11264 81 rqlrqhvgfvfQNFNLfphrtvLENIIEGPVIvkGEPKEEATARARELLAKVGL--AGKETSYPRR---LSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 779 ARAVYCDSDIYLFDDPLSAVDAH-VGKHIfeNVIgpKGMLKNK-TRLLVTHSISYLPQV-DVIIVMTGGKISEMGSYQEL 855
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDPElVGEVL--NTI--RQLAQEKrTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGPAKAL 231
|
..
gi 1953392644 856 LA 857
Cdd:PRK11264 232 FA 233
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
664-890 |
9.73e-16 |
|
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: 80.54 E-value: 9.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 664 ITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-----------------SVAYVPQQAWI-QNDSLREN 725
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrkgiflppekrRIGYVFQEARLfPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 726 ILFGRQ-----LQERYYKAVIEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDA 800
Cdd:TIGR02142 96 LRYGMKrarpsERRISFERVIELLGIGHLLGRLPG-----------RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 801 HVGKHI---FENVIGPKGMlknkTRLLVTHSISYLPQV-DVIIVMTGGKISEMGSYQELLAR---DGAFAEFLRTYASGD 873
Cdd:TIGR02142 165 PRKYEIlpyLERLHAEFGI----PILYVSHSLQEVLRLaDRVVVLEDGRVAAAGPIAEVWASpdlPWLAREDQGSLIEGV 240
|
250
....*....|....*..
gi 1953392644 874 QEQAEQDDGLTGVSSPG 890
Cdd:TIGR02142 241 VAEHDQHYGLTALRLGG 257
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
661-855 |
1.05e-15 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 78.05 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVAIKG-SVAYVP----------QQ-AWIQNDSLRENIL 727
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLR-LIAGFETPtSGEILLDGkDITNLPphkrpvntvfQNyALFPHLTVFENIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 728 FGRQLQeRYYKAVIEACALlpdlEILPSGDRTEIGEKGVN-LSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVGKHI 806
Cdd:cd03300 95 FGLRLK-KLPKAEIKERVA----EALDLVQLEGYANRKPSqLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDM 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1953392644 807 FENVigpKGMLKN--KTRLLVTH------SISylpqvDVIIVMTGGKISEMGSYQEL 855
Cdd:cd03300 170 QLEL---KRLQKElgITFVFVTHdqeealTMS-----DRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
661-866 |
1.07e-15 |
|
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: 78.15 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGS-----------VAYVPQQ-AWIQNDSLRENILF 728
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQNyALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 729 GRQLQER----YYKAVIEACALLPDLEILpsgDRteigeKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAhvgk 804
Cdd:cd03299 95 GLKKRKVdkkeIERKVLEIAEMLGIDHLL---NR-----KPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV---- 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953392644 805 HIFENVIgpkGMLK------NKTRLLVTHSIS-YLPQVDVIIVMTGGKISEMGSYQELLAR--DGAFAEFL 866
Cdd:cd03299 163 RTKEKLR---EELKkirkefGVTVLHVTHDFEeAWALADKVAIMLNGKLIQVGKPEEVFKKpkNEFVAEFL 230
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
643-867 |
1.10e-15 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 78.13 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 643 SITVKNATFTWARSdpPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSAL-LAEMDKvEGHVAIKGS-------------- 707
Cdd:COG4161 2 SIQLKNINCFYGSH--QALFDINLECPSGETLVLLGPSGAGKSSLLRVLnLLETPD-SGQLNIAGHqfdfsqkpsekair 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 708 -----VAYVPQQ--AWiQNDSLRENILFG--RQLQERYYKAVIEACALLPDLEILPSGDRTEIgekgvNLSGGQKQRVSL 778
Cdd:COG4161 79 llrqkVGMVFQQynLW-PHLTVMENLIEApcKVLGLSKEQAREKAMKLLARLRLTDKADRFPL-----HLSGGQQQRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 779 ARAVYCDSDIYLFDDPLSAVDAHVGKHIFE--NVIGPKGMlknkTRLLVTHSISYLPQV-DVIIVMTGGKISEMGSyQEL 855
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDPEITAQVVEiiRELSQTGI----TQVIVTHEVEFARKVaSQVVYMEKGRIIEQGD-ASH 227
|
250
....*....|....
gi 1953392644 856 LA--RDGAFAEFLR 867
Cdd:COG4161 228 FTqpQTEAFAHYLS 241
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
639-868 |
1.70e-15 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 78.03 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 639 GGANSITVKNATFTWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-SVAYVPQQAWI 717
Cdd:cd03288 15 GLGGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGiDISKLPLHTLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 718 QNDS--LRENILFGRQLQ-----------ERYYKAvIEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYC 784
Cdd:cd03288 95 SRLSiiLQDPILFSGSIRfnldpeckctdDRLWEA-LEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 785 DSDIYLFDDPLSAVDAHVgkhifENVIGPKGMLKNKTRLLVT--HSISYLPQVDVIIVMTGGKISEMGSYQELLAR-DGA 861
Cdd:cd03288 174 KSSILIMDEATASIDMAT-----ENILQKVVMTAFADRTVVTiaHRVSTILDADLVLVLSRGILVECDTPENLLAQeDGV 248
|
....*..
gi 1953392644 862 FAEFLRT 868
Cdd:cd03288 249 FASLVRT 255
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
664-846 |
2.22e-15 |
|
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: 76.56 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 664 ITFSIPEGsLVAVVGQVGCGKSSLLSaLLAEMDKVE-GHVAIKGS-----------------VAYVPQQ-AWIQNDSLRE 724
Cdd:cd03297 17 IDFDLNEE-VTGIFGASGAGKSTLLR-CIAGLEKPDgGTIVLNGTvlfdsrkkinlppqqrkIGLVFQQyALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 725 NILFGRQLQERYYKAVIEAcallpdlEILPSGDRTEIGEKGV-NLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVg 803
Cdd:cd03297 95 NLAFGLKRKRNREDRISVD-------ELLDLLGLDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL- 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1953392644 804 KHIFENVIgpKGMLK--NKTRLLVTHSISYLPQV-DVIIVMTGGKI 846
Cdd:cd03297 167 RLQLLPEL--KQIKKnlNIPVIFVTHDLSEAEYLaDRIVVMEDGRL 210
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1291-1427 |
2.71e-15 |
|
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: 76.74 E-value: 2.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1291 GRVEFRDYGLRYRENLD-LVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIGLHDLRVK 1369
Cdd:cd03248 10 GIVKFQNVTFAYPTRPDtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1953392644 1370 ITIIPQDPVLFSGSLRMNLD-PFSQYSDEEVWTSLELAHLKDFVSGLPDKLNQECAEGG 1427
Cdd:cd03248 90 VSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKG 148
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
976-1264 |
3.34e-15 |
|
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: 77.86 E-value: 3.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 976 FLSIFLFLCNHVASLVsNYWLSLWT-DDPIVNGTQEHTKIRLSVYGALGISQGITVFGYSMAVSIGGIFASRRLHVDLLQ 1054
Cdd:cd18542 2 LLAILALLLATALNLL-IPLLIRRIiDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1055 NVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFNVIGAcIIILLA-----TPIASIIIPPLGLI-YFF 1128
Cdd:cd18542 81 HLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGA-LIIMFSinwklTLISLAIIPFIALFsYVF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1129 ---VQRFYVASSRQLKRLESVsrspvyshFNETLLGVSVIRAF----EEQERFIRQSDLKVDENQKA------YYPSIVA 1195
Cdd:cd18542 160 fkkVRPAFEEIREQEGELNTV--------LQENLTGVRVVKAFaredYEIEKFDKENEEYRDLNIKLakllakYWPLMDF 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953392644 1196 nrwlavrLECVGNCIVLFAALFSVIsRHSLSAG-LVGLSvSYslqvTTYLNWLVRMS----SEMETNIVAVERL 1264
Cdd:cd18542 232 -------LSGLQIVLVLWVGGYLVI-NGEITLGeLVAFI-SY----LWMLIWPVRQLgrliNDMSRASASAERI 292
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1310-1411 |
4.63e-15 |
|
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: 73.84 E-value: 4.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1310 LKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIGLHDLRVKITIIPQDPVLFSG-SLRMNL 1388
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110
....*....|....*....|....*....|
gi 1953392644 1389 -------DPFSQYSDEEVWTSLELAHLKDF 1411
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEKLGLGDL 110
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
602-1418 |
6.45e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 80.46 E-value: 6.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 602 VISSIVQASVSLKRLRIFLSH-----EELEPDS-----IERRPV----KDGG---GANSITVKNATFTW-ARSDPPTLSG 663
Cdd:PTZ00265 324 VISILLGVLISMFMLTIILPNiteymKSLEATNslyeiINRKPLvennDDGKklkDIKKIQFKNVRFHYdTRKDVEIYKD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 664 ITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGS--------------VAYVPQQAWIQNDSLRENILFG 729
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdinlkwwrskIGVVSQDPLLFSNSIKNNIKYS 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 730 -------RQLQERY-------------YKAVIEACA-----------------------LLPDLEI-------------- 752
Cdd:PTZ00265 484 lyslkdlEALSNYYnedgndsqenknkRNSCRAKCAgdlndmsnttdsneliemrknyqTIKDSEVvdvskkvlihdfvs 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 753 -LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDaHVGKHIFENVIGPKGMLKNKTRLLVTHSISY 831
Cdd:PTZ00265 564 aLPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINNLKGNENRITIIIAHRLST 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 832 LPQVDVIIVMT-----------------------------------------------GGKISEMGSYQELLARDGAFAE 864
Cdd:PTZ00265 643 IRYANTIFVLSnrergstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnaGSYIIEQGTHDALMKNKNGIYY 722
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 865 FLRTYASGDQEQAEQDDGLTGVSSPGKEVKQMENGMLVTDVAGKQLQRQLSNSSSYSGDVSRHHTSTAElqkAGPKNEDA 944
Cdd:PTZ00265 723 TMINNQKVSSKKSSNNDNDKDSDMKSSAYKDSERGYDPDEMNGNSKHENESASNKKSCKMSDENASENN---AGGKLPFL 799
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 945 WKLVEADKAQTGQVKLsVY---WDYMKAIGlfISFLSIFLF--LCNHVASLVSNYWLSLWTDDPIVNGTQEHTKIRLSVY 1019
Cdd:PTZ00265 800 RNLFKRKPKAPNNLRI-VYreiFSYKKDVT--IIALSILVAggLYPVFALLYAKYVSTLFDFANLEANSNKYSLYILVIA 876
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1020 GALGISQGITVFgYSMAVsigGIFASRRLHVDLLQNVLRSPMSFFER---TPsGNLVNRFSKELDTVDSMIPQVIKMFMG 1096
Cdd:PTZ00265 877 IAMFISETLKNY-YNNVI---GEKVEKTMKRRLFENILYQEISFFDQdkhAP-GLLSAHINRDVHLLKTGLVNNIVIFTH 951
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1097 SLFNVIGACIIILLATPIASIIippLGLIYFFVQRFYVASSR-------QLKRLESVSRSPVYSH-----------FNET 1158
Cdd:PTZ00265 952 FIVLFLVSMVMSFYFCPIVAAV---LTGTYFIFMRVFAIRARltankdvEKKEINQPGTVFAYNSddeifkdpsflIQEA 1028
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1159 LLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFS--VISRHSLSAGLVGLSVSY 1236
Cdd:PTZ00265 1029 FYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGsfLIRRGTILVDDFMKSLFT 1108
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1237 SLQVTTYLNWLVRMSSEMETNIVAVERLkeYSETEKEAPWQIQE---MAPPSTWPQVGRVEFRDYGLRY--RENLDlVLK 1311
Cdd:PTZ00265 1109 FLFTGSYAGKLMSLKGDSENAKLSFEKY--YPLIIRKSNIDVRDnggIRIKNKNDIKGKIEIMDVNFRYisRPNVP-IYK 1185
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1312 HINITINGGEKVGIVGRTGAGKSSL--------------------------------------TLGLFRINESA------ 1347
Cdd:PTZ00265 1186 DLTFSCDSKKTTAIVGETGSGKSTVmsllmrfydlkndhhivfknehtndmtneqdyqgdeeqNVGMKNVNEFSltkegg 1265
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1348 ----------EGEIIIDDINIAKIGLHDLRVKITIIPQDPVLFSGSLRMNLDpFSQ--YSDEEVWTSLELAHLKDFVSGL 1415
Cdd:PTZ00265 1266 sgedstvfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK-FGKedATREDVKRACKFAAIDEFIESL 1344
|
...
gi 1953392644 1416 PDK 1418
Cdd:PTZ00265 1345 PNK 1347
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
661-850 |
7.29e-15 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 76.23 E-value: 7.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSAL-----LAEMDKVEGHVAIKG---------------SVAYVPQQAwiqN- 719
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndLIPGARVEGEILLDGediydpdvdvvelrrRVGMVFQKP---Np 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 720 --DSLRENILFGRQLQERYYKAVIEA--------CALLPDLEilpsgDRteIGEKGVNLSGGQKQRVSLARAVYCDSDIY 789
Cdd:COG1117 104 fpKSIYDNVAYGLRLHGIKSKSELDEiveeslrkAALWDEVK-----DR--LKKSALGLSGGQQQRLCIARALAVEPEVL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953392644 790 LFDDPLSAVDAHVGKHIfENVIgpkGMLKNK-TRLLVTHS------ISylpqvDVIIVMTGGKISEMG 850
Cdd:COG1117 177 LMDEPTSALDPISTAKI-EELI---LELKKDyTIVIVTHNmqqaarVS-----DYTAFFYLGELVEFG 235
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
644-864 |
8.11e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 76.59 E-value: 8.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGSVaYVPQQAW------- 716
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV-LSEETVWdvrrqvg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 717 --IQN-------DSLRENILFG--------RQLQERYYKAViEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLA 779
Cdd:PRK13635 85 mvFQNpdnqfvgATVQDDVAFGlenigvprEEMVERVDQAL-RQVGMEDFLNREPH-----------RLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 780 RAVYCDSDIYLFDDPLSAVDAhVGKhifENVIGPKGMLKNKTRLLV---THSISYLPQVDVIIVMTGGKISEMGSYQELL 856
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDP-RGR---REVLETVRQLKEQKGITVlsiTHDLDEAAQADRVIVMNKGEILEEGTPEEIF 228
|
....*...
gi 1953392644 857 ARDGAFAE 864
Cdd:PRK13635 229 KSGHMLQE 236
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
642-855 |
1.22e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 75.99 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 642 NSITVKNATFTWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSS---LLSALLAEMDKVEGHVAIKGsVAYVPQQAW-- 716
Cdd:PRK13640 4 NIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDG-ITLTAKTVWdi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 717 -------IQND-------SLRENILFG-------RQLQERYYKAVIEACALLPDLEILPSgdrteigekgvNLSGGQKQR 775
Cdd:PRK13640 83 rekvgivFQNPdnqfvgaTVGDDVAFGlenravpRPEMIKIVRDVLADVGMLDYIDSEPA-----------NLSGGQKQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 776 VSLARAVYCDSDIYLFDDPLSAVDAHVGKHIFENVIgpkgMLKNKTRLLV---THSISYLPQVDVIIVMTGGKISEMGSY 852
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIR----KLKKKNNLTVisiTHDIDEANMADQVLVLDDGKLLAQGSP 227
|
...
gi 1953392644 853 QEL 855
Cdd:PRK13640 228 VEI 230
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
644-864 |
1.23e-14 |
|
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: 76.05 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLaEMDKVEGHVAIKG-------------SVAY 710
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvswnsvplqkwrkAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 711 VPQQAWIQNDSLRENI-LFGRQLQERYYKaVIEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYCDSDIY 789
Cdd:cd03289 82 IPQKVFIFSGTFRKNLdPYGKWSDEEIWK-VAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953392644 790 LFDDPLSAVDAhVGKHIFENVIgpKGMLKNKTRLLVTHSISYLPQVDVIIVMTGGKISEMGSYQELLARDGAFAE 864
Cdd:cd03289 161 LLDEPSAHLDP-ITYQVIRKTL--KQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQ 232
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
643-858 |
1.55e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 76.81 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 643 SITVKNATFTWArSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVAIKGSV-----------AY 710
Cdd:PRK11650 3 GLKLQAVRKSYD-GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLR-MVAGLERItSGEIWIGGRVvnelepadrdiAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 711 VpqqawIQNDSL------RENILFG---R-----QLQERyykaVIEACALLpdlEILPSGDRteigeKGVNLSGGQKQRV 776
Cdd:PRK11650 81 V-----FQNYALyphmsvRENMAYGlkiRgmpkaEIEER----VAEAARIL---ELEPLLDR-----KPRELSGGQRQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 777 SLARAVYCDSDIYLFDDPLSAVDAHVGKHifenvigpkgM---LK------NKTRLLVTHSisylpQV------DVIIVM 841
Cdd:PRK11650 144 AMGRAIVREPAVFLFDEPLSNLDAKLRVQ----------MrleIQrlhrrlKTTSLYVTHD-----QVeamtlaDRVVVM 208
|
250
....*....|....*..
gi 1953392644 842 TGGKISEMGSYQELLAR 858
Cdd:PRK11650 209 NGGVAEQIGTPVEVYEK 225
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
544-856 |
1.72e-14 |
|
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: 79.18 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 544 YLAAVGTFTWVCTPFLVALSTFAVYVTVDKNNILDAQKAFvslalfnILRFPLNILPM----VISSIVQASVSLKRLRIF 619
Cdd:TIGR01271 1104 YLSTLRWFQMRIDIIFVFFFIAVTFIAIGTNQDGEGEVGI-------ILTLAMNILSTlqwaVNSSIDVDGLMRSVSRVF 1176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 620 ----LSHEELEPDS------------IERRPVKD---GGGanSITVKNATFTWARSDPPTLSGITFSIPEGSLVAVVGQV 680
Cdd:TIGR01271 1177 kfidLPQEEPRPSGgggkyqlstvlvIENPHAQKcwpSGG--QMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRT 1254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 681 GCGKSSLLSALLaEMDKVEGHVAIKG-------------SVAYVPQQAWIQNDSLRENILFGRQLQERYYKAVIEACALL 747
Cdd:TIGR01271 1255 GSGKSTLLSALL-RLLSTEGEIQIDGvswnsvtlqtwrkAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLK 1333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 748 PDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAhVGKHIFENVIgpKGMLKNKTRLLVTH 827
Cdd:TIGR01271 1334 SVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDP-VTLQIIRKTL--KQSFSNCTVILSEH 1410
|
330 340
....*....|....*....|....*....
gi 1953392644 828 SISYLPQVDVIIVMTGGKISEMGSYQELL 856
Cdd:TIGR01271 1411 RVEALLECQQFLVIEGSSVKQYDSIQKLL 1439
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1294-1377 |
1.85e-14 |
|
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: 74.04 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1294 EFRDYGLRYRENLDLVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIGLHDLRVKITII 1373
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
....
gi 1953392644 1374 PQDP 1377
Cdd:cd03225 81 FQNP 84
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
644-845 |
2.02e-14 |
|
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: 71.71 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWarSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAI--KGSVAYVPQqawiqnds 721
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWgsTVKIGYFEQ-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 722 lrenilfgrqlqeryykavieacallpdleilpsgdrteigekgvnLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAH 801
Cdd:cd03221 71 ----------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE 104
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1953392644 802 vGKHIFENvigpkgMLKN--KTRLLVTHSISYLPQV-DVIIVMTGGK 845
Cdd:cd03221 105 -SIEALEE------ALKEypGTVILVSHDRYFLDQVaTKIIELEDGK 144
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1313-1427 |
2.10e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 77.96 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1313 INITINGGEKVGIVGRTGAGKSSLT---LGLFrineSAEGEIIIDDINIAKIGLHDLRVKITIIPQDPVLFSGSLRMNL- 1388
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLnalLGFL----PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVl 444
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1953392644 1389 --DPfsQYSDEEVWTSLELAHLKDFVSGLPDKLNQECAEGG 1427
Cdd:PRK11174 445 lgNP--DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQA 483
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1299-1375 |
2.64e-14 |
|
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: 71.89 E-value: 2.64e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953392644 1299 GLRYRENLDLVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIGLHDLRVKITIIPQ 1375
Cdd:cd00267 4 NLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
659-867 |
3.22e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 73.97 E-value: 3.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 659 PTLSGITFSIPEGSLVAVVGQVGCGKSSLLSAL--LAEMD---------KVEGHVA----IKGSVAYVPQQAWI--QNDS 721
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEITsgdlivdglKVNDPKVderlIRQEAGMVFQQFYLfpHLTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 722 LrENILFGRQLQERYYKAVIEACALlpdlEILpsgDRTEIGEKG----VNLSGGQKQRVSLARAVYCDSDIYLFDDPLSA 797
Cdd:PRK09493 95 L-ENVMFGPLRVRGASKEEAEKQAR----ELL---AKVGLAERAhhypSELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953392644 798 VDAHVgKHIFENV---IGPKGMlknkTRLLVTHSISYLPQVDV-IIVMTGGKISEMGSYQELLAR--DGAFAEFLR 867
Cdd:PRK09493 167 LDPEL-RHEVLKVmqdLAEEGM----TMVIVTHEIGFAEKVASrLIFIDKGRIAEDGDPQVLIKNppSQRLQEFLQ 237
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
661-858 |
5.55e-14 |
|
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: 74.70 E-value: 5.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSA---LLAEMDKVEGHVAIKGS-----------------VAYVPQqawiqnD 720
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAilgLLPPPGITSGEILFDGEdllklsekelrkirgreIQMIFQ------D 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 721 ---SLreNILF--GRQLQE--RY---------YKAVIEacaLLPDLEILPSGDRteigekgVN-----LSGGQKQRVSLA 779
Cdd:COG0444 95 pmtSL--NPVMtvGDQIAEplRIhgglskaeaRERAIE---LLERVGLPDPERR-------LDrypheLSGGMRQRVMIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 780 RAVYCDSDIYLFDDPLSAVDAHVGKHIFEnvigpkgMLK------NKTRLLVTHSISYLPQV-DVIIVMTGGKISEMGSY 852
Cdd:COG0444 163 RALALEPKLLIADEPTTALDVTIQAQILN-------LLKdlqrelGLAILFITHDLGVVAEIaDRVAVMYAGRIVEEGPV 235
|
....*.
gi 1953392644 853 QELLAR 858
Cdd:COG0444 236 EELFEN 241
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
661-848 |
7.21e-14 |
|
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: 72.85 E-value: 7.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVAIKG-----------------SVAYVpQQAW--IQND 720
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLG-LLAGLDRPtSGTVRLAGqdlfaldedararlrarHVGFV-FQSFqlLPTL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 721 SLRENI-----LFG-RQLQERYyKAVIEACALLPDLEILPSGdrteigekgvnLSGGQKQRVSLARAVYCDSDIYLFDDP 794
Cdd:COG4181 106 TALENVmlpleLAGrRDARARA-RALLERVGLGHRLDHYPAQ-----------LSGGEQQRVALARAFATEPAILFADEP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953392644 795 LSAVDAHVGKHI----FEnvigpkgmlKNKTR----LLVTHSISYLPQVDVIIVMTGGKISE 848
Cdd:COG4181 174 TGNLDAATGEQIidllFE---------LNRERgttlVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
642-858 |
8.27e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 73.02 E-value: 8.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 642 NSITVKNATFTWArsDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSAL--LAEM---DKVEGHVAIKGS--------- 707
Cdd:PRK14247 2 NKIEIRDLKVSFG--QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELypeARVSGEVYLDGQdifkmdvie 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 708 -------VAYVPQQawIQNDSLRENILFG----------RQLQERYYKAvIEACALLPDLEilpsgDRteIGEKGVNLSG 770
Cdd:PRK14247 80 lrrrvqmVFQIPNP--IPNLSIFENVALGlklnrlvkskKELQERVRWA-LEKAQLWDEVK-----DR--LDAPAGKLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 771 GQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVGKHIFENVIGPKgmlKNKTRLLVTHsisYLPQV----DVIIVMTGGKI 846
Cdd:PRK14247 150 GQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELK---KDMTIVLVTH---FPQQAarisDYVAFLYKGQI 223
|
250
....*....|..
