|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
7-1527 |
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: 3186.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 7 CSADGSDPLWDWNVTWHTSNPDFTKCFQNTVLTWVPCFYLWSCFPLYFFYLSRHDRGYIQMTHLNKTKTALGFFLWIICW 86
Cdd:TIGR00957 1 CSADGSDPLWDWNVTWHTSNPDFTKCFQNTVLAWVPCFYLWVCFPCYFLYLSRHDRGYIQMTHLNKTKTALGFLLWIVCW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 87 ADLFYSFWERSQGVLRAPVLLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVALLCALAILRSKIISALKKDAH 166
Cdd:TIGR00957 81 ADLFYSFWERSHGRAPAPVFLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVALVCALAILRSKILLALKEDAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 167 VDVFRDSTFYLYFTLVLVQLVLSCFSDCSPLFSETVHDRNPCPESSASFLSRITFWWITGMMVHGYRQPLESSDLWSLNK 246
Cdd:TIGR00957 161 VDPFRDTTFYIYFALVLSQLVLSCFSDKSPLFSETNHDPNPCPESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 247 EDTSEEVVPVLVNNWKKECDKSRKQPVRIVYAPpKDPSKPKGSSQLDVNEEVEALIVKSPHKDREPSLFKVLYKTFGPYF 326
Cdd:TIGR00957 241 EDTSEMVVPVLVENWKKECKKTRKQPVSAVYGK-KDPSKPKGSSQLDANEEVEALIVKSPHKPRKPSLFKVLYKTFGPYF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 327 LMSFLYKALHDLMMFAGPKILELIINFVNDREAPDWQGYFYTALLFVSACLQTLALHQYFHICFVSGMRIKTAVVGAVYR 406
Cdd:TIGR00957 320 LMSFCFKAIHDLMMFIGPQILSLLIRFVNDPMAPDWQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 407 KALLITNAARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLSLGPSVLAGVAVMILMVPLNAVMAM 486
Cdd:TIGR00957 400 KALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAM 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 487 KTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMSIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTF 566
Cdd:TIGR00957 480 KTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITF 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 567 AVFVTVDERNILDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRSIKSGEGNSITV 646
Cdd:TIGR00957 560 AVYVTVDENNILDAEKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGEGNSITV 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 647 KNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQQAWIQNDSLRENI 726
Cdd:TIGR00957 640 HNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENI 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 727 LFGHPLQENYYKAVMEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHI 806
Cdd:TIGR00957 720 LFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 807 FEKVVGPMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAEFLRTYANAEQDLASEDD---SV 883
Cdd:TIGR00957 800 FEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEQQGHLEDSwtaLV 879
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 884 SGSGKESKPVENGMLVTDTVGKHLQRHLSNSSSHSGDTSQQHSSIAELQKAGAKEETWKLMEADKAQTGQVQLSVYWNYM 963
Cdd:TIGR00957 880 SGEGKEAKLIENGMLVTDVVGKQLQRQLSASSSDSGDQSRHHGSSAELQKAEAKEETWKLMEADKAQTGQVELSVYWDYM 959
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 964 KAIGLFITFLSIFLFLCNHVSALASNYWLSLWTDDpPVVNGTQANRNFRLSVYGALGILQGAAIFGYSMAVSIGGIFASR 1043
Cdd:TIGR00957 960 KAIGLFITFLSIFLFVCNHVSALASNYWLSLWTDD-PMVNGTQNNTSLRLSVYGALGILQGFAVFGYSMAVSIGGIQASR 1038
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1044 RLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLGLVY 1123
Cdd:TIGR00957 1039 VLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLY 1118
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1124 FFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECV 1203
Cdd:TIGR00957 1119 FFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECV 1198
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1204 GNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPST 1283
Cdd:TIGR00957 1199 GNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSG 1278
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1284 WPHSGRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNL 1363
Cdd:TIGR00957 1279 WPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL 1358
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1364 RFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLR 1443
Cdd:TIGR00957 1359 RFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLR 1438
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1444 KTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIFYSMAK 1523
Cdd:TIGR00957 1439 KTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSMAK 1518
|
....
gi 6678848 1524 DAGL 1527
Cdd:TIGR00957 1519 DAGL 1522
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
103-1526 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 1068.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 103 APVLLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVALLCALAILRSKIISaLKkdahvDVFRDSTFYLYFTLV 182
Cdd:PLN03130 108 PPFEIVSLIVEALTWCSMLVMIGVETKIYIREFRWYVRFAVIYVLVGDAVMLNLVLS-VK-----EYYSSFVLYLYISEV 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 183 LVQLVLSCF-----------SDCSPLFSETVHD---------RNPCPESSASFLSRITFWWITGMMVHGYRQPLESSDLW 242
Cdd:PLN03130 182 AAQVLFGILllvyfpnldpyPGYTPIGSESVDDyeyeelpggEQICPERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVW 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 243 SLNKEDTSEEVVPVLVNNWKKECdksrkqpvrivyappkdpSKPKgssqldvneevealivksphkdrePSLFKVLYKTF 322
Cdd:PLN03130 262 KLDTWDQTETLYRSFQKCWDEEL------------------KKPK------------------------PWLLRALNNSL 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 323 GPYFLMSFLYKALHDLMMFAGPKILELIINFVNDREaPDWQGYFYTALLFVSACLQTLALHQYFHICFVSGMRIKTAVVG 402
Cdd:PLN03130 300 GGRFWLGGFFKIGNDLSQFVGPLLLNLLLESMQNGE-PAWIGYIYAFSIFVGVVLGVLCEAQYFQNVMRVGFRLRSTLVA 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 403 AVYRKALLITNAARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLSLGPSVLAGVAVMILMVPLNA 482
Cdd:PLN03130 379 AVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLVLMFPIQT 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 483 VMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMSIRQEELKVLKKSAYLAAVGTFTWVCTPFLVA 562
Cdd:PLN03130 459 FIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSFILNSIPVLVT 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 563 LSTFAVFVTVDerNILDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEE--LEPDSierrSIKSGE 640
Cdd:PLN03130 539 VVSFGVFTLLG--GDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLLAEErvLLPNP----PLEPGL 612
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 641 gNSITVKNATFTW-ARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVE-GHVTLKGSVAYVPQQAWIQ 718
Cdd:PLN03130 613 -PAISIKNGYFSWdSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGTVAYVPQVSWIF 691
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 719 NDSLRENILFGHPLQENYYKAVMEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAV 798
Cdd:PLN03130 692 NATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 799 DAHVGKHIFEKVVgpMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLdRDGAFAEFLRTYANAEQDLAS 878
Cdd:PLN03130 772 DAHVGRQVFDKCI--KDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELS-NNGPLFQKLMENAGKMEEYVE 848
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 879 EDDSVSGSGKESKPVENGmlvtdtVGKHLQRhlsNSSShsgdtsqqhssiaelqKAGAKEETWKLMEADKAQTGQVQLSV 958
Cdd:PLN03130 849 ENGEEEDDQTSSKPVANG------NANNLKK---DSSS----------------KKKSKEGKSVLIKQEERETGVVSWKV 903
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 959 YWNYMKAIGLFitFLSIFLFLC---NHVSALASNYWLSLWTDD-PPVVNGTqanrNFRLSVYGALGILQGAAIFGYSMAV 1034
Cdd:PLN03130 904 LERYKNALGGA--WVVMILFLCyvlTEVFRVSSSTWLSEWTDQgTPKTHGP----LFYNLIYALLSFGQVLVTLLNSYWL 977
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1035 SIGGIFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAV 1114
Cdd:PLN03130 978 IMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVSTISLW 1057
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1115 IIPPLGLVYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANR 1194
Cdd:PLN03130 1058 AIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTLVNMSSNR 1137
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1195 WLAVRLECVGNCIVLFAALFAVI-----SRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYSETEK 1269
Cdd:PLN03130 1138 WLAIRLETLGGLMIWLTASFAVMqngraENQAAFASTMGLLLSYALNITSLLTAVLRLASLAENSLNAVERVGTYIDLPS 1217
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1270 EAPWQIQETAPPSTWPHSGRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEII 1349
Cdd:PLN03130 1218 EAPLVIENNRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRIL 1297
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1350 IDGVNIAKIGLHNLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSV 1429
Cdd:PLN03130 1298 IDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSV 1377
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1430 GQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPS 1509
Cdd:PLN03130 1378 GQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPE 1457
|
1450
....*....|....*...
gi 6678848 1510 ELLQ-QRGIFYSMAKDAG 1526
Cdd:PLN03130 1458 NLLSnEGSAFSKMVQSTG 1475
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
206-1526 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 968.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 206 NPCPESSASFLSRITFWWITGMMVHGYRQPLESSDLWSLNKEDTSEEVVPVLVNNWKKEcdkSRKqpvrivyappkdpsk 285
Cdd:PLN03232 225 NICPERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTEE---SRR--------------- 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 286 PKgssqldvneevealivksphkdrePSLFKVLYKTFGPYFLMSFLYKALHDLMMFAGPKILELIINFVNDREaPDWQGY 365
Cdd:PLN03232 287 PK------------------------PWLLRALNNSLGGRFWLGGIFKIGHDLSQFVGPVILSHLLQSMQEGD-PAWVGY 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 366 FYTALLFVSACLQTLALHQYFHICFVSGMRIKTAVVGAVYRKALLITNAARKSSTVGEIVNLMSVDAQRFMDLATYINMI 445
Cdd:PLN03232 342 VYAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGL 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 446 WSAPLQVILALYFLWLSLGPSVLAGVAVMILMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAF 525
Cdd:PLN03232 422 WSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSF 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 526 QDKVMSIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTFAVFVTVDerNILDAKKAFVSLALFNILRFPLNILPMVIS 605
Cdd:PLN03232 502 ESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLVSFGVFVLLG--GDLTPARAFTSLSLFAVLRSPLNMLPNLLS 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 606 SIVQASVSLKRLR-IFLSHEE-------LEPDSierrsiksgegNSITVKNATFTW-ARGEPPTLNGITFSIPEGALVAV 676
Cdd:PLN03232 580 QVVNANVSLQRIEeLLLSEERilaqnppLQPGA-----------PAISIKNGYFSWdSKTSKPTLSDINLEIPVGSLVAI 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 677 VGQVGCGKSSLLSALLAEMDKVE-GHVTLKGSVAYVPQQAWIQNDSLRENILFGHPLQENYYKAVMEACALLPDLEILPS 755
Cdd:PLN03232 649 VGGTGEGKTSLISAMLGELSHAEtSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPG 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 756 GDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVGPMglLKNKTRILVTHGISYLPQV 835
Cdd:PLN03232 729 RDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDE--LKGKTRVLVTNQLHFLPLM 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 836 DVIIVMSGGKISEMGSYQELLDRDGAFAEFLRTYA--NAEQDLASEDDSVSGSGkeskpvengmlvtdtvgkhlqrhlsn 913
Cdd:PLN03232 807 DRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGkmDATQEVNTNDENILKLG-------------------------- 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 914 sSSHSGDTSQQhsSIAELQKAgaKEETWKLMEADKAQTGQVQLSVYWNYMKAIG-LFITFLSIFLFLCNHVSALASNYWL 992
Cdd:PLN03232 861 -PTVTIDVSER--NLGSTKQG--KRGRSVLVKQEERETGIISWNVLMRYNKAVGgLWVVMILLVCYLTTEVLRVSSSTWL 935
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 993 SLWTDDPPVVNGTQAnrnFRLSVYGALGILQGAAIFGYSMAVSIGGIFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNR 1072
Cdd:PLN03232 936 SIWTDQSTPKSYSPG---FYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINR 1012
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1073 FSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLGLVYFFVQRFYVASSRQLKRLESVSRSPVYSHF 1152
Cdd:PLN03232 1013 FSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQF 1092
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1153 NETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVI-----SRHSLSAGLV 1227
Cdd:PLN03232 1093 GEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLrngnaENQAGFASTM 1172
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1228 GLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSTWPHSGRVEFRDYCLRYREDLDLVL 1307
Cdd:PLN03232 1173 GLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVL 1252
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1308 KHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSGSLRMNLDP 1387
Cdd:PLN03232 1253 HGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDP 1332
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1388 FSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQS 1467
Cdd:PLN03232 1333 FSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQR 1412
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1468 TIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRG-IFYSMAKDAG 1526
Cdd:PLN03232 1413 TIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTsAFFRMVHSTG 1472
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
291-1526 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 789.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 291 QLDVNEEVEALIVKSPHKDREPSLFKVLYKTFGPYFLMSFLYKALHDLMMFAGPKILELIINFVNDREAPDWQGYFYTAL 370
Cdd:PTZ00243 211 RLYLSSTGSVVRPGPPPTPKRLSLLRTLFAALPYYVWWQIPFKLLSDVCTLTLPVLLKYFVKFLDADNATWGRGLGLVLT 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 371 LFVSACLQTLALHQYFHICFVSGMRIKTAVVGAVYRKALLITNA--ARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSA 448
Cdd:PTZ00243 291 LFLTQLIQSVCLHRFYYISIRCGLQYRSALNALIFEKCFTISSKslAQPDMNTGRIINMMSTDVERINSFMQYCMYLWSS 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 449 PLQVILALYFLWLSLGPSVLAGVAVMILMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDK 528
Cdd:PTZ00243 371 PMVLLLSILLLSRLVGWCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVAN 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 529 VMSIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTFAVFVTVDerNILDAKKAFVSLALFNILRFPLNILPMVISSIV 608
Cdd:PTZ00243 451 IEDKRARELRYLRDVQLARVATSFVNNATPTLMIAVVFTVYYLLG--HELTPEVVFPTIALLGVLRMPFFMIPWVFTTVL 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 609 QASVSLKRLRIFLSHE--------ELEPDSIERRSIKSGEGNSITVKNATFT-----------------------W---- 653
Cdd:PTZ00243 529 QFLVSIKRISTFLECDnatcstvqDMEEYWREQREHSTACQLAAVLENVDVTafvpvklprapkvktsllsralrMlcce 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 654 -----ARGEPPT-------------------------------------------------------LNGITFSIPEGAL 673
Cdd:PTZ00243 609 qcrptKRHPSPSvvvedtdygspssasrhiveggtgggheatptsersaktpkmktddffelepkvlLRDVSVSVPRGKL 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 674 VAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQQAWIQNDSLRENILFGHPLQENYYKAVMEACALLPDLEIL 753
Cdd:PTZ00243 689 TVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQL 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 754 PSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVgpMGLLKNKTRILVTHGISYLP 833
Cdd:PTZ00243 769 GGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECF--LGALAGKTRVLATHQVHVVP 846
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 834 QVDVIIVMSGGKISEMGSYqelldrdgafAEFLRTyaNAEQDLASED-DSVSGSGKESKPVENGMLVTDTVGKHlqrhls 912
Cdd:PTZ00243 847 RADYVVALGDGRVEFSGSS----------ADFMRT--SLYATLAAELkENKDSKEGDADAEVAEVDAAPGGAVD------ 908
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 913 nsssHSGDTSQQHSSIAELQKAGAKEETWKLMEADKAQTGQVQLSVYWNYMKAIG-LFITFLSIFLFLCNHVSALASNYW 991
Cdd:PTZ00243 909 ----HEPPVAKQEGNAEGGDGAALDAAAGRLMTREEKASGSVPWSTYVAYLRFCGgLHAAGFVLATFAVTELVTVSSGVW 984
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 992 LSLWTddppvvngtqaNRNFRLS------VYgaLGI-LQGAAIFGYSMAVSIGGI-FASRRLHLDLLYNVLRSPMSFFER 1063
Cdd:PTZ00243 985 LSMWS-----------TRSFKLSaatylyVY--LGIvLLGTFSVPLRFFLSYEAMrRGSRNMHRDLLRSVSRGTMSFFDT 1051
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1064 TPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLGLVYFFVQRFYVASSRQLKRLESV 1143
Cdd:PTZ00243 1052 TPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSV 1131
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1144 SRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVI------ 1217
Cdd:PTZ00243 1132 AKSPVFTLLEEALQGSATITAYGKAHLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIALIGVIgtmlra 1211
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1218 SRHSLsaGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYS-ETEKEAPWQ---------------------- 1274
Cdd:PTZ00243 1212 TSQEI--GLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTdEVPHEDMPEldeevdalerrtgmaadvtgtv 1289
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1275 -IQETAPPSTWPH---SGRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII 1350
Cdd:PTZ00243 1290 vIEPASPTSAAPHpvqAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRV 1369
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1351 DGVNIAKIGLHNLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVG 1430
Cdd:PTZ00243 1370 NGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVG 1449
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1431 QRQLVCLARALLRK-TKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPS 1509
Cdd:PTZ00243 1450 QRQLMCMARALLKKgSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPR 1529
|
1370
....*....|....*...