gi 1953392644 847 SEMGSYQELLAR 858
Cdd:PRK14247 224 VEWGPTREVFTN 235
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
643-835 |
9.33e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 73.15 E-value: 9.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 643 SITVKNATFTWarSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSAlLAEMDKVEGHVAIKGSVAYVPQQAW---IQN 719
Cdd:PRK14258 7 AIKVNNLSFYY--DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGRVEFFNQNIYerrVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 720 DSLRENI--------LFGRQLqeryYKAVIEACALL---PDLEI-------LPSGD-----RTEIGEKGVNLSGGQKQRV 776
Cdd:PRK14258 84 NRLRRQVsmvhpkpnLFPMSV----YDNVAYGVKIVgwrPKLEIddivesaLKDADlwdeiKHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1953392644 777 SLARAVYCDSDIYLFDDPLSAVDAHVGKHIfENVIGPKGMLKNKTRLLVTHSisyLPQV 835
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKV-ESLIQSLRLRSELTMVIVSHN---LHQV 214
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
657-854 |
1.77e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 71.28 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 657 DPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGS-------------VAYVPQQAWIQNDSLR 723
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdistlkpeiyrqqVSYCAQTPTLFGDTVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 724 ENILFGRQLQeryyKAVIEACALLPDLEI--LPSgdrtEIGEKGVN-LSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDA 800
Cdd:PRK10247 99 DNLIFPWQIR----NQQPDPAIFLDDLERfaLPD----TILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1953392644 801 HvGKHIFENVIGPKGMLKNKTRLLVTHSISYLPQVDVIIVMTggkiSEMGSYQE 854
Cdd:PRK10247 171 S-NKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQ----PHAGEMQE 219
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1293-1377 |
2.26e-13 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 71.00 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1293 VEFRDYGLRYRENLDLV--LKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIGLHDLRV-- 1368
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIrr 81
|
90
....*....|
gi 1953392644 1369 -KITIIPQDP 1377
Cdd:cd03257 82 kEIQMVFQDP 91
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1294-1387 |
2.31e-13 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 69.55 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1294 EFRDYGLRYRENLDLVLKHINITINGGEKVGIVGRTGAGKSSLT---LGLFRineSAEGEIIIDDINIAKIGLHDLRVKI 1370
Cdd:cd03246 2 EVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLArliLGLLR---PTSGRVRLDGADISQWDPNELGDHV 78
|
90
....*....|....*..
gi 1953392644 1371 TIIPQDPVLFSGSLRMN 1387
Cdd:cd03246 79 GYLPQDDELFSGSIAEN 95
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
644-858 |
2.37e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 73.19 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWARSDPPT--LSGITFSIPEGSLVAVVGQVGCGKSSLLS--ALLAEMDkvEGHVAIKG------------- 706
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRciNLLERPT--SGSVLVDGvdltalserelra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 707 ---SVAYVPQQAwiqndSL------RENILFGRQLQeRYYKAVIEACALlpdlEILpsgDRTEIGEKG----VNLSGGQK 773
Cdd:COG1135 80 arrKIGMIFQHF-----NLlssrtvAENVALPLEIA-GVPKAEIRKRVA----ELL---ELVGLSDKAdaypSQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 774 QRVSLARAVYCDSDIYLFDDPLSAVDAHVGKHIFEnvigpkgMLK--NK----TRLLVTHsisylpQVDVI--I-----V 840
Cdd:COG1135 147 QRVGIARALANNPKVLLCDEATSALDPETTRSILD-------LLKdiNRelglTIVLITH------EMDVVrrIcdrvaV 213
|
250
....*....|....*...
gi 1953392644 841 MTGGKISEMGSYQELLAR 858
Cdd:COG1135 214 LENGRIVEQGPVLDVFAN 231
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
642-855 |
2.45e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 72.09 E-value: 2.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 642 NSITVKNATFTWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVaikgsvaYVPQQAwIQNDS 721
Cdd:PRK13648 6 SIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI-------FYNNQA-ITDDN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 722 LRE-----------------------NILFGRQLQERYYKAVIEACA-LLPDLEILPSGDrteigEKGVNLSGGQKQRVS 777
Cdd:PRK13648 78 FEKlrkhigivfqnpdnqfvgsivkyDVAFGLENHAVPYDEMHRRVSeALKQVDMLERAD-----YEPNALSGGQKQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953392644 778 LARAVYCDSDIYLFDDPLSAVDAHVGKHIFENVIGPKGMlKNKTRLLVTHSISYLPQVDVIIVMTGGKISEMGSYQEL 855
Cdd:PRK13648 153 IAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSE-HNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
644-859 |
2.55e-13 |
|
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: 71.16 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFtwARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-SVAYVPQQAWI----- 717
Cdd:COG1127 6 IEVRNLTK--SFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqDITGLSEKELYelrrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 718 -----QN----DSL--RENILFGrqLQERY-------YKAVIEACAL--LPDLEIL-PSgdrteigEkgvnLSGGQKQRV 776
Cdd:COG1127 84 igmlfQGgalfDSLtvFENVAFP--LREHTdlseaeiRELVLEKLELvgLPGAADKmPS-------E----LSGGMRKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 777 SLARAVYCDSDIYLFDDPLSAVDAhVGKHIFENVIgpkgmLK-----NKTRLLVTHSISYLPQV-DVIIVMTGGKISEMG 850
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDP-ITSAVIDELI-----RElrdelGLTSVVVTHDLDSAFAIaDRVAVLADGKIIAEG 224
|
....*....
gi 1953392644 851 SYQELLARD 859
Cdd:COG1127 225 TPEELLASD 233
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
644-857 |
2.69e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 71.94 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWArSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGSVAYVPQQAW------- 716
Cdd:PRK13644 2 IRLENVSYSYP-DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQgirklvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 717 --IQNDslrENILFGRQLQERYYKAVIEACalLPDLEILPSGDRT--EIG-EK-----GVNLSGGQKQRVSLARAVYCDS 786
Cdd:PRK13644 81 ivFQNP---ETQFVGRTVEEDLAFGPENLC--LPPIEIRKRVDRAlaEIGlEKyrhrsPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953392644 787 DIYLFDDPLSAVDAHVGKHIFENVigPKGMLKNKTRLLVTHSISYLPQVDVIIVMTGGKISEMGSYQELLA 857
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERI--KKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
661-856 |
2.73e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 71.41 E-value: 2.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSAL-----LAEMDKVEGHVAIKGSVAYVPQQAWIQ----------------N 719
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDVDPIEvrrevgmvfqypnpfpH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 720 DSLRENILFG----------RQLQERYYKAVIEAcALLPDLEilpsgDRteIGEKGVNLSGGQKQRVSLARAVYCDSDIY 789
Cdd:PRK14267 100 LTIYDNVAIGvklnglvkskKELDERVEWALKKA-ALWDEVK-----DR--LNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953392644 790 LFDDPLSAVDAHVGKHIFENVIGPKgmlKNKTRLLVTHSISYLPQV-DVIIVMTGGKISEMGSYQELL 856
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELK---KEYTIVLVTHSPAQAARVsDYVAFLYLGKLIEVGPTRKVF 236
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
657-854 |
2.73e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 73.44 E-value: 2.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 657 DPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVAIKG-SVAYVPQQ-----------AWIQNDSLR 723
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLR-LIAGFETPdSGRIMLDGqDITHVPAEnrhvntvfqsyALFPHMTVF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 724 ENILFGRQLQER----YYKAVIEACALLpDLEILpsGDRteigeKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVD 799
Cdd:PRK09452 105 ENVAFGLRMQKTpaaeITPRVMEALRMV-QLEEF--AQR-----KPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 800 AHVGKHifenvigpkgM---LKNKTRLL------VTH------SISylpqvDVIIVMTGGKISEMGSYQE 854
Cdd:PRK09452 177 YKLRKQ----------MqneLKALQRKLgitfvfVTHdqeealTMS-----DRIVVMRDGRIEQDGTPRE 231
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
661-850 |
3.07e-13 |
|
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: 70.64 E-value: 3.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVAIKGSVAYVPQ-QAWIQND-SLRENILF-GR--QLQE 734
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLR-LLAGIYPPdSGTVTVRGRVSSLLGlGGGFNPElTGRENIYLnGRllGLSR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 735 RYYKAVIEacallpdlEILpsgDRTEIGEKG----VNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAH----VGKHI 806
Cdd:cd03220 117 KEIDEKID--------EII---EFSELGDFIdlpvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfqekCQRRL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1953392644 807 FEnvigpkgMLKN-KTRLLVTHSISYLPQV-DVIIVMTGGKISEMG 850
Cdd:cd03220 186 RE-------LLKQgKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
652-794 |
4.13e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.56 E-value: 4.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 652 TWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG--SVAYVPQQAWIQND-SLRENILF 728
Cdd:COG0488 5 SKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLDDDlTVLDTVLD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 729 G----RQLQERYYKAVI-----------------------------EACALLPDLEILPSGDRTEIGEkgvnLSGGQKQR 775
Cdd:COG0488 85 GdaelRALEAELEELEAklaepdedlerlaelqeefealggweaeaRAEEILSGLGFPEEDLDRPVSE----LSGGWRRR 160
|
170
....*....|....*....
gi 1953392644 776 VSLARAVYCDSDIYLFDDP 794
Cdd:COG0488 161 VALARALLSEPDLLLLDEP 179
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
654-811 |
4.36e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.90 E-value: 4.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 654 ARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLL---SALLAemdKVEGHVAIKG----------SVAYV-PQQAWIQN 719
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLrliAGLLP---PAAGTIKLDGgdiddpdvaeACHYLgHRNAMKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 720 DSLRENILFGRQLQERYYKAVIEA-CAL-LPDLEILPSGdrteigekgvNLSGGQKQRVSLARAVYCDSDIYLFDDPLSA 797
Cdd:PRK13539 88 LTVAENLEFWAAFLGGEELDIAAAlEAVgLAPLAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170
....*....|....
gi 1953392644 798 VDAHvGKHIFENVI 811
Cdd:PRK13539 158 LDAA-AVALFAELI 170
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
979-1179 |
4.99e-13 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 71.30 E-value: 4.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 979 IFLFLCNHVASLVSnyWLSLWTDDPIVNGTQEHTKIRLSVYGALGI-----SQGITVFGYSMAVSIGGIFASRRLHVDLL 1053
Cdd:cd18552 2 ALAILGMILVAATT--AALAWLLKPLLDDIFVEKDLEALLLVPLAIiglflLRGLASYLQTYLMAYVGQRVVRDLRNDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1054 QNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFNVIGaCIIILLA-----TPIASIIIPPLGL-IYF 1127
Cdd:cd18552 80 DKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIG-LLGVLFYldwklTLIALVVLPLAALpIRR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1953392644 1128 FVQRFYVASSRQLKRLESVSrspvySHFNETLLGVSVIRAF----EEQERFIRQSD 1179
Cdd:cd18552 159 IGKRLRKISRRSQESMGDLT-----SVLQETLSGIRVVKAFgaedYEIKRFRKANE 209
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
661-855 |
5.46e-13 |
|
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: 70.19 E-value: 5.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVAIKGSVAYVP---QQAWIQNDSL------RENILFG- 729
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLN-LISGLAQpTSGGVILEGKQITEPgpdRMVVFQNYSLlpwltvRENIALAv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 730 ----RQLQERYYKAVIEACALLPDLeilpsgdrTEIGEKGVN-LSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVgk 804
Cdd:TIGR01184 80 drvlPDLSKSERRAIVEEHIALVGL--------TEAADKRPGqLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT-- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953392644 805 hifenvigpKGMLKNK----------TRLLVTHSI-SYLPQVDVIIVMTGGKISEMGSYQEL 855
Cdd:TIGR01184 150 ---------RGNLQEElmqiweehrvTVLMVTHDVdEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
644-855 |
5.52e-13 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 70.40 E-value: 5.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWArSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG----------------S 707
Cdd:TIGR02315 2 LEVENLSKVYP-NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGtditklrgkklrklrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 708 VAYVPQQ-AWIQNDSLRENILFGRQlqerYYKAVIEAC-ALLPDLEI---LPSGDRTEIGEKGV----NLSGGQKQRVSL 778
Cdd:TIGR02315 81 IGMIFQHyNLIERLTVLENVLHGRL----GYKPTWRSLlGRFSEEDKeraLSALERVGLADKAYqradQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 779 ARAVYCDSDIYLFDDPLSAVD---AHVGKHIFENVIGPKGmlknKTRLLVTHSISYLPQ-VDVIIVMTGGKISEMGSYQE 854
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDpktSKQVMDYLKRINKEDG----ITVIINLHQVDLAKKyADRIVGLKAGEIVFDGAPSE 232
|
.
gi 1953392644 855 L 855
Cdd:TIGR02315 233 L 233
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
643-850 |
5.82e-13 |
|
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: 69.12 E-value: 5.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 643 SITVKNATFT----WARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSAL--LAEMDKVEGHVAIKG---------- 706
Cdd:cd03213 3 TLSFRNLTVTvkssPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGrpldkrsfrk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 707 SVAYVPQQ-AWIQNDSLRENILFGRQLQeryykavieacallpdleilpsgdrteigekgvNLSGGQKQRVSLARAVYCD 785
Cdd:cd03213 83 IIGYVPQDdILHPTLTVRETLMFAAKLR---------------------------------GLSGGERKRVSIALELVSN 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953392644 786 SDIYLFDDPLSAVDAHVGKHIFEnvigpkgMLK-----NKTRLLVTHSISYL--PQVDVIIVMTGGKISEMG 850
Cdd:cd03213 130 PSLLFLDEPTSGLDSSSALQVMS-------LLRrladtGRTIICSIHQPSSEifELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
641-859 |
6.55e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 70.92 E-value: 6.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 641 ANSITVKNATFTWaRSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGSVAYVPQQAWIQNd 720
Cdd:PRK13647 2 DNIIEVEDLHFRY-KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 721 slRENILFGRQLQERYYKAVIEACALLP-DLEILPS--GDRTEIGEKGVN-----------LSGGQKQRVSLARAVYCDS 786
Cdd:PRK13647 80 --KVGLVFQDPDDQVFSSTVWDDVAFGPvNMGLDKDevERRVEEALKAVRmwdfrdkppyhLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953392644 787 DIYLFDDPLSAVDAHVGKHIFE--NVIGPKGmlknKTRLLVTHSISYLPQ-VDVIIVMTGGKISEMGSyQELLARD 859
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEilDRLHNQG----KTVIVATHDVDLAAEwADQVIVLKEGRVLAEGD-KSLLTDE 228
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
644-862 |
8.97e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 71.80 E-value: 8.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTwaRSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-------------SVAY 710
Cdd:PRK09536 4 IDVSDLSVE--FGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraasrRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 711 VPQQAWIQND-SLRENILFGR--------QLQERYYKAVIEAcallpdleiLPSGDRTEIGEKGV-NLSGGQKQRVSLAR 780
Cdd:PRK09536 82 VPQDTSLSFEfDVRQVVEMGRtphrsrfdTWTETDRAAVERA---------MERTGVAQFADRPVtSLSGGERQRVLLAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 781 AVYCDSDIYLFDDPLSAVDAHVGKHIFENV--IGPKGmlknKTRLLVTHSISYLPQ-VDVIIVMTGGKISEMGSYQELLA 857
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQVRTLELVrrLVDDG----KTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLT 228
|
....*...
gi 1953392644 858 RD---GAF 862
Cdd:PRK09536 229 ADtlrAAF 236
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
627-856 |
1.06e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 71.02 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 627 PDSIERRPvkdgGGANSITVKNATFTWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG 706
Cdd:PRK13536 27 SEAKASIP----GSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 707 svAYVPQQAWI---------QNDSL------RENIL-FGR--QLQERYYKAVIEAcalLPDLEILPSGDRTEIGEkgvnL 768
Cdd:PRK13536 103 --VPVPARARLararigvvpQFDNLdleftvRENLLvFGRyfGMSTREIEAVIPS---LLEFARLESKADARVSD----L 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 769 SGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVGKHIFENVigpKGML-KNKTRLLVTHSISYLPQV-DVIIVMTGG-K 845
Cdd:PRK13536 174 SGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERL---RSLLaRGKTILLTTHFMEEAERLcDRLCVLEAGrK 250
|
250
....*....|.
gi 1953392644 846 ISEmGSYQELL 856
Cdd:PRK13536 251 IAE-GRPHALI 260
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
659-800 |
1.24e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 69.73 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 659 PTLSGITFSIPEGSLVAVVGQVGCGKSSLLSaLLA------------EMDKVEGHVAIKGSVayvpqqawIQNDSL---- 722
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLN-LIAgfvpyqhgsitlDGKPVEGPGAERGVV--------FQNEGLlpwr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 723 --RENILFGRQLQ-----ERYYKAvieacallpdLEILPSGDRTEIGEKGV-NLSGGQKQRVSLARAVYCDSDIYLFDDP 794
Cdd:PRK11248 86 nvQDNVAFGLQLAgvekmQRLEIA----------HQMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
....*.
gi 1953392644 795 LSAVDA 800
Cdd:PRK11248 156 FGALDA 161
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
659-857 |
1.32e-12 |
|
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: 68.61 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 659 PTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGS--------------VAYVPQ-QAWIQNDSLR 723
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEgRRIFPELTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 724 ENILFGRQLQERY-YKAVIE-ACALLPDLEilpsgDRteIGEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDP---LSAV 798
Cdd:cd03224 94 ENLLLGAYARRRAkRKARLErVYELFPRLK-----ER--RKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPsegLAPK 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953392644 799 dahVGKHIFENV--IGPKGMlknkTRLLVTHSISYLPQV-DVIIVMTGGKISEMGSYQELLA 857
Cdd:cd03224 167 ---IVEEIFEAIreLRDEGV----TILLVEQNARFALEIaDRAYVLERGRVVLEGTAAELLA 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
656-877 |
1.33e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.97 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 656 SDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGS--------------VAYVP----QQAWI 717
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprdairagIAYVPedrkGEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 718 QNDSLRENI------------LFGRQLQERYYKAVIEacallpDLEILPSGDRTEIGekgvNLSGGQKQRVSLARAVYCD 785
Cdd:COG1129 343 LDLSIRENItlasldrlsrggLLDRRRERALAEEYIK------RLRIKTPSPEQPVG----NLSGGNQQKVVLAKWLATD 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 786 SDIYLFDDPLSAVDahVG-KHIFENVIgpkGML--KNKTRLLVThsiSYLPQV----DVIIVMTGGKISEMgsyqelLAR 858
Cdd:COG1129 413 PKVLILDEPTRGID--VGaKAEIYRLI---RELaaEGKAVIVIS---SELPELlglsDRILVMREGRIVGE------LDR 478
|
250
....*....|....*....
gi 1953392644 859 DGAFAEFLRTYASGDQEQA 877
Cdd:COG1129 479 EEATEEAIMAAATGGAAAA 497
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
643-866 |
1.36e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 69.27 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 643 SITVKNATFTWARSDppTLSGITFSIPEGSLVAVVGQVGCGKSSLLSAL-LAEMDKvEGHVAIKGS-------------- 707
Cdd:PRK11124 2 SIQLNGINCFYGAHQ--ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEMPR-SGTLNIAGNhfdfsktpsdkair 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 708 -----VAYVPQQ--AW-----IQNdsLRE---NILfGRQLQEryykAVIEACALLPDLEILPSGDRTEIgekgvNLSGGQ 772
Cdd:PRK11124 79 elrrnVGMVFQQynLWphltvQQN--LIEapcRVL-GLSKDQ----ALARAEKLLERLRLKPYADRFPL-----HLSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 773 KQRVSLARAVYCDSDIYLFDDPLSAVD----AHVGKHIFEnvIGPKGMlknkTRLLVTHSISYLPQVDVIIV-MTGGKIS 847
Cdd:PRK11124 147 QQRVAIARALMMEPQVLLFDEPTAALDpeitAQIVSIIRE--LAETGI----TQVIVTHEVEVARKTASRVVyMENGHIV 220
|
250 260
....*....|....*....|
gi 1953392644 848 EMGSYQELLA-RDGAFAEFL 866
Cdd:PRK11124 221 EQGDASCFTQpQTEAFKNYL 240
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
661-846 |
1.60e-12 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 68.45 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSAL---LAEMDKVEGHVAIKG----------SVAYVPQQ-AWIQNDSLRENI 726
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNGqprkpdqfqkCVAYVRQDdILLPGLTVRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 727 LFGRQLQERY-----YKAVIEACALLPDLEILPSGdrteiGEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAH 801
Cdd:cd03234 103 TYTAILRLPRkssdaIRKKRVEDVLLRDLALTRIG-----GNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1953392644 802 VGKHIFEnvigpkgMLK-----NKTRLLVTHSisylPQVDV------IIVMTGGKI 846
Cdd:cd03234 178 TALNLVS-------TLSqlarrNRIVILTIHQ----PRSDLfrlfdrILLLSSGEI 222
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
644-801 |
2.57e-12 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 68.60 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTwaRSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-------------SVAY 710
Cdd:COG4559 2 LEAENLSVR--LGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGrplaawspwelarRRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 711 VPQQAWIQND-SLRENILFGR---QLQERYYKAVIEACALLPDLEILPSGDRTEigekgvnLSGGQKQRVSLARA---VY 783
Cdd:COG4559 80 LPQHSSLAFPfTVEEVVALGRaphGSSAAQDRQIVREALALVGLAHLAGRSYQT-------LSGGEQQRVQLARVlaqLW 152
|
170 180
....*....|....*....|...
gi 1953392644 784 CDSDI---YLF-DDPLSAVD-AH 801
Cdd:COG4559 153 EPVDGgprWLFlDEPTSALDlAH 175
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
644-857 |
2.72e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 68.97 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWAR-SDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGSvAYVPQQAW------ 716
Cdd:PRK13642 5 LEVENLVFKYEKeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE-LLTAENVWnlrrki 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 717 ---IQND-------SLRENILFGRQLQ----ERYYKAVIEAcalLPDLEILPSGDRteigeKGVNLSGGQKQRVSLARAV 782
Cdd:PRK13642 84 gmvFQNPdnqfvgaTVEDDVAFGMENQgiprEEMIKRVDEA---LLAVNMLDFKTR-----EPARLSGGQKQRVAVAGII 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953392644 783 YCDSDIYLFDDPLSAVDAhVGKHIFENVIGPKGMLKNKTRLLVTHSISYLPQVDVIIVMTGGKISEMGSYQELLA 857
Cdd:PRK13642 156 ALRPEIIILDESTSMLDP-TGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
660-829 |
3.08e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 68.26 E-value: 3.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 660 TLSGITFSIPEGSLVAVVGQVGCGKSSLLSALlAEMDKVEGHVAIKGSVAY---------------------VPQQAWIQ 718
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSI-NRMNDLNPEVTITGSIVYnghniysprtdtvdlrkeigmVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 719 NDSLRENILFGRQLQERYYKAVIEAcALLPDLEILPSGD--RTEIGEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLS 796
Cdd:PRK14239 99 PMSIYENVVYGLRLKGIKDKQVLDE-AVEKSLKGASIWDevKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
170 180 190
....*....|....*....|....*....|....