gi 6678848 1510 ELLQQR-GIFYSMAKDAG 1526
Cdd:PTZ00243 1530 ELVMNRqSIFHSMVEALG 1547
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
209-1518 |
1.25e-170 |
|
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: 552.98 E-value: 1.25e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 209 PESSASFLSRITFWWITGMMVHGYRQPLESSDLWSLNKEDTSEEVVPVLVNNWKKECDKSRKQPvrivyappkdpskpkg 288
Cdd:TIGR01271 5 PVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELASAKKNP---------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 289 ssqldvneevealivksphkdrepSLFKVLYKTFGPYFLMSFLYKALHDLMMFAGPKILELIINFVNDREAPDWQGYFYT 368
Cdd:TIGR01271 69 ------------------------KLLNALRRCFFWRFVFYGILLYFGEATKAVQPLLLGRIIASYDPFNAPEREIAYYL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 369 A----LLFVsacLQTLALHQYFHICFVSGMRIKTAVVGAVYRKALLITNAARKSSTVGEIVNLMSVDAQRFMDLATYINM 444
Cdd:TIGR01271 125 AlglcLLFI---VRTLLLHPAIFGLHHLGMQMRIALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHF 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 445 IWSAPLQVILALYFLWLSLGPSVLAGVAVMILMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELA 524
Cdd:TIGR01271 202 VWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 525 FQDKVMSIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALST---FAVFVTVDERNIldakkaFVSLALFNILRFPLN-IL 600
Cdd:TIGR01271 282 MEKIIKNIRQDELKLTRKIAYLRYFYSSAFFFSGFFVVFLSvvpYALIKGIILRRI------FTTISYCIVLRMTVTrQF 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 601 PMVISSIVQASVSLKRLRIFLSHEELepdsierrsiKSGEGN----SITVKNATFTW----------------ARGEP-- 658
Cdd:TIGR01271 356 PGAIQTWYDSLGAITKIQDFLCKEEY----------KTLEYNltttEVEMVNVTASWdegigelfekikqnnkARKQPng 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 659 --------------PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQQAWIQNDSLRE 724
Cdd:TIGR01271 426 ddglffsnfslyvtPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKD 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 725 NILFGHPLQENYYKAVMEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGK 804
Cdd:TIGR01271 506 NIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEK 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 805 HIFEKVVgpMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAEFLRTYANAEQDLAS------ 878
Cdd:TIGR01271 586 EIFESCL--CKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLLGLEAFDNFSAErrnsil 663
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 879 ---------EDDSVSGSGKESK-------PVE------------------------------NGMLVTDTVGKHLQRHLS 912
Cdd:TIGR01271 664 tetlrrvsiDGDSTVFSGPETIkqsfkqpPPEfaekrkqsiilnpiasarkfsfvqmgpqkaQATTIEDAVREPSERKFS 743
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 913 --------------NSSSHSGDTSQ-----------QHSSIAELQKAGAKEETWKLMEADKAQTGQVQLSVY-------- 959
Cdd:TIGR01271 744 lvpedeqgeeslprGNQYHHGLQHQaqrrqsvlqlmTHSNRGENRREQLQTSFRKKSSITQQNELASELDIYsrrlskds 823
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 960 -----------------------------WN-YMKAIGLF--ITFLSIFLFLCNHVSALASNYWLSLWTDDPPVVN---G 1004
Cdd:TIGR01271 824 vyeiseeineedlkecfaderenvfetttWNtYLRYITTNrnLVFVLIFCLVIFLAEVAASLLGLWLITDNPSAPNyvdQ 903
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1005 TQANRNFRLSVYGALgILQGAAIFGYSMAVSIG------GIF-----------ASRRLHLDLLYNVLRSPMSFFERTPSG 1067
Cdd:TIGR01271 904 QHANASSPDVQKPVI-ITPTSAYYIFYIYVGTAdsvlalGFFrglplvhtlltVSKRLHEQMLHSVLQAPMAVLNTMKAG 982
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1068 NLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLGLVYFFVQRFYVASSRQLKRLESVSRSP 1147
Cdd:TIGR01271 983 RILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSP 1062
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1148 VYSHFNETLLGVSVIRAFEEQ---ERFIHQSdlkVDENQKAYYPSIVANRWLAVRLECVgncIVLF--AALFAVISRHSL 1222
Cdd:TIGR01271 1063 IFSHLITSLKGLWTIRAFGRQsyfETLFHKA---LNLHTANWFLYLSTLRWFQMRIDII---FVFFfiAVTFIAIGTNQD 1136
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1223 SAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAP--PST------------WPHSG 1288
Cdd:TIGR01271 1137 GEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEPRPSGGGGKyqLSTvlvienphaqkcWPSGG 1216
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1289 RVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRInESAEGEIIIDGVNIAKIGLHNLRFKIT 1368
Cdd:TIGR01271 1217 QMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVTLQTWRKAFG 1295
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1369 IIPQDPVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKIL 1448
Cdd:TIGR01271 1296 VIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKIL 1375
|
1450 1460 1470 1480 1490 1500 1510
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1449 VLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIF 1518
Cdd:TIGR01271 1376 LLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLF 1445
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
329-617 |
4.40e-170 |
|
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: 511.63 E-value: 4.40e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 329 SFLYKALHDLMMFAGPKILELIINFVNDREAPDWQGYFYTALLFVSACLQTLALHQYFHICFVSGMRIKTAVVGAVYRKA 408
Cdd:cd18595 2 AALLKLLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 409 LLITNAARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLSLGPSVLAGVAVMILMVPLNAVMAMKT 488
Cdd:cd18595 82 LRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 489 KTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMSIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTFAV 568
Cdd:cd18595 162 KKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLATFAT 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 6678848 569 FVTVDERNILDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 617
Cdd:cd18595 242 YVLSDPDNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
971-1265 |
5.79e-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: 508.94 E-value: 5.79e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 971 TFLSIFLFLCNHVSALASNYWLSLWTDDPPV-VNGTQANRNFRLSVYGALGILQGAAIFGYSMAVSIGGIFASRRLHLDL 1049
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSDDPALnGTQDTEQRDYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHNKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1050 LYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLGLVYFFVQRF 1129
Cdd:cd18603 81 LHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1130 YVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVL 1209
Cdd:cd18603 161 YVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLIVL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 6678848 1210 FAALFAVISRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYS 1265
Cdd:cd18603 241 FAALFAVLSRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEYS 296
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1288-1508 |
1.71e-133 |
|
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: 411.12 E-value: 1.71e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1288 GRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKI 1367
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1368 TIIPQDPVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKI 1447
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6678848 1448 LVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAP 1508
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
328-617 |
3.01e-128 |
|
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: 400.05 E-value: 3.01e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 328 MSFLYKALHDLMMFAGPKILELIINFVNDREAPDWQGYFYTALLFVSACLQTLALHQYFHICFVSGMRIKTAVVGAVYRK 407
Cdd:cd18559 1 SFLLIKLVLCNHVFSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 408 ALLITNAARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLSLGPSVLAGVAVMILMVPLNAVMAMK 487
Cdd:cd18559 81 ALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 488 TKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMSIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTFA 567
Cdd:cd18559 161 SRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 6678848 568 VFVTVDERNILDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 617
Cdd:cd18559 241 AYVSRHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
972-1523 |
5.17e-124 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 399.92 E-value: 5.17e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 972 FLSIFLFLCNHVSALASNYWLSLWTDDppVVNGTQANRNFRLS-VYGALGILQGAAIFGYSMAVSIGGIFASRRLHLDLL 1050
Cdd:COG1132 24 ILALLLLLLSALLELLLPLLLGRIIDA--LLAGGDLSALLLLLlLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1051 YNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLGLVYFFVQRFY 1130
Cdd:COG1132 102 EHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLF 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1131 VASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLF 1210
Cdd:COG1132 182 GRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLAL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1211 AALFAV--ISRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPstwPHSG 1288
Cdd:COG1132 262 VLLVGGllVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPDPPGAVPLP---PVRG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1289 RVEFRDYCLRYREDlDLVLKHINVTIEGGEKVGIVGRTGAGKSSLT---LGLFRINEsaeGEIIIDGVNIAKIGLHNLRF 1365
Cdd:COG1132 339 EIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGKSTLVnllLRFYDPTS---GRILIDGVDIRDLTLESLRR 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1366 KITIIPQDPVLFSGSLRMNL---DPfsQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALL 1442
Cdd:COG1132 415 QIGVVPQDTFLFSGTIRENIrygRP--DATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALL 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1443 RKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIFYSMA 1522
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLY 572
|
.
gi 6678848 1523 K 1523
Cdd:COG1132 573 R 573
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
329-617 |
1.34e-118 |
|
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: 373.74 E-value: 1.34e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 329 SFLYKALHDLMMFAGPKILELIINFVNDREAPD-WQGYFYTALLFVSACLQTLALHQYFHICFVSGMRIKTAVVGAVYRK 407
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPlSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 408 ALLITNAARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLSLGPSVLAGVAVMILMVPLNAVMAMK 487
Cdd:cd18579 82 ALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 488 TKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMSIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTFA 567
Cdd:cd18579 162 ISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFA 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 6678848 568 VFVTVDerNILDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 617
Cdd:cd18579 242 TYVLLG--NPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
972-1265 |
9.79e-117 |
|
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: 368.85 E-value: 9.79e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 972 FLSIFLFLCNHVSALASNYWLSLWTDDPpvVNGTQANRNFRLSVYGALGILQGAAIFGYSMAVSIGGIFASRRLHLDLLY 1051
Cdd:cd18559 2 FLLIKLVLCNHVFSGPSNLWLLLWFDDP--VNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1052 NVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIpPLGLVYFFVQRFYV 1131
Cdd:cd18559 80 KALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGI-PLGLLYVPVNRVYA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1132 ASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDeNQKAYYPSIVANRWLAVRLECVGNCIVLFA 1211
Cdd:cd18559 159 ASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRD-NELAYLPSIVYLRALAVRLWCVGPCIVLFA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 6678848 1212 ALFAVISRHSLsAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYS 1265
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 |
1.58e-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: 361.79 E-value: 1.58e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWARGE---PPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQQAWIQND 720
Cdd:cd03250 1 ISVEDASFTWDSGEqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 721 SLRENILFGHPLQENYYKAVMEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDA 800
Cdd:cd03250 81 TIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6678848 801 HVGKHIFEKVVGPMgLLKNKTRILVTHGISYLPQVDVIIVMSGGK 845
Cdd:cd03250 161 HVGRHIFENCILGL-LLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
972-1265 |
7.78e-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: 360.67 E-value: 7.78e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 972 FLSIFLFLCNHVSALASNYWLSLWTDDppVVNGTQANRNFRLSVYGALGILQGAA-IFGYSMAVSIGGIFASRRLHLDLL 1050
Cdd:cd18580 2 LLLLLLLLLLAFLSQFSNIWLDWWSSD--WSSSPNSSSGYYLGVYAALLVLASVLlVLLRWLLFVLAGLRASRRLHDKLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1051 YNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLGLVYFFVQRFY 1130
Cdd:cd18580 80 RSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1131 VASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLF 1210
Cdd:cd18580 160 LRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALLALV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 1211 AALFAVISRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYS 1265
Cdd:cd18580 240 VALLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
972-1265 |
8.79e-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: 346.77 E-value: 8.79e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 972 FLSIFLFLCNHVSALASNYWLSLWTDDPPvvngtQANRNFRLSVYGALGILQGAAIFGYSMAVSIGGIFASRRLHLDLLY 1051
Cdd:cd18606 2 PLLLLLLILSQFAQVFTNLWLSFWTEDFF-----GLSQGFYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1052 NVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLGLVYFFVQRFYV 1131
Cdd:cd18606 77 RVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1132 ASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFA 1211
Cdd:cd18606 157 ASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLLVLIV 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 6678848 1212 ALFAVISRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYS 1265
Cdd:cd18606 237 ALLCVTRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHYA 290
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1017-1523 |
1.83e-98 |
|
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: 333.34 E-value: 1.83e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1017 GALGILQGAAIFGYSMAVSIGGIFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSkELDTVDSMIP-QVIKMFMGSL 1095
Cdd:COG2274 203 LLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTgSLLTALLDLL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1096 FSVIGAVIIILLATPIAAV---IIPPLGLVYFFVQRFYVASSRQlkrlESVSRSPVYSHFNETLLGVSVIRAFEEQERFI 1172
Cdd:COG2274 282 FVLIFLIVLFFYSPPLALVvllLIPLYVLLGLLFQPRLRRLSRE----ESEASAKRQSLLVETLRGIETIKALGAESRFR 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1173 HQSDLKVDE----NQKAYYPSIVANRWLAVrLECVGNCIVLFAALFAVISRHsLSAG-LVGlSVSYSLQITAYLNWLVRM 1247
Cdd:COG2274 358 RRWENLLAKylnaRFKLRRLSNLLSTLSGL-LQQLATVALLWLGAYLVIDGQ-LTLGqLIA-FNILSGRFLAPVAQLIGL 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1248 SSEMETNIVAVERLKEYSETEKEAPWQIQETAPPstwPHSGRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTG 1327
Cdd:COG2274 435 LQRFQDAKIALERLDDILDLPPEREEGRSKLSLP---RLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSG 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1328 AGKSSLT---LGLFRINEsaeGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSGSLRMNL---DPfsQYSDEEVWMALE 1401
Cdd:COG2274 512 SGKSTLLkllLGLYEPTS---GRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItlgDP--DATDEEIIEAAR 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1402 LAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTI 1481
Cdd:COG2274 587 LAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIII 666
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 6678848 1482 AHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIFYSMAK 1523
Cdd:COG2274 667 AHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1284-1508 |
7.38e-97 |
|
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: 310.11 E-value: 7.38e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1284 WPHSGRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNL 1363
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1364 RFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWMALELahlkgfvsalpdklnhecAEGGENLSVGQRQLVCLARALLR 1443
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALRV------------------SEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 1444 KTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAP 1508
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
972-1265 |
6.93e-92 |
|
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: 299.77 E-value: 6.93e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 972 FLSIFLFLCNHVSALASNYWLSLWT---DDPPVVNGTQANRNFRLSVYGALGILQGAAIFGYSMAVSIGGIFASRRLHLD 1048
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIWAsayETSSALPPSEVSVLYYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1049 LLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLGLVYFFVQR 1128
Cdd:cd18604 82 LLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1129 FYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIV 1208
Cdd:cd18604 162 LYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALFS 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 6678848 1209 LFAALFAViSRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYS 1265
Cdd:cd18604 242 FATAALLV-YGPGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
971-1265 |
2.96e-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: 287.19 E-value: 2.96e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 971 TFLSIFLFLCNHVSALASNYWLSLWTD------DPPVVNGTQANRN----FRLSVYGALGILQGAAIFGYSMAVSIGGIF 1040
Cdd:cd18602 1 VALVLALALLKQGLRVATDFWLADWTEanhdvaSVVFNITSSSLEDdevsYYISVYAGLSLGAVILSLVTNLAGELAGLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1041 ASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLG 1120
Cdd:cd18602 81 AARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPII 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1121 LVYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRL 1200
Cdd:cd18602 161 IVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6678848 1201 ECVGNCIVLFAALFAVISRH--SLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYS 1265
Cdd:cd18602 241 DYLGAVIVFLAALSSLTAALagYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEYT 307
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
969-1264 |
4.14e-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: 280.57 E-value: 4.14e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 969 FITFLsIFLFLCnHVSALASNYWLSLWTDD--PPVVNGTQANRNFRLSVYGALGILQGAAIFGYSMAVSIGGIFASRRLH 1046
Cdd:cd18605 1 LILIL-LSLILM-QASRNLIDFWLSYWVSHsnNSFFNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1047 LDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLGLVYFFV 1126
Cdd:cd18605 79 NKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1127 QRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNC 1206
Cdd:cd18605 159 QRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGVL 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6678848 1207 IVLFAALFAVISRH---SLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEY 1264
Cdd:cd18605 239 IVTFVALTAVVQHFfglSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQY 299
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
330-617 |
3.64e-84 |
|
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: 278.22 E-value: 3.64e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 330 FLYKALHDLMMFAGPKILELIINFV-NDREAPDWQGYFYTALLFVSACLQTLALHQYFHICFVSGMRIKTAVVGAVYRKA 408
Cdd:cd18596 3 ALLAVLSSVLSFAPPFFLNRLLRYLeDPGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFEKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 409 LLI-------------------TNAARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLSLGPSVLA 469
Cdd:cd18596 83 LRRrdksgssksseskkkdkeeDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSALV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 470 GVAVMILMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMSIRQEELKVLKKSAYLAAV 549
Cdd:cd18596 163 GLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLDLL 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6678848 550 GTFTWVCTPFLVALSTFAVFVTVdERNILDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 617
Cdd:cd18596 243 LSLLWFLIPILVTVVTFATYTLV-MGQELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLDRI 309
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1288-1523 |
6.83e-84 |
|
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: 275.63 E-value: 6.83e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1288 GRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKI 1367
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1368 TIIPQDPVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKI 1447
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6678848 1448 LVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELL-QQRGIFYSMAK 1523
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLVR 254
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
331-617 |
5.95e-81 |
|
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: 268.27 E-value: 5.95e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 331 LYKALHDLMMFAGPKILELIINFVNDREAPDWQGYFYTALLFVSACLQTLALHQY-FHICFVSgMRIKTAVVGAVYRKAL 409
Cdd:cd18598 4 LLKLLADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGALLSSHYnFQMNKVS-LKVRAALVTAVYRKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 410 LITNAARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLSLGPSVLAGVAVMILMVPLNAVMAMKTK 489
Cdd:cd18598 83 RVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAKRIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 490 TYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMSIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTFAVF 569
Cdd:cd18598 163 ALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALCVYFWATTPVLISILTFATY 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 6678848 570 VTVdeRNILDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 617
Cdd:cd18598 243 VLM--GNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
313-873 |
1.46e-78 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 272.04 E-value: 1.46e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 313 SLFKVLYKTFGPY---FLMSFLYKALHDLMMFAGPKILELIINFVNDreAPDWQG-YFYTALLFVSACLQTLALHQYFHI 388
Cdd:COG1132 7 KLLRRLLRYLRPYrglLILALLLLLLSALLELLLPLLLGRIIDALLA--GGDLSAlLLLLLLLLGLALLRALLSYLQRYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 389 CFVSGMRIKTAVVGAVYRKALLITNAARKSSTVGEIVNLMSVDAQRFMD-LATYINMIWSAPLQVILALYFLwLSLGPSV 467
Cdd:COG1132 85 LARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQfLAHGLPQLVRSVVTLIGALVVL-FVIDWRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 468 -LAGVAVMILMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYA---WELA-FQDKVMSIRQEELKVLKK 542
Cdd:COG1132 164 aLIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGreeRELErFREANEELRRANLRAARL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 543 SA-YLAAVGTFTWVCTPFLVALSTFAVF---VTVDErnildakkaFVS-LALFNILRFPLNILPMVISSIVQASVSLKRL 617
Cdd:COG1132 244 SAlFFPLMELLGNLGLALVLLVGGLLVLsgsLTVGD---------LVAfILYLLRLFGPLRQLANVLNQLQRALASAERI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 618 RIFLSHEELEPDSIERRSIKSGEGnSITVKNATFTWArGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDK 697
Cdd:COG1132 315 FELLDEPPEIPDPPGAVPLPPVRG-EIEFENVSFSYP-GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 698 VEGHVTLKG-------------SVAYVPQQAWIQNDSLRENILFGHP---LQEnyykaVMEACA---LLPDLEILPSGDR 758
Cdd:COG1132 393 TSGRILIDGvdirdltleslrrQIGVVPQDTFLFSGTIRENIRYGRPdatDEE-----VEEAAKaaqAHEFIEALPDGYD 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 759 TEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRILVTHGISYLPQVDVI 838
Cdd:COG1132 468 TVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEAL---ERLMKGRTTIVIAHRLSTIRNADRI 544
|
570 580 590
....*....|....*....|....*....|....*
gi 6678848 839 IVMSGGKISEMGSYQELLDRDGAFAEFLRTYANAE 873
Cdd:COG1132 545 LVLDDGRIVEQGTHEELLARGGLYARLYRLQFGEE 579
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
328-617 |
9.14e-78 |
|
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: 259.31 E-value: 9.14e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 328 MSFLYKALHDLMMFAGPKILELIINFVNDREA-----PDWQGYFYTALLFVSACLQTLALHQYFHICFVSGMRIKTAVVG 402
Cdd:cd18597 1 LAGLLKLLADVLQVLSPLLLKYLINFVEDAYLggpppSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 403 AVYRKALLITNAARKSSTVGEIVNLMSVDAQRfMDLA-TYINMIWSAPLQVILALYFLWLSLGPSVLAGVAVMILMVPLN 481
Cdd:cd18597 81 AIYRKSLRLSGKSRHEFPNGKITNLMSTDLSR-IDFAlGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 482 AVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMSIRQEELKVLKKSAYLAAVGTFTWVCTPFLV 561
Cdd:cd18597 160 GFLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 6678848 562 ALSTFAVFVTVDerNILDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 617
Cdd:cd18597 240 SMLSFITYYATG--HTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1018-1516 |
9.83e-76 |
|
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: 263.16 E-value: 9.83e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1018 ALGILQGAAIFGYSMAVSIGGIFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFskeLDTVDSM-------IPQVIKM 1090
Cdd:COG4988 66 AVLLLRALLAWLRERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLL---TEGVEALdgyfaryLPQLFLA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1091 FMGSLfsVIGAVI--------IILLATpiaAVIIPplgLVYFFVQRFY-VASSRQLKRLESVSrspvySHFNETLLGVSV 1161
Cdd:COG4988 143 ALVPL--LILVAVfpldwlsgLILLVT---APLIP---LFMILVGKGAaKASRRQWRALARLS-----GHFLDRLRGLTT 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1162 IRAF----EEQERFIHQSD---------LKVdenqkAYYPSIVanrwlavrLECVGnciVLFAALFAVISRHSLSAGLVG 1228
Cdd:COG4988 210 LKLFgrakAEAERIAEASEdfrkrtmkvLRV-----AFLSSAV--------LEFFA---SLSIALVAVYIGFRLLGGSLT 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1229 LSVSYSLQITA---YL-------NWLVRMSsemetNIVAVERLKEYSETEKEAPWQIQETAPpstWPHSGRVEFRDYCLR 1298
Cdd:COG4988 274 LFAALFVLLLApefFLplrdlgsFYHARAN-----GIAAAEKIFALLDAPEPAAPAGTAPLP---AAGPPSIELEDVSFS 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1299 YrEDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFS 1378
Cdd:COG4988 346 Y-PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFA 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1379 GSLRMNL---DPfsQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATA 1455
Cdd:COG4988 425 GTIRENLrlgRP--DASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTA 502
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6678848 1456 AVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRG 1516
Cdd:COG4988 503 HLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1288-1516 |
1.45e-74 |
|
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: 247.52 E-value: 1.45e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1288 GRVEFRDYCLRYREDlDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKI 1367
Cdd:cd03254 1 GEIEFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1368 TIIPQDPVLFSGSLRMNLDPFSQYSDEEVWM-ALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTK 1446
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIeAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1447 ILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRG 1516
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
967-1265 |
3.19e-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: 244.39 E-value: 3.19e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 967 GLFITFLSIFLFLCNHVSALASNYWLSLWTDDPpvvNGTQANR-----------------NFRLSVYG--ALGILQGAAI 1027
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWLKQG---SGNTTNNvdnstvdsgnisdnpdlNFYQLVYGgsILVILLLSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1028 --FGYSMAVsiggIFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIII 1105
Cdd:cd18599 78 rgFVFVKVT----LRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIII 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1106 LLATPIAAVIIPPLGLVYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKA 1185
Cdd:cd18599 154 AIVFPWFLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1186 YYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYS 1265
Cdd:cd18599 234 FFLFNCAMRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
331-617 |
3.79e-72 |
|
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: 243.68 E-value: 3.79e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 331 LYKALHDLMMFAGPKILELIINFVNDREAPDWQ------------------GYFYTALLFVSACLQTLALHQYFHICFVS 392
Cdd:cd18591 4 ILKLLGDLLGFVGPLCISGIVDYVEENTYSSSNstdklsvsyvtveeffsnGYVLAVILFLALLLQATFSQASYHIVIRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 393 GMRIKTAVVGAVYRKALLIT--NAARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLSLGPSVLAG 470
Cdd:cd18591 84 GIRLKTALQAMIYEKALRLSswNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSALIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 471 VAVMILMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMSIRQEELKVLKKSAYLAAVG 550
Cdd:cd18591 164 AALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYWSLM 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6678848 551 TFTWVCTPFLVALSTFAVFVTVDERNiLDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 617
Cdd:cd18591 244 TFLTQASPILVTLVTFGLYPYLEGEP-LTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1019-1521 |
1.28e-70 |
|
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: 248.48 E-value: 1.28e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1019 LGILQGAAIFGYSMAVSIGGIFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSV 1098
Cdd:TIGR02203 63 LAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1099 IGAVIIILLA----TPIAAVIIPPLGLVyffvqrfyvaSSRQLKRLESVSRSPVYSH------FNETLLGVSVIRAF--- 1165
Cdd:TIGR02203 143 IGLFIVLLYYswqlTLIVVVMLPVLSIL----------MRRVSKRLRRISKEIQNSMgqvttvAEETLQGYRVVKLFggq 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1166 -EEQERFIHQSD------LKVDENQKAYYPSI--VANRWLAVrlecvgnciVLFAALFAVISRHSLSAGLVGLSVSySLQ 1236
Cdd:TIGR02203 213 aYETRRFDAVSNrnrrlaMKMTSAGSISSPITqlIASLALAV---------VLFIALFQAQAGSLTAGDFTAFITA-MIA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1237 ITAYLNWLVRMSSEMETNIVAVERLKEYSETEKEApwQIQETAPPSTwphSGRVEFRDYCLRYREDLDLVLKHINVTIEG 1316
Cdd:TIGR02203 283 LIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEK--DTGTRAIERA---RGDVEFRNVTFRYPGRDRPALDSISLVIEP 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1317 GEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSGSLRMNL---DPfSQYSD 1393
Cdd:TIGR02203 358 GETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRT-EQADR 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1394 EEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQF 1473
Cdd:TIGR02203 437 AEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLM 516
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 6678848 1474 EDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIF---YSM 1521
Cdd:TIGR02203 517 QGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYaqlHNM 567
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1066-1523 |
1.17e-69 |
|
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: 245.45 E-value: 1.17e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1066 SGNLVNRFSKELDTVDSMIPQVIkmfmgslFSVIGAVIIILLATPIAAVIIPPLGLVYF------------FVQRFYVAS 1133
Cdd:COG4987 111 SGDLLNRLVADVDALDNLYLRVL-------LPLLVALLVILAAVAFLAFFSPALALVLAlglllaglllplLAARLGRRA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1134 SRQLKRLesvsRSPVYSHFNETLLGVSVIRAFEEQERFIHQsdlkVDENQKAYypsiVANRWLAVRLECVGNCIVLFAAL 1213
Cdd:COG4987 184 GRRLAAA----RAALRARLTDLLQGAAELAAYGALDRALAR----LDAAEARL----AAAQRRLARLSALAQALLQLAAG 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1214 FAVI----------SRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYSETEKeapwQIQETAPPST 1283
Cdd:COG4987 252 LAVVavlwlaaplvAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDAPP----AVTEPAEPAP 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1284 WPHSGRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNL 1363
Cdd:COG4987 328 APGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1364 RFKITIIPQDPVLFSGSLRMNL---DPfsQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARA 1440
Cdd:COG4987 408 RRRIAVVPQRPHLFDTTLRENLrlaRP--DATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARA 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1441 LLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIFYS 1520
Cdd:COG4987 486 LLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQ 565
|
...
gi 6678848 1521 MAK 1523
Cdd:COG4987 566 LYQ 568
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
308-867 |
3.09e-68 |
|
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: 245.13 E-value: 3.09e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 308 KDREPSLFKVLYKTFGPY---FLMSFLYKALHDLMMFAGPKILELIINFVNDREAPDWqGYFYTALLFVSACLQTL--AL 382
Cdd:COG2274 137 RGEKPFGLRWFLRLLRRYrrlLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLST-LWVLAIGLLLALLFEGLlrLL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 383 HQYF--HIcfvsGMRIKTAVVGAVYRKALLITNAARKSSTVGEIVNlmsvdaqRFMDLATYINMIWSAPLQVILALYFLW 460
Cdd:COG2274 216 RSYLllRL----GQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLAS-------RFRDVESIREFLTGSLLTALLDLLFVL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 461 LSL-------GPSVLAGVAVMILMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMSIR 533
Cdd:COG2274 285 IFLivlffysPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLL 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 534 QEELKVLKKSAYLAAVGTFTwvcTPFLVALSTFAVFVT----VDERNI-LDAKKAFVSLalfnILRF--PLNILPMVISS 606
Cdd:COG2274 365 AKYLNARFKLRRLSNLLSTL---SGLLQQLATVALLWLgaylVIDGQLtLGQLIAFNIL----SGRFlaPVAQLIGLLQR 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 607 IVQASVSLKRLRIFLSHEeLEPDSIERRSIKSGEGNSITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSS 686
Cdd:COG2274 438 FQDAKIALERLDDILDLP-PEREEGRSKLSLPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKST 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 687 LLSALLAEMDKVEGHVTLKG-------------SVAYVPQQAWIQNDSLRENILFGHPLQEnyYKAVMEAC---ALLPDL 750
Cdd:COG2274 517 LLKLLLGLYEPTSGRILIDGidlrqidpaslrrQIGVVLQDVFLFSGTIRENITLGDPDAT--DEEIIEAArlaGLHDFI 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 751 EILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRILVTHGIS 830
Cdd:COG2274 595 EALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENL---RRLLKGRTVIIIAHRLS 671
|
570 580 590
....*....|....*....|....*....|....*..