gi 1953392644 797 AVDAHVGKHIFENVIGpkgmLKNK-TRLLVTHSI 829
Cdd:PRK14239 178 ALDPISAGKIEETLLG----LKDDyTMLLVTRSM 207
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
644-850 |
3.08e-12 |
|
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: 67.22 E-value: 3.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWARSDppTLSGITFSIPEGsLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGS------------VAYV 711
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqpqklrrrIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 712 PQQ-AWIQNDSLRENIlfgrqlqerYYKAVI----------EACALLPDLEILPSGDRtEIGEkgvnLSGGQKQRVSLAR 780
Cdd:cd03264 78 PQEfGVYPNFTVREFL---------DYIAWLkgipskevkaRVDEVLELVNLGDRAKK-KIGS----LSGGMRRRVGIAQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953392644 781 AVYCDSDIYLFDDPLSAVDAhVGKHIFENVIGPKGmlKNKTRLLVTHSISylpqvDV------IIVMTGGKISEMG 850
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDP-EERIRFRNLLSELG--EDRIVILSTHIVE-----DVeslcnqVAVLNKGKLVFEG 211
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
643-856 |
4.81e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 67.73 E-value: 4.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 643 SITVKNATFTWArsDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-------------SVA 709
Cdd:PRK11231 2 TLRTENLTVGYG--TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 710 YVPQQAWIQND-SLRENILFGR--------QLQERYYKAVIEAcalLPDLEIlpsgdrTEIGEKGV-NLSGGQKQRVSLA 779
Cdd:PRK11231 80 LLPQHHLTPEGiTVRELVAYGRspwlslwgRLSAEDNARVNQA---MEQTRI------NHLADRRLtDLSGGQRQRAFLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 780 RAVYCDSDIYLFDDPLSAVDAHvgkHIFEnVIGPKGMLKN--KTRLLVTHSIS----YlpqVDVIIVMTGGKISEMGSYQ 853
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDIN---HQVE-LMRLMRELNTqgKTVVTVLHDLNqasrY---CDHLVVLANGHVMAQGTPE 223
|
...
gi 1953392644 854 ELL 856
Cdd:PRK11231 224 EVM 226
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
976-1263 |
5.42e-12 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 68.20 E-value: 5.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 976 FLSIFLFLCNHVASLVSNYWLSLWTDDpIVNGTQEHTKIRLS-----------VYGALGISQgiTVFGYSMAVSIGGIfa 1044
Cdd:cd18547 2 ILVIILAIISTLLSVLGPYLLGKAIDL-IIEGLGGGGGVDFSgllrilllllgLYLLSALFS--YLQNRLMARVSQRT-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1045 SRRLHVDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFNVIGAcIIILLAT--PIASIIIPPL 1122
Cdd:cd18547 77 VYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGT-LIMMLYIspLLTLIVLVTV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1123 GLIYFFV-------QRFYVASSRQLKRLEsvsrspvySHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIVA 1195
Cdd:cd18547 156 PLSLLVTkfiakrsQKYFRKQQKALGELN--------GYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFY 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953392644 1196 NRWL--AVRLecVGN----CIVLFAALFSVisRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVER 1263
Cdd:cd18547 228 SGLLmpIMNF--INNlgyvLVAVVGGLLVI--NGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAER 297
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
643-854 |
5.59e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 68.15 E-value: 5.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 643 SITVKNATFTWARSDP---PTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG------------- 706
Cdd:PRK13637 2 SIKIENLTHIYMEGTPfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 707 --SVAYVPQQAWIQ--NDSLRENILFG-RQL---QERYYKAVIEACALLpdleilpsG-DRTEIGEKG-VNLSGGQKQRV 776
Cdd:PRK13637 82 rkKVGLVFQYPEYQlfEETIEKDIAFGpINLglsEEEIENRVKRAMNIV--------GlDYEDYKDKSpFELSGGQKRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 777 SLARAVYCDSDIYLFDDPLSAVDAHVGKHIFENVigpKGMLK--NKTRLLVTHSISYLPQ-VDVIIVMTGGKISEMGSYQ 853
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDPKGRDEILNKI---KELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPR 230
|
.
gi 1953392644 854 E 854
Cdd:PRK13637 231 E 231
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
644-858 |
9.59e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 67.34 E-value: 9.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWARSDP---PTLSGITFSIPEGSLVAVVGQVGCGKSSLLS------------------ALLAEMDKVEGHV 702
Cdd:PRK13645 7 IILDNVSYTYAKKTPfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQltngliisetgqtivgdyAIPANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 703 AIKGSVAYV---PQQAWIQnDSLRENILFGR----QLQERYYKAVIEacalLPDLEILPsgdRTEIGEKGVNLSGGQKQR 775
Cdd:PRK13645 87 RLRKEIGLVfqfPEYQLFQ-ETIEKDIAFGPvnlgENKQEAYKKVPE----LLKLVQLP---EDYVKRSPFELSGGQKRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 776 VSLARAVYCDSDIYLFDDPLSAVDAHvGKHIFENVIGPKGMLKNKTRLLVTHSISYLPQV-DVIIVMTGGKISEMG---- 850
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPK-GEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIaDEVIVMHEGKVISIGspfe 237
|
250
....*....|
gi 1953392644 851 --SYQELLAR 858
Cdd:PRK13645 238 ifSNQELLTK 247
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
661-846 |
1.00e-11 |
|
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: 64.76 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGSvayvPQQAWIQNDSLRENILFGRQLqeryykav 740
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK----EVSFASPRDARRAGIAMVYQL-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 741 ieacallpdleilpsgdrteigekgvnlSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVGKHIFEnVIgpkGMLKN- 819
Cdd:cd03216 84 ----------------------------SVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK-VI---RRLRAq 131
|
170 180
....*....|....*....|....*....
gi 1953392644 820 -KTRLLVTHSISYLPQV-DVIIVMTGGKI 846
Cdd:cd03216 132 gVAVIFISHRLDEVFEIaDRVTVLRDGRV 160
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
661-880 |
1.08e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 66.73 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSAL-----LAEMDKVEGHVAIKGSVAYVP---------------QQAWIQND 720
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrlndLIPGFRVEGKVTFHGKNLYAPdvdpvevrrrigmvfQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 721 SLRENILFG----------RQLQERYYKAvieacALLPDlEIlpsgdRTEIGEKGVNLSGGQKQRVSLARAVYCDSDIYL 790
Cdd:PRK14243 106 SIYDNIAYGaringykgdmDELVERSLRQ-----AALWD-EV-----KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 791 FDDPLSAVDAHVGKHIFENVigpKGMLKNKTRLLVTHSISYLPQVDVIIVMTGGKISEMGSyqellaRDGAFAEFLRTYA 870
Cdd:PRK14243 175 MDEPCSALDPISTLRIEELM---HELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGG------RYGYLVEFDRTEK 245
|
250
....*....|..
gi 1953392644 871 --SGDQEQAEQD 880
Cdd:PRK14243 246 ifNSPQQQATRD 257
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
656-846 |
1.35e-11 |
|
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: 64.76 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 656 SDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGS--------------VAYVP----QQAWI 717
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtrrsprdairagIAYVPedrkREGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 718 QNDSLRENILFGRQLqeryykavieacallpdleilpsgdrteigekgvnlSGGQKQRVSLARAVYCDSDIYLFDDPLSA 797
Cdd:cd03215 91 LDLSVAENIALSSLL------------------------------------SGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1953392644 798 VDahVG--KHIFENVIGPKGmlKNKTRLLVThsiSYLPQV----DVIIVMTGGKI 846
Cdd:cd03215 135 VD--VGakAEIYRLIRELAD--AGKAVLLIS---SELDELlglcDRILVMYEGRI 182
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1293-1377 |
1.50e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 66.55 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1293 VEFRDYGLRYRENLDLVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIGLHDLRVKITI 1372
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
....*
gi 1953392644 1373 IPQDP 1377
Cdd:PRK13632 88 IFQNP 92
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
659-800 |
1.97e-11 |
|
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: 65.12 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 659 PTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-SVAYVPQQA----------------WIQNDS 721
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqDVSDLRGRAipylrrkigvvfqdfrLLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 722 LRENILF--------GRQLQERyYKAVIEACALLPDLEILPSGdrteigekgvnLSGGQKQRVSLARAVYCDSDIYLFDD 793
Cdd:cd03292 95 VYENVAFalevtgvpPREIRKR-VPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIADE 162
|
....*..
gi 1953392644 794 PLSAVDA 800
Cdd:cd03292 163 PTGNLDP 169
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
643-855 |
2.22e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 67.36 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 643 SITVKNATFTWArsDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAI-----------KGSVAYV 711
Cdd:PRK11000 3 SVTLRNVTKAYG--DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIgekrmndvppaERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 712 PQQ-AWIQNDSLRENILFGRQL----QERYYKAVIEACALLPDLEILpsgDRteigeKGVNLSGGQKQRVSLARAVYCDS 786
Cdd:PRK11000 81 FQSyALYPHLSVAENMSFGLKLagakKEEINQRVNQVAEVLQLAHLL---DR-----KPKALSGGQRQRVAIGRTLVAEP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953392644 787 DIYLFDDPLSAVDA--HVGKHIfenVIGPKGMLKNKTRLLVTH-SISYLPQVDVIIVMTGGKISEMGSYQEL 855
Cdd:PRK11000 153 SVFLLDEPLSNLDAalRVQMRI---EISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
652-800 |
2.39e-11 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 64.69 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 652 TWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG------------SVAYVPQQAWIQN 719
Cdd:TIGR01189 7 ACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtplaeqrdepheNILYLGHLPGLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 720 D-SLRENILFGRQLQERYYKAVIEACAL--LPDLEILPSGdrteigekgvNLSGGQKQRVSLARAVYCDSDIYLFDDPLS 796
Cdd:TIGR01189 87 ElSALENLHFWAAIHGGAQRTIEDALAAvgLTGFEDLPAA----------QLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
....
gi 1953392644 797 AVDA 800
Cdd:TIGR01189 157 ALDK 160
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1294-1375 |
2.40e-11 |
|
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: 63.99 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1294 EFRDYGLRYRENLdlVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIGLHDLRVKITII 1373
Cdd:cd03214 1 EVENLSVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
..
gi 1953392644 1374 PQ 1375
Cdd:cd03214 79 PQ 80
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
643-857 |
2.67e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 65.63 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 643 SITVKNATFTWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLlSALLAEMDK-------VEGHVAIKGSVAYVPQQa 715
Cdd:COG4167 11 SKTFKYRTGLFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTL-AKMLAGIIEptsgeilINGHKLEYGDYKYRCKH- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 716 wIQ------NDSLRENILFGRQL------------QERYYK--AVIEACALLPD-LEILPSgdrteigekgvNLSGGQKQ 774
Cdd:COG4167 89 -IRmifqdpNTSLNPRLNIGQILeeplrlntdltaEEREERifATLRLVGLLPEhANFYPH-----------MLSSGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 775 RVSLARAVYCDSDIYLFDDPLSAVDAHVGKHIFeNVigpkgMLKNKTRL-----LVTHS------ISylpqvDVIIVMTG 843
Cdd:COG4167 157 RVALARALILQPKIIIADEALAALDMSVRSQII-NL-----MLELQEKLgisyiYVSQHlgivkhIS-----DKVLVMHQ 225
|
250
....*....|....
gi 1953392644 844 GKISEMGSYQELLA 857
Cdd:COG4167 226 GEVVEYGKTAEVFA 239
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
644-858 |
3.29e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 65.81 E-value: 3.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWARSDP---PTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIkGSVAYVPQQAWIQND 720
Cdd:PRK13634 3 ITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 721 SLRE--------------------NILFG-------RQLQERYYKAVIEACALLPDLEilpsgDRTEIgekgvNLSGGQK 773
Cdd:PRK13634 82 PLRKkvgivfqfpehqlfeetvekDICFGpmnfgvsEEDAKQKAREMIELVGLPEELL-----ARSPF-----ELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 774 QRVSLARAVYCDSDIYLFDDPLSAVDAHVGKHI---FENVIGPKGMlknkTRLLVTHSISYLPQ-VDVIIVMTGGKISEM 849
Cdd:PRK13634 152 RRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMmemFYKLHKEKGL----TTVLVTHSMEDAARyADQIVVMHKGTVFLQ 227
|
....*....
gi 1953392644 850 GSYQELLAR 858
Cdd:PRK13634 228 GTPREIFAD 236
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1293-1377 |
4.18e-11 |
|
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: 67.24 E-value: 4.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1293 VEFRDYGLRYRENLDLVLKHINITINGGEKVGIVGRTGAGKSSLTL---GLFRINESAEGEIIIDDINIAKIGLHDLRVK 1369
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALalmGLLPHGGRISGEVLLDGRDLLELSEALRGRR 84
|
....*...
gi 1953392644 1370 ITIIPQDP 1377
Cdd:COG1123 85 IGMVFQDP 92
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1293-1376 |
4.53e-11 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 64.30 E-value: 4.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1293 VEFRDYGLRYRENLDlVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKI---GLHDLRVK 1369
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
....*..
gi 1953392644 1370 ITIIPQD 1376
Cdd:COG2884 81 IGVVFQD 87
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1310-1377 |
5.46e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 65.07 E-value: 5.46e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1310 LKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIA--KIGLHDLRVKITIIPQDP 1377
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQYP 92
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
644-862 |
5.57e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 65.49 E-value: 5.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWARSDP---PTLSGITFSIPEGSLVAVVGQVGCGKSSL---LSALL--------------------AEMDK 697
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtelKALDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALLlpdtgtiewifkdeknkkktKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 698 VEGHVAIKGS--------------VAYVPQQAWIQ--NDSLRENILFG-------RQLQERYYKAVIEACALlpDLEILP 754
Cdd:PRK13651 83 VLEKLVIQKTrfkkikkikeirrrVGVVFQFAEYQlfEQTIEKDIIFGpvsmgvsKEEAKKRAAKYIELVGL--DESYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 755 sgdrteigEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVGKHIFEnvIGPKGMLKNKTRLLVTHSI-SYLP 833
Cdd:PRK13651 161 --------RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLNKQGKTIILVTHDLdNVLE 230
|
250 260
....*....|....*....|....*....
gi 1953392644 834 QVDVIIVMTGGKISEMGSYQELLaRDGAF 862
Cdd:PRK13651 231 WTKRTIFFKDGKIIKDGDTYDIL-SDNKF 258
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
664-809 |
5.83e-11 |
|
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: 67.08 E-value: 5.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 664 ITFSIPEGSLVAVVGQVGCGKSSLLSaLLAEMDKVEGHVAIK---GSVAYVPQQAWIQNDSLRENILFGRQLQERYYKAV 740
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGGRLTKpakGKLFYVPQRPYMTLGTLRDQIIYPDSSEDMKRRGL 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 741 IEAcallpDLE-ILPSGDRTEIGEKGVN----------LSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVGKHIFEN 809
Cdd:TIGR00954 550 SDK-----DLEqILDNVQLTHILEREGGwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRL 624
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
640-855 |
6.63e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 64.72 E-value: 6.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 640 GANSITVKNATFTWARSD----PPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGSVAYVPQQA 715
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 716 W-IQNdslRENILFGRQLQERYYKAVIEACALLPD-LEILPSGDRTEIGE--KGVN-----------LSGGQKQRVSLAR 780
Cdd:PRK13633 81 WdIRN---KAGMVFQNPDNQIVATIVEEDVAFGPEnLGIPPEEIRERVDEslKKVGmyeyrrhaphlLSGGQKQRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953392644 781 AVYCDSDIYLFDDPLSAVDAhVGKHIFENVIGPKGMLKNKTRLLVTHSISYLPQVDVIIVMTGGKISEMGSYQEL 855
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDP-SGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
641-858 |
1.04e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 64.37 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 641 ANSITVKNATFTW-ARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSS---LLSALL-AEmdkvEGHVAIKGSvAYVPQQA 715
Cdd:PRK13650 2 SNIIEVKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGLLeAE----SGQIIIDGD-LLTEENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 716 W---------IQND-------SLRENILFG--------RQLQERyykaVIEAcallpdLEILPSGDRTEigEKGVNLSGG 771
Cdd:PRK13650 77 WdirhkigmvFQNPdnqfvgaTVEDDVAFGlenkgiphEEMKER----VNEA------LELVGMQDFKE--REPARLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 772 QKQRVSLARAVYCDSDIYLFDDPLSAVDahvgkhifenvigPKGMLK------------NKTRLLVTHSISYLPQVDVII 839
Cdd:PRK13650 145 QKQRVAIAGAVAMRPKIIILDEATSMLD-------------PEGRLEliktikgirddyQMTVISITHDLDEVALSDRVL 211
|
250
....*....|....*....
gi 1953392644 840 VMTGGKISEMGSYQELLAR 858
Cdd:PRK13650 212 VMKNGQVESTSTPRELFSR 230
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
972-1230 |
1.04e-10 |
|
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: 64.41 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 972 LFISFLSIFLFLcnhVASLVSNYWLSLWTDDPIVNGTQEHTKIRLSVYGALGISQGITVFGYSMAVSIGG---IFASRRl 1048
Cdd:cd18545 2 LLLALLLMLLST---AASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGqriLYDLRQ- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1049 hvDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFNVIGAcIIILLA-----TPIASIIIPPLG 1123
Cdd:cd18545 78 --DLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGI-VIIMFSlnvrlALVTLAVLPLLV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1124 LIYFFVQRFyvasSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPSIVANR--WLAV 1201
Cdd:cd18545 155 LVVFLLRRR----ARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNAlfWPLV 230
|
250 260 270
....*....|....*....|....*....|
gi 1953392644 1202 RL-ECVGNCIVLFAALFSVISrHSLSAGLV 1230
Cdd:cd18545 231 ELiSALGTALVYWYGGKLVLG-GAITVGVL 259
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
661-857 |
1.41e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 63.45 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGSVAYVPQQAWIQNDSLRENILfgRQLQERY---- 736
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVADKNQL--RLLRTRLtmvf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 737 -----------YKAVIEACALLPDLEILPSGDRTE-------IGEKG-----VNLSGGQKQRVSLARAVYCDSDIYLFDD 793
Cdd:PRK10619 99 qhfnlwshmtvLENVMEAPIQVLGLSKQEARERAVkylakvgIDERAqgkypVHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953392644 794 PLSAVDAHVGKHIFEnvIGPKGMLKNKTRLLVTHSISYLPQVDV-IIVMTGGKISEMGSYQELLA 857
Cdd:PRK10619 179 PTSALDPELVGEVLR--IMQQLAEEGKTMVVVTHEMGFARHVSShVIFLHQGKIEEEGAPEQLFG 241
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
969-1190 |
1.44e-10 |
|
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: 64.03 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 969 AIGLFISFLS-----IFLFLCNHVASLVSNYWLSLWTDDPIVNGTQEHTKIrlsvYGALGISQGITVFGYSMAVSIGGIF 1043
Cdd:cd18577 2 IIGLLAAIAAgaalpLMTIVFGDLFDAFTDFGSGESSPDEFLDDVNKYALY----FVYLGIGSFVLSYIQTACWTITGER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1044 ASRRLHVDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFNVIGACII----------ILLATp 1113
Cdd:cd18577 78 QARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIafiyswkltlVLLAT- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953392644 1114 iasiiIPPLGLIYFFVQRFYV-ASSRQLKRLESVSrspvySHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYY 1190
Cdd:cd18577 157 -----LPLIAIVGGIMGKLLSkYTKKEQEAYAKAG-----SIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGI 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
602-870 |
1.59e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.58 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 602 VISSIVQaSVSLKRLRIFLSHEELEPDSIERRPVKDGGGANSI-TVKNATftwaRSDPPTLSGITFSIPEGSLVAVVGQV 680
Cdd:PRK09700 224 VCSGMVS-DVSNDDIVRLMVGRELQNRFNAMKENVSNLAHETVfEVRNVT----SRDRKKVRDISFSVCRGEILGFAGLV 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 681 GCGKSSLLSALLAEMDKVEGHV--------------AIKGSVAYVPQQ----AWIQNDSLRENILFGRQLQERYYKAVI- 741
Cdd:PRK09700 299 GSGRTELMNCLFGVDKRAGGEIrlngkdisprspldAVKKGMAYITESrrdnGFFPNFSIAQNMAISRSLKDGGYKGAMg 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 742 ---------EACALLPDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVGKHIFenvig 812
Cdd:PRK09700 379 lfhevdeqrTAENQRELLALKCHSVNQNITE----LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIY----- 449
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953392644 813 pKGMLK----NKTRLLVThsiSYLPQV----DVIIVMTGGKISemgsyQELLARDGAFAEFLRTYA 870
Cdd:PRK09700 450 -KVMRQladdGKVILMVS---SELPEIitvcDRIAVFCEGRLT-----QILTNRDDMSEEEIMAWA 506
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
644-866 |
1.70e-10 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 62.85 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWarsdPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSaLLAEMDKVE-GHVAIKG-SVAYVP--------- 712
Cdd:COG3840 2 LRLDDLTYRY----GDFPLRFDLTIAAGERVAILGPSGAGKSTLLN-LIAGFLPPDsGRILWNGqDLTALPpaerpvsml 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 713 -QQawiqND-----SLRENILFGRQ----LQERYYKAVIEACAllpdleilpsgdRTEIGEKG----VNLSGGQKQRVSL 778
Cdd:COG3840 77 fQE----NNlfphlTVAQNIGLGLRpglkLTAEQRAQVEQALE------------RVGLAGLLdrlpGQLSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 779 ARAVYCDSDIYLFDDPLSAvdahvgkhifenvIGP---KGMLK---------NKTRLLVTHSIS-YLPQVDVIIVMTGGK 845
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSA-------------LDPalrQEMLDlvdelcrerGLTVLMVTHDPEdAARIADRVLLVADGR 207
|
250 260
....*....|....*....|...
gi 1953392644 846 ISEMGSYQELLARDG--AFAEFL 866
Cdd:COG3840 208 IAADGPTAALLDGEPppALAAYL 230
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1293-1428 |
2.05e-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: 62.20 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1293 VEFRDYGLRYREnlDLVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINES-----AEGEIIIDDINIAKIGLHD-- 1365
Cdd:cd03260 1 IELRDLNVYYGD--KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVle 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953392644 1366 LRVKITIIPQDPVLFSGSLRMNLDpfsqYS------------DEEVWTSLELAHLKDFVSglpDKLNQECAEGGE 1428
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVA----YGlrlhgiklkeelDERVEEALRKAALWDEVK---DRLHALGLSGGQ 146
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
979-1187 |
2.06e-10 |
|
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: 63.58 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 979 IFLFLCNhVASLVSNYWLSLWTDDpIVNGTQEHTKIRLSVYGALGISQGITVFGYSMAVSIGGifASRRLHVDL----LQ 1054
Cdd:cd18541 6 LFLILVD-LLQLLIPRIIGRAIDA-LTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFG--ASRRIEYDLrndlFA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1055 NVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFnVIGACIIILLA-----TPIASIIIPPLGL-IYFF 1128
Cdd:cd18541 82 HLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALF-LGVLVLVMMFTispklTLIALLPLPLLALlVYRL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953392644 1129 VQRFYVASSRQLKRLESVSrspvySHFNETLLGVSVIRAF----EEQERFIRQSDLKVDENQK 1187
Cdd:cd18541 161 GKKIHKRFRKVQEAFSDLS-----DRVQESFSGIRVIKAFvqeeAEIERFDKLNEEYVEKNLR 218
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
661-846 |
2.83e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 64.75 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSaLLAEMDKVeghvaiKGSVAYVPQQ--AWIQNDSL----RENilFGRQLQe 734
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDKP------TSGTYRVAGQdvATLDADALaqlrREH--FGFIFQ- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 735 RYY-------------KAVI----------EACALLPDLEIlpsGDRteIGEKGVNLSGGQKQRVSLARAVYCDSDIYLF 791
Cdd:PRK10535 94 RYHllshltaaqnvevPAVYaglerkqrllRAQELLQRLGL---EDR--VEYQPSQLSGGQQQRVSIARALMNGGQVILA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1953392644 792 DDPLSAVDAHVGkhifENVIGPKGMLKNK--TRLLVTHSISYLPQVDVIIVMTGGKI 846
Cdd:PRK10535 169 DEPTGALDSHSG----EEVMAILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
1040-1263 |
3.26e-10 |
|
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: 62.95 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1040 GGIFA------SRRLHVDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFNVIGACIIILLATP 1113
Cdd:cd18572 57 GGCFSyagtrlVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSW 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1114 ----IASIIIPPLGLIYFFVQRFYvassRQLKRLESVSRSPVYSHFNETLLGVSVIRAF--EEQE--RFIRQSDLKVDEN 1185
Cdd:cd18572 137 rltlLAFITVPVIALITKVYGRYY----RKLSKEIQDALAEANQVAEEALSNIRTVRSFatEEREarRYERALDKALKLS 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1186 QK---AYypsiVANRWLAVRLECVGNCIVLFAALFSVISrHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVE 1262
Cdd:cd18572 213 VRqalAY----AGYVAVNTLLQNGTQVLVLFYGGHLVLS-GRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAE 287
|
.