gi 6678848 831 YLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAEFLR 867
Cdd:COG2274 672 TIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
349-617 |
1.65e-66 |
|
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: 227.13 E-value: 1.65e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 349 LIINFVNDREAPDWQGYFYTALLFVSACLQTLALHQYFHICFVSGMRIKTAVVGAVYRKALLITNAARKSSTVGEIVNLM 428
Cdd:cd18594 23 LVAYFVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKKTLKLSSSALSKITTGHIVNLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 429 SVDAQRFMDLATYINMIWSAPLQVILALYFLWLSLGPSVLAGVAVMILMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNE 508
Cdd:cd18594 103 SNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFAKYRRKTAGLTDERVKIMNE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 509 ILNGIKVLKLYAWELAFQDKVMSIRQEELKVLKKSAYLAAVGTFTWVCTPFLVALSTFAVFVTVdeRNILDAKKAFVSLA 588
Cdd:cd18594 183 IISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATFVPYVLT--GNTLTARKVFTVIS 260
|
250 260 270
....*....|....*....|....*....|
gi 6678848 589 LFNILRFPLNI-LPMVISSIVQASVSLKRL 617
Cdd:cd18594 261 LLNALRMTITRfFPESIQTLSESRVSLKRI 290
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
644-844 |
3.44e-65 |
|
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: 220.28 E-value: 3.44e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWARGePPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTL-----------------KG 706
Cdd:cd03290 1 VQVTNGYFSWGSG-LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWsnknesepsfeatrsrnRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 707 SVAYVPQQAWIQNDSLRENILFGHPLQENYYKAVMEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNS 786
Cdd:cd03290 80 SVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 787 DIYLFDDPLSAVDAHVGKHIFEKvvGPMGLLKN--KTRILVTHGISYLPQVDVIIVMSGG 844
Cdd:cd03290 160 NIVFLDDPFSALDIHLSDHLMQE--GILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1290-1521 |
7.08e-65 |
|
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: 220.18 E-value: 7.08e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITI 1369
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1370 IPQDPVLFSGSLRMNLdpfsQY-----SDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRK 1444
Cdd:cd03251 81 VSQDVFLFNDTVAENI----AYgrpgaTREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6678848 1445 TKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIFYSM 1521
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
967-1265 |
2.44e-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: 221.43 E-value: 2.44e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 967 GLFITFLSIFLFLCNHVSALASNYWLSLW----------TDDPPVVNGTQA-----NRNFRLSVYGalGILQGAAIFGYS 1031
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWanleeklndtTDRVQGENSTNVdiedlDRDFNLGIYA--GLTAATFVFGFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1032 MAVSI--GGIFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLAT 1109
Cdd:cd18601 79 RSLLFfhVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1110 PIAAVIIPPLGLVYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPS 1189
Cdd:cd18601 159 PWVLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLF 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6678848 1190 IVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYS 1265
Cdd:cd18601 239 LATSRWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEYS 314
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1043-1521 |
4.70e-64 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 229.99 E-value: 4.70e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1043 RRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLfSVIGAVIIILLATP-----IAAVIIP 1117
Cdd:PRK10790 98 QQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSA-ALIGAMLVAMFSLDwrmalVAIMIFP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1118 PLGLVYFFVQRFyvaSSRQLKRLESVsRSPVYSHFNETLLGVSVIRAFEEQERFihqsDLKVDENQKAYYPSivanRWLA 1197
Cdd:PRK10790 177 AVLVVMVIYQRY---STPIVRRVRAY-LADINDGFNEVINGMSVIQQFRQQARF----GERMGEASRSHYMA----RMQT 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1198 VRLE--CVGNCIVLFAALF--AVISRHSLSA-GLVGLSVSYslqitAYLNWLVRMS----------SEMETNIVAVERLK 1262
Cdd:PRK10790 245 LRLDgfLLRPLLSLFSALIlcGLLMLFGFSAsGTIEVGVLY-----AFISYLGRLNeplielttqqSMLQQAVVAGERVF 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1263 EYSETEKeapwqiQETAPPSTWPHSGRVEFRDYCLRYREDlDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINE 1342
Cdd:PRK10790 320 ELMDGPR------QQYGNDDRPLQSGRIDIDNVSFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYP 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1343 SAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAE 1422
Cdd:PRK10790 393 LTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGE 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1423 GGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEV 1502
Cdd:PRK10790 473 QGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQA 552
|
490
....*....|....*....
gi 6678848 1503 RECGAPSELLQQRGIFYSM 1521
Cdd:PRK10790 553 VEQGTHQQLLAAQGRYWQM 571
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
362-617 |
1.06e-63 |
|
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: 219.01 E-value: 1.06e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 362 WQGYFYTALLFVSACLQTLALHQYFHICFVSGMRIKTAVVGAVYRKALLITNAARKSSTVGEIVNLMSVDAQRFMDLATY 441
Cdd:cd18593 37 TEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLIYRKALRLSQAALGKTTVGQIVNLLSNDVNRFDQAVLF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 442 INMIWSAPLQVILALYFLWLSLGPSVLAGVAVMILMVPLNAVMAmktktYQVAHMKSK-----DNRIKLMNEILNGIKVL 516
Cdd:cd18593 117 LHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFG-----KLFSKLRRKtaartDKRIRIMNEIINGIRVI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 517 KLYAWELAFQDKVMSIRQEELKVLKKSAYLAAV-GTFTWVCTPfLVALSTFAVFVTVDerNILDAKKAFVSLALFNILRF 595
Cdd:cd18593 192 KMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALnMGLFFVSSK-LILFLTFLAYILLG--NILTAERVFVTMALYNAVRL 268
|
250 260
....*....|....*....|...
gi 6678848 596 PLNI-LPMVISSIVQASVSLKRL 617
Cdd:cd18593 269 TMTLfFPFAIQFGSELSVSIRRI 291
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1290-1521 |
7.42e-63 |
|
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: 214.40 E-value: 7.42e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDYCLRYREDLDlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITI 1369
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1370 IPQDPVLFSGSLRMNLdpfsQY-----SDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRK 1444
Cdd:cd03253 80 VPQDTVLFNDTIGYNI----RYgrpdaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6678848 1445 TKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIFYSM 1521
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1290-1501 |
2.61e-62 |
|
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: 209.93 E-value: 2.61e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITI 1369
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1370 IPQDPVLFSGSLRMNLdpfsqysdeevwmalelahlkgfvsalpdklnhecaeggenLSVGQRQLVCLARALLRKTKILV 1449
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6678848 1450 LDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGE 1501
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1290-1523 |
1.46e-60 |
|
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: 207.78 E-value: 1.46e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDYCLRY--REDLdLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKI 1367
Cdd:cd03249 1 IEFKNVSFRYpsRPDV-PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1368 TIIPQDPVLFSGSLRMNL-----DPfsqySDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALL 1442
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIrygkpDA----TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1443 RKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIFYSMA 1522
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLV 235
|
.
gi 6678848 1523 K 1523
Cdd:cd03249 236 K 236
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1037-1521 |
5.44e-60 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 220.75 E-value: 5.44e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1037 GGIF------ASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATP 1110
Cdd:TIGR00958 222 GGSFnytmarINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSP 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1111 IAAVI----IPPLGLVYFFVQRFYVASSRQLKrlESVSRSPVYSHfnETLLGVSVIRAF--EEQE--RFIHQSDLKVDEN 1182
Cdd:TIGR00958 302 RLTMVtlinLPLVFLAEKVFGKRYQLLSEELQ--EAVAKANQVAE--EALSGMRTVRSFaaEEGEasRFKEALEETLQLN 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1183 QK---AYYPSIVANRWLAVRLECvgncIVLFAALFAVISRHSLSAGLVGLsVSYSLQITAYLNWLVRMSSEMETNIVAVE 1259
Cdd:TIGR00958 378 KRkalAYAGYLWTTSVLGMLIQV----LVLYYGGQLVLTGKVSSGNLVSF-LLYQEQLGEAVRVLSYVYSGMMQAVGASE 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1260 RLKEYSETEKEAPwQIQETAPPstwPHSGRVEFRDYCLRY--REDLdLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGL 1337
Cdd:TIGR00958 453 KVFEYLDRKPNIP-LTGTLAPL---NLEGLIEFQDVSFSYpnRPDV-PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALL 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1338 FRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSGSLRMNLD-PFSQYSDEEVWMALELAHLKGFVSALPDKL 1416
Cdd:TIGR00958 528 QNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAyGLTDTPDEEIMAAAKAANAHDFIMEFPNGY 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1417 NHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTirTQFEDCTVLTIAHRLNTIMDYTRVIV 1496
Cdd:TIGR00958 608 DTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIAHRLSTVERADQILV 685
|
490 500
....*....|....*....|....*
gi 6678848 1497 LDKGEVRECGAPSELLQQRGIFYSM 1521
Cdd:TIGR00958 686 LKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1217-1521 |
2.55e-59 |
|
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: 216.22 E-value: 2.55e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1217 ISRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYSETEKEapwqIQET--APPSTwPHSGRVEFRD 1294
Cdd:COG5265 288 VVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPE----VADApdAPPLV-VGGGEVRFEN 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1295 YCLRYREDlDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDP 1374
Cdd:COG5265 363 VSFGYDPE-RPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDT 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1375 VLFSGSLRMNLdpfsQY-----SDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILV 1449
Cdd:COG5265 442 VLFNDTIAYNI----AYgrpdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILI 517
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6678848 1450 LDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIFYSM 1521
Cdd:COG5265 518 FDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
452-867 |
9.51e-59 |
|
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: 213.47 E-value: 9.51e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 452 VILALYFLWLSLGPSVLAGVAVMILMVPLNAVMAMKTKTYQVAHMKSkDNRIKLMnEILNGIKVLKLY-AWElAFQDKVM 530
Cdd:COG4987 146 AVAFLAFFSPALALVLALGLLLAGLLLPLLAARLGRRAGRRLAAARA-ALRARLT-DLLQGAAELAAYgALD-RALARLD 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 531 SIRQEELKVLKKSAYLAAVGTFTwvcTPFLVALSTFAVFVTVD---ERNILDAKK----AFVSLALFNILRfPLnilPMV 603
Cdd:COG4987 223 AAEARLAAAQRRLARLSALAQAL---LQLAAGLAVVAVLWLAAplvAAGALSGPLlallVLAALALFEALA-PL---PAA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 604 ISSIVQASVSLKRLRIFLSHEELEPDSIErrSIKSGEGNSITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCG 683
Cdd:COG4987 296 AQHLGRVRAAARRLNELLDAPPAVTEPAE--PAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSG 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 684 KSSLLSALLAEMDKVEGHVTLKG-------------SVAYVPQQAWIQNDSLRENILFGHP-LQENYYKAVMEACALLPD 749
Cdd:COG4987 374 KSTLLALLLRFLDPQSGSITLGGvdlrdldeddlrrRIAVVPQRPHLFDTTLRENLRLARPdATDEELWAALERVGLGDW 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 750 LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRILVTHGI 829
Cdd:COG4987 454 LAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADL---LEALAGRTVLLITHRL 530
|
410 420 430
....*....|....*....|....*....|....*...
gi 6678848 830 SYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAEFLR 867
Cdd:COG4987 531 AGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1288-1518 |
5.73e-57 |
|
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: 198.93 E-value: 5.73e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1288 GRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRInESAEGEIIIDGVNIAKIGLHNLRFKI 1367
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1368 TIIPQDPVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKI 1447
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6678848 1448 LVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIF 1518
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1057-1518 |
6.55e-55 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 202.56 E-value: 6.55e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1057 PMSFFERTPSGNLVNRFskeldTVDSmiPQVIKMFMGSLFSVI--GAVIIILLA----------------TPIAAVIIpp 1118
Cdd:PRK11176 112 PVSFFDKQSTGTLLSRI-----TYDS--EQVASSSSGALITVVreGASIIGLFImmfyyswqlsliliviAPIVSIAI-- 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1119 lGLVyffVQRFyvassRQLKRLESVSRSPVYSHFNETLLGVSVIRAF----EEQERF------IHQSDLKVDENQKAYYP 1188
Cdd:PRK11176 183 -RVV---SKRF-----RNISKNMQNTMGQVTTSAEQMLKGHKEVLIFggqeVETKRFdkvsnrMRQQGMKMVSASSISDP 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1189 SI--VANRWLAVrlecvgnciVLFAALFAVIsRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEY-- 1264
Cdd:PRK11176 254 IIqlIASLALAF---------VLYAASFPSV-MDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAIld 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1265 SETEKEAPWQIQETAppstwphSGRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESA 1344
Cdd:PRK11176 324 LEQEKDEGKRVIERA-------KGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDID 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1345 EGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSGSLRMNLDPFS--QYSDEEVWMALELAHLKGFVSALPDKLNHECAE 1422
Cdd:PRK11176 397 EGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARteQYSREQIEEAARMAYAMDFINKMDNGLDTVIGE 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1423 GGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEV 1502
Cdd:PRK11176 477 NGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEI 556
|
490
....*....|....*.
gi 6678848 1503 RECGAPSELLQQRGIF 1518
Cdd:PRK11176 557 VERGTHAELLAQNGVY 572
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1290-1521 |
3.67e-54 |
|
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: 189.23 E-value: 3.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITI 1369
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1370 IPQDPVLFSGSLRMNL---DPfsQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTK 1446
Cdd:cd03252 81 VLQENVLFNRSIRDNIalaDP--GMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 1447 ILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIFYSM 1521
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
620-860 |
2.66e-52 |
|
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: 194.21 E-value: 2.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 620 FLSHEELEPDSIERrSIKSGEGNSITVKNATFTWArGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVE 699
Cdd:COG4988 314 LLDAPEPAAPAGTA-PLPAAGPPSIELEDVSFSYP-GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYS 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 700 GHVTLKG-------------SVAYVPQQAWIQNDSLRENILFGHP------LQenyykAVMEACALLPDLEILPSGDRTE 760
Cdd:COG4988 392 GSILINGvdlsdldpaswrrQIAWVPQNPYLFAGTIRENLRLGRPdasdeeLE-----AALEAAGLDEFVAALPDGLDTP 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 761 IGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRILVTHGISYLPQVDVIIV 840
Cdd:COG4988 467 LGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQAL---RRLAKGRTVILITHRLALLAQADRILV 543
|
250 260
....*....|....*....|
gi 6678848 841 MSGGKISEMGSYQELLDRDG 860
Cdd:COG4988 544 LDDGRIVEQGTHEELLAKNG 563
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
341-617 |
2.69e-52 |
|
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: 185.84 E-value: 2.69e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 341 FAGPKIL-ELIINFVNDREAPDWQGYFYTALLFVSACLQTLALHQYFHICFVSGMRIKTAVVGAVYRKALLITNAARKSs 419
Cdd:cd18592 14 FIGPTILiRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYKKILRLRSLGDKS- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 420 tVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLSLGPSVLAGVAVMILMVPLNAVMAMKTKTYQVAHMKSK 499
Cdd:cd18592 93 -VGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAKLTGKFRRKAIVIT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 500 DNRIKLMNEILNGIKVLKLYAWELAFQDKVMSIRQEELKVLKKSAYLAAVGTftwVCTPFLVALSTFAVFVT-VDERNIL 578
Cdd:cd18592 172 DKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISI---SLAPIVPVIASVVTFLAhVALGNDL 248
|
250 260 270
....*....|....*....|....*....|....*....
gi 6678848 579 DAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 617
Cdd:cd18592 249 TAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1288-1502 |
4.10e-52 |
|
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: 182.79 E-value: 4.10e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1288 GRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLT---LGLFRineSAEGEIIIDGVNIAKIGLHNLR 1364
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLkllAGLYK---PTSGSVLLDGTDIRQLDPADLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1365 FKITIIPQDPVLFSGSLRMNLDPFSQY-SDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLR 1443
Cdd:cd03245 78 RNIGYVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6678848 1444 KTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEV 1502
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
659-883 |
6.40e-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: 178.90 E-value: 6.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 659 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQQAWIQNDSLRENILFGHPLQENYYK 738
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 739 AVMEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVgpMGLLK 818
Cdd:cd03291 131 SVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCV--CKLMA 208
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 819 NKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAEFLRTYANAEQDLASEDDSV 883
Cdd:cd03291 209 NKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLMGYDTFDQFSAERRNSI 273
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
972-1241 |
3.25e-49 |
|
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: 176.68 E-value: 3.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 972 FLSIFLFLCNHVSALASNYWLSLWTDDPPVVNGTQANR-NFRLSVYGALGILQGAAIFGYSMAVSIGGIFASRRLHLDLL 1050
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQAlNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1051 YNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIIPPLGLVYFFVQRFY 1130
Cdd:pfam00664 82 KKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1131 VASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLF 1210
Cdd:pfam00664 162 AKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYAL 241
|
250 260 270
....*....|....*....|....*....|...