gi 1953392644 1263 R 1263
Cdd:cd18572 288 K 288
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
665-872 |
3.30e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 63.90 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 665 TFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGSvayvpQQAWIQNDSLREnilfgrqLQERYYKAVIEAC 744
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGV-----DIAKISDAELRE-------VRRKKIAMVFQSF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 745 ALLPDLEIL------------PSGDRTE-----IGEKGVN---------LSGGQKQRVSLARAVYCDSDIYLFDDPLSAV 798
Cdd:PRK10070 116 ALMPHMTVLdntafgmelagiNAEERREkaldaLRQVGLEnyahsypdeLSGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953392644 799 DAHVGKHIFENVIGPKGMlKNKTRLLVTHSISYLPQV-DVIIVMTGGKISEMGSYQELLarDGAFAEFLRTYASG 872
Cdd:PRK10070 196 DPLIRTEMQDELVKLQAK-HQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEIL--NNPANDYVRTFFRG 267
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
667-850 |
3.64e-10 |
|
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: 61.35 E-value: 3.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 667 SIPEGSLVAVVGQVGCGKSSLLSaLLAEMDKVE-GHVAIKG------SVAYVPQQAWIQNDSL------RENILFGR--- 730
Cdd:cd03298 20 TFAQGEITAIVGPSGSGKSTLLN-LIAGFETPQsGRVLINGvdvtaaPPADRPVSMLFQENNLfahltvEQNVGLGLspg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 731 -QLQERYYKAVIEACAllpdleilpsgdRTEIGEKGV----NLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVGKH 805
Cdd:cd03298 99 lKLTAEDRQAIEVALA------------RVGLAGLEKrlpgELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1953392644 806 IFENVIGPKGMLKNkTRLLVTHSISYLPQV-DVIIVMTGGKISEMG 850
Cdd:cd03298 167 MLDLVLDLHAETKM-TVLMVTHQPEDAKRLaQRVVFLDNGRIAAQG 211
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
661-856 |
3.87e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 64.30 E-value: 3.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSAL---LAEMDKVEGHVAIKGSVAYVPQQ----AWIQNDSL-------RENI 726
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALafrSPKGVKGSGSVLLNGMPIDAKEMraisAYVQQDDLfiptltvREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 727 LF------GRQLQERYYKAVIEAcaLLPDLEILPSGDrTEIGEKGV--NLSGGQKQRVSLARAVYCDSDIYLFDDPLSAV 798
Cdd:TIGR00955 121 MFqahlrmPRRVTKKEKRERVDE--VLQALGLRKCAN-TRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGL 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953392644 799 DAHVGKHIFENVigpKGM-LKNKTRLLVTHSISY--LPQVDVIIVMTGGKISEMGSYQELL 856
Cdd:TIGR00955 198 DSFMAYSVVQVL---KGLaQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
663-855 |
5.24e-10 |
|
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: 61.23 E-value: 5.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 663 GITFSIPEGSLVAVVGQVGCGKSSLLSAL--LAEMDKVEGHVA----------IKGSVAYVPQQAWIQND-SLRENILF- 728
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLttLLKPTSGRATVAghdvvrepreVRRRIGIVFQDLSVDDElTGWENLYIh 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 729 -------GRQLQERyykavIEacallpdlEILPSGDRTEIGEKGV-NLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDA 800
Cdd:cd03265 98 arlygvpGAERRER-----ID--------ELLDFVGLLEAADRLVkTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1953392644 801 HVGKHIFENVigpKGMLK--NKTRLLVTHSISYLPQV-DVIIVMTGGKISEMGSYQEL 855
Cdd:cd03265 165 QTRAHVWEYI---EKLKEefGMTILLTTHYMEEAEQLcDRVAIIDHGRIIAEGTPEEL 219
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
589-800 |
6.59e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 63.67 E-value: 6.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 589 FNILRFPLNILPMVISSIVQASVSLKRLRIF---LSHEELEPDSIERRPVKDGGGansITVKNATFTwARSDPPTLSGIT 665
Cdd:COG4178 308 FGQVQGALSWFVDNYQSLAEWRATVDRLAGFeeaLEAADALPEAASRIETSEDGA---LALEDLTLR-TPDGRPLLEDLS 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 666 FSIPEGSLVAVVGQVGCGKSSLLSAlLAEM-DKVEGHVAI--KGSVAYVPQQAWIQNDSLRENILF---GRQLQERYYKA 739
Cdd:COG4178 384 LSLKPGERLLITGPSGSGKSTLLRA-IAGLwPYGSGRIARpaGARVLFLPQRPYLPLGTLREALLYpatAEAFSDAELRE 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953392644 740 VIEAC---ALLPDLEILPSGDRTeigekgvnLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDA 800
Cdd:COG4178 463 ALEAVglgHLAERLDEEADWDQV--------LSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
664-890 |
9.03e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 62.55 E-value: 9.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 664 ITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-SVAYVP-----------QQAWIQNDSLRENILFGRQ 731
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvDLSHVPpyqrpinmmfqSYALFPHMTVEQNIAFGLK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 732 lQERYYKAVI-----EACALLPDLEIlpsgdrteIGEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVGKH- 805
Cdd:PRK11607 118 -QDKLPKAEIasrvnEMLGLVHMQEF--------AKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRm 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 806 ------IFENVigpkgmlkNKTRLLVTHSI-SYLPQVDVIIVMTGGKISEMGSYQELLARDGA--FAEFLRTYASGDQE- 875
Cdd:PRK11607 189 qlevvdILERV--------GVTCVMVTHDQeEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTrySAEFIGSVNVFEGVl 260
|
250
....*....|....*
gi 1953392644 876 QAEQDDGLTgVSSPG 890
Cdd:PRK11607 261 KERQEDGLV-IDSPG 274
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
660-843 |
9.71e-10 |
|
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: 60.88 E-value: 9.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 660 TLSGITFSIPEGSL-----VAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-SVAYVPQQAWIQNDSLRENILFG---R 730
Cdd:cd03237 9 TLGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYIKADYEGTVRDLLSSitkD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 731 QLQERYYKAVIeacalLPDLEILPSGDRtEIGEkgvnLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVD-------AHVG 803
Cdd:cd03237 89 FYTHPYFKTEI-----AKPLQIEQILDR-EVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDveqrlmaSKVI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1953392644 804 KHIFENvigpkgmlKNKTRLLVTHSI---SYLpqVDVIIVMTG 843
Cdd:cd03237 159 RRFAEN--------NEKTAFVVEHDIimiDYL--ADRLIVFEG 191
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
643-859 |
1.11e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 61.33 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 643 SITVKNATFTWARSDP---PTLSGITFSIPEGSLVAVVGQVGCGKSSL---LSALL------AEMDKVEGHVAIK----- 705
Cdd:PRK13646 2 TIRFDNVSYTYQKGTPyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLiqnINALLkpttgtVTVDDITITHKTKdkyir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 706 ------GSVAYVPQQAWIQnDSLRENILFG--------RQLQERYYKavieacaLLPDLEIlpsgDRTEIGEKGVNLSGG 771
Cdd:PRK13646 82 pvrkriGMVFQFPESQLFE-DTVEREIIFGpknfkmnlDEVKNYAHR-------LLMDLGF----SRDVMSQSPFQMSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 772 QKQRVSLARAVYCDSDIYLFDDPLSAVDAHVGKHIFEnvigpkgMLK------NKTRLLVTHSISYLPQ-VDVIIVMTGG 844
Cdd:PRK13646 150 QMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMR-------LLKslqtdeNKTIILVSHDMNEVARyADEVIVMKEG 222
|
250
....*....|....*
gi 1953392644 845 KISEMGSYQELLARD 859
Cdd:PRK13646 223 SIVSQTSPKELFKDK 237
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
634-858 |
1.31e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 61.52 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 634 PVKDGGGANSITVKnatftwarsdppTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGSVAYVPQ 713
Cdd:PRK11308 16 PVKRGLFKPERLVK------------ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 714 QAWIQNDSLRENILF-------------GRQLQEryykavieacallPdLEILPSGDRTEIGEKG------VNL------ 768
Cdd:PRK11308 84 PEAQKLLRQKIQIVFqnpygslnprkkvGQILEE-------------P-LLINTSLSAAERREKAlammakVGLrpehyd 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 769 ------SGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVGKHIFeNVIgpkgM-LKNKTRL---LVTHSISYLPQV-DV 837
Cdd:PRK11308 150 ryphmfSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVL-NLM----MdLQQELGLsyvFISHDLSVVEHIaDE 224
|
250 260
....*....|....*....|.
gi 1953392644 838 IIVMTGGKISEMGSYQELLAR 858
Cdd:PRK11308 225 VMVMYLGRCVEKGTKEQIFNN 245
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1301-1388 |
1.70e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 62.42 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1301 RYRENLDLVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIGLHDLRVKITIIPQDPVLF 1380
Cdd:PRK10789 322 TYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLF 401
|
....*...
gi 1953392644 1381 SGSLRMNL 1388
Cdd:PRK10789 402 SDTVANNI 409
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
664-799 |
1.91e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 60.39 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 664 ITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGS-------------VAYVPQQAWIQND-SLRENILFG 729
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiqhyaskevarrIGLLAQNATTPGDiTVQELVARG 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953392644 730 R----QLQERYYKAVIEACAllpdlEILPSGDRTEIGEKGVN-LSGGQKQRVSLARAVYCDSDIYLFDDPLSAVD 799
Cdd:PRK10253 106 RyphqPLFTRWRKEDEEAVT-----KAMQATGITHLADQSVDtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
1001-1254 |
1.93e-09 |
|
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: 60.57 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1001 DDPIVNGTQEHTKIRLSVYGALGISQGITVFGYSMAVSIGGIFASRRLHVDLLQNVLRSPMSFFERTPSGNLVNRFSKEL 1080
Cdd:cd18543 27 DGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1081 dtvdsmipQVIKMFMGSLFNVIGACIIILLATPIASIIIPPLGLIYFFVQRF-YVASSRQLKRLESVSRSP------VYS 1153
Cdd:cd18543 107 --------SLVQRFLAFGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPlVLVARRFRRRYFPASRRAqdqagdLAT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1154 HFNETLLGVSVIRAF----EEQERFIRQSD-LKVDENQKAyypSIVANRWLAVR-LECVGNCIVLFAALFSVIsRHSLSA 1227
Cdd:cd18543 179 VVEESVTGIRVVKAFgrerRELDRFEAAARrLRATRLRAA---RLRARFWPLLEaLPELGLAAVLALGGWLVA-NGSLTL 254
|
250 260
....*....|....*....|....*...
gi 1953392644 1228 G-LVGLSvSYSlqvtTYLNWLVRMSSEM 1254
Cdd:cd18543 255 GtLVAFS-AYL----TMLVWPVRMLGWL 277
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
661-866 |
1.95e-09 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 59.61 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGS--------------VAYVPQQAWI-QNDSLREN 725
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditglpphriarlgIGYVPEGRRIfPSLTVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 726 IL---FGRQLQERYYKAVIEACALLPDLEilpsgDRteIGEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDP---LSAVd 799
Cdd:COG0410 99 LLlgaYARRDRAEVRADLERVYELFPRLK-----ER--RRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPslgLAPL- 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 800 ahVGKHIFENV--IGPKGMlknkTRLLVTHSISYLPQV-DVIIVMTGGKISEMGSYQELLARDGAFAEFL 866
Cdd:COG0410 171 --IVEEIFEIIrrLNREGV----TILLVEQNARFALEIaDRAYVLERGRIVLEGTAAELLADPEVREAYL 234
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
644-856 |
2.29e-09 |
|
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: 59.71 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATftWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVA--------------IKGSVA 709
Cdd:COG1119 4 LELRNVT--VRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlfgerrggedvweLRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 710 YV-P--QQAWIQNDSLRENILFGR----QLQERYYKAVIE-ACALLPDLEILPSGDRTeIGEkgvnLSGGQKQRVSLARA 781
Cdd:COG1119 82 LVsPalQLRFPRDETVLDVVLSGFfdsiGLYREPTDEQRErARELLELLGLAHLADRP-FGT----LSQGEQRRVLIARA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953392644 782 VYCDSDIYLFDDPLSAVDAHvGKHIFENVIGPKGMLKNKTRLLVTHSISYLPQ-VDVIIVMTGGKISEMGSYQELL 856
Cdd:COG1119 157 LVKDPELLILDEPTAGLDLG-ARELLLALLDKLAAEGAPTLVLVTHHVEEIPPgITHVLLLKDGRVVAAGPKEEVL 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1293-1377 |
2.57e-09 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 61.46 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1293 VEFRD----YGLRYRENLDlVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIG---LHD 1365
Cdd:COG1123 261 LEVRNlskrYPVRGKGGVR-AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRE 339
|
90
....*....|..
gi 1953392644 1366 LRVKITIIPQDP 1377
Cdd:COG1123 340 LRRRVQMVFQDP 351
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
658-866 |
2.94e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 62.10 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 658 PPTLSGITFSIPEGSLVAVVGQVGCGKSSLLsalLAEMDKVE---GHVAIKGS--VAY-----------VPQQAWIQNDS 721
Cdd:PTZ00243 1323 PLVLRGVSFRIAPREKVGIVGRTGSGKSTLL---LTFMRMVEvcgGEIRVNGReiGAYglrelrrqfsmIPQDPVLFDGT 1399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 722 LRENILFGRQLQERYYKAVIEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYC-DSDIYLFDDPLSAVDA 800
Cdd:PTZ00243 1400 VRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGFILMDEATANIDP 1479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953392644 801 HVGKHIFENVIGPkgmLKNKTRLLVTHSISYLPQVDVIIVMTGGKISEMGSYQEL-LARDGAFAEFL 866
Cdd:PTZ00243 1480 ALDRQIQATVMSA---FSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHSMV 1543
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
663-858 |
3.43e-09 |
|
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: 61.24 E-value: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 663 GITFSIPEGSLVAVVGQVGCGKSSLLSALLAeMDKVEGHVAIKG-SVAYVPQQAW------IQ------NDSL--RENI- 726
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGqDLDGLSRRALrplrrrMQvvfqdpFGSLspRMTVg 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 727 --------LFGRQL--QERYyKAVIEACA---LLPDleilpSGDR--TEigekgvnLSGGQKQRVSLARAVYCDSDIYLF 791
Cdd:COG4172 383 qiiaeglrVHGPGLsaAERR-ARVAEALEevgLDPA-----ARHRypHE-------FSGGQRQRIAIARALILEPKLLVL 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953392644 792 DDPLSAVDAHVGKHIFEnvigpkgMLKnktRLLVTHSISYL-----PQV-----DVIIVMTGGKISEMGSYQELLAR 858
Cdd:COG4172 450 DEPTSALDVSVQAQILD-------LLR---DLQREHGLAYLfishdLAVvralaHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
644-838 |
3.69e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 61.95 E-value: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHV------------AIKGSVAYV 711
Cdd:TIGR01257 929 VCVKNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVlvggkdietnldAVRQSLGMC 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 712 PQQAWI-QNDSLRENILFGRQLQERYY-KAVIEACALLPDleilpSGDRTEIGEKGVNLSGGQKQRVSLARAVYCDSDIY 789
Cdd:TIGR01257 1009 PQHNILfHHLTVAEHILFYAQLKGRSWeEAQLEMEAMLED-----TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVV 1083
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1953392644 790 LFDDPLSAVDAHVGKHIFENvigpkgMLKNKTRLLVTHSISYLPQVDVI 838
Cdd:TIGR01257 1084 VLDEPTSGVDPYSRRSIWDL------LLKYRSGRTIIMSTHHMDEADLL 1126
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
652-800 |
4.26e-09 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 57.89 E-value: 4.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 652 TWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG------------SVAYVPQQAWIQN 719
Cdd:cd03231 7 TCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGgpldfqrdsiarGLLYLGHAPGIKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 720 D-SLRENILFGRQLQERyyKAVIEACAL--LPDLEILPSGdrteigekgvNLSGGQKQRVSLARAVYCDSDIYLFDDPLS 796
Cdd:cd03231 87 TlSVLENLRFWHADHSD--EQVEEALARvgLNGFEDRPVA----------QLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
....
gi 1953392644 797 AVDA 800
Cdd:cd03231 155 ALDK 158
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
663-859 |
4.52e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 59.43 E-value: 4.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 663 GITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGS------------VAYVPQQAWIQND-SLRENIL-F 728
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpvpsrarharqrVGVVPQFDNLDPDfTVRENLLvF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 729 GRqlqerYYKAVIEAC-ALLPDL---EILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVGK 804
Cdd:PRK13537 105 GR-----YFGLSAAAArALVPPLlefAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARH 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1953392644 805 HIFENVigpKGML-KNKTRLLVTHSISYLPQV--DVIIVMTGGKISEmGSYQELLARD 859
Cdd:PRK13537 176 LMWERL---RSLLaRGKTILLTTHFMEEAERLcdRLCVIEEGRKIAE-GAPHALIESE 229
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
665-857 |
5.00e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 58.44 E-value: 5.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 665 TFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGS--VAYVPQQAWI----QNDSL------RENILFG--- 729
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhTTTPPSRRPVsmlfQENNLfshltvAQNIGLGlnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 730 ---------RQLQERYYKAVIEACallpdLEILPSgdrteigekgvNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDA 800
Cdd:PRK10771 99 glklnaaqrEKLHAIARQMGIEDL-----LARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSALDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953392644 801 HVGKHIF---ENVIGPKGMlknkTRLLVTHSISYLPQV-DVIIVMTGGKISEMGSYQELLA 857
Cdd:PRK10771 163 ALRQEMLtlvSQVCQERQL----TLLMVSHSLEDAARIaPRSLVVADGRIAWDGPTDELLS 219
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
661-857 |
5.41e-09 |
|
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: 58.22 E-value: 5.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-SVAYVPQQAWI--------QNDSL------REN 725
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGeDITGLPPHEIArlgigrtfQIPRLfpeltvLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 726 ILFGRQLQERYYKAVIEACALLPDL-----EILpsgDRTEIGEKG----VNLSGGQKQRVSLARAVYCDSDIYLFDDP-- 794
Cdd:cd03219 96 VMVAAQARTGSGLLLARARREEREAreraeELL---ERVGLADLAdrpaGELSYGQQRRLEIARALATDPKLLLLDEPaa 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953392644 795 -LSAVDAHVGKHIFENvIGPKGMlknkTRLLVTHSISYLPQV-DVIIVMTGGKISEMGSYQELLA 857
Cdd:cd03219 173 gLNPEETEELAELIRE-LRERGI----TVLLVEHDMDVVMSLaDRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1309-1381 |
6.52e-09 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 56.81 E-value: 6.52e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953392644 1309 VLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIGLH--DLRVKITIIPQDPVLFS 1381
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRIGMVFQDFALFP 89
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
661-848 |
6.54e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 58.54 E-value: 6.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSAL-----------------LAEMDKvEGHVAIKGSVAYVPQQA-------- 715
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLvglespsqgnvswrgepLAKLNR-AQRKAFRRDIQMVFQDSisavnprk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 716 ---WIQNDSLRENILFGRQLQERYYKAVIEACALLP-DLEILPSgdrteigekgvNLSGGQKQRVSLARAVYCDSDIYLF 791
Cdd:PRK10419 107 tvrEIIREPLRHLLSLDKAERLARASEMLRAVDLDDsVLDKRPP-----------QLSGGQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953392644 792 DDPLSAVDAHVGKHIFEnvigpkgMLKNKTR------LLVTHSIS---YLPQvdVIIVMTGGKISE 848
Cdd:PRK10419 176 DEAVSNLDLVLQAGVIR-------LLKKLQQqfgtacLFITHDLRlveRFCQ--RVMVMDNGQIVE 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
613-794 |
6.63e-09 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 60.08 E-value: 6.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 613 LKRLriflshEELEPDSIERR--------PVKDGGGANSITVKNATFTWArsDPPTLSGITFSIPEGSLVAVVGQVGCGK 684
Cdd:COG0488 283 IKAL------EKLEREEPPRRdktveirfPPPERLGKKVLELEGLSKSYG--DKTLLDDLSLRIDRGDRIGLIGPNGAGK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 685 SSLLSALLAEMDKVEGHVAIkGS---VAYVPQQawiQ-----NDSLRENIlfgRQLQERyyKAVIEACALLPDLeiLPSG 756
Cdd:COG0488 355 STLLKLLAGELEPDSGTVKL-GEtvkIGYFDQH---QeeldpDKTVLDEL---RDGAPG--GTEQEVRGYLGRF--LFSG 423
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1953392644 757 DR--TEIGekgvNLSGGQKQRVSLARAVYCDSDIYLFDDP 794
Cdd:COG0488 424 DDafKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEP 459
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
661-830 |
6.74e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 57.90 E-value: 6.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVAIKGsvayvpqQAWIQNDSLRENILFGRQLQERYyka 739
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLH-LLGGLDTpTSGDVIFNG-------QPMSKLSSAAKAELRNQKLGFIY--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 740 viEACALLPDLEILPS---------GDRTEIGEKGVN-----------------LSGGQKQRVSLARAVYCDSDIYLFDD 793
Cdd:PRK11629 94 --QFHHLLPDFTALENvamplligkKKPAEINSRALEmlaavglehranhrpseLSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 1953392644 794 PLSAVDAHVGKHIFEnVIGPKGMLKNKTRLLVTHSIS 830
Cdd:PRK11629 172 PTGNLDARNADSIFQ-LLGELNRLQGTAFLVVTHDLQ 207
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
656-856 |
7.07e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 58.52 E-value: 7.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 656 SDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGSVAYVPQQAWiQNDSLRENILFGRQLQE- 734
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIF-QIDAIKLRKEVGMVFQQp 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 735 ------------------------RYYKAVIEACALLPDL--EILpsgDRteIGEKGVNLSGGQKQRVSLARAVYCDSDI 788
Cdd:PRK14246 100 npfphlsiydniayplkshgikekREIKKIVEECLRKVGLwkEVY---DR--LNSPASQLSGGQQQRLTIARALALKPKV 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 789 YLFDDPLSAVDAhVGKHIFENVIGPkgmLKNK-TRLLVTHSISYLPQV-DVIIVMTGGKISEMGSYQELL 856
Cdd:PRK14246 175 LLMDEPTSMIDI-VNSQAIEKLITE---LKNEiAIVIVSHNPQQVARVaDYVAFLYNGELVEWGSSNEIF 240
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1293-1376 |
7.25e-09 |
|
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: 57.42 E-value: 7.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1293 VEFRDYGLRYRENLdLVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAkiGLHD-----LR 1367
Cdd:cd03292 1 IEFINVTKTYPNGT-AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS--DLRGraipyLR 77
|
....*....
gi 1953392644 1368 VKITIIPQD 1376
Cdd:cd03292 78 RKIGVVFQD 86
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
644-799 |
8.18e-09 |
|
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: 56.39 E-value: 8.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTwARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSAlLAEMDKV-EGHVAI--KGSVAYVPQQAWIQND 720
Cdd:cd03223 1 IELENLSLA-TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRA-LAGLWPWgSGRIGMpeGEDLLFLPQRPYLPLG 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953392644 721 SLRENIlfgrqlqeryykavieacallpdleILPSGDRteigekgvnLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVD 799
Cdd:cd03223 79 TLREQL-------------------------IYPWDDV---------LSGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1310-1387 |
8.31e-09 |
|
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: 60.08 E-value: 8.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1310 LKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESaEGEIIIDDINIAKIG---LHDLRVKITIIPQDPvlFsGSL-- 1384
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--F-GSLsp 377
|
...
gi 1953392644 1385 RMN 1387
Cdd:COG4172 378 RMT 380
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
644-858 |
8.82e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 59.82 E-value: 8.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWarSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSAL--LAEMDKVEG----HVAIKGSVAYVPQQA-- 715
Cdd:TIGR03269 1 IEVKNLTKKF--DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGriiyHVALCEKCGYVERPSkv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 716 ------------------WIQNDSLREN------ILFGRQL----QERYYKAVIEAC---------ALLPDLEILpsgDR 758
Cdd:TIGR03269 79 gepcpvcggtlepeevdfWNLSDKLRRRirkriaIMLQRTFalygDDTVLDNVLEALeeigyegkeAVGRAVDLI---EM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 759 TEIGEK----GVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVGKHIFENVIgpKGMLKNKTRLLVThsiSYLPQ 834
Cdd:TIGR03269 156 VQLSHRithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALE--EAVKASGISMVLT---SHWPE 230
|
250 260
....*....|....*....|....*....
gi 1953392644 835 V-----DVIIVMTGGKISEMGSYQELLAR 858
Cdd:TIGR03269 231 ViedlsDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
635-855 |
9.03e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 58.95 E-value: 9.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 635 VKDGGGANSITVKNATFtWARsdPPTL---SGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-SVAY 710
Cdd:PRK15079 11 VADLKVHFDIKDGKQWF-WQP--PKTLkavDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGkDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 711 VPQQAW------IQ---NDSL-----RENI--------------LFGRQLQERyYKAVIEACALLPDLeilpsgdrteIG 762
Cdd:PRK15079 88 MKDDEWravrsdIQmifQDPLaslnpRMTIgeiiaeplrtyhpkLSRQEVKDR-VKAMMLKVGLLPNL----------IN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 763 EKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAhvgkHIFENVIgpkGMLKNKTR------LLVTHSISYLPQV- 835
Cdd:PRK15079 157 RYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV----SIQAQVV---NLLQQLQRemglslIFIAHDLAVVKHIs 229
|
250 260
....*....|....*....|
gi 1953392644 836 DVIIVMTGGKISEMGSYQEL 855
Cdd:PRK15079 230 DRVLVMYLGHAVELGTYDEV 249
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
661-858 |
1.15e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 58.66 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSA--LLAEMDkvEGHVAIKGS--VAYVPQQawiqndsLRE------------ 724
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCinLLERPT--SGRVLVDGQdlTALSEKE-------LRKarrqigmifqhf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 725 NILFGRqlqeryykAVIEACALlPdLEIlpSG-DRTEIGEK--------GV---------NLSGGQKQRVSLARAVYCDS 786
Cdd:PRK11153 92 NLLSSR--------TVFDNVAL-P-LEL--AGtPKAEIKARvtellelvGLsdkadrypaQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953392644 787 DIYLFDDPLSAVDAHVGKHIFEnvigpkgMLK--NK----TRLLVTHSISYLPQV-DVIIVMTGGKISEMGSYQELLAR 858
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILE-------LLKdiNRelglTIVLITHEMDVVKRIcDRVAVIDAGRLVEQGTVSEVFSH 231
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
668-843 |
1.26e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.44 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 668 IPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGSVAYVPQqaWIQNDS-------LRENilfGRQLQERYYKAv 740
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQ--YIKPDYdgtvedlLRSI---TDDLGSSYYKS- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 741 ieacallpdlEILPSGDRTEIGEKGVN-LSGGQKQRVSLARAVYCDSDIYLFDDPLSAVD-------AHVGKHIFENvig 812
Cdd:PRK13409 436 ----------EIIKPLQLERLLDKNVKdLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavAKAIRRIAEE--- 502
|
170 180 190
....*....|....*....|....*....|....
gi 1953392644 813 pkgmlKNKTRLLVTHSIS---YLpqVDVIIVMTG 843
Cdd:PRK13409 503 -----REATALVVDHDIYmidYI--SDRLMVFEG 529
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
977-1263 |
1.44e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 57.90 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 977 LSIFLFLCNHVASLVSNYWLSLWTDDPIVNGTQEHTKIRLSVY-----GALGISQGITVF-GYSMAVSIGGIfaSRRLHV 1050
Cdd:cd18563 3 LGFLLMLLGTALGLVPPYLTKILIDDVLIQLGPGGNTSLLLLLvlglaGAYVLSALLGILrGRLLARLGERI--TADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1051 DLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFNVIGACIIILLATP----IASIIIPPLG-LI 1125
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWklalLVLIPVPLVVwGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1126 YFFVQRFYVASSRQLKRlesvsRSPVYSHFNETLLGVSVIRAF----EEQERFIRQSDLKVDENQKA------YYPSIVA 1195
Cdd:cd18563 161 YFFWKKIRRLFHRQWRR-----WSRLNSVLNDTLPGIRVVKAFgqekREIKRFDEANQELLDANIRAeklwatFFPLLTF 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953392644 1196 nrwlavrLECVGNCIVLFAALFSVISRHsLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVER 1263
Cdd:cd18563 236 -------LTSLGTLIVWYFGGRQVLSGT-MTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAER 295
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1309-1382 |
1.53e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 58.92 E-value: 1.53e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953392644 1309 VLKHINITINGGEKVGIVGRTGAGKSSltlgLFRInesAEGEIIID--DINIAKiglhdlRVKITIIPQDPVLFSG 1382
Cdd:COG0488 13 LLDDVSLSINPGDRIGLVGRNGAGKST----LLKI---LAGELEPDsgEVSIPK------GLRIGYLPQEPPLDDD 75
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1309-1380 |
1.87e-08 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 56.38 E-value: 1.87e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953392644 1309 VLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINI--AKIGLHDLRVKITIIPQDPVLF 1380
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLF 88
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1309-1381 |
1.90e-08 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 57.78 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1309 VLKHINITINGGEKVGIVGRTGAGKSSltlgLFR-IN--ESA-EGEIIIDDINIAKI---GLHDLRVKITIIPQDPVLFS 1381
Cdd:COG1135 20 ALDDVSLTIEKGEIFGIIGYSGAGKST----LIRcINllERPtSGSVLVDGVDLTALserELRAARRKIGMIFQHFNLLS 95
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1309-1377 |
2.34e-08 |
|
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: 57.37 E-value: 2.34e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953392644 1309 VLKHINITINGGEKVGIVGRTGAGKSSLT---LGLFRINESAEGEIIIDDINIAKIG---LHDLRVK-ITIIPQDP 1377
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLAraiLGLLPPPGITSGEILFDGEDLLKLSekeLRKIRGReIQMIFQDP 95
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
661-799 |
2.38e-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: 56.40 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG--------------SVAYVPQQAWIQND-SLREN 725
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditklpmhkrarlGIGYLPQEASIFRKlTVEEN 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953392644 726 ILFGRQLQERYYKAVIE-ACALLPDLEILPSGDRteigeKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVD 799
Cdd:cd03218 96 ILAVLEIRGLSKKEREEkLEELLEEFHITHLRKS-----KASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
661-921 |
2.72e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 58.36 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSlLSALLAEMD-KVEGHVAIKGSVAYVPQQAWIQND-SLRENILFgRQLQERYYK 738
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKST-LSNLIAGVTmPNKGTVDIKGSAALIAISSGLNGQlTGIENIEL-KGLMMGLTK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 739 AVIEacallpdlEILPSG-DRTEIGeKGVN-----LSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVGKHIFE--NV 810
Cdd:PRK13545 118 EKIK--------EIIPEIiEFADIG-KFIYqpvktYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDkmNE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 811 IGPKGmlknKTRLLVTHSISylpQVDVI----IVMTGGKISEMGSYQELLARdgaFAEFLRTYASGDQEQAEQddgltgv 886
Cdd:PRK13545 189 FKEQG----KTIFFISHSLS---QVKSFctkaLWLHYGQVKEYGDIKEVVDH---YDEFLKKYNQMSVEERKD------- 251
|
250 260 270
....*....|....*....|....*....|....*
gi 1953392644 887 sSPGKEVKQMENGMLVTDVAGKQLQRQLSNSSSYS 921
Cdd:PRK13545 252 -FREEQISQFQHGLLQEDQTGRERKRKKGKKTSRK 285
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
661-827 |
2.93e-08 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 55.75 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGSvayvPQQAWIQNDslrenilFGRQLQER--YYK 738
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK----PLDIAARNR-------IGYLPEERglYPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 739 -AVIEACALLPDL------EILPSGD----RTEIGEKGV----NLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAhVG 803
Cdd:cd03269 85 mKVIDQLVYLAQLkglkkeEARRRIDewleRLELSEYANkrveELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VN 163
|
170 180
....*....|....*....|....*.
gi 1953392644 804 KHIFENVIGPkgmLK--NKTRLLVTH 827
Cdd:cd03269 164 VELLKDVIRE---LAraGKTVILSTH 186
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
659-858 |
3.01e-08 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 58.16 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 659 PTLSGITFSIPEGSLVAVVGQVGCGKS-SLLSA--LLAEmdkveGHVAIKGSVAY-------VPQQAWIQ---ND----- 720
Cdd:COG4172 24 EAVKGVSFDIAAGETLALVGESGSGKSvTALSIlrLLPD-----PAAHPSGSILFdgqdllgLSERELRRirgNRiamif 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 721 -----SLreNILF--GRQLQE--RYYKAVIEACALLPDLEILpsgDRTEI--GEKGVN-----LSGGQKQRVSLARAVYC 784
Cdd:COG4172 99 qepmtSL--NPLHtiGKQIAEvlRLHRGLSGAAARARALELL---ERVGIpdPERRLDayphqLSGGQRQRVMIAMALAN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 785 DSDIYLFDDPLSAVDAHVGKHIFEnvigpkgMLKNKTR------LLVTHSisyLPQV----DVIIVMTGGKISEMGSYQE 854
Cdd:COG4172 174 EPDLLIADEPTTALDVTVQAQILD-------LLKDLQRelgmalLLITHD---LGVVrrfaDRVAVMRQGEIVEQGPTAE 243
|
....
gi 1953392644 855 LLAR 858
Cdd:COG4172 244 LFAA 247
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
643-857 |
3.06e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 56.76 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 643 SITVKNATFTWARSDP---PTLSGITFSIPEGSLVAVVGQVGCGKSSLL---SALL----AEMDKVEGHV---------- 702
Cdd:PRK13641 2 SIKFENVDYIYSPGTPmekKGLDNISFELEEGSFVALVGHTGSGKSTLMqhfNALLkpssGTITIAGYHItpetgnknlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 703 AIKGSVAYVPQ--QAWIQNDSLRENILFG-RQLQERYYKAVIEACALLPDLeilpsGDRTEIGEKG-VNLSGGQKQRVSL 778
Cdd:PRK13641 82 KLRKKVSLVFQfpEAQLFENTVLKDVEFGpKNFGFSEDEAKEKALKWLKKV-----GLSEDLISKSpFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 779 ARAVYCDSDIYLFDDPLSAVDAHVGKHIFEnvigpkgMLKN-----KTRLLVTHSISYLPQ-VDVIIVMTGGKISEMGSY 852
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMMQ-------LFKDyqkagHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASP 229
|
....*
gi 1953392644 853 QELLA 857
Cdd:PRK13641 230 KEIFS 234
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1309-1376 |
3.39e-08 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 55.57 E-value: 3.39e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953392644 1309 VLKHINITINGGEKVGIVGRTGAGKSSL--TLGLfrINESAEGEIIIDDINIAKIGLHDL----RVKITIIPQD 1376
Cdd:cd03255 19 ALKGVSLSIEKGEFVAIVGPSGSGKSTLlnILGG--LDRPTSGEVRVDGTDISKLSEKELaafrRRHIGFVFQS 90
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1293-1427 |
3.65e-08 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 55.97 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1293 VEFRDYGLRYRENLdlVLKHINITINGGEKVGIVGRTGAGKSSLT---LGLFRineSAEGEIIIDDINIAK---IGLHDL 1366
Cdd:cd03261 1 IELRGLTKSFGGRT--VLKGVDLDVRRGEILAIIGPSGSGKSTLLrliVGLLR---PDSGEVLIDGEDISGlseAELYRL 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953392644 1367 RVKITIIPQDPVLFSG-SLRMN----LDPFSQYSDEEVwtsLELAHLK-DFVsGLPDKLNQECAE--GG 1427
Cdd:cd03261 76 RRRMGMLFQSGALFDSlTVFENvafpLREHTRLSEEEI---REIVLEKlEAV-GLRGAEDLYPAElsGG 140
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
661-850 |
3.69e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 54.64 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEmdkvEGHVAIKGSVAYVPQQAWIQNDSLRENILFGrqlqeryykav 740
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYA----SGKARLISFLPKFSRNKLIFIDQLQFLIDVG----------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 741 ieacallpdLEILPsgdrteIGEKGVNLSGGQKQRVSLARAVYCDSD--IYLFDDPLSAVDaHVGKHIFENVIGPKGMLK 818
Cdd:cd03238 76 ---------LGYLT------LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH-QQDINQLLEVIKGLIDLG 139
|
170 180 190
....*....|....*....|....*....|....*...
gi 1953392644 819 NkTRLLVTHSISYLPQVDVIIVM------TGGKISEMG 850
Cdd:cd03238 140 N-TVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1307-1429 |
4.05e-08 |
|
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: 55.17 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1307 DLVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFrinesaeGEIIIDDINIAKIGlhdlrvKITIIPQDPVLFSGSLRM 1386
Cdd:cd03250 18 SFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALL-------GELEKLSGSVSVPG------SIAYVSQEPWIQNGTIRE 84
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1953392644 1387 NLDPFSQYSDEEVWTSLELAHLKDFVSGLPDKLNQECAEGGEN 1429
Cdd:cd03250 85 NILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGIN 127
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
656-858 |
4.94e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 55.86 E-value: 4.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 656 SDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALL----AEMDKVEGHVAIKGsVAYVPQQ------AWI-QN----- 719
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALgilpAGVRQTAGRVLLDG-KPVAPCAlrgrkiATImQNprsaf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 720 -------DSLRENIL-FGRQLQERYYKAVIEACALLPDLEILPSgdrteigeKGVNLSGGQKQRVSLARAVYCDSDIYLF 791
Cdd:PRK10418 93 nplhtmhTHARETCLaLGKPADDATLTAALEAVGLENAARVLKL--------YPFEMSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953392644 792 DDPLSAVDAHVGKHIF---ENVI---GPkGMlknktrLLVTHSISYLPQV-DVIIVMTGGKISEMGSYQELLAR 858
Cdd:PRK10418 165 DEPTTDLDVVAQARILdllESIVqkrAL-GM------LLVTHDMGVVARLaDDVAVMSHGRIVEQGDVETLFNA 231
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
644-850 |
6.61e-08 |
|
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: 54.68 E-value: 6.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNAT--FTWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-SVAYVPQQAW---- 716
Cdd:cd03266 2 ITADALTkrFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEARrrlg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 717 IQND--------SLRENIL-FGR--QLQERYYKAVIEACALLpdLEILPSGDRteigeKGVNLSGGQKQRVSLARAVYCD 785
Cdd:cd03266 82 FVSDstglydrlTARENLEyFAGlyGLKGDELTARLEELADR--LGMEELLDR-----RVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953392644 786 SDIYLFDDPLSAVDAHVGKHIFENVIGPKGMlkNKTRLLVTHSISYLPQV-DVIIVMTGGKISEMG 850
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRAL--GKCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
655-800 |
8.01e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 54.19 E-value: 8.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 655 RSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSAL---LAEMDKVEGHVAIKG------------SVAYVPQQAW-IQ 718
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGipykefaekypgEIIYVSEEDVhFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 719 NDSLRENILFGRQLQeryykavieacallpdleilpsGDRTEIGekgvnLSGGQKQRVSLARAVYCDSDIYLFDDPLSAV 798
Cdd:cd03233 97 TLTVRETLDFALRCK----------------------GNEFVRG-----ISGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
..
gi 1953392644 799 DA 800
Cdd:cd03233 150 DS 151
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
661-855 |
8.82e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 55.02 E-value: 8.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLL---SALLAEMDKVEGHVAIKGSV------------------AYVPQQAWIQN 719
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLrhlSGLITGDKSAGSHIELLGRTvqregrlardirksrantGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 720 D-SLRENILFGRQLQERYYKAVIEACALLPDLEILPSGDRTEIG----EKGVNLSGGQKQRVSLARAVYCDSDIYLFDDP 794
Cdd:PRK09984 100 RlSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALTRVGMVhfahQRVSTLSGGQQQRVAIARALMQQAKVILADEP 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953392644 795 LSAVDAHVGKHIFENVigpKGMLKNK--TRLLVTHSISY-LPQVDVIIVMTGGKISEMGSYQEL 855
Cdd:PRK09984 180 IASLDPESARIVMDTL---RDINQNDgiTVVVTLHQVDYaLRYCERIVALRQGHVFYDGSSQQF 240
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
662-801 |
1.01e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 54.04 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 662 SGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG------------SVAYVPQQAWIQND-SLRENILF 728
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGepirrqrdeyhqDLLYLGHQPGIKTElTALENLRF 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953392644 729 GRQLQERYYKAVIEAcAL----LPDLEILPSGdrteigekgvNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAH 801
Cdd:PRK13538 98 YQRLHGPGDDEALWE-ALaqvgLAGFEDVPVR----------QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1293-1380 |
1.10e-07 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 54.61 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1293 VEFRDYGLRYRENLDLVlKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIGLHDLRVKITI 1372
Cdd:cd03295 1 IEFENVTKRYGGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
....*...
gi 1953392644 1373 IPQDPVLF 1380
Cdd:cd03295 80 VIQQIGLF 87
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1047-1380 |
1.18e-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: 56.34 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1047 RLHVDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVD---SMIPQVIKMFMgslfnVIGACIIIL--LATPIASIIIPP 1121
Cdd:COG4615 82 RLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISqafVRLPELLQSVA-----LVLGCLAYLawLSPPLFLLTLVL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1122 LGLIyFFVQRFYVASSRQLKRLESVSRSPVYSHFNetllgvSVIRAFEE----QER--FIRQSDLKV------DENQKAY 1189
Cdd:COG4615 157 LGLG-VAGYRLLVRRARRHLRRAREAEDRLFKHFR------ALLEGFKElklnRRRrrAFFDEDLQPtaeryrDLRIRAD 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1190 YPSIVANRWlavrlecvGNCIvLFAALFSVIsrhslsAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNI----------V 1259
Cdd:COG4615 230 TIFALANNW--------GNLL-FFALIGLIL------FLLPALGWADPAVLSGFVLVLLFLRGPLSQLVgalptlsranV 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1260 AVERLKEYSETEKEAPWQIQEMAPPSTWPQVGRVEFRDYGLRYRENLD---LVLKHINITINGGEKVGIVGRTGAGKSSL 1336
Cdd:COG4615 295 ALRKIEELELALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGdegFTLGPIDLTIRRGELVFIVGGNGSGKSTL 374
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1953392644 1337 T---LGLFRineSAEGEIIIDDINIAKIGLHDLRVKITIIPQDPVLF 1380
Cdd:COG4615 375 AkllTGLYR---PESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF 418
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1033-1264 |
1.24e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 55.21 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1033 YSMAvSIGGIFASRrLHVDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFNVIGACIIIL--- 1109
Cdd:cd18564 76 YLTA-LVGQRVVLD-LRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFwld 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1110 --LAtpIASIIIPPLgliyffvqrFYVASSRQLKRLESVSR------SPVYSHFNETLLGVSVIRAF----EEQERFIRQ 1177
Cdd:cd18564 154 wqLA--LIALAVAPL---------LLLAARRFSRRIKEASReqrrreGALASVAQESLSAIRVVQAFgreeHEERRFARE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1178 SDLKVDENQKAYYPSIVANRWLAVrLECVGNCIVLFAALFSVIsRHSLSAGlvGLSVsyslqVTTYLNWL---VRMSSEM 1254
Cdd:cd18564 223 NRKSLRAGLRAARLQALLSPVVDV-LVAVGTALVLWFGAWLVL-AGRLTPG--DLLV-----FLAYLKNLykpVRDLAKL 293
|
250
....*....|....
gi 1953392644 1255 ETNI----VAVERL 1264
Cdd:cd18564 294 TGRIakasASAERV 307
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
661-839 |
1.26e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.33 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG--SVAYVPQQAWIQNDSLRENILFG----RQLQE 734
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwQLAWVNQETPALPQPALEYVIDGdreyRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 735 RYYKA-----------------VIEACALLPDLEILPSG---DRTEIGEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDP 794
Cdd:PRK10636 97 QLHDAnerndghaiatihgkldAIDAWTIRSRAASLLHGlgfSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEP 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1953392644 795 LSAVDahvgkhiFENVIGPKGMLKN--KTRLLVTHSISYL-PQVDVII 839
Cdd:PRK10636 177 TNHLD-------LDAVIWLEKWLKSyqGTLILISHDRDFLdPIVDKII 217
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
644-859 |
1.31e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 54.81 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWaRSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGS-------------VAY 710
Cdd:PRK13652 4 IETRDLCYSY-SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 711 VPQQA--WIQNDSLRENILFG---RQLQERYYKAVIEACALLPDLEILpsgdRTEIGEkgvNLSGGQKQRVSLARAVYCD 785
Cdd:PRK13652 83 VFQNPddQIFSPTVEQDIAFGpinLGLDEETVAHRVSSALHMLGLEEL----RDRVPH---HLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953392644 786 SDIYLFDDPLSAVDAHVGKHIFE---NVIGPKGMlknkTRLLVTHSISYLPQV-DVIIVMTGGKISEMGSYQELLARD 859
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDflnDLPETYGM----TVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
659-879 |
1.51e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.78 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 659 PTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGS--VAYVPQQ------AWIQNDSLRENILFGR 730
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHevVTRSPQDglangiVYISEDRKRDGLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 731 QLQE-------RYYKAviEACALLPDLEIL-------------PSGDRTeIGekgvNLSGGQKQRVSLARAVYCDSDIYL 790
Cdd:PRK10762 346 SVKEnmsltalRYFSR--AGGSLKHADEQQavsdfirlfniktPSMEQA-IG----LLSGGNQQKVAIARGLMTRPKVLI 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 791 FDDPLSAVDAHVGKHIFE--NVIGPKGMlknkTRLLVThsiSYLPQV----DVIIVMTGGKISemGSYQellaRDGAFAE 864
Cdd:PRK10762 419 LDEPTRGVDVGAKKEIYQliNQFKAEGL----SIILVS---SEMPEVlgmsDRILVMHEGRIS--GEFT----REQATQE 485
|
250
....*....|....*
gi 1953392644 865 FLRTYASGDQEQAEQ 879
Cdd:PRK10762 486 KLMAAAVGKLNRVNQ 500
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
661-867 |
1.72e-07 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 54.04 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSAL-LAEMDKvEGHVAIKG-SVAYVPQQA-------WIQNDSLR-------- 723
Cdd:COG4598 24 LKGVSLTARKGDVISIIGSSGSGKSTFLRCInLLETPD-SGEIRVGGeEIRLKPDRDgelvpadRRQLQRIRtrlgmvfq 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 724 -----------ENILFG-RQLQERYYKAVIE-ACALLpdleilpsgDRTEIGEKG----VNLSGGQKQRVSLARAVYCDS 786
Cdd:COG4598 103 sfnlwshmtvlENVIEApVHVLGRPKAEAIErAEALL---------AKVGLADKRdaypAHLSGGQQQRAAIARALAMEP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 787 DIYLFDDPLSAVDAH-VGKhifenvigpkgMLK--------NKTRLLVTHSISYLPQV-DVIIVMTGGKISEMGSYQELL 856
Cdd:COG4598 174 EVMLFDEPTSALDPElVGE-----------VLKvmrdlaeeGRTMLVVTHEMGFARDVsSHVVFLHQGRIEEQGPPAEVF 242
|
250
....*....|...