gi 6678848 1211 AALFAV--ISRHSLSAGLVGLSVSYSLQITAYL 1241
Cdd:pfam00664 242 ALWFGAylVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
644-864 |
4.20e-49 |
|
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: 174.73 E-value: 4.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWARGEPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAY 710
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 711 VPQQAWIQNDSLRENILFGHP--LQENYYKAVmEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDI 788
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRPdaTDEEVIEAA-KAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6678848 789 YLFDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAE 864
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAAL---RDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAE 231
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1054-1523 |
1.04e-48 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 186.32 E-value: 1.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1054 LRSPMSFFERTPSGNLVNRfskeLDTVDSMIPQ----VIKMFMGSLFSVIGAVII-------ILLATPIAAVIIpplgLV 1122
Cdd:TIGR03797 220 LRLPVSFFRQYSTGDLASR----AMGISQIRRIlsgsTLTTLLSGIFALLNLGLMfyyswklALVAVALALVAI----AV 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1123 YFFVQRFYVASSRQLKRLESVSRSPVYSHFNetllGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLec 1202
Cdd:TIGR03797 292 TLVLGLLQVRKERRLLELSGKISGLTVQLIN----GISKLRVAGAENRAFARWAKLFSRQRKLELSAQRIENLLTVFN-- 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1203 VGNCIVLFAALFAVISRHSLSAGL-VGLSVSYSLQITAYLNWLVRMSSEMeTNIVAV----ERLKEYSETEKEAPwqiQE 1277
Cdd:TIGR03797 366 AVLPVLTSAALFAAAISLLGGAGLsLGSFLAFNTAFGSFSGAVTQLSNTL-ISILAViplwERAKPILEALPEVD---EA 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1278 TAPPStwPHSGRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSL---TLGlFRINESaeGEIIIDGVN 1354
Cdd:TIGR03797 442 KTDPG--KLSGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLlrlLLG-FETPES--GSVFYDGQD 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1355 IAKIGLHNLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQL 1434
Cdd:TIGR03797 517 LAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQR 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1435 VCLARALLRKTKILVLDEATAAVDLETDNLI-QSTIRTQfedCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQ 1513
Cdd:TIGR03797 597 LLIARALVRKPRILLFDEATSALDNRTQAIVsESLERLK---VTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMA 673
|
490
....*....|
gi 6678848 1514 QRGIFYSMAK 1523
Cdd:TIGR03797 674 REGLFAQLAR 683
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1017-1521 |
2.12e-48 |
|
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: 185.71 E-value: 2.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1017 GALGILQGAAIFGY------SMAVSIGGIFASRRLHLDLLYN----VLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQ 1086
Cdd:TIGR01193 193 GTLGIISIGLIIAYiiqqilSYIQIFLLNVLGQRLSIDIILSyikhLFELPMSFFSTRRTGEIVSRFTDASSIIDALAST 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1087 VIKMFMG-SLFSVIGAVI---------IILLATPIAAVIIpplglvYFFVQRFYVASSRQLKrlesvSRSPVYSHFNETL 1156
Cdd:TIGR01193 273 ILSLFLDmWILVIVGLFLvrqnmllflLSLLSIPVYAVII------ILFKRTFNKLNHDAMQ-----ANAVLNSSIIEDL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1157 LGVSVIRAF-EEQERFIHQSDLKVDENQKA--YYPSIVANRWLAVRLECVGNCIVLFAALFAVIsRHSLSAGLVglsVSY 1233
Cdd:TIGR01193 342 NGIETIKSLtSEAERYSKIDSEFGDYLNKSfkYQKADQGQQAIKAVTKLILNVVILWTGAYLVM-RGKLTLGQL---ITF 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1234 SLQITAYLNWL---VRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAppSTWPHsGRVEFRDYCLRYREDlDLVLKHI 1310
Cdd:TIGR01193 418 NALLSYFLTPLeniINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTE--LNNLN-GDIVINDVSYSYGYG-SNILSDI 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1311 NVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSGSLRMNLDPFSQ 1390
Cdd:TIGR01193 494 SLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAK 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1391 --YSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQST 1468
Cdd:TIGR01193 574 enVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNN 653
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 6678848 1469 IrTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIFYSM 1521
Cdd:TIGR01193 654 L-LNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1053-1528 |
6.77e-48 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 181.70 E-value: 6.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1053 VLRSPMSFFERTPSGNLVNRFskeLDTVDSMIpQVIKMFMGSLFSVIGAVIIILlatPIA-------AVIIPPLGLVYFF 1125
Cdd:PRK13657 99 IIQLPLAWHSQRGSGRALHTL---LRGTDALF-GLWLEFMREHLATLVALVVLL---PLAlfmnwrlSLVLVVLGIVYTL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1126 VQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAF---EEQERFIHQSdlkVDENQKAYYPsiVANRW-LAVRLE 1201
Cdd:PRK13657 172 ITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYnriEAETQALRDI---ADNLLAAQMP--VLSWWaLASVLN 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1202 CVGNCIVLFAALF---AVISRHSLSAGLVGLSVSYSlqiTAYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPwQIQEt 1278
Cdd:PRK13657 247 RAASTITMLAILVlgaALVQKGQLRVGEVVAFVGFA---TLLIGRLDQVVAFINQVFMAAPKLEEFFEVEDAVP-DVRD- 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1279 aPPSTWPH---SGRVEFRDYCLRY---REDLDlvlkHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG 1352
Cdd:PRK13657 322 -PPGAIDLgrvKGAVEFDDVSFSYdnsRQGVE----DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDG 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1353 VNIAKIGLHNLRFKITIIPQDPVLFSGSLRMNL-----DPfsqySDEEVWMALELAHLKGFVSALPDKLNHECAEGGENL 1427
Cdd:PRK13657 397 TDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIrvgrpDA----TDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQL 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1428 SVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGA 1507
Cdd:PRK13657 473 SGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGS 552
|
490 500
....*....|....*....|.
gi 6678848 1508 PSELLQQRGIFYSMAKDAGLV 1528
Cdd:PRK13657 553 FDELVARGGRFAALLRAQGML 573
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
644-864 |
6.08e-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: 162.79 E-value: 6.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAY 710
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlaslrrQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 711 VPQQAWIQNDSLRENILFGHPlqENYYKAVMEAC--ALLPDL-EILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSD 787
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRP--GATREEVEEAAraANAHEFiMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 788 IYLFDDPLSAVDAHVGKHI---FEKvvgpmgLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAE 864
Cdd:cd03251 159 ILILDEATSALDTESERLVqaaLER------LMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAK 232
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
973-1485 |
1.68e-44 |
|
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: 170.23 E-value: 1.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 973 LSIFLFLCNHVSALA----SNYWLSLWTDDPPVVNGTQANRNFRlsvygALGILQGAA-----IFGYSMAVSIGGifasr 1043
Cdd:TIGR02868 17 LAVLLGALALGSAVAllgvSAWLISRAAEMPPVLYLSVAAVAVR-----AFGIGRAVFrylerLVGHDAALRSLG----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1044 RLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIkmfmgslFSVIGAVIIILLATPIAAVIIPPLGLV- 1122
Cdd:TIGR02868 87 ALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVI-------VPAGVALVVGAAAVAAIAVLSVPAALIl 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1123 -------YFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRW 1195
Cdd:TIGR02868 160 aaglllaGFVAPLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1196 LAVRLECVGNCIVLFAALFAV--ISRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPW 1273
Cdd:TIGR02868 240 GAALTLLAAGLAVLGALWAGGpaVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAGPVAE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1274 QIQETAPPSTwPHSGRVEFRDYCLRYrEDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGV 1353
Cdd:TIGR02868 320 GSAPAAGAVG-LGKPTLELRDLSAGY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1354 NIAKIGLHNLRFKITIIPQDPVLFSGSLRMNL---DPfsQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVG 1430
Cdd:TIGR02868 398 PVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLrlaRP--DATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGG 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 1431 QRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRL 1485
Cdd:TIGR02868 476 ERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1288-1502 |
2.11e-44 |
|
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: 161.10 E-value: 2.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1288 GRVEFRDYCLRYREDLD-LVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFK 1366
Cdd:cd03248 10 GIVKFQNVTFAYPTRPDtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1367 ITIIPQDPVLFSGSLRMNLD-PFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKT 1445
Cdd:cd03248 90 VSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6678848 1446 KILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEV 1502
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1017-1497 |
2.50e-44 |
|
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: 169.77 E-value: 2.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1017 GALGILQGAAIFGYSMAVSiggifasRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDS----MIPQVIKMFM 1092
Cdd:TIGR02857 58 ALLGWLQERAAARAAAAVK-------SQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGyfarYLPQLVLAVI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1093 GSLfsVIGAVIiiLLATPIAAVII---PPLgLVYFFVQRFYVASSRQLKRLESVSRspVYSHFNETLLGVSVIRAF---- 1165
Cdd:TIGR02857 131 VPL--AILAAV--FPQDWISGLILlltAPL-IPIFMILIGWAAQAAARKQWAALSR--LSGHFLDRLRGLPTLKLFgrak 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1166 EEQERFIHQSD---------LKVdenqkAYYPSIVanrwlavrLEcvgncivLFA----ALFAVISRHSLSAGLVGLSVS 1232
Cdd:TIGR02857 204 AQAAAIRRSSEeyrertmrvLRI-----AFLSSAV--------LE-------LFAtlsvALVAVYIGFRLLAGDLDLATG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1233 YSLQITA---YLNwLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPpSTWPHSGRVEFRDYCLRYrEDLDLVLKH 1309
Cdd:TIGR02857 264 LFVLLLApefYLP-LRQLGAQYHARADGVAAAEALFAVLDAAPRPLAGKAP-VTAAPASSLEFSGVSVAY-PGRRPALRP 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1310 INVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSGSLRMNL---D 1386
Cdd:TIGR02857 341 VSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIrlaR 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1387 PFSqySDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQ 1466
Cdd:TIGR02857 421 PDA--SDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVL 498
|
490 500 510
....*....|....*....|....*....|.
gi 6678848 1467 STIRTQFEDCTVLTIAHRLNTIMDYTRVIVL 1497
Cdd:TIGR02857 499 EALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
644-867 |
5.00e-44 |
|
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: 160.40 E-value: 5.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTW-ARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS-------------VA 709
Cdd:cd03249 1 IEFKNVSFRYpSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrsqIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 710 YVPQQAWIQNDSLRENILFGHPLQENyyKAVMEAC--ALLPD-LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNS 786
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATD--EEVEEAAkkANIHDfIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 787 DIYLFDDPLSAVDAHVGKHIFEKVVGPMgllKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAEFL 866
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAM---KGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLV 235
|
.
gi 6678848 867 R 867
Cdd:cd03249 236 K 236
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
644-845 |
1.68e-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: 156.00 E-value: 1.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAY 710
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 711 VPQQAWIQNDSLRENILfghplqenyykavmeacallpdleilpsgdrteigekgvnlSGGQKQRVSLARAVYSNSDIYL 790
Cdd:cd03228 81 VPQDPFLFSGTIRENIL-----------------------------------------SGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 791 FDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRILVTHGISYLPQVDVIIVMSGGK 845
Cdd:cd03228 120 LDEATSALDPETEALILEAL---RALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1310-1521 |
1.11e-42 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 166.17 E-value: 1.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1310 INVTIEGGEKVGIVGRTGAGKSSLT---LGLFrineSAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSGSLRMNL- 1385
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLnalLGFL----PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVl 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1386 --DPfsQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDN 1463
Cdd:PRK11174 445 lgNP--DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQ 522
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6678848 1464 LIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIFYSM 1521
Cdd:PRK11174 523 LVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
644-860 |
1.83e-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: 155.46 E-value: 1.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWARGEPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAY 710
Cdd:cd03254 3 IEFENVNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 711 VPQQAWIQNDSLRENILFGHPlqENYYKAVMEACALL-PDLEI--LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSD 787
Cdd:cd03254 82 VLQDTFLFSGTIMENIRLGRP--NATDEEVIEAAKEAgAHDFImkLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6678848 788 IYLFDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDG 860
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEAL---EKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1255-1521 |
2.08e-40 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 158.83 E-value: 2.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1255 IVAVERLKEYSETEKEAPWQIQETAPPStwphSGRVEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLT 1334
Cdd:PRK11160 308 IASARRINEITEQKPEVTFPTTSTAAAD----QVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1335 LGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSGSLRMNL---DPfsQYSDEEVWMALELAHLKGFVSA 1411
Cdd:PRK11160 384 QLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGLEKLLED 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1412 lPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTI--M 1489
Cdd:PRK11160 462 -DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLeqF 540
|
250 260 270
....*....|....*....|....*....|..
gi 6678848 1490 DytRVIVLDKGEVRECGAPSELLQQRGIFYSM 1521
Cdd:PRK11160 541 D--RICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
326-597 |
4.36e-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: 150.10 E-value: 4.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 326 FLMSFLYKALHDLMMFAGPKILELIINFVNDREAPDWQ--GYFYTALLFVSACLQTLALHQyFHICFVSGMRIKTAVVGA 403
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQalNVYSLALLLLGLAQFILSFLQ-SYLLNHTGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 404 VYRKALLITNAARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLSLGPSV-LAGVAVMILMVPLNA 482
Cdd:pfam00664 80 LFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLtLVLLAVLPLYILVSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 483 VMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMSIRQEELKV-LKKSAYLAAVGTFTWVCTPFLV 561
Cdd:pfam00664 160 VFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAgIKKAVANGLSFGITQFIGYLSY 239
|
250 260 270
....*....|....*....|....*....|....*.
gi 6678848 562 ALSTFAVFVTVDeRNILDAKKAFVSLALFNILRFPL 597
Cdd:pfam00664 240 ALALWFGAYLVI-SGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
643-846 |
2.65e-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: 146.20 E-value: 2.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 643 SITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVA 709
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 710 YVPQQAWIQNDSLRENILFGHPLQENyyKAVMEACALL---PDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNS 786
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGAPLADD--ERILRAAELAgvtDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 787 DIYLFDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKI 846
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERL---RQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1290-1515 |
1.92e-38 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 144.01 E-value: 1.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDYCLRYREDlDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTL---GLFRINEsaeGEIIIDGVNIAKIGLHNLRFK 1366
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRllnGLLKPTS---GEVLVDGKDITKKNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1367 ITIIPQDPV--LFSGSLR-------MNLdpfsQYSDEE----VWMALELAHLKGFvsalpdkLNHECAEggenLSVGQRQ 1433
Cdd:COG1122 77 VGLVFQNPDdqLFAPTVEedvafgpENL----GLPREEirerVEEALELVGLEHL-------ADRPPHE----LSGGQKQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1434 LVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRT-QFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSEL 1511
Cdd:COG1122 142 RVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAELAdRVIVLDDGRIVADGTPREV 221
|
....
gi 6678848 1512 LQQR 1515
Cdd:COG1122 222 FSDY 225
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
450-841 |
4.36e-38 |
|
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: 151.29 E-value: 4.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 450 LQVILALYFLWLSLGPSVLAGVaVMILMVPLNAV-MA---MKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAF 525
Cdd:TIGR02857 127 LAVIVPLAILAAVFPQDWISGL-ILLLTAPLIPIfMIligWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQ 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 526 QDKVMSI----RQEELKVLKKSAYLAAVgtftwvcTPFLVALSTFAVFVTVDERNI---LDAKKAFVSLALFNILRFPLN 598
Cdd:TIGR02857 206 AAAIRRSseeyRERTMRVLRIAFLSSAV-------LELFATLSVALVAVYIGFRLLagdLDLATGLFVLLLAPEFYLPLR 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 599 ILPMVISSIVQASVSLKRLRIFLSHEELEpdSIERRSIKSGEGNSITVKNATFTWaRGEPPTLNGITFSIPEGALVAVVG 678
Cdd:TIGR02857 279 QLGAQYHARADGVAAAEALFAVLDAAPRP--LAGKAPVTAAPASSLEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVG 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 679 QVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAYVPQQAWIQNDSLRENILFGHPLQ-ENYYKAVMEAC 744
Cdd:TIGR02857 356 PSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIAWVPQHPFLFAGTIAENIRLARPDAsDAEIREALERA 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 745 ALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRIL 824
Cdd:TIGR02857 436 GLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEAL---RALAQGRTVLL 512
|
410
....*....|....*..