gi 1953392644 857 A--RDGAFAEFLR 867
Cdd:COG4598 243 GnpKSERLRQFLS 255
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
661-855 |
2.34e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 54.47 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIK----------GSVAYVPQQAWIQN-DSLRENILFG 729
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdkknnHELITNPYSKKIKNfKELRRRVSMV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 730 RQLQE-RYYKAVIEACALLPDLEI-LPSGDRTEIGEKGVN---------------LSGGQKQRVSLARAVYCDSDIYLFD 792
Cdd:PRK13631 122 FQFPEyQLFKDTIEKDIMFGPVALgVKKSEAKKLAKFYLNkmglddsylerspfgLSGGQKRRVAIAGILAIQPEILIFD 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953392644 793 DPLSAVDAHVGKHIFENVIGPKGmlKNKTRLLVTHSISYLPQV-DVIIVMTGGKISEMGSYQEL 855
Cdd:PRK13631 202 EPTAGLDPKGEHEMMQLILDAKA--NNKTVFVITHTMEHVLEVaDEVIVMDKGKILKTGTPYEI 263
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
632-827 |
2.77e-07 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 53.11 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 632 RRPVKDGGGANSItvkNATFTWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGsvaYV 711
Cdd:cd03267 11 RVYSKEPGLIGSL---KSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG---LV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 712 PqqaWIQNDSLRENI--LFGRQLQERYYKAVIEACALLPDLEILPSG-------------DRTEIGEKGV-NLSGGQKQR 775
Cdd:cd03267 85 P---WKRRKKFLRRIgvVFGQKTQLWWDLPVIDSFYLLAAIYDLPPArfkkrldelsellDLEELLDTPVrQLSLGQRMR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1953392644 776 VSLARAVYCDSDIYLFDDPLSAVDAhVGKHIFENVIGPKGMLKNKTRLLVTH 827
Cdd:cd03267 162 AEIAAALLHEPEILFLDEPTIGLDV-VAQENIRNFLKEYNRERGTTVLLTSH 212
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
661-879 |
3.23e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 53.56 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHvAIKGSVAYVPQQAWIQNDSL----RENILFGR------ 730
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGY-RYSGDVLLGGRSIFNYRDVLefrrRVGMLFQRpnpfpm 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 731 QLQERYYkAVIEACALLPDLEI--LPSGDRTEIG----------EKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAV 798
Cdd:PRK14271 116 SIMDNVL-AGVRAHKLVPRKEFrgVAQARLTEVGlwdavkdrlsDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSAL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 799 DAHVGKHIFENVigpKGMLKNKTRLLVTHSISYLPQV-DVIIVMTGGKISEMGSYQELLARDgAFAEFLRTYA--SGDQE 875
Cdd:PRK14271 195 DPTTTEKIEEFI---RSLADRLTVIIVTHNLAQAARIsDRAALFFDGRLVEEGPTEQLFSSP-KHAETARYVAglSGDVK 270
|
....
gi 1953392644 876 QAEQ 879
Cdd:PRK14271 271 DAKR 274
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1239-1422 |
3.47e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 54.81 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1239 QVTTYLNWLVRMSSEMeTNIVA-VERLKEYSETEKEAPwQIQEMAPPSTWPQVGRVEFRDYGLRyRENLDLVLKHINITI 1317
Cdd:COG4178 310 QVQGALSWFVDNYQSL-AEWRAtVDRLAGFEEALEAAD-ALPEAASRIETSEDGALALEDLTLR-TPDGRPLLEDLSLSL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1318 NGGEKVGIVGRTGAGKSSltlgLFR----INESAEGEIIIDDiniakiglhdlRVKITIIPQDPVLFSGSLRMNL---DP 1390
Cdd:COG4178 387 KPGERLLITGPSGSGKST----LLRaiagLWPYGSGRIARPA-----------GARVLFLPQRPYLPLGTLREALlypAT 451
|
170 180 190
....*....|....*....|....*....|..
gi 1953392644 1391 FSQYSDEEVWTSLELAHLKDFVsglpDKLNQE 1422
Cdd:COG4178 452 AEAFSDAELREALEAVGLGHLA----ERLDEE 479
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
667-843 |
3.92e-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: 54.79 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 667 SIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGSVAYVPQqaWIQNDS-------LRENIlfGRQLQERYYKA 739
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQ--YISPDYdgtveefLRSAN--TDDFGSSYYKT 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 740 VIeacaLLPdLEIlpsgdrTEIGEKGV-NLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVD-------AHVGKHIFENvi 811
Cdd:COG1245 438 EI----IKP-LGL------EKLLDKNVkDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavAKAIRRFAEN-- 504
|
170 180 190
....*....|....*....|....*....|...
gi 1953392644 812 gpkgmlKNKTRLLVTHSISYLPQV-DVIIVMTG 843
Cdd:COG1245 505 ------RGKTAMVVDHDIYLIDYIsDRLMVFEG 531
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
1056-1228 |
4.81e-07 |
|
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: 53.26 E-value: 4.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1056 VLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFNVIGACIIILLATP----IASIIIPPLGLIYFFVQR 1131
Cdd:cd18546 82 LQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPrlalVALAALPPLALATRWFRR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1132 fyvASSRQLKRL-ESVSRspVYSHFNETLLGVSVIRAF----EEQERFIRQSDLKVDENQKA------YYPSIvanRWLA 1200
Cdd:cd18546 162 ---RSSRAYRRArERIAA--VNADLQETLAGIRVVQAFrrerRNAERFAELSDDYRDARLRAqrlvaiYFPGV---ELLG 233
|
170 180
....*....|....*....|....*...
gi 1953392644 1201 VrlecVGNCIVLFAALFSVIsRHSLSAG 1228
Cdd:cd18546 234 N----LATAAVLLVGAWRVA-AGTLTVG 256
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1293-1418 |
5.08e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 52.93 E-value: 5.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1293 VEFRDYGLRYRENLDlVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDD--INIAKIGLHDLRVKI 1370
Cdd:PRK13636 6 LKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1953392644 1371 TIIPQDP--VLFSGSLR-------MNLdpfsQYSDEEVWTSLELAHLKDFVSGLPDK 1418
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYqdvsfgaVNL----KLPEDEVRKRVDNALKRTGIEHLKDK 137
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1293-1375 |
5.13e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 53.65 E-value: 5.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1293 VEFRDYGLRYRENLDLV--LKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKI---GLHDLR 1367
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALsekELRKAR 81
|
....*...
gi 1953392644 1368 VKITIIPQ 1375
Cdd:PRK11153 82 RQIGMIFQ 89
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
1021-1188 |
5.17e-07 |
|
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: 53.22 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1021 ALGISQGITVFGYSMAVSIGGIFASRRLHVDLLQNVLRSPMSFFERTP--SGNLVNRFSKELDTVDSMIPQVIKMFMGSL 1098
Cdd:cd18578 60 VLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDDPEnsTGALTSRLSTDASDVRGLVGDRLGLILQAI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1099 FNVIGACIIILLA----TPIASIIIPPLGLIYFFVQRFYVASSRQLKR-LESVSRspvysHFNETLLGVSVIRAFEEQER 1173
Cdd:cd18578 140 VTLVAGLIIAFVYgwklALVGLATVPLLLLAGYLRMRLLSGFEEKNKKaYEESSK-----IASEAVSNIRTVASLTLEDY 214
|
170
....*....|....*
gi 1953392644 1174 FIRQSDLKVDENQKA 1188
Cdd:cd18578 215 FLEKYEEALEEPLKK 229
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
1016-1187 |
5.22e-07 |
|
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: 52.93 E-value: 5.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1016 LSVYGAlgisQGITVFGYSMAVSIGGIFASRRLHVDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFM 1095
Cdd:cd18574 49 LGLYLL----QSLLTFAYISLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1096 GSLFNVIGACIIILLATP----IASIIIPPLGLIYFFVQRFYVASSRQLKRLESVSRspvySHFNETLLGVSVIRAF--- 1168
Cdd:cd18574 125 RSVTQTVGCVVSLYLISPkltlLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKAT----GVADEALGNIRTVRAFame 200
|
170 180
....*....|....*....|
gi 1953392644 1169 -EEQERFIRQSDLKVDENQK 1187
Cdd:cd18574 201 dRELELYEEEVEKAAKLNEK 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
630-847 |
6.55e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.88 E-value: 6.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 630 IERRPVKDGggANSITVKNATFTwARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGS-- 707
Cdd:COG3845 246 VEKAPAEPG--EVVLEVENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEdi 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 708 ------------VAYVPQ----QAWIQNDSLRENILFGRQLQERY-------YKAVIEACA-LLPDLEILPSGDRTEIGe 763
Cdd:COG3845 323 tglsprerrrlgVAYIPEdrlgRGLVPDMSVAENLILGRYRRPPFsrggfldRKAIRAFAEeLIEEFDVRTPGPDTPAR- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 764 kgvNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVD----AHVGKHIFEnvigpkgmLKNKTR--LLVTH------SISy 831
Cdd:COG3845 402 ---SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDvgaiEFIHQRLLE--------LRDAGAavLLISEdldeilALS- 469
|
250
....*....|....*.
gi 1953392644 832 lpqvDVIIVMTGGKIS 847
Cdd:COG3845 470 ----DRIAVMYEGRIV 481
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
652-799 |
6.92e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.77 E-value: 6.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 652 TWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGS----------VAYVPQQAWIQND- 720
Cdd:PRK13543 18 AFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatrgdrsrfMAYLGHLPGLKADl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 721 SLRENILFGRQLQERYYKAvieacallpdleiLPSGDRTEIGEKGV------NLSGGQKQRVSLARAVYCDSDIYLFDDP 794
Cdd:PRK13543 98 STLENLHFLCGLHGRRAKQ-------------MPGSALAIVGLAGYedtlvrQLSAGQKKRLALARLWLSPAPLWLLDEP 164
|
....*
gi 1953392644 795 LSAVD 799
Cdd:PRK13543 165 YANLD 169
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
661-799 |
7.92e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.98 E-value: 7.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSaLLAEMDKV-EGHV--------------AIKGSVAYVPQqawi---qndSL 722
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLS-LIAGARKIqQGRVevlggdmadarhrrAVCPRIAYMPQglgknlyptlSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 723 RENI-----LFGRQLQERyyKAVIE----ACALLPDLEiLPSGdrteigekgvNLSGGQKQRVSLARAVYCDSDIYLFDD 793
Cdd:NF033858 96 FENLdffgrLFGQDAAER--RRRIDellrATGLAPFAD-RPAG----------KLSGGMKQKLGLCCALIHDPDLLILDE 162
|
....*.
gi 1953392644 794 PLSAVD 799
Cdd:NF033858 163 PTTGVD 168
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1309-1388 |
9.30e-07 |
|
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: 51.28 E-value: 9.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1309 VLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIGLHD-LRVKITIIPQDPVLFSG-SLRM 1386
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVEE 94
|
..
gi 1953392644 1387 NL 1388
Cdd:cd03224 95 NL 96
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1293-1377 |
9.38e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 52.00 E-value: 9.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1293 VEFRDygLRYRENLD-LVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIID--DINIAKIGLHDLRVK 1369
Cdd:PRK13639 2 LETRD--LKYSYPDGtEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKgePIKYDKKSLLEVRKT 79
|
....*...
gi 1953392644 1370 ITIIPQDP 1377
Cdd:PRK13639 80 VGIVFQNP 87
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1292-1410 |
9.74e-07 |
|
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: 50.94 E-value: 9.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1292 RVEFRDYGLRYRENLdlVLKHINITINGGEKVGIVGRTGAGKSSL--TL-GLFRInesAEGEIIIDDINIAKIGlHDLRV 1368
Cdd:COG4133 2 MLEAENLSCRRGERL--LFSGLSFTLAAGEALALTGPNGSGKTTLlrILaGLLPP---SAGEVLWNGEPIRDAR-EDYRR 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1953392644 1369 KITIIPQDPVLFSG-SLRMNLDpFSQ------YSDEEVWTSLE---LAHLKD 1410
Cdd:COG4133 76 RLAYLGHADGLKPElTVRENLR-FWAalyglrADREAIDEALEavgLAGLAD 126
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1293-1377 |
1.06e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 52.06 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1293 VEFRDYGLRYRENLDLVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIGLHDLRVKITI 1372
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
....*
gi 1953392644 1373 IPQDP 1377
Cdd:PRK13648 88 VFQNP 92
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
661-857 |
1.12e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 52.00 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG--------SVAYVPQQAWI--QN--DSL-----R 723
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikydkkSLLEVRKTVGIvfQNpdDQLfaptvE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 724 ENILFG--------RQLQERyykaVIEACAllpdleilpsgdrtEIGEKGV------NLSGGQKQRVSLARAVYCDSDIY 789
Cdd:PRK13639 98 EDVAFGplnlglskEEVEKR----VKEALK--------------AVGMEGFenkpphHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953392644 790 LFDDPLSAVDAHVGKHIFENV--IGPKGMlknkTRLLVTHSISYLP-QVDVIIVMTGGKISEMGSYQELLA 857
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLydLNKEGI----TIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
643-851 |
1.15e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 52.05 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 643 SITVKNATFTWARSDP---PTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHV----------------- 702
Cdd:PRK13649 2 GINLQNVSYTYQAGTPfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVrvddtlitstsknkdik 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 703 AIKGSVAYVPQQAWIQ--NDSLRENILFGRQ----LQERYYKAVIEACALLpdleilpsGDRTEIGEKG-VNLSGGQKQR 775
Cdd:PRK13649 82 QIRKKVGLVFQFPESQlfEETVLKDVAFGPQnfgvSQEEAEALAREKLALV--------GISESLFEKNpFELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 776 VSLARAVYCDSDIYLFDDPLSAVDAHVGKH---IFENvIGPKGMlknkTRLLVTHSISYLPQ-VDVIIVMTGGKISEMGS 851
Cdd:PRK13649 154 VAIAGILAMEPKILVLDEPTAGLDPKGRKElmtLFKK-LHQSGM----TIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1293-1381 |
1.22e-06 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 51.43 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1293 VEFRDYGLRYRENLDLV--LKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKI---GLHDLR 1367
Cdd:cd03258 2 IELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLsgkELRKAR 81
|
90
....*....|....
gi 1953392644 1368 VKITIIPQDPVLFS 1381
Cdd:cd03258 82 RRIGMIFQHFNLLS 95
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
968-1168 |
1.30e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 51.74 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 968 KAIGLFISFLSIFLFLCNhvaslVSNYWLSLW-TDDPIVNGTQEHTKIRLSVYGALGISQGITVFGYSMAVSIGGIFASR 1046
Cdd:cd18555 1 KKLLISILLLSLLLQLLT-----LLIPILTQYvIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1047 RLHVDLLQNVLRSPMSFFERTPSGNLVNRFSkELDTVDSMIP-QVIKMFMGSLFnVIGACIIILLATPIASIIIPPLGLI 1125
Cdd:cd18555 76 SLMSDFFEHLLKLPYSFFENRSSGDLLFRAN-SNVYIRQILSnQVISLIIDLLL-LVIYLIYMLYYSPLLTLIVLLLGLL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1953392644 1126 YFFvqrFYVASSRQLKRL---ESVSRSPVYSHFNETLLGVSVIRAF 1168
Cdd:cd18555 154 IVL---LLLLTRKKIKKLnqeEIVAQTKVQSYLTETLYGIETIKSL 196
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
1046-1228 |
1.32e-06 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 51.67 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1046 RRLHVDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFNVIGACI-----------IILLATPI 1114
Cdd:cd18551 69 LDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVlmflldwvltlVTLAVVPL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1115 ASIIIPPLGliyffvQRFYVASSRQLKRLESVSrspvySHFNETLLGVSVIRAFEEQERFIRQSDlkvDENQKAYYPSIV 1194
Cdd:cd18551 149 AFLIILPLG------RRIRKASKRAQDALGELS-----AALERALSAIRTVKASNAEERETKRGG---EAAERLYRAGLK 214
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1953392644 1195 ANRWLAVrLECVGNcIVLFAALFSVI-------SRHSLSAG 1228
Cdd:cd18551 215 AAKIEAL-IGPLMG-LAVQLALLVVLgvggarvASGALTVG 253
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1309-1382 |
1.43e-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: 50.60 E-value: 1.43e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953392644 1309 VLKHINITINGGEKVGIVGRTGAGKSSL--TLGLFRINESAEGEIIIDDINIAKIGLHDlRVK--ITIIPQDPVLFSG 1382
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLakTIMGHPKYEVTEGEILFKGEDITDLPPEE-RARlgIFLAFQYPPEIPG 91
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1293-1380 |
1.84e-06 |
|
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: 50.55 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1293 VEFRDYGLRYRENLD--LVLKHINITINGGEKVGIVGRTGAGKSSL---TLGLFRInesAEGEIIIDDINIAkiglhDLR 1367
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLlriIAGLERP---TSGEVLVDGEPVT-----GPG 72
|
90
....*....|...
gi 1953392644 1368 VKITIIPQDPVLF 1380
Cdd:cd03293 73 PDRGYVFQQDALL 85
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
1045-1172 |
1.91e-06 |
|
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: 51.36 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1045 SRRLHVDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFNVIGACIIILLATP----IASIIIP 1120
Cdd:cd18573 73 VARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPkltlVMLLVVP 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1953392644 1121 PLGLIYFFVQRFYVASSRQLkrLESVSRSpvySHF-NETLLGVSVIRAF--EEQE 1172
Cdd:cd18573 153 PIAVGAVFYGRYVRKLSKQV--QDALADA---TKVaEERLSNIRTVRAFaaERKE 202
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
1027-1250 |
2.00e-06 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) 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: 349992 [Multi-domain] Cd Length: 292 Bit Score: 51.25 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1027 GITVFGYSMAVsIGGIFAS-------RRLHVDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLF 1099
Cdd:cd18548 47 LLALLGLIAGI-LAGYFAAkasqgfgRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1100 NVIGACIIILLATP----IASIIIPPLGLIYFFVQRF-YVASSRQLKRLESVSRSpvyshFNETLLGVSVIRAF----EE 1170
Cdd:cd18548 126 MLIGAIIMAFRINPklalILLVAIPILALVVFLIMKKaIPLFKKVQKKLDRLNRV-----VRENLTGIRVIRAFnredYE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1171 QERFIrqsdlkvDENQKAYYPSIVANRWLAVR---LECVGN----CIVLFAALFsvISRHSLSAG-LVGLsVSYSLQVTT 1242
Cdd:cd18548 201 EERFD-------KANDDLTDTSLKAGRLMALLnplMMLIMNlaivAILWFGGHL--INAGSLQVGdLVAF-INYLMQILM 270
|
....*...
gi 1953392644 1243 YLNWLVRM 1250
Cdd:cd18548 271 SLMMLSMV 278
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
657-799 |
2.73e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.56 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 657 DPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGS------VAYVPQQAWIQNDS-------LR 723
Cdd:PRK13540 13 DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsikkdlCTYQKQLCFVGHRSginpyltLR 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953392644 724 ENILFGRQLQERYYKaVIEACAL--LPDLEILPSGdrteigekgvNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVD 799
Cdd:PRK13540 93 ENCLYDIHFSPGAVG-ITELCRLfsLEHLIDYPCG----------LLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
1052-1167 |
3.06e-06 |
|
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: 50.67 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1052 LLQNVLRSPMSFFERTPSGNLVNRFSkELDTV-DSMIPQVIKMFMGSLFNVIGACIIILLA---TPIASIIIPPLGLIYF 1127
Cdd:cd18782 81 IIDHLLRLPLGFFDKRPVGELSTRIS-ELDTIrGFLTGTALTTLLDVLFSVIYIAVLFSYSpllTLVVLATVPLQLLLTF 159
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1953392644 1128 FVQRFYvasSRQLKRLESvSRSPVYSHFNETLLGVSVIRA 1167
Cdd:cd18782 160 LFGPIL---RRQIRRRAE-ASAKTQSYLVESLTGIQTVKA 195
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
972-1264 |
3.30e-06 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 50.52 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 972 LFISFLSIFLFLcnhvASLVSNYWLSLWTDDPIVNGTQEH-TKIRLSVYGALGISQGITVF-GYSMavsiggIFASRRLH 1049
Cdd:cd18570 5 ILILLLSLLITL----LGIAGSFFFQILIDDIIPSGDINLlNIISIGLILLYLFQSLLSYIrSYLL------LKLSQKLD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1050 VDLLQN----VLRSPMSFFERTPSGNLVNRFSkELDTVDSMIPQV-IKMFMGSLFNVIGACIIILLATPIASIIIPPLgL 1124
Cdd:cd18570 75 IRLILGyfkhLLKLPLSFFETRKTGEIISRFN-DANKIREAISSTtISLFLDLLMVIISGIILFFYNWKLFLITLLII-P 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1125 IYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKAYYPS---IVANRWLAV 1201
Cdd:cd18570 153 LYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLgklSNLQSSIKG 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953392644 1202 RLECVGNCIVLFAALFSVISrHSLSAG-LVGLsvsYSLQV--TTYLNWLVRMSSEMETNIVAVERL 1264
Cdd:cd18570 233 LISLIGSLLILWIGSYLVIK-GQLSLGqLIAF---NALLGyfLGPIENLINLQPKIQEAKVAADRL 294
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
664-857 |
3.52e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 50.17 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 664 ITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG----------------------SVAYVPQQ--AWIQN 719
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgdysyrsqrirmifqdpSTSLNPRQriSQILD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 720 DSLRENILFGRQLQERYYKAVIEACALLPD-LEILPSGdrteigekgvnLSGGQKQRVSLARAVYCDSDIYLFDDPLSAV 798
Cdd:PRK15112 112 FPLRLNTDLEPEQREKQIIETLRQVGLLPDhASYYPHM-----------LAPGQKQRLGLARALILRPKVIIADEALASL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953392644 799 DAHVGKHIFeNVigpkgMLKnktrLLVTHSISYLPQV----------DVIIVMTGGKISEMGSYQELLA 857
Cdd:PRK15112 181 DMSMRSQLI-NL-----MLE----LQEKQGISYIYVTqhlgmmkhisDQVLVMHQGEVVERGSTADVLA 239
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1309-1336 |
4.24e-06 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 49.69 E-value: 4.24e-06
10 20
....*....|....*....|....*...
gi 1953392644 1309 VLKHINITINGGEKVGIVGRTGAGKSSL 1336
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTL 68
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1005-1173 |
4.34e-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: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1005 VNGTQEHTKIRLSVYGALGI--SQGITVFGYSMAVSIGGIFASRRLHVDLLQNVLRSPMSFFERTPSGNLVNRFSKELDT 1082
Cdd:cd18576 26 ALGGGDTASLNQIALLLLGLflLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1083 VDSMIPQVIKMFMGSLFNVIGACIIILLATP----IASIIIPPLGLIYFFVQRFYVASSRQlkRLESVSRSPVysHFNET 1158
Cdd:cd18576 106 IQDTLTTTLAEFLRQILTLIGGVVLLFFISWkltlLMLATVPVVVLVAVLFGRRIRKLSKK--VQDELAEANT--IVEET 181
|
170
....*....|....*..
gi 1953392644 1159 LLGVSVIRAF--EEQER 1173
Cdd:cd18576 182 LQGIRVVKAFtrEDYEI 198
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1048-1194 |
4.37e-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: 350051 [Multi-domain] Cd Length: 293 Bit Score: 50.23 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1048 LHVDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFNVIGACIIILLATPI-ASIIIPPLGLIY 1126
Cdd:cd18778 75 LRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKlALLTLIPIPFLA 154
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953392644 1127 FFVqRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAF----EEQERFIRQSDLKVDENQKA------YYPSIV 1194
Cdd:cd18778 155 LGA-WLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFgreeEEAKRFEALSRRYRKAQLRAmklwaiFHPLME 231
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1310-1377 |
4.82e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 49.99 E-value: 4.82e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953392644 1310 LKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIG-LHDLRVKITIIPQDP 1377
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGIVFQNP 86
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
661-801 |
4.96e-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: 4.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSAL--LAEMDkvEGHVAIKGS--------------VAYVPQQ-AWIQNDSLR 723
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILsgVYQPD--SGEILLDGEpvrfrsprdaqaagIAIIHQElNLVPNLSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 724 ENILFGRQL-------QERYYKAVIEACALLpDLEILPsgdRTEIGEkgvnLSGGQKQRVSLARAVYCDSDIYLFDDPLS 796
Cdd:COG1129 98 ENIFLGREPrrgglidWRAMRRRARELLARL-GLDIDP---DTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTA 169
|
....*
gi 1953392644 797 AVDAH 801
Cdd:COG1129 170 SLTER 174
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
664-847 |
7.56e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.29 E-value: 7.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 664 ITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHV--------------AIKGSVAYVP----QQAWIQNDSLREN 725
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVyldgkpidirsprdAIRAGIMLCPedrkAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 726 I---------LFG--------RQLQERYYKAvieacallpdLEILPSGDRTEIGekgvNLSGGQKQRVSLARAVYCDSDI 788
Cdd:PRK11288 352 InisarrhhlRAGclinnrweAENADRFIRS----------LNIKTPSREQLIM----NLSGGNQQKAILGRWLSEDMKV 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953392644 789 YLFDDPLSAVDahVG-KHIFENVI---GPKGMlknkTRLLVThsiSYLPQV----DVIIVMTGGKIS 847
Cdd:PRK11288 418 ILLDEPTRGID--VGaKHEIYNVIyelAAQGV----AVLFVS---SDLPEVlgvaDRIVVMREGRIA 475
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1292-1377 |
7.86e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 49.24 E-value: 7.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1292 RVEFRDYglRYRENLDLVLKHINITINGGEKVGIVGRTGAGKSSLT---LGLFRineSAEGEIIIDDINIAKIGLHDLRV 1368
Cdd:PRK13635 7 RVEHISF--RYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAkllNGLLL---PEAGTITVGGMVLSEETVWDVRR 81
|
....*....
gi 1953392644 1369 KITIIPQDP 1377
Cdd:PRK13635 82 QVGMVFQNP 90
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
654-801 |
8.47e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.05 E-value: 8.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 654 ARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMD--------KVEGHVAIKGSV-------------AYVP 712
Cdd:PRK13547 10 ARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGEPlaaidaprlarlrAVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 713 QQAwiQND---SLRENILFGRQLQERYYKAV------IEACAL-LPDLEILPSGDRTeigekgvNLSGGQKQRVSLARAV 782
Cdd:PRK13547 90 QAA--QPAfafSAREIVLLGRYPHARRAGALthrdgeIAWQALaLAGATALVGRDVT-------TLSGGELARVQFARVL 160
|
170 180
....*....|....*....|....*....
gi 1953392644 783 ---------YCDSDIYLFDDPLSAVD-AH 801
Cdd:PRK13547 161 aqlwpphdaAQPPRYLLLDEPTAALDlAH 189
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1309-1354 |
9.12e-06 |
|
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: 48.30 E-value: 9.12e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1953392644 1309 VLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIID 1354
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVR 82
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
768-855 |
9.41e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 49.35 E-value: 9.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 768 LSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVGKHIFENVIGPKGMlKNKTRLLVTHSISYLPQV-DVIIVMTGGKI 846
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQK-ENMALVLITHDLALVAEAaHKIIVMYAGQV 232
|
....*....
gi 1953392644 847 SEMGSYQEL 855
Cdd:PRK11022 233 VETGKAHDI 241
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
661-827 |
9.88e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 48.42 E-value: 9.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKgsvayVPQQAWIQNDSLRENILFGRQLQERyyKAV 740
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-----VPDNQFGREASLIDAIGRKGDFKDA--VEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 741 IEACALlpdleilpsGDRTEIGEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVD---AHVGKHIFENVIGPKGml 817
Cdd:COG2401 119 LNAVGL---------SDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtAKRVARNLQKLARRAG-- 187
|
170
....*....|
gi 1953392644 818 knKTRLLVTH 827
Cdd:COG2401 188 --ITLVVATH 195
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1259-1381 |
9.98e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 49.97 E-value: 9.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1259 VAVERLKEYSETEKEAPWQIQemAPPSTWPqvgRVEFRDYGLRYRENlDLVLKHINITINGGEKVGIVGRTGAGKSSLTL 1338
Cdd:PRK10522 294 VAFNKLNKLALAPYKAEFPRP--QAFPDWQ---TLELRNVTFAYQDN-GFSVGPINLTIKRGELLFLIGGNGSGKSTLAM 367
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1953392644 1339 GLFRINESAEGEIIIDDINIAKIGLHDLRVKITIIPQDPVLFS 1381
Cdd:PRK10522 368 LLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFD 410
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1309-1380 |
1.06e-05 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 48.35 E-value: 1.06e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953392644 1309 VLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIGLHD-LRVKITIIPQDPVLF 1380
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQEASIF 90
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
582-859 |
1.08e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 49.97 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 582 AFVSLALFnILRFPL----NILPMVISsivqASVSLKRLRIFlsheELEPDSIERRPVKDGGGANSITVKNATFTWArsD 657
Cdd:PRK10522 266 ATYSLTLL-FLRTPLlsavGALPTLLS----AQVAFNKLNKL----ALAPYKAEFPRPQAFPDWQTLELRNVTFAYQ--D 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 658 PP-TLSGITFSIPEGSLVAVVGQVGCGKSSLlSALLAEMDK-VEGHVAIKGS-VAYVPQQAWIQNDS--LRENILFGRQL 732
Cdd:PRK10522 335 NGfSVGPINLTIKRGELLFLIGGNGSGKSTL-AMLLTGLYQpQSGEILLDGKpVTAEQPEDYRKLFSavFTDFHLFDQLL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 733 QERYYKAVIEACALLpdLEILPSGDRTEIGEKGV---NLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVgKHIFEN 809
Cdd:PRK10522 414 GPEGKPANPALVEKW--LERLKMAHKLELEDGRIsnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHF-RREFYQ 490
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1953392644 810 VIGPKGMLKNKTRLLVTHSISYLPQVDVIIVMTGGKISEM-GSYQELLARD 859
Cdd:PRK10522 491 VLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSELtGEERDAASRD 541
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1001-1263 |
1.13e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 49.01 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1001 DDPIVNGTQEHTKIRLSVYGALGISQGITVFGYSMAVSIGGIFASRRLHVDLLQNVLRSPMSFFERTPSGNLVNRFSKEL 1080
Cdd:cd18540 30 DHFITPGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1081 DTVDSMIPQVIKMFMGSLFNVIGACIIILLATP----IASIIIPPLGLIYFFVQRFYVASSRQLKRLESVsrspVYSHFN 1156
Cdd:cd18540 110 QRLGEIISWGLVDLVWGITYMIGILIVMLILNWklalIVLAVVPVLAVVSIYFQKKILKAYRKVRKINSR----ITGAFN 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1157 ETLLGVSVIRAF--EEQ--ERFirqsdLKVDENQKAYypSIVANRWLAVRLECVGNCIVLFAALFSVISRHSLSAGLV-- 1230
Cdd:cd18540 186 EGITGAKTTKTLvrEEKnlREF-----KELTEEMRRA--SVRAARLSALFLPIVLFLGSIATALVLWYGGILVLAGAIti 258
|
250 260 270
....*....|....*....|....*....|....*.
gi 1953392644 1231 -GLSV--SYSLQVTTYLNWLVRMSSEMETNIVAVER 1263
Cdd:cd18540 259 gTLVAfiSYATQFFEPIQQLARVLAELQSAQASAER 294
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
644-886 |
1.22e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 48.96 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 644 ITVKNATFTWARSDP---PTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-SVAYVPQQAWIQN 719
Cdd:PRK13643 2 IKFEKVNYTYQPNSPfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDiVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 720 DSLRENILFGRQLQERYYKAVIEACALLPD----------------LEILpsGDRTEIGEKG-VNLSGGQKQRVSLARAV 782
Cdd:PRK13643 82 VRKKVGVVFQFPESQLFEETVLKDVAFGPQnfgipkekaekiaaekLEMV--GLADEFWEKSpFELSGGQMRRVAIAGIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 783 YCDSDIYLFDDPLSAVDAHVG---KHIFENVigpkgMLKNKTRLLVTHSISYLPQ-VDVIIVMTGGKISEMGSYQELLAR 858
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKARiemMQLFESI-----HQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQE 234
|
250 260 270
....*....|....*....|....*....|
gi 1953392644 859 dgafAEFLRTYASGDQEQAEQDDGL--TGV 886
Cdd:PRK13643 235 ----VDFLKAHELGVPKATHFADQLqkTGA 260
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
661-806 |
1.32e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 48.24 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-----------------SVAYVPQQ-AWIQNDSL 722
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqplhqmdeearaklrakHVGFVFQSfMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 723 RENILFGRQLQ-ERYYKAVIEACALLPDLEIlpsGDRteIGEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAH 801
Cdd:PRK10584 106 LENVELPALLRgESSRQSRNGAKALLEQLGL---GKR--LDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
|
....*
gi 1953392644 802 VGKHI 806
Cdd:PRK10584 181 TGDKI 185
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
1047-1188 |
1.45e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 48.73 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1047 RLHVDLLQNVLRSPMSFFERTPSGNLVNRFsKELDTV-DSMIPQVIKMFMGSLFNVIGACIIILLATPIASIiipPLGLI 1125
Cdd:cd18566 76 RLSNAAFEHLLSLPLSFFEREPSGAHLERL-NSLEQIrEFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLV---PLVLL 151
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953392644 1126 YFFVQRFYVASSRQLKRLESVSRSPV--YSHFNETLLGVSVIR--AFEEQ--ERFIRQSDLKVDENQKA 1188
Cdd:cd18566 152 GLFVLVAILLGPILRRALKERSRADErrQNFLIETLTGIHTIKamAMEPQmlRRYERLQANAAYAGFKV 220
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
659-801 |
1.56e-05 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 47.81 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 659 PTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAemdkveGHVAIKGSVAYVPQQAWIqnD----------SLRENIL- 727
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG------NYLPDSGSILVRHDGGWV--DlaqaspreilALRRRTIg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 728 ----FGR-------------QLQERYY---KAVIEACALLpdleilpsgDRTEIGEKGVNL-----SGGQKQRVSLARAV 782
Cdd:COG4778 97 yvsqFLRviprvsaldvvaePLLERGVdreEARARARELL---------ARLNLPERLWDLppatfSGGEQQRVNIARGF 167
|
170
....*....|....*....
gi 1953392644 783 YCDSDIYLFDDPLSAVDAH 801
Cdd:COG4778 168 IADPPLLLLDEPTASLDAA 186
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1303-1420 |
1.57e-05 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 48.88 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1303 RENLDLVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIG---LHDLRVK--------IT 1371
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaeLREVRRKkiamvfqsFA 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1372 IIPQDPVLFSGSLRMNLDPF-SQYSDEEVWTSLELAHLKDFVSGLPDKLN 1420
Cdd:PRK10070 117 LMPHMTVLDNTAFGMELAGInAEERREKALDALRQVGLENYAHSYPDELS 166
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
754-869 |
1.77e-05 |
|
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: 46.80 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 754 PSGDRTE-------IGEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVGKHIfENVIGPKGMLKNKTRLLVT 826
Cdd:cd03222 51 PNGDNDEwdgitpvYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNA-ARAIRRLSEEGKKTALVVE 129
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1953392644 827 HSISYLPQV-DVIIVMTGgkisEMGSYQELLARDG---AFAEFLRTY 869
Cdd:cd03222 130 HDLAVLDYLsDRIHVFEG----EPGVYGIASQPKGtreGINRFLRGY 172
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
648-855 |
1.92e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.08 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 648 NATFTWARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG--------SVAYVPQQAWIQN 719
Cdd:PRK10261 19 NIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrQVIELSEQSAAQM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 720 DSLRE--------------NILF--GRQLQE--RYYK------AVIEACALLPDLEILPSgdRTEIGEKGVNLSGGQKQR 775
Cdd:PRK10261 99 RHVRGadmamifqepmtslNPVFtvGEQIAEsiRLHQgasreeAMVEAKRMLDQVRIPEA--QTILSRYPHQLSGGMRQR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 776 VSLARAVYCDSDIYLFDDPLSAVDAHVGKHIFENVigpkGMLKNKTRL---LVTHSISYLPQV-DVIIVMTGGKISEMGS 851
Cdd:PRK10261 177 VMIAMALSCRPAVLIADEPTTALDVTIQAQILQLI----KVLQKEMSMgviFITHDMGVVAEIaDRVLVMYQGEAVETGS 252
|
....
gi 1953392644 852 YQEL 855
Cdd:PRK10261 253 VEQI 256
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1293-1411 |
2.04e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 48.19 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1293 VEFRDYGLRYRENLDlVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIGLHDLRVKITI 1372
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1373 IPQDP--VLFS---------GSLRMNLDPfsQYSDEEVWTSLELAHLKDF 1411
Cdd:PRK13647 84 VFQDPddQVFSstvwddvafGPVNMGLDK--DEVERRVEEALKAVRMWDF 131
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
1042-1264 |
2.23e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 47.94 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1042 IFASRRLHVDLL----QNVLRSPMSFFERTPSGNLVNRFsKELDTVDSMI-PQVIKMFMGSLFNVIgaCIIILLA----- 1111
Cdd:cd18568 67 DYFANRIDLSLLsdfyKHLLSLPLSFFASRKVGDIITRF-QENQKIRRFLtRSALTTILDLLMVFI--YLGLMFYynlql 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1112 TPIASIIIPPLGLIyffvqrfYVASSRQLKRLES---VSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDLKVDENQKA 1188
Cdd:cd18568 144 TLIVLAFIPLYVLL-------TLLSSPKLKRNSReifQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNT 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1189 YYPSIVanrwLAVRLECV-------GNCIVLFAALFSVISrHSLSAG-LVGLSVSYSLqVTTYLNWLVRMSSEMETNIVA 1260
Cdd:cd18568 217 RFRGQK----LSIVLQLIsslinhlGTIAVLWYGAYLVIS-GQLTIGqLVAFNMLFGS-VINPLLALVGLWDELQETRIS 290
|
....
gi 1953392644 1261 VERL 1264
Cdd:cd18568 291 VERL 294
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1293-1377 |
2.41e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 47.87 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1293 VEFRDYGLRYRENLDLVLKHINITINGGEKVGIVGRTGAGKSS---LTLGLFRINESAEGEIIIDDINIAKIGLHDLRVK 1369
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
....*...
gi 1953392644 1370 ITIIPQDP 1377
Cdd:PRK13640 86 VGIVFQNP 93
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1308-1336 |
2.51e-05 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 45.52 E-value: 2.51e-05
10 20
....*....|....*....|....*....
gi 1953392644 1308 LVLKHINITINGGEKVGIVGRTGAGKSSL 1336
Cdd:cd03221 14 LLLKDISLTINPGDRIGLVGRNGAGKSTL 42
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
671-827 |
2.54e-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: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 671 GSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIkgsvayvpqqawIQNDSLRENILFGRQLqeryykavieacallpdl 750
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY------------IDGEDILEEVLDQLLL------------------ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 751 eilpsgdrTEIGEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVGKHIFENVIGPKGMLKNKTR----LLVT 826
Cdd:smart00382 52 --------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKnltvILTT 123
|
.
gi 1953392644 827 H 827
Cdd:smart00382 124 N 124
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1309-1366 |
2.65e-05 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 47.04 E-value: 2.65e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953392644 1309 VLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDD----INIAKIGLHDL 1366
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHdggwVDLAQASPREI 87
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1029-1193 |
2.79e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 47.95 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1029 TVFGYSMAVSIGGiFASRRLH---VDLLQNVLRSPMSFFERTPSGNL-------VNRFSKELDTVDSMIPQVIKMFMGsl 1098
Cdd:cd18565 68 SLFQYLSGVLWRR-FAQRVQHdlrTDTYDHVQRLDMAFFEDRQTGDLmsvlnndVNQLERFLDDGANSIIRVVVTVLG-- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1099 fnvIGAcIIILLATPIASIIIPPLGLIYFFVQRFyvasSRQLKRLESVSRSPV---YSHFNETLLGVSVIRAF----EEQ 1171
Cdd:cd18565 145 ---IGA-ILFYLNWQLALVALLPVPLIIAGTYWF----QRRIEPRYRAVREAVgdlNARLENNLSGIAVIKAFtaedFER 216
|
170 180
....*....|....*....|....*...
gi 1953392644 1172 ERFIRQSDLKVDENQKA------YYPSI 1193
Cdd:cd18565 217 ERVADASEEYRDANWRAirlraaFFPVI 244
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
664-854 |
3.73e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 47.56 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 664 ITFSIPEGSLVAVVGQVGCGKSSLLSAL--LAEMDkvEGHVAIKGSV-----------------AYVPQQAWI-QNDSLR 723
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAIsgLTRPQ--KGRIVLNGRVlfdaekgiclppekrriGYVFQDARLfPHYKVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 724 ENILFG--RQLQErYYKAVIEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDah 801
Cdd:PRK11144 95 GNLRYGmaKSMVA-QFDKIVALLGIEPLLDRYPG-----------SLSGGEKQRVAIGRALLTAPELLLMDEPLASLD-- 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 802 vgkhifenvigpkgmLKNKTRLL----------------VTHSISYLPQV-DVIIVMTGGKISEMGSYQE 854
Cdd:PRK11144 161 ---------------LPRKRELLpylerlareinipilyVSHSLDEILRLaDRVVVLEQGKVKAFGPLEE 215
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1294-1375 |
4.24e-05 |
|
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: 46.37 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1294 EFRDYGLRYRENLdlVLKHINITINGGEKVGIVGRTGAGKSSLT---LGLFRineSAEGEIIIDDINIAKIglhdlRVKI 1370
Cdd:cd03235 1 EVEDLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLkaiLGLLK---PTSGSIRVFGKPLEKE-----RKRI 70
|
....*
gi 1953392644 1371 TIIPQ 1375
Cdd:cd03235 71 GYVPQ 75
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
647-880 |
4.34e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 46.73 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 647 KNATFTwarsdppTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGSVAYVPQQAWIqNDSLR--E 724
Cdd:PRK13546 33 KNKTFF-------ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGL-SGQLTgiE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 725 NILFgRQLQERYYKAVIEacALLPdlEILpsgDRTEIGE---KGV-NLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDA 800
Cdd:PRK13546 105 NIEF-KMLCMGFKRKEIK--AMTP--KII---EFSELGEfiyQPVkKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 801 HVGKHIFENVIGPKGmlKNKTRLLVTHSISYLPQVDVIIV-MTGGKISEMGSYQELLARDGAFAEFLRTYASGDQEQAEQ 879
Cdd:PRK13546 177 TFAQKCLDKIYEFKE--QNKTIFFVSHNLGQVRQFCTKIAwIEGGKLKDYGELDDVLPKYEAFLNDFKKKSKAEQKEFRN 254
|
.
gi 1953392644 880 D 880
Cdd:PRK13546 255 K 255
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1309-1377 |
4.71e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.78 E-value: 4.71e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953392644 1309 VLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESaEGEIIIDDINIAKIG---LHDLRVKITIIPQDP 1377
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-QGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDP 371
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
972-1242 |
4.91e-05 |
|
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: 47.07 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 972 LFISFLSIFLflcnHVASLVSNYWLSLWTDDPIVNGTQEhtkirLSVYGALGISqGITVF--GYSMAVSIGGIFASRRLH 1049
Cdd:cd18567 5 LQILLLSLAL----ELFALASPLYLQLVIDEVIVSGDRD-----LLTVLAIGFG-LLLLLqaLLSALRSWLVLYLSTSLN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1050 VDLLQNV----LRSPMSFFERTPSGNLVNRFSkELDTVDSMIPQVikmFMGSLFN---VIGACIIILLATPIASIIIPPL 1122
Cdd:cd18567 75 LQWTSNLfrhlLRLPLSYFEKRHLGDIVSRFG-SLDEIQQTLTTG---FVEALLDglmAILTLVMMFLYSPKLALIVLAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1123 GLIYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAF-EEQERFIRQSDLKVDE-NQkayypSIVANRWLA 1200
Cdd:cd18567 151 VALYALLRLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFgREAEREARWLNLLVDAiNA-----DIRLQRLQI 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1953392644 1201 VR------LECVGNCIVLFAALFSVISRHsLSAG-LVGLsVSYSLQVTT 1242
Cdd:cd18567 226 LFsaanglLFGLENILVIYLGALLVLDGE-FTVGmLFAF-LAYKDQFSS 272
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1293-1380 |
5.23e-05 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 46.24 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1293 VEFRDYGLRYRENLdlVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIID--DINIAKIGLHDLRVKI 1370
Cdd:PRK09493 2 IEFKNVSKHFGPTQ--VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDglKVNDPKVDERLIRQEA 79
|
90
....*....|
gi 1953392644 1371 TIIPQDPVLF 1380
Cdd:PRK09493 80 GMVFQQFYLF 89
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1309-1427 |
8.07e-05 |
|
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: 46.39 E-value: 8.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1309 VLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIiiddiniakigLHDLRvkITIIPQDPVLFSGSLRMNL 1388
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-----------KHSGR--ISFSSQFSWIMPGTIKENI 118
|
90 100 110
....*....|....*....|....*....|....*....
gi 1953392644 1389 DPFSQYSDEEVWTSLELAHLKDFVSGLPDKLNQECAEGG 1427
Cdd:cd03291 119 IFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGG 157
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1293-1410 |
8.70e-05 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 45.85 E-value: 8.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1293 VEFRDYGLRYRENLdlVLKHINITINGGEKVGIVGRTGAGKSSL--------------TLGLF---RINESaegeiiIDD 1355
Cdd:COG1119 4 LELRNVTVRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTLlslitgdlpptygnDVRLFgerRGGED------VWE 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953392644 1356 INiAKIGL------HDLRVKITIIpqDPVL--FSGSlrmnLDPFSQYSDEEV-----W-TSLELAHLKD 1410
Cdd:COG1119 76 LR-KRIGLvspalqLRFPRDETVL--DVVLsgFFDS----IGLYREPTDEQRerareLlELLGLAHLAD 137
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
661-810 |
1.01e-04 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 45.64 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG--------------SVAYVPQQAWI-QNDSLREN 725
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGkditdwqtakimreAVAIVPEGRRVfSRMTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 726 ILFGRQLQER--YYKAVIEACALLPDLEilpsgDRTEigEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVG 803
Cdd:PRK11614 101 LAMGGFFAERdqFQERIKWVYELFPRLH-----ERRI--QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173
|
....*..