gi 6678848 825 VTHGISYLPQVDVIIVM 841
Cdd:TIGR02857 513 VTHRLALAALADRIVVL 529
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
644-1525 |
2.55e-37 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 154.03 E-value: 2.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTW-ARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS--------------V 708
Cdd:PTZ00265 383 IQFKNVRFHYdTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdinlkwwrskI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 709 AYVPQQAWIQNDSLRENILF------------------GHPLQE--NYYKAVMEACA----------------------- 745
Cdd:PTZ00265 463 GVVSQDPLLFSNSIKNNIKYslyslkdlealsnyynedGNDSQEnkNKRNSCRAKCAgdlndmsnttdsneliemrknyq 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 746 LLPDLEI---------------LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDaHVGKHIFEKV 810
Cdd:PTZ00265 543 TIKDSEVvdvskkvlihdfvsaLPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKT 621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 811 VGPMGLLKNKTRILVTHGISYLPQVDVIIVMS-----------------------------------------------G 843
Cdd:PTZ00265 622 INNLKGNENRITIIIAHRLSTIRYANTIFVLSnrergstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnaG 701
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 844 GKISEMGSYQELL-DRDGAFAEFLRTyanaeQDLASEDDSVSGSGKES-------KPVENGMLVTDTVGKHLQRHLSNSS 915
Cdd:PTZ00265 702 SYIIEQGTHDALMkNKNGIYYTMINN-----QKVSSKKSSNNDNDKDSdmkssayKDSERGYDPDEMNGNSKHENESASN 776
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 916 SHSGDTSQQHSSIAElqkAGAKEETWKLMEADKAQTGQVQLSVY---WNYMKAIGlfITFLSIFLF--LCNHVSALASNY 990
Cdd:PTZ00265 777 KKSCKMSDENASENN---AGGKLPFLRNLFKRKPKAPNNLRIVYreiFSYKKDVT--IIALSILVAggLYPVFALLYAKY 851
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 991 WLSLWTddppvVNGTQANRNfRLSVYG---ALGILQGAAIFGYSMAVSigGIFASRRLHLDLLYNVLRSPMSFFER---T 1064
Cdd:PTZ00265 852 VSTLFD-----FANLEANSN-KYSLYIlviAIAMFISETLKNYYNNVI--GEKVEKTMKRRLFENILYQEISFFDQdkhA 923
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1065 PsGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAVIippLGLVYFFVQRFYVASSR-------QL 1137
Cdd:PTZ00265 924 P-GLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYFCPIVAAV---LTGTYFIFMRVFAIRARltankdvEK 999
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1138 KRLESVSRSPVYSH-----------FNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNC 1206
Cdd:PTZ00265 1000 KEINQPGTVFAYNSddeifkdpsflIQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLF 1079
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1207 IVLFAALFA--VISRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERLkeYSETEKEAPWQIQETAP---P 1281
Cdd:PTZ00265 1080 INSFAYWFGsfLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKY--YPLIIRKSNIDVRDNGGiriK 1157
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1282 STWPHSGRVEFRDYCLRYREDLDL-VLKHINVTIEGGEKVGIVGRTGAGKSSL--------------------------- 1333
Cdd:PTZ00265 1158 NKNDIKGKIEIMDVNFRYISRPNVpIYKDLTFSCDSKKTTAIVGETGSGKSTVmsllmrfydlkndhhivfknehtndmt 1237
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1334 -----------TLGLFRINESA----------------EGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSGSLRMNLD 1386
Cdd:PTZ00265 1238 neqdyqgdeeqNVGMKNVNEFSltkeggsgedstvfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK 1317
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1387 pFSQ--YSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNL 1464
Cdd:PTZ00265 1318 -FGKedATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKL 1396
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6678848 1465 IQSTIR--TQFEDCTVLTIAHRLNTIMDYTRVIVLDKGE-----VRECGAPSELLQ-QRGIFYSMAKDA 1525
Cdd:PTZ00265 1397 IEKTIVdiKDKADKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLSvQDGVYKKYVKLA 1465
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
620-867 |
9.48e-37 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 148.07 E-value: 9.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 620 FLSHEELEPDSiERRSIKSGEGNSITVKNATFTWARGEPptLNG-ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMdKV 698
Cdd:PRK11174 327 FLETPLAHPQQ-GEKELASNDPVTIEAEDLEILSPDGKT--LAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PY 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 699 EGHVTLKG------SVAYVPQQ-AWI-QN-----DSLRENILFGHP-LQENYYKAVMEACALLPDLEILPSGDRTEIGEK 764
Cdd:PRK11174 403 QGSLKINGielrelDPESWRKHlSWVgQNpqlphGTLRDNVLLGNPdASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQ 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 765 GVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVGPMgllKNKTRILVTHGISYLPQVDVIIVMSGG 844
Cdd:PRK11174 483 AAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAS---RRQTTLMVTHQLEDLAQWDQIWVMQDG 559
|
250 260
....*....|....*....|...
gi 6678848 845 KISEMGSYQELLDRDGAFAEFLR 867
Cdd:PRK11174 560 QIVQQGDYAELSQAGGLFATLLA 582
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
395-827 |
2.75e-36 |
|
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: 145.97 E-value: 2.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 395 RIKTAVVGAVYRKALLITNAARKSSTVGEIVNLMS--VDAQRFMDLATYINMIWSAPLQVI--LALYFLWLSLGPSVLAG 470
Cdd:TIGR02868 83 RSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGadVDALQDLYVRVIVPAGVALVVGAAavAAIAVLSVPAALILAAG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 471 VAVMILMVPLNAVMAMKTKTYQVAHMKSKDNRiKLMnEILNGIKVLKLYAWELAFQDKVMSIRQEELKVLKKSAYLAAVG 550
Cdd:TIGR02868 163 LLLAGFVAPLVSLRAARAAEQALARLRGELAA-QLT-DALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 551 T--FTWVCTpfLVALSTFAVFVTVDERNILD----AKKAFVSLALFNilrfPLNILPMVISSIVQASVSLKRLRIFLSHE 624
Cdd:TIGR02868 241 AalTLLAAG--LAVLGALWAGGPAVADGRLApvtlAVLVLLPLAAFE----AFAALPAAAQQLTRVRAAAERIVEVLDAA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 625 ELEPD-SIERRSIKSGEGNSITVKNATFTWArGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVT 703
Cdd:TIGR02868 315 GPVAEgSAPAAGAVGLGKPTLELRDLSAGYP-GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVT 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 704 LKGS-------------VAYVPQQAWIQNDSLRENILFGHP--LQENYYKAvMEACALLPDLEILPSGDRTEIGEKGVNL 768
Cdd:TIGR02868 394 LDGVpvssldqdevrrrVSVCAQDAHLFDTTVRENLRLARPdaTDEELWAA-LERVGLADWLRALPDGLDTVLGEGGARL 472
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 6678848 769 SGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVGPMgllKNKTRILVTH 827
Cdd:TIGR02868 473 SGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAAL---SGRTVVLITH 528
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
634-867 |
7.03e-35 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 142.47 E-value: 7.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 634 RSIKSGEGNsITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG------- 706
Cdd:PRK11176 333 RVIERAKGD-IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrdyt 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 707 ------SVAYVPQQAWIQNDSLRENIlfGHPLQENYYKAVMEACALLPD----LEILPSGDRTEIGEKGVNLSGGQKQRV 776
Cdd:PRK11176 412 laslrnQVALVSQNVHLFNDTIANNI--AYARTEQYSREQIEEAARMAYamdfINKMDNGLDTVIGENGVLLSGGQRQRI 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 777 SLARAVYSNSDIYLFDDPLSAVDAHVGKHI---FEKvvgpmgLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQ 853
Cdd:PRK11176 490 AIARALLRDSPILILDEATSALDTESERAIqaaLDE------LQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHA 563
|
250
....*....|....
gi 6678848 854 ELLDRDGAFAEFLR 867
Cdd:PRK11176 564 ELLAQNGVYAQLHK 577
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
643-867 |
3.97e-34 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 139.96 E-value: 3.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 643 SITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVA 709
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGqpiadyseaalrqAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 710 YVPQQAWIQNDSLRENILFGHP-LQENYYKAVMEACALLPDLEIlPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDI 788
Cdd:PRK11160 418 VVSQRVHLFSATLRDNLLLAAPnASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPL 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 789 YLFDDPLSAVDAHVGKHIFEkvvgpmgLL----KNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAE 864
Cdd:PRK11160 497 LLLDEPTEGLDAETERQILE-------LLaehaQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQ 569
|
...
gi 6678848 865 FLR 867
Cdd:PRK11160 570 LKQ 572
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1290-1506 |
1.18e-33 |
|
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: 128.20 E-value: 1.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLtLGLFRINESA-EGEIIIDGVNIAKIGlHNLRFKIT 1368
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTL-LQLLTGDLKPqQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1369 IIPQDPVLFSGSLRMNLdpfsqysdeevwmalelahlkgfvsalpdklnhecaegGENLSVGQRQLVCLARALLRKTKIL 1448
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6678848 1449 VLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECG 1506
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1291-1502 |
1.36e-33 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 127.72 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1291 EFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLT---LGLFRineSAEGEIIIDGVNIAKIGLHNLRFKI 1367
Cdd:cd03246 2 EVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLArliLGLLR---PTSGRVRLDGADISQWDPNELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1368 TIIPQDPVLFSGSLRMNLdpfsqysdeevwmalelahlkgfvsalpdklnhecaeggenLSVGQRQLVCLARALLRKTKI 1447
Cdd:cd03246 79 GYLPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6678848 1448 LVLDEATAAVDLETDNLIQSTI-RTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEV 1502
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIaALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1291-1501 |
1.84e-33 |
|
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: 128.74 E-value: 1.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1291 EFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITII 1370
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1371 PQDP------------VLFsgSLRmNLdpfsQYSDEEVWMALELAhLKGFvsALPDKLNHECAEggenLSVGQRQLVCLA 1438
Cdd:cd03225 81 FQNPddqffgptveeeVAF--GLE-NL----GLPEEEIEERVEEA-LELV--GLEGLRDRSPFT----LSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 1439 RALLRKTKILVLDEATAAVDLETDNLIQSTIRT-QFEDCTVLTIAHRLNTIMDY-TRVIVLDKGE 1501
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
644-863 |
2.12e-33 |
|
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: 129.53 E-value: 2.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL----LAEMDKV--EGH-------VTLKGSVAY 710
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIqrfyVPENGRVlvDGHdlaladpAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 711 VPQQAWIQNDSLRENILFGHPLQEnyYKAVMEACALLPDLEI---LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSD 787
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMS--MERVIEAAKLAGAHDFiseLPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6678848 788 IYLFDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFA 863
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNM---HDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYA 231
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
643-851 |
3.05e-33 |
|
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: 128.77 E-value: 3.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 643 SITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVT-------------LKGSVA 709
Cdd:cd03244 2 DIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILidgvdiskiglhdLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 710 YVPQQAWIQNDSLRENIlfgHPLQENYYKAVMEA---CALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNS 786
Cdd:cd03244 82 IIPQDPVLFSGTIRSNL---DPFGEYSDEELWQAlerVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 787 DIYLFDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGS 851
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTI---REAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
583-892 |
1.89e-32 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 135.09 E-value: 1.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 583 AFVSLALFNILRfplniLPMVISSIVQASVSLKRLRIFLSHEELEPDSIER---RSIKSGEGnSITVKNATFTWArGEPP 659
Cdd:PRK13657 277 AFVGFATLLIGR-----LDQVVAFINQVFMAAPKLEEFFEVEDAVPDVRDPpgaIDLGRVKG-AVEFDDVSFSYD-NSRQ 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 660 TLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAYVPQQAWIQNDSLRENI 726
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdirtvtraslrrNIAVVFQDAGLFNRSIEDNI 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 727 LFGHP--LQENYYKAvMEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGk 804
Cdd:PRK13657 430 RVGRPdaTDEEMRAA-AERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETE- 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 805 hifEKVVGPM-GLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAEFLRTyanaeQDLASEDDSV 883
Cdd:PRK13657 508 ---AKVKAALdELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRA-----QGMLQEDERR 579
|
....*....
gi 6678848 884 SGSGKESKP 892
Cdd:PRK13657 580 KQPAAEGAN 588
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
596-864 |
2.22e-32 |
|
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: 134.95 E-value: 2.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 596 PLNILPMVISSIVQASVSLKRLriF-LSHEELEP-DSIERRSIKSGEGnSITVKNATFTWaRGEPPTLNGITFSIPEGAL 673
Cdd:COG5265 311 PLNFLGFVYREIRQALADMERM--FdLLDQPPEVaDAPDAPPLVVGGG-EVRFENVSFGY-DPERPILKGVSFEVPAGKT 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 674 VAVVGQVGCGKSSLLSALLAEMDKVEG----------HVT---LKGSVAYVPQQAWIQNDSLRENILFGHP--LQENYYK 738
Cdd:COG5265 387 VAIVGPSGAGKSTLARLLFRFYDVTSGrilidgqdirDVTqasLRAAIGIVPQDTVLFNDTIAYNIAYGRPdaSEEEVEA 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 739 AVmEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFE--KVVGpmgl 816
Cdd:COG5265 467 AA-RAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAalREVA---- 541
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 6678848 817 lKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAE 864
Cdd:COG5265 542 -RGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQ 588
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1306-1506 |
2.56e-32 |
|
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: 126.08 E-value: 2.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIG---LHNLRFKITIIPQDPvlfSGSL- 1381
Cdd:cd03257 20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKEIQMVFQDP---MSSLn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1382 -RMN-----LDPF------SQYSDEEVWMALELAHLkGFVSALPDKLNHEcaeggenLSVGQRQLVCLARALLRKTKILV 1449
Cdd:cd03257 97 pRMTigeqiAEPLrihgklSKKEARKEAVLLLLVGV-GLPEEVLNRYPHE-------LSGGQRQRVAIARALALNPKLLI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6678848 1450 LDEATAAVDLETD----NLIQsTIRTQFeDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECG 1506
Cdd:cd03257 169 ADEPTSALDVSVQaqilDLLK-KLQEEL-GLTLLFITHDLGVVAKIAdRVAVMYAGKIVEEG 228
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
609-864 |
2.89e-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: 135.64 E-value: 2.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 609 QASVSLKRL-RIFLSHEELEpDSIERRSIKSGEGNsITVKNATFTWARGEPpTLNGITFSIPEGALVAVVGQVGCGKSSL 687
Cdd:TIGR01193 440 AARVANNRLnEVYLVDSEFI-NKKKRTELNNLNGD-IVINDVSYSYGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTL 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 688 LSALLAEMDKVEGHV-------------TLKGSVAYVPQQAWIQNDSLRENILFGHP--LQENYYKAVMEACALLPDLEI 752
Cdd:TIGR01193 517 AKLLVGFFQARSGEIllngfslkdidrhTLRQFINYLPQEPYIFSGSILENLLLGAKenVSQDEIWAACEIAEIKDDIEN 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 753 LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVGpmglLKNKTRILVTHGISYL 832
Cdd:TIGR01193 597 MPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN----LQDKTIIFVAHRLSVA 672
|
250 260 270
....*....|....*....|....*....|..
gi 6678848 833 PQVDVIIVMSGGKISEMGSYQELLDRDGAFAE 864
Cdd:TIGR01193 673 KQSDKIIVLDHGKIIEQGSHDELLDRNGFYAS 704
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1291-1501 |
7.22e-32 |
|
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: 122.35 E-value: 7.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1291 EFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITII 1370
Cdd:cd00267 1 EIENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1371 PQdpvlfsgslrmnldpfsqysdeevwmalelahlkgfvsalpdklnhecaeggenLSVGQRQLVCLARALLRKTKILVL 1450
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6678848 1451 DEATAAVDLETDNLIQSTIRTQFED-CTVLTIAHRLNTIMDYT-RVIVLDKGE 1501
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAAdRVIVLKDGK 157
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
644-869 |
1.30e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 124.82 E-value: 1.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFtwARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG--------SVAYVPQQA 715
Cdd:COG1121 7 IELENLTV--SYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkpprrarrRIGYVPQRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 716 WIQND---SLRENILFG--------HPLQENYYKAVMEAcalLPDLEILPSGDRTeIGEkgvnLSGGQKQRVSLARAVYS 784
Cdd:COG1121 85 EVDWDfpiTVRDVVLMGrygrrglfRRPSRADREAVDEA---LERVGLEDLADRP-IGE----LSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 785 NSDIYLFDDPLSAVDAHVGKHIFEkvvgpmgLLK-----NKTRILVTHGISYLPQ-VDVIIVMSGGKISEmGSYQELLDR 858
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYE-------LLRelrreGKTILVVTHDLGAVREyFDRVLLLNRGLVAH-GPPEEVLTP 228
|
250
....*....|.
gi 6678848 859 DgafaEFLRTY 869
Cdd:COG1121 229 E----NLSRAY 235
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
597-885 |
1.64e-31 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 131.76 E-value: 1.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 597 LNILPMV----ISSIVQ-ASVSLKRLRIFLSHEELEPDSIErrSIKSGEGnSITVKNATFTWARGEPPTLNGITFSIPEG 671
Cdd:PRK10789 265 LMIWPMLalawMFNIVErGSAAYSRIRAMLAEAPVVKDGSE--PVPEGRG-ELDVNIRQFTYPQTDHPALENVNFTLKPG 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 672 ALVAVVGQVGCGKSSLLSALLAEMDKVEGHVT-------------LKGSVAYVPQQAWIQNDSLRENILFGHPlqeNYYK 738
Cdd:PRK10789 342 QMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRfhdipltklqldsWRSRLAVVSQTPFLFSDTVANNIALGRP---DATQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 739 AVMEACALLP----DLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIfekvvgpm 814
Cdd:PRK10789 419 QEIEHVARLAsvhdDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQI-------- 490
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6678848 815 glLKN-------KTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAEFLRtYANAEQDLASEDDSVSG 885
Cdd:PRK10789 491 --LHNlrqwgegRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYR-YQQLEAALDDAPEIREE 565
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1289-1512 |
1.97e-31 |
|
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: 124.39 E-value: 1.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1289 RVEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKIT 1368
Cdd:COG1120 1 MLEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1369 IIPQDPVL-FSGSLR----M----NLDPFSQYSDEE---VWMALELAHLkgfvSALPDKLNHEcaeggenLSVGQRQLVC 1436
Cdd:COG1120 79 YVPQEPPApFGLTVRelvaLgrypHLGLFGRPSAEDreaVEEALERTGL----EHLADRPVDE-------LSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1437 LARALLRKTKILVLDEATAAVDL----ETDNLIQSTIRTQfeDCTVLTIAHRLNTIMDY-TRVIVLDKGEVRECGAPSEL 1511
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARER--GRTVVMVLHDLNLAARYaDRLVLLKDGRIVAQGPPEEV 225
|
.
gi 6678848 1512 L 1512
Cdd:COG1120 226 L 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1290-1514 |
5.62e-31 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 129.25 E-value: 5.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTL---GLFRINESAEGEIIIDGVNIAKIGLHNLRFK 1366
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALalmGLLPHGGRISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1367 ITIIPQDP------------VLFsgSLRMNLDPFSQySDEEVWMALELAHLKGFVSALPdklnHEcaeggenLSVGQRQL 1434
Cdd:COG1123 85 IGMVFQDPmtqlnpvtvgdqIAE--ALENLGLSRAE-ARARVLELLEAVGLERRLDRYP----HQ-------LSGGQRQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1435 VCLARALLRKTKILVLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSEL 1511
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVAEIAdRVVVMDDGRIVEDGPPEEI 230
|
...
gi 6678848 1512 LQQ 1514
Cdd:COG1123 231 LAA 233
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1307-1455 |
1.38e-30 |
|
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: 118.52 E-value: 1.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1307 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSGS-----L 1381
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLtvrenL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 1382 RMNLDPFSQYSDE-EVWMALELAHLKgfvsaLPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATA 1455
Cdd:pfam00005 81 RLGLLLKGLSKREkDARAEEALEKLG-----LGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1290-1521 |
1.88e-29 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 125.60 E-value: 1.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDYClrYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITI 1369
Cdd:PRK10789 316 VNIRQFT--YPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAV 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1370 IPQDPVLFSGSLRMNL---DPfsQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTK 1446
Cdd:PRK10789 394 VSQTPFLFSDTVANNIalgRP--DATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAE 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 1447 ILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIFYSM 1521
Cdd:PRK10789 472 ILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDM 546
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
644-846 |
2.56e-29 |
|
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: 115.78 E-value: 2.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS-------------VAY 710
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdpnelgdhVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 711 VPQQAWIQNDSLRENIlfghplqenyykavmeacallpdleilpsgdrteigekgvnLSGGQKQRVSLARAVYSNSDIYL 790
Cdd:cd03246 81 LPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6678848 791 FDDPLSAVDaHVGKHIFEKVVGPMGlLKNKTRILVTHGISYLPQVDVIIVMSGGKI 846
Cdd:cd03246 120 LDEPNSHLD-VEGERALNQAIAALK-AAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1290-1514 |
4.20e-29 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 123.86 E-value: 4.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRD----YCLRYREDLDlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIG---LHN 1362
Cdd:COG1123 261 LEVRNlskrYPVRGKGGVR-AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1363 LRFKITIIPQDPvlfSGSL--RMN--------LDPFSQYSDEEVW-MALELAHLKGFVSALPDKLNHEcaeggenLSVGQ 1431
Cdd:COG1123 340 LRRRVQMVFQDP---YSSLnpRMTvgdiiaepLRLHGLLSRAERReRVAELLERVGLPPDLADRYPHE-------LSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1432 RQLVCLARALLRKTKILVLDEATAAVDLetdnLIQSTIRTQFED------CTVLTIAHRLNTIMDYT-RVIVLDKGEVRE 1504
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDV----SVQAQILNLLRDlqrelgLTYLFISHDLAVVRYIAdRVAVMYDGRIVE 485
|
250
....*....|
gi 6678848 1505 CGAPSELLQQ 1514
Cdd:COG1123 486 DGPTEEVFAN 495
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
661-796 |
5.38e-29 |
|
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: 113.90 E-value: 5.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAYVPQQAWIQND-SLRENI 726
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderkslrkEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6678848 727 LFGHPLQENYYKAV-MEACALLPDLEILPSGDRTeIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLS 796
Cdd:pfam00005 81 RLGLLLKGLSKREKdARAEEALEKLGLGDLADRP-VGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
644-846 |
6.85e-29 |
|
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: 116.05 E-value: 6.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWARGEPPT--LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVTLKG-------------- 706
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVRVDGtdisklsekelaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 707 ---SVAYVPQQ-AWIQNDSLRENILFGHPLQENYYKAVMEACALLpdLEILPSGDRteIGEKGVNLSGGQKQRVSLARAV 782
Cdd:cd03255 80 rrrHIGFVFQSfNLLPDLTALENVELPLLLAGVPKKERRERAEEL--LERVGLGDR--LNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 783 YSNSDIYLFDDPLSAVDAHVGKHIfekvvgpMGLLK------NKTRILVTHGISYLPQVDVIIVMSGGKI 846
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEV-------MELLRelnkeaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
646-845 |
9.23e-29 |
|
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: 115.26 E-value: 9.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 646 VKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAYVP 712
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltklslkelrrKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 713 QQAWIQ--NDSLRENILFGhplQENY-------YKAVMEACALLpDLEILPsgDRtEIGEkgvnLSGGQKQRVSLARAVY 783
Cdd:cd03225 82 QNPDDQffGPTVEEEVAFG---LENLglpeeeiEERVEEALELV-GLEGLR--DR-SPFT----LSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 784 SNSDIYLFDDPLSAVDAHVGKHIFEKVVGpmglLKN--KTRILVTHGISYLPQV-DVIIVMSGGK 845
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKK----LKAegKTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
606-858 |
1.51e-28 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 122.55 E-value: 1.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 606 SIVQASVSLKRLRIFLSHEELEPdsiERRSIKSGEGNsITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKS 685
Cdd:COG4618 297 QFVSARQAYRRLNELLAAVPAEP---ERMPLPRPKGR-LSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKS 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 686 SLLSALLAEMDKVEGHVTLKG-------------SVAYVPQQAWIQNDSLRENI-LFGHPLQEnyykAVMEACAL--LPD 749
Cdd:COG4618 373 TLARLLVGVWPPTAGSVRLDGadlsqwdreelgrHIGYLPQDVELFDGTIAENIaRFGDADPE----KVVAAAKLagVHE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 750 LeI--LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAhvgkhifekvVGPMGLL--------KN 819
Cdd:COG4618 449 M-IlrLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD----------EGEAALAaairalkaRG 517
|
250 260 270
....*....|....*....|....*....|....*....
gi 6678848 820 KTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDR 858
Cdd:COG4618 518 ATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1290-1501 |
1.68e-28 |
|
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: 114.49 E-value: 1.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDYCLRY---REDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLfrINESA--EGEIIIDGvniakiglhnlr 1364
Cdd:cd03250 1 ISVEDASFTWdsgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL--LGELEklSGSVSVPG------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1365 fKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRK 1444
Cdd:cd03250 67 -SIAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6678848 1445 TKILVLDEATAAVDLETDNLIqstirtqFEDC---------TVLTIAHRLNTIMDYTRVIVLDKGE 1501
Cdd:cd03250 146 ADIYLLDDPLSAVDAHVGRHI-------FENCilglllnnkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
644-863 |
2.51e-28 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 123.29 E-value: 2.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTW-ARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVA 709
Cdd:TIGR00958 479 IEFQDVSFSYpNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqydhhylhrQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 710 YVPQQAWIQNDSLRENILFG--HPLQENYYKAVMEACALLPDLEiLPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSD 787
Cdd:TIGR00958 559 LVGQEPVLFSGSVRENIAYGltDTPDEEIMAAAKAANAHDFIME-FPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPR 637
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6678848 788 IYLFDDPLSAVDAHVgkhifEKVVGPMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFA 863
Cdd:TIGR00958 638 VLILDEATSALDAEC-----EQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYK 708
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1290-1511 |
3.35e-28 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 114.20 E-value: 3.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINES-----AEGEIIIDGVNIAKIGLH--N 1362
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDvlE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1363 LRFKITIIPQDPVLFSGSLRMNLDpfsqYS------------DEEVWMALELAHLKGFVSalpDKLNhecaegGENLSVG 1430
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVA----YGlrlhgiklkeelDERVEEALRKAALWDEVK---DRLH------ALGLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1431 QRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNT---IMDYTrvIVLDKGEVRECGA 1507
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQaarVADRT--AFLLNGRLVEFGP 223
|
....
gi 6678848 1508 PSEL 1511
Cdd:cd03260 224 TEQI 227
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
646-846 |
4.05e-28 |
|
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: 113.40 E-value: 4.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 646 VKNATFTWarGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG--------SVAYVPQQAWI 717
Cdd:cd03235 2 VEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 718 QND---SLRENIL--------FGHPLQENYYKAVMEAcalLPDLEILPSGDRTeIGEkgvnLSGGQKQRVSLARAVYSNS 786
Cdd:cd03235 80 DRDfpiSVRDVVLmglyghkgLFRRLSKADKAKVDEA---LERVGLSELADRQ-IGE----LSGGQQQRVLLARALVQDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6678848 787 DIYLFDDPLSAVDAHVGKHIFEkvvgpmgLLK-----NKTRILVTHGI-SYLPQVDVIIVMSGGKI 846
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYE-------LLRelrreGMTILVVTHDLgLVLEYFDRVLLLNRTVV 210
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1290-1514 |
8.25e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 113.65 E-value: 8.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSL---TLGLFRInesAEGEIIIDGVNIAK----IG--- 1359
Cdd:COG1121 7 IELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLlkaILGLLPP---TSGTVRLFGKPPRRarrrIGyvp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1360 ---LHNLRFKITIipQDPVLfsgslrMNLDP----FSQYSDEE---VWMALELAHLKGF----VSALpdklnhecaegge 1425
Cdd:COG1121 82 qraEVDWDFPITV--RDVVL------MGRYGrrglFRRPSRADreaVDEALERVGLEDLadrpIGEL------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1426 nlSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRT-QFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVR 1503
Cdd:COG1121 141 --SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREYfDRVLLLNRGLVA 218
|
250
....*....|.
gi 6678848 1504 eCGAPSELLQQ 1514
Cdd:COG1121 219 -HGPPEEVLTP 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1306-1513 |
2.72e-27 |
|
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: 112.20 E-value: 2.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPvlfSGSL--RM 1383
Cdd:COG1124 20 VLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDP---YASLhpRH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1384 NLD-----PFS----QYSDEEVWMALELAHLKgfvSALPDKLNHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEAT 1454
Cdd:COG1124 97 TVDrilaePLRihglPDREERIAELLEQVGLP---PSFLDRYPHQ-------LSGGQRQRVAIARALILEPELLLLDEPT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 1455 AAVDL----ETDNLIQStIRTQfEDCTVLTIAHRLNTImDY--TRVIVLDKGEVRECGAPSELLQ 1513
Cdd:COG1124 167 SALDVsvqaEILNLLKD-LREE-RGLTYLFVSHDLAVV-AHlcDRVAVMQNGRIVEELTVADLLA 228
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1258-1500 |
3.33e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 118.76 E-value: 3.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1258 VERLKEYSETEKEAPwQIQETAPPSTWPHSGRVEFRDYCLRyREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLtlgl 1337
Cdd:COG4178 332 VDRLAGFEEALEAAD-ALPEAASRIETSEDGALALEDLTLR-TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTL---- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1338 FR----INESAEGEIII-DGVNIAkiglhnlrfkitIIPQDPVLFSGSLRMNL---DPFSQYSDEEVWMALELAHLkgfv 1409
Cdd:COG4178 406 LRaiagLWPYGSGRIARpAGARVL------------FLPQRPYLPLGTLREALlypATAEAFSDAELREALEAVGL---- 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1410 SALPDKLnHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRlNTIM 1489
Cdd:COG4178 470 GHLAERL-DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR-STLA 547
|
250
....*....|..
gi 6678848 1490 DY-TRVIVLDKG 1500
Cdd:COG4178 548 AFhDRVLELTGD 559
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
960-1261 |
3.40e-27 |
|
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: 114.13 E-value: 3.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 960 WN-YMKAIG-----LFITFLSIFLFLcnhVSALASNYWLSLWTDDPPVVNGTQANrnfrlSVYGALGILQGAAIFGYSMA 1033
Cdd:cd18600 3 WNtYLRYITshkslIFVLILCLVIFA---IEVAASLVGLWLLRSQADRVNTTRPE-----SSSNTYAVIVTFTSSYYVFY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1034 VSIG--------GIF-----------ASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGS 1094
Cdd:cd18600 75 IYVGvadsllamGFFrglplvhtlitVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1095 LFSVIGAVIIILLATPIAAVIIPPLGLVYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERF--- 1171
Cdd:cd18600 155 FLIVIGAITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFetl 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1172 IHQSdlkVDENQKAYYPSIVANRWLAVRLECVgncIVLF--AALFAVISRHSLSAGLVGLSVSYSLQITAYLNWLVRMSS 1249
Cdd:cd18600 235 FHKA---LNLHTANWFLYLSTLRWFQMRIEMI---FVIFftAVTFISIGTTGDGEGRVGIILTLAMNIMSTLQWAVNTSI 308
|
330
....*....|..
gi 6678848 1250 EMETNIVAVERL 1261
Cdd:cd18600 309 DVDSLMRSVSRI 320
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1306-1516 |
7.43e-27 |
|
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: 110.72 E-value: 7.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRfKITIIPQDPVLFSG-SLRMN 1384
Cdd:COG4555 16 ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARR-QIGVLPDERGLYDRlTVREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1385 LD---PFSQYSDEEVWMALE-LAHLKGfvsaLPDKLNHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1460
Cdd:COG4555 95 IRyfaELYGLFDEELKKRIEeLIELLG----LEEFLDRRVGE----LSTGMKKKVALARALVHDPKVLLLDEPTNGLDVM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6678848 1461 TDNLIQSTIRTQF-EDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELLQQRG 1516
Cdd:COG4555 167 ARRLLREILRALKkEGKTVLFSSHIMQEVEALCdRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1306-1506 |
8.61e-27 |
|
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: 108.68 E-value: 8.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQdpvlfsgSLRmnl 1385
Cdd:cd03214 14 VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ-------ALE--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1386 dpfsqysdeevwmALELAHLKgfvsalpDKLNHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDL----ET 1461
Cdd:cd03214 84 -------------LLGLAHLA-------DRPFNE-------LSGGERQRVLLARALAQEPPILLLDEPTSHLDIahqiEL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6678848 1462 DNLIQSTIRTqfEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVRECG 1506
Cdd:cd03214 137 LELLRRLARE--RGKTVVMVLHDLNLAARYaDRVILLKDGRIVAQG 180
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
638-848 |
8.83e-27 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 111.33 E-value: 8.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 638 SGEGNSITVKNA--TFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVTLKG-------- 706
Cdd:COG1116 2 SAAAPALELRGVskRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLR-LIAGLEKPtSGEVLVDGkpvtgpgp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 707 SVAYVPQQawiqnDSL------RENILFGHPLQ----ENYYKAVMEACAL--LPDLE-ILPSgdrteigekgvNLSGGQK 773
Cdd:COG1116 81 DRGVVFQE-----PALlpwltvLDNVALGLELRgvpkAERRERARELLELvgLAGFEdAYPH-----------QLSGGMR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 774 QRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVvgpMGLLK--NKTRILVTHGIS---YLpqVDVIIVMSG--GKI 846
Cdd:COG1116 145 QRVAIARALANDPEVLLMDEPFGALDALTRERLQDEL---LRLWQetGKTVLFVTHDVDeavFL--ADRVVVLSArpGRI 219
|
..