gi 1953392644 804 KHIFENV 810
Cdd:PRK11614 174 QQIFDTI 180
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1309-1378 |
1.45e-04 |
|
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: 43.96 E-value: 1.45e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953392644 1309 VLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIGLHD-LRVKITIIPQDPV 1378
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMVYQLSV 85
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
661-798 |
1.57e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.93 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG--------------SVAYVPQQAWIQND-SLREN 725
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynkldhklaaqlGIGIIYQELSVIDElTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 726 ILFGRQLQER--------YYKAVIEACALLpdleiLPSGDRTEIGEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSA 797
Cdd:PRK09700 101 LYIGRHLTKKvcgvniidWREMRVRAAMML-----LRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
|
.
gi 1953392644 798 V 798
Cdd:PRK09700 176 L 176
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1310-1377 |
1.64e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.10 E-value: 1.64e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1310 LKHINITINGGEKVGIVGRTGAGKSSLTLGLfrinesaEGEIIIDD--INIAKiglhDLRVkiTIIPQDP 1377
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDDgrIIYEQ----DLIV--ARLQQDP 75
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
978-1133 |
1.70e-04 |
|
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: 45.38 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 978 SIFLFLCNhVASLVSNYWLSLWTDDPIVNGTQEhtKIRLSVygalgISQGITVFGYSMAVSI-GGIF---ASR---RLHV 1050
Cdd:cd18784 2 FFFLLAAA-VGEIFIPYYTGQVIDGIVIEKSQD--KFSRAI-----IIMGLLAIASSVAAGIrGGLFtlaMARlniRIRN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1051 DLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFNVIGACIIILLAT---PIASIIIPPLGliyF 1127
Cdd:cd18784 74 LLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSwqlSLVTLIGLPLI---A 150
|
....*.
gi 1953392644 1128 FVQRFY 1133
Cdd:cd18784 151 IVSKVY 156
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1309-1380 |
1.72e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 45.78 E-value: 1.72e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953392644 1309 VLKHINITINGGEKVGIVGRTGAGKSslTL-----GLFRINesaEGEIIIDDINIAKIGLHD-LRVKITIIPQDPVLF 1380
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKS--TLmkilsGVYQPD---SGEILLDGEPVRFRSPRDaQAAGIAIIHQELNLV 91
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
661-829 |
1.79e-04 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 44.48 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG---------SVAYVPQQ-AWIQNDslrENILFGR 730
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhditrlknrEVPFLRRQiGMIFQD---HHLLMDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 731 QLQERYYKAVIEACALLPDLEILPSGDRTEIG--EKGVN----LSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVGK 804
Cdd:PRK10908 95 TVYDNVAIPLIIAGASGDDIRRRVSAALDKVGllDKAKNfpiqLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSE 174
|
170 180 190
....*....|....*....|....*....|
gi 1953392644 805 HI---FE--NVIGpkgmlknKTRLLVTHSI 829
Cdd:PRK10908 175 GIlrlFEefNRVG-------VTVLMATHDI 197
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
664-799 |
1.93e-04 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 44.88 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 664 ITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAI--------------KGSVAYVPQQAWI-QNDSLRENILF 728
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddedisllplharaRRGIGYLPQEASIfRRLSVYDNLMA 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953392644 729 GRQLQERYYKAVIE--ACALLPDLEIlpSGDRTEIGEkgvNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVD 799
Cdd:PRK10895 102 VLQIRDDLSAEQREdrANELMEEFHI--EHLRDSMGQ---SLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1308-1336 |
2.16e-04 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 45.44 E-value: 2.16e-04
10 20
....*....|....*....|....*....
gi 1953392644 1308 LVLKHINITINGGEKVGIVGRTGAGKSSL 1336
Cdd:COG0488 329 TLLDDLSLRIDRGDRIGLIGPNGAGKSTL 357
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1299-1336 |
2.32e-04 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 44.76 E-value: 2.32e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1953392644 1299 GLRYRENLDLVLKHINITINGGEKVGIVGRTGAGKSSL 1336
Cdd:PRK13548 7 NLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTL 44
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1309-1340 |
2.51e-04 |
|
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: 44.35 E-value: 2.51e-04
10 20 30
....*....|....*....|....*....|..
gi 1953392644 1309 VLKHINITINGGEKVGIVGRTGAGKSSLtLGL 1340
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTL-LGL 57
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
750-847 |
2.58e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.57 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 750 LEILPSGDRtEIGEkgvnLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDahvgkhIFE-----NVIgpKGMLKNKTRLL 824
Cdd:PRK13409 200 LGLENILDR-DISE----LSGGELQRVAIAAALLRDADFYFFDEPTSYLD------IRQrlnvaRLI--RELAEGKYVLV 266
|
90 100 110
....*....|....*....|....*....|.
gi 1953392644 825 VTHSIS---YLpqVDVIIVMTG-----GKIS 847
Cdd:PRK13409 267 VEHDLAvldYL--ADNVHIAYGepgayGVVS 295
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
768-857 |
2.59e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.47 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 768 LSGGQKQRVSLARAVYCDSDIYLFDDPLSAVDAHVGKHIFENVIGPKGMLkNKTRLLVTHSISYLPQV-DVIIVMTGGKI 846
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQEL-NMGLLFITHNLSIVRKLaDRVAVMQNGRC 235
|
90
....*....|.
gi 1953392644 847 SEMGSYQELLA 857
Cdd:PRK15134 236 VEQNRAATLFS 246
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1308-1377 |
2.80e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 44.69 E-value: 2.80e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953392644 1308 LVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIG-LHDLRVKITIIPQDP 1377
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIRNKAGMVFQNP 94
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
703-799 |
2.97e-04 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 44.25 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 703 AIKGsVAYVPQQAWI-QNDSLRENILFGRQLQERYYKAVIEAC-ALLPDLEILPSGDRteigeKGVNLSGGQKQRVSLAR 780
Cdd:COG1137 76 ARLG-IGYLPQEASIfRKLTVEDNILAVLELRKLSKKEREERLeELLEEFGITHLRKS-----KAYSLSGGERRRVEIAR 149
|
90
....*....|....*....
gi 1953392644 781 AVYCDSDIYLFDDPLSAVD 799
Cdd:COG1137 150 ALATNPKFILLDEPFAGVD 168
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
1027-1174 |
3.45e-04 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 44.25 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1027 GITVFGYSMAVSI-GGIFA------SRRLHVDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLF 1099
Cdd:cd18590 43 CLFSLGSSLSAGLrGGLFMctlsrlNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1100 NVIGACIIILLATP----IASIIIPPLGLIyffvQRFYVASSRQLKR--LESVSRSPvySHFNETLLGVSVIRAF----E 1169
Cdd:cd18590 123 KTLGMLGFMLSLSWqltlLTLIEMPLTAIA----QKVYNTYHQKLSQavQDSIAKAG--ELAREAVSSIRTVRSFkaeeE 196
|
....*
gi 1953392644 1170 EQERF 1174
Cdd:cd18590 197 EACRY 201
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1272-1421 |
3.73e-04 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 44.31 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1272 KEAPWQiqemaPPSTWPQVGRVEFRDYGlryrenldlvlkhinitingGEKVGIVGRTGAGKSSLTLGLFRINESAEGEI 1351
Cdd:PRK15079 24 KQWFWQ-----PPKTLKAVDGVTLRLYE--------------------GETLGVVGESGCGKSTFARAIIGLVKATDGEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1352 II---DDINIAKIGLHDLRVKITIIPQDPvLFSGSLRMNL-----DPFSQY----SDEEVWTSLELAHLKdfVSGLPDKL 1419
Cdd:PRK15079 79 AWlgkDLLGMKDDEWRAVRSDIQMIFQDP-LASLNPRMTIgeiiaEPLRTYhpklSRQEVKDRVKAMMLK--VGLLPNLI 155
|
..
gi 1953392644 1420 NQ 1421
Cdd:PRK15079 156 NR 157
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
1063-1264 |
4.61e-04 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). 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. 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: 349998 [Multi-domain] Cd Length: 299 Bit Score: 43.95 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1063 FFERTPSGNLVNRFSKELD-TVDSMIPQVIKMFMGSLFNVIGACIIILL---ATPIASIIIPplglIYFFVQRFYVASSR 1138
Cdd:cd18554 96 YYANNRSGEIISRVINDVEqTKDFITTGLMNIWLDMITIIIAICIMLVLnpkLTFVSLVIFP----FYILAVKYFFGRLR 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1139 QLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIRQSDlkvDENQKAYYPSIVANRWLAVRLECV------GNCIVL 1212
Cdd:cd18554 172 KLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFD---KRNGHFLTRALKHTRWNAKTFSAVntitdlAPLLVI 248
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1953392644 1213 FAALFSVISrHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERL 1264
Cdd:cd18554 249 GFAAYLVIE-GNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
659-855 |
4.79e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 44.66 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 659 PTLSGITFSIPEGSLVAVVGQVGCGKSSLLS--ALLAEMD----KVEGHVAIKGSVA-------Y-VPQQAWI-QNDSLR 723
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKiiAGIVPPDsgtlEIGGNPCARLTPAkahqlgiYlVPQEPLLfPNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 724 ENILFG---RQLQERYYKAVIEA--CALLPD-----LEIlpsGDRteigekgvnlsggqkQRVSLARAVYCDSDIYLFDD 793
Cdd:PRK15439 105 ENILFGlpkRQASMQKMKQLLAAlgCQLDLDssagsLEV---ADR---------------QIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953392644 794 PLSAVDAHVGKHIFENVigpkGMLKNKTRLLV--THSISYLPQV-DVIIVMTGGKISEMGSYQEL 855
Cdd:PRK15439 167 PTASLTPAETERLFSRI----RELLAQGVGIVfiSHKLPEIRQLaDRISVMRDGTIALSGKTADL 227
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1309-1381 |
5.26e-04 |
|
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: 42.92 E-value: 5.26e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953392644 1309 VLKHINITINGGEKVGIVGRTGAGKSSL--TLGLFRINESAEGEIIIDDINiakIGLHDLRVKITIIPQDPVLFS 1381
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLlnALAGRRTGLGVSGEVLINGRP---LDKRSFRKIIGYVPQDDILHP 95
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1302-1388 |
6.30e-04 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 42.78 E-value: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1302 YRENLDLVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIGLHDLRVKITIIPQDPVLFS 1381
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFG 94
|
....*..
gi 1953392644 1382 GSLRMNL 1388
Cdd:PRK10247 95 DTVYDNL 101
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1309-1352 |
6.92e-04 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 44.02 E-value: 6.92e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1953392644 1309 VLKHINITINGGEKVGIVGRTGAGKSSLtLGLFRINESAE---GEII 1352
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMDQYEptsGRII 60
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1051-1173 |
7.64e-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: 43.24 E-value: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1051 DLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFNVIGACI-----------IILLATPIasIII 1119
Cdd:cd18575 74 AVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVmlfitspkltlLVLLVIPL--VVL 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1953392644 1120 PplglIYFFVQRFYVASSRQLKRLESVSrspvySHFNETLLGVSVIRAF--EEQER 1173
Cdd:cd18575 152 P----IILFGRRVRRLSRASQDRLADLS-----AFAEETLSAIKTVQAFtrEDAER 198
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
661-797 |
9.25e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.45 E-value: 9.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-SVAY----VPQQAWIQ----------NDSLREN 725
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGkEVTFngpkSSQEAGIGiihqelnlipQLTIAEN 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953392644 726 ILFGRQLQER-----YYKAVIEACALLPDLEiLPSGDRTEIGEkgvnLSGGQKQRVSLARAVYCDSDIYLFDDPLSA 797
Cdd:PRK10762 100 IFLGREFVNRfgridWKKMYAEADKLLARLN-LRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTDA 171
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1292-1377 |
1.16e-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: 43.13 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1292 RVEFRDYGLRYRenldlVLKHINITINGGEKVGIVGRTGAGKS--SL-TLGLF-RINESAEGEIIIDDINIAKIGLHDLR 1367
Cdd:COG4172 13 SVAFGQGGGTVE-----AVKGVSFDIAAGETLALVGESGSGKSvtALsILRLLpDPAAHPSGSILFDGQDLLGLSERELR 87
|
90
....*....|....
gi 1953392644 1368 ----VKITIIPQDP 1377
Cdd:COG4172 88 rirgNRIAMIFQEP 101
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1309-1355 |
1.17e-03 |
|
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: 41.88 E-value: 1.17e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1953392644 1309 VLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDD 1355
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG 61
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
643-800 |
1.18e-03 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 41.85 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 643 SITVKNATFT--WARSDPPTLSGITFSIPEGSLVAVVGQVGCGKSSLLSALLA--EMDKVEGHVAIKG---------SVA 709
Cdd:cd03232 3 VLTWKNLNYTvpVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGrpldknfqrSTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 710 YVPQQ-AWIQNDSLRENILFGRQLQEryykavieacallpdleilpsgdrteigekgvnLSGGQKQRVSLARAVYCDSDI 788
Cdd:cd03232 83 YVEQQdVHSPNLTVREALRFSALLRG---------------------------------LSVEQRKRLTIGVELAAKPSI 129
|
170
....*....|..
gi 1953392644 789 YLFDDPLSAVDA 800
Cdd:cd03232 130 LFLDEPTSGLDS 141
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
661-857 |
1.21e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 43.16 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSALLaEMDKVEGHVAIKGSvayvPQQAW-----------IQ------NDSL- 722
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTTGLALL-RLINSQGEIWFDGQ----PLHNLnrrqllpvrhrIQvvfqdpNSSLn 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 723 -RENI--------------LFGRQLQERYyKAVIEACALLPDLEI-LPSgdrteigekgvNLSGGQKQRVSLARAVYCDS 786
Cdd:PRK15134 377 pRLNVlqiieeglrvhqptLSAAQREQQV-IAVMEEVGLDPETRHrYPA-----------EFSGGQRQRIAIARALILKP 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 787 DIYLFDDPLSAVDAHVGKHIFEnvigpkgMLKnktRLLVTHSISYL-------------PQVdviIVMTGGKISEMGSYQ 853
Cdd:PRK15134 445 SLIILDEPTSSLDKTVQAQILA-------LLK---SLQQKHQLAYLfishdlhvvralcHQV---IVLRQGEVVEQGDCE 511
|
....
gi 1953392644 854 ELLA 857
Cdd:PRK15134 512 RVFA 515
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1293-1377 |
1.29e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 42.31 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1293 VEFRDYGLRYRENL---DLVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIA----KIGLHD 1365
Cdd:PRK13634 3 ITFQKVEHRYQYKTpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkkNKKLKP 82
|
90
....*....|..
gi 1953392644 1366 LRVKITIIPQDP 1377
Cdd:PRK13634 83 LRKKVGIVFQFP 94
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1293-1412 |
1.83e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 42.10 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1293 VEFRDYGLRYRENLDlVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIGLHDLRVKITI 1372
Cdd:PRK13652 4 IETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1953392644 1373 IPQDP--VLFS---------GSLRMNLDPFS-QYSDEEVWTSLELAHLKDFV 1412
Cdd:PRK13652 83 VFQNPddQIFSptveqdiafGPINLGLDEETvAHRVSSALHMLGLEELRDRV 134
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1299-1355 |
2.00e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 41.01 E-value: 2.00e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1299 GLRYRENLDLVLKHINITINGGEKVGIVGRTGAGKSSL--TL-GLFRInesAEGEIIIDD 1355
Cdd:PRK13539 7 DLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLlrLIaGLLPP---AAGTIKLDG 63
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1320-1377 |
2.02e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 42.54 E-value: 2.02e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953392644 1320 GEKVGIVGRTGAGKSSLTLGLFRINESAEGEII-----IDDINIAKigLHDLRVKITIIPQDP 1377
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIfngqrIDTLSPGK--LQALRRDIQFIFQDP 410
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1309-1377 |
2.38e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 41.61 E-value: 2.38e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953392644 1309 VLKHINITINGGEKVGIVGRTGAGKSSLT--LGLFRINESAEGEIIIDDINIAKIGLHDLRVKITIIPQDP 1377
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIehLNALLLPDTGTIEWIFKDEKNKKKTKEKEKVLEKLVIQKT 92
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
750-799 |
2.54e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 42.08 E-value: 2.54e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1953392644 750 LEILPSGDRtEIGEkgvnLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVD 799
Cdd:COG1245 200 LGLENILDR-DISE----LSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1280-1358 |
2.72e-03 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 41.10 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1280 EMAPPSTwPQVGRVeFRDYGLRYRENLDLVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRI--NESAEGEIIIDDIN 1357
Cdd:COG2401 18 SSVLDLS-ERVAIV-LEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAlkGTPVAGCVDVPDNQ 95
|
.
gi 1953392644 1358 I 1358
Cdd:COG2401 96 F 96
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1297-1377 |
2.73e-03 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 41.53 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1297 DYGLRYREnlDLVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII--DDINIAKIGLHDLRVKITIIP 1374
Cdd:PRK13638 6 DLWFRYQD--EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWqgKPLDYSKRGLLALRQQVATVF 83
|
...
gi 1953392644 1375 QDP 1377
Cdd:PRK13638 84 QDP 86
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1300-1349 |
2.95e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.08 E-value: 2.95e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1300 LRYRENLDLVLKHINITINGGEKVGIVGRTGAGKSSLtLGLFRINESAEG 1349
Cdd:PRK10636 7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTL-LALLKNEISADG 55
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1309-1336 |
3.02e-03 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 42.02 E-value: 3.02e-03
10 20
....*....|....*....|....*...
gi 1953392644 1309 VLKHINITINGGEKVGIVGRTGAGKSSL 1336
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTL 50
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1309-1388 |
3.09e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 41.96 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1309 VLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIG---LHDLrvKITIIPQDPVLFSG-SL 1384
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpakAHQL--GIYLVPQEPLLFPNlSV 103
|
....
gi 1953392644 1385 RMNL 1388
Cdd:PRK15439 104 KENI 107
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
670-799 |
3.43e-03 |
|
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: 40.81 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 670 EGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHvaikgsvaYVPQQAWiqNDSLREniLFGRQLQErYYKAVIEA---CAL 746
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--------FDDPPDW--DEILDE--FRGSELQN-YFTKLLEGdvkVIV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 747 LP---DL----------EILPSGDRTEIGEKGV--------------NLSGGQKQRVSLARAVYCDSDIYLFDDPLSAVD 799
Cdd:cd03236 92 KPqyvDLipkavkgkvgELLKKKDERGKLDELVdqlelrhvldrnidQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
661-800 |
3.55e-03 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 41.73 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSALLA--EMDKVEGHVAIKGS--------------VAYVPQQ-AWIQNDSLR 723
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWSGSplkasnirdteragIVIIHQElTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 724 ENILFGRQLQER----YYKAVIEAC-ALLPDLEILPSGDRTEIGEKGvnlsGGQKQRVSLARAVYCDSDIYLFDDPLSAV 798
Cdd:TIGR02633 97 ENIFLGNEITLPggrmAYNAMYLRAkNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
..
gi 1953392644 799 DA 800
Cdd:TIGR02633 173 TE 174
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1299-1377 |
3.89e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 40.93 E-value: 3.89e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953392644 1299 GLRYRENLDLVlKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIGLHDLRVKITIIPQDP 1377
Cdd:PRK15112 19 GWFRRQTVEAV-KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDP 96
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
718-868 |
4.05e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.77 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 718 QNDSLRENILfGRQLQERY--------YKAVIEACALLPDLEILPsgdrtEIGEKGVN-LSGGQKQRVSLARAVYCDSDI 788
Cdd:PLN03073 292 NKDGVDKDAV-SQRLEEIYkrlelidaYTAEARAASILAGLSFTP-----EMQVKATKtFSGGWRMRIALARALFIEPDL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 789 YLFDDPLSAVDAHVgkhifenVIGPKGMLKN--KTRLLVTHSISYLPQVDVIIVMTGGkisemgsyQELLARDGAFAEFL 866
Cdd:PLN03073 366 LLLDEPTNHLDLHA-------VLWLETYLLKwpKTFIVVSHAREFLNTVVTDILHLHG--------QKLVTYKGDYDTFE 430
|
..
gi 1953392644 867 RT 868
Cdd:PLN03073 431 RT 432
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1313-1384 |
4.11e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 41.10 E-value: 4.11e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953392644 1313 INITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIA---KIGLHDLRVKITIIPQDPVlfsGSL 1384
Cdd:PRK11308 34 VSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadPEAQKLLRQKIQIVFQNPY---GSL 105
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1310-1429 |
4.66e-03 |
|
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: 40.39 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1310 LKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKIGLHDL----RVKITIIPQDPVLFSGSLR 1385
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1953392644 1386 MNLDPFSQYSDEEVWTSLELAHLKDFVSGLPDKLNQECAEGGEN 1429
Cdd:cd03290 97 ENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGIN 140
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1293-1377 |
5.18e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 40.46 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1293 VEFRDYGLRYRENLDL-VLKHINITINGGEKVGIVGRTGAGKSS---LTLGLFrinESAEGEIIIDDINIAKIGLHDLRV 1368
Cdd:PRK13642 5 LEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTtarLIDGLF---EEFEGKVKIDGELLTAENVWNLRR 81
|
....*....
gi 1953392644 1369 KITIIPQDP 1377
Cdd:PRK13642 82 KIGMVFQNP 90
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1295-1377 |
5.67e-03 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 40.44 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1295 FRDYGLRYRENLDLVLKHINITINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDDINIAKI---GLHDLRVKIT 1371
Cdd:PRK10419 13 YAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQ 92
|
....*.
gi 1953392644 1372 IIPQDP 1377
Cdd:PRK10419 93 MVFQDS 98
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
661-807 |
6.45e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.87 E-value: 6.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 661 LSGITFSIPEGSLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGS--------------VAYVPQQA-WIQNDSLREN 725
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeidfksskealengISMVHQELnLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 726 ILFGRQL-------QERYYKAVIEACALLpDLEILPSgdrteigEKGVNLSGGQKQRVSLARAVYCDSDIYLFDDPLSAV 798
Cdd:PRK10982 94 MWLGRYPtkgmfvdQDKMYRDTKAIFDEL-DIDIDPR-------AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
....*....
gi 1953392644 799 DAHVGKHIF 807
Cdd:PRK10982 166 TEKEVNHLF 174
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1309-1355 |
7.16e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 40.60 E-value: 7.16e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1953392644 1309 VLKHINITINGGEKVGIVGRTGAGKSSLtL----GLFRInesAEGEIIIDD 1355
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTL-LrmvaGLERI---TSGEIWIGG 65
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
1029-1125 |
9.66e-03 |
|
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: 39.93 E-value: 9.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953392644 1029 TVFGYSMAVSIGGIFAS--------------RRLHVDLLQNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMF 1094
Cdd:cd18780 44 AVLILLGVVLIGSIATFlrswlftlagervvARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSML 123
|
90 100 110
....*....|....*....|....*....|....*.
gi 1953392644 1095 MGSLFNVIGAcIIILLA-----TPIASIIIPPLGLI 1125
Cdd:cd18780 124 LRYLVQIIGG-LVFMFTtswklTLVMLSVVPPLSIG 158
|
|
| |