gi 6678848 847 SE 848
Cdd:COG1116 220 VE 221
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1290-1513 |
9.15e-27 |
|
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: 110.28 E-value: 9.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLT---LGLFRineSAEGEIIIDGVNIAK---IGLHNL 1363
Cdd:cd03261 1 IELRGLTKSFGGRT--VLKGVDLDVRRGEILAIIGPSGSGKSTLLrliVGLLR---PDSGEVLIDGEDISGlseAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1364 RFKITIIPQDPVLFSG-SLRMN----LDPFSQYSDEE----VWMALELAHLKGFVSALPDklnhecaeggeNLSVGQRQL 1434
Cdd:cd03261 76 RRRMGMLFQSGALFDSlTVFENvafpLREHTRLSEEEireiVLEKLEAVGLRGAEDLYPA-----------ELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1435 VCLARALLRKTKILVLDEATAAVD----LETDNLIQSTIRTQfeDCTVLTIAHRLNTIM---DytRVIVLDKGEVRECGA 1507
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDpiasGVIDDLIRSLKKEL--GLTSIMVTHDLDTAFaiaD--RIAVLYDGKIVAEGT 220
|
....*.
gi 6678848 1508 PSELLQ 1513
Cdd:cd03261 221 PEELRA 226
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1306-1514 |
1.76e-26 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 115.91 E-value: 1.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSGSLRMNL 1385
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1386 DPFSQYSD-EEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDN- 1463
Cdd:TIGR01842 413 ARFGENADpEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQa 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6678848 1464 LIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQ 1514
Cdd:TIGR01842 493 LANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1306-1514 |
2.30e-26 |
|
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: 116.00 E-value: 2.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSL---TLGLFRineSAEGEIIIDGVNIA-----KIGLHnlrfkITIIPQDPVLF 1377
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLarlLVGVWP---PTAGSVRLDGADLSqwdreELGRH-----IGYLPQDVELF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1378 SGSLRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAV 1457
Cdd:COG4618 419 DGTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNL 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6678848 1458 DLETDNLIQSTIRTQFED-CTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQ 1514
Cdd:COG4618 499 DDEGEAALAAAIRALKARgATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
651-850 |
3.18e-26 |
|
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: 107.99 E-value: 3.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 651 FTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVTLKG-----------SVAYVPQQ-AWI 717
Cdd:cd03259 6 LSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLR-LIAGLERPdSGEILIDGrdvtgvpperrNIGMVFQDyALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 718 QNDSLRENILFG----HPLQENYYKAVMEACALLpdlEILPSGDRTeIGEkgvnLSGGQKQRVSLARAVYSNSDIYLFDD 793
Cdd:cd03259 85 PHLTVAENIAFGlklrGVPKAEIRARVRELLELV---GLEGLLNRY-PHE----LSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 794 PLSAVDAHVGKHIFEKVVgpmGLLKN--KTRILVTHGIS-YLPQVDVIIVMSGGKISEMG 850
Cdd:cd03259 157 PLSALDAKLREELREELK---ELQRElgITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1283-1501 |
6.47e-26 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 116.67 E-value: 6.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1283 TWPHSGRVEFRDYCLRY--REDLDlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII-DGVNIAKIG 1359
Cdd:PTZ00265 376 KLKDIKKIQFKNVRFHYdtRKDVE-IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDIN 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1360 LHNLRFKITIIPQDPVLFSGSLRMNL-------------------DPFSQYSDEEVWMAL------------------EL 1402
Cdd:PTZ00265 455 LKWWRSKIGVVSQDPLLFSNSIKNNIkyslyslkdlealsnyyneDGNDSQENKNKRNSCrakcagdlndmsnttdsnEL 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1403 AHLK---------------------GFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET 1461
Cdd:PTZ00265 535 IEMRknyqtikdsevvdvskkvlihDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 6678848 1462 DNLIQSTIRT--QFEDCTVLTIAHRLNTIMDYTRVIVLDKGE 1501
Cdd:PTZ00265 615 EYLVQKTINNlkGNENRITIIIAHRLSTIRYANTIFVLSNRE 656
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1306-1515 |
9.51e-26 |
|
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: 107.65 E-value: 9.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIG---LHNLRFKITIIPQDP-------- 1374
Cdd:cd03256 16 ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQIGMIFQQFnlierlsv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1375 ---VLfSGSL-RMNLDP--FSQYSDEEVWMALELAHLKGfvsaLPDKLNHECAEggenLSVGQRQLVCLARALLRKTKIL 1448
Cdd:cd03256 96 lenVL-SGRLgRRSTWRslFGLFPKEEKQRALAALERVG----LLDKAYQRADQ----LSGGQQQRVAIARALMQQPKLI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1449 VLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELLQQR 1515
Cdd:cd03256 167 LADEPVASLDPASSRQVMDLLKriNREEGITVIVSLHQVDLAREYAdRIVGLKDGRIVFDGPPAELTDEV 236
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1291-1500 |
1.48e-25 |
|
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: 106.08 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1291 EFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLT---LGLFRineSAEGEIIIDGVNIAKIglhnlRFKI 1367
Cdd:cd03235 1 EVEDLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLkaiLGLLK---PTSGSIRVFGKPLEKE-----RKRI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1368 TIIPQ----D---PVLFSGSLRMNLDP----FSQYSDEE---VWMALELAHLKGFvsalpdkLNHECAEggenLSVGQRQ 1433
Cdd:cd03235 71 GYVPQrrsiDrdfPISVRDVVLMGLYGhkglFRRLSKADkakVDEALERVGLSEL-------ADRQIGE----LSGGQQQ 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6678848 1434 LVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRT-QFEDCTVLTIAHRLNTIMDYT-RVIVLDKG 1500
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYFdRVLLLNRT 208
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1306-1512 |
1.70e-25 |
|
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: 106.51 E-value: 1.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKI---GLHNLRFKITIIPQDPVLFSgslr 1382
Cdd:cd03258 20 ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLsgkELRKARRRIGMIFQHFNLLS---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1383 mnldpfSQYSDEEVWMALELAHLKG------------FVsALPDKLNHECAeggeNLSVGQRQLVCLARALLRKTKILVL 1450
Cdd:cd03258 96 ------SRTVFENVALPLEIAGVPKaeieervlelleLV-GLEDKADAYPA----QLSGGQKQRVGIARALANNPKVLLC 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6678848 1451 DEATAAVDLE-TDNLIQ--STIRTQFeDCTVLTIAHRLNTIMDY-TRVIVLDKGEVRECGAPSELL 1512
Cdd:cd03258 165 DEATSALDPEtTQSILAllRDINREL-GLTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEEVF 229
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
644-848 |
2.67e-25 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 105.90 E-value: 2.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWARGEPPT--LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVTLKG-------------- 706
Cdd:COG1136 5 LELRNLTKSYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVLIDGqdisslserelarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 707 ---SVAYVPQQA-WIQNDSLRENILFghPLQ---ENYYKAVMEACALLPDLEIlpsGDRTE--IGEkgvnLSGGQKQRVS 777
Cdd:COG1136 84 rrrHIGFVFQFFnLLPELTALENVAL--PLLlagVSRKERRERARELLERVGL---GDRLDhrPSQ----LSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6678848 778 LARAVYSNSDIYLFDDPLSAVDAHVGKHIFEkvvgpmgLLK------NKTRILVTHGISYLPQVDVIIVMSGGKISE 848
Cdd:COG1136 155 IARALVNRPKLILADEPTGNLDSKTGEEVLE-------LLRelnrelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
643-858 |
3.32e-25 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 109.01 E-value: 3.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 643 SITVKNATFTWarGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVTLKG-----------SVAY 710
Cdd:COG3839 3 SLELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLR-MIAGLEDPtSGEILIGGrdvtdlppkdrNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 711 VPQQ-AWIQNDSLRENILFG-----HPLQEnYYKAVMEACALLpdlEILPSGDRteigeKGVNLSGGQKQRVSLARAVYS 784
Cdd:COG3839 80 VFQSyALYPHMTVYENIAFPlklrkVPKAE-IDRRVREAAELL---GLEDLLDR-----KPKQLSGGQRQRVALGRALVR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 785 NSDIYLFDDPLSAVDAHvgkhifekvvgpmglLKNKTR--------------ILVTHGisylpQV------DVIIVMSGG 844
Cdd:COG3839 151 EPKVFLLDEPLSNLDAK---------------LRVEMRaeikrlhrrlgtttIYVTHD-----QVeamtlaDRIAVMNDG 210
|
250
....*....|....
gi 6678848 845 KISEMGSYQELLDR 858
Cdd:COG3839 211 RIQQVGTPEELYDR 224
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
644-850 |
3.65e-25 |
|
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: 103.93 E-value: 3.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS------------VAYV 711
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdlekalsslISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 712 PQQAWIQNDSLRENIlfghplqenyykavmeacallpdleilpsgdrteigekGVNLSGGQKQRVSLARAVYSNSDIYLF 791
Cdd:cd03247 81 NQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6678848 792 DDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMG 850
Cdd:cd03247 123 DEPTVGLDPITERQLLSLI---FEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1290-1502 |
3.74e-25 |
|
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: 105.26 E-value: 3.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDYCLRYREDLD--LVLKHINVTIEGGEKVGIVGRTGAGKSSL--TLGLfrINESAEGEIIIDGVNIAKIGLHNL-- 1363
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLlnILGG--LDRPTSGEVRVDGTDISKLSEKELaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1364 --RFKITIIPQDPvlfsgslrmNLDP-FSQYsdEEVWMALELAHLKGFVSA-----------LPDKLNHECAEggenLSV 1429
Cdd:cd03255 79 frRRHIGFVFQSF---------NLLPdLTAL--ENVELPLLLAGVPKKERReraeellervgLGDRLNHYPSE----LSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 1430 GQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEV 1502
Cdd:cd03255 144 GQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRelNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
644-893 |
3.90e-25 |
|
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: 111.53 E-value: 3.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSA---LLAEMDKVEGHVTLKG-------------S 707
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALAlmgLLPHGGRISGEVLLDGrdllelsealrgrR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 708 VAYVPQQAWIQNDSLR--ENILFGhPLQENYYKAVMEACAllpdLEILPSGDRTEIGEKGVN-LSGGQKQRVSLARAVYS 784
Cdd:COG1123 85 IGMVFQDPMTQLNPVTvgDQIAEA-LENLGLSRAEARARV----LELLEAVGLERRLDRYPHqLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 785 NSDIYLFDDPLSAVDAHVGKHIFEkvvgpmgLLK------NKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLD 857
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILD-------LLRelqrerGTTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEEILA 232
|
250 260 270
....*....|....*....|....*....|....*.
gi 6678848 858 RDGAFAeflrtyanAEQDLASEDDSVSGSGKESKPV 893
Cdd:COG1123 233 APQALA--------AVPRLGAARGRAAPAAAAAEPL 260
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
644-864 |
6.96e-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: 104.72 E-value: 6.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWaRGEPPTLNGITFSIPEGALVAVVGQVGCGKSSL---LSALLAEMdkvEGHVTLKG-------------S 707
Cdd:COG1122 1 IELENLSFSY-PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLlrlLNGLLKPT---SGEVLVDGkditkknlrelrrK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 708 VAYVPQQAWIQ--NDSLRENILFGhPLQ-----ENYYKAVMEACALLpDLEilpsgdrtEIGEKGV-NLSGGQKQRVSLA 779
Cdd:COG1122 77 VGLVFQNPDDQlfAPTVEEDVAFG-PENlglprEEIRERVEEALELV-GLE--------HLADRPPhELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 780 RAVYSNSDIYLFDDPLSAVDAHVGKHIFEkvvgpmgLLK-----NKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQ 853
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLE-------LLKrlnkeGKTVIIVTHDLDLVAELaDRVIVLDDGRIVADGTPR 219
|
250
....*....|.
gi 6678848 854 ELLDRDGAFAE 864
Cdd:COG1122 220 EVFSDYELLEE 230
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
644-846 |
8.42e-25 |
|
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: 104.09 E-value: 8.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWARGEPPT--LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVTLKG--------SVAYVP 712
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtaLEDISLSVEEGEFVALVGPSGCGKSTLLR-IIAGLERPtSGEVLVDGepvtgpgpDRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 713 QQA----WIqndSLRENILFGhplqenyykavmeacallpdLEI--LPSGDRTEIGEKGVN--------------LSGGQ 772
Cdd:cd03293 80 QQDallpWL---TVLDNVALG--------------------LELqgVPKAEARERAEELLElvglsgfenayphqLSGGM 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 773 KQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKvvgpmgLLK-----NKTRILVTHGIS---YLPqvDVIIVMSG- 843
Cdd:cd03293 137 RQRVALARALAVDPDVLLLDEPFSALDALTREQLQEE------LLDiwretGKTVLLVTHDIDeavFLA--DRVVVLSAr 208
|
....
gi 6678848 844 -GKI 846
Cdd:cd03293 209 pGRI 212
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
645-845 |
1.07e-24 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 101.94 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 645 TVKNATFTWarGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTlkgsvayvpqqawiqndslre 724
Cdd:cd00267 1 EIENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL--------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 725 niLFGHPLQENYYKAVMEACALLPDleilpsgdrteigekgvnLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHvGK 804
Cdd:cd00267 58 --IDGKDIAKLPLEELRRRIGYVPQ------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA-SR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6678848 805 HIFEKVVGPMgLLKNKTRILVTHGISYLPQV-DVIIVMSGGK 845
Cdd:cd00267 117 ERLLELLREL-AEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
647-846 |
1.86e-24 |
|
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: 103.32 E-value: 1.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 647 KNATFTW-ARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS-------------VAYVP 712
Cdd:cd03248 15 QNVTFAYpTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkylhskVSLVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 713 QQAWIQNDSLRENILFGhpLQENYYKAVMEACALL---PDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIY 789
Cdd:cd03248 95 QEPVLFARSLQDNIAYG--LQSCSFECVKEAAQKAhahSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6678848 790 LFDDPLSAVDAHvGKHIFEKVVgpMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKI 846
Cdd:cd03248 173 ILDEATSALDAE-SEQQVQQAL--YDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
644-859 |
2.18e-24 |
|
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: 103.97 E-value: 2.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFtwARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAY 710
Cdd:COG1120 2 LEAENLSV--GYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelarRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 711 VPQQAwIQNDSL--RENILFG-HPLQENY-------YKAVMEACALLpdlEILPSGDRTeIGEkgvnLSGGQKQRVSLAR 780
Cdd:COG1120 80 VPQEP-PAPFGLtvRELVALGrYPHLGLFgrpsaedREAVEEALERT---GLEHLADRP-VDE----LSGGERQRVLIAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 781 AVYSNSDIYLFDDPLSAVDAHvgkHIFEkVvgpMGLLK------NKTRILVTHgisYLPQV----DVIIVMSGGKISEMG 850
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLA---HQLE-V---LELLRrlarerGRTVVMVLH---DLNLAaryaDRLVLLKDGRIVAQG 220
|
....*....
gi 6678848 851 SYQELLDRD 859
Cdd:COG1120 221 PPEEVLTPE 229
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1306-1502 |
2.86e-24 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 100.94 E-value: 2.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLT---LGLFRINEsaeGEIIIDGVNIAKIGlHNLRFKITIIPQDPVLFSgslr 1382
Cdd:cd03230 15 ALDDISLTVEKGEIYGLLGPNGAGKTTLIkiiLGLLKPDS---GEIKVLGKDIKKEP-EEVKRRIGYLPEEPSLYE---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1383 mnldpfsqysdeevwmalelaHLKGFvsalpdklnhecaeggENL--SVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1460
Cdd:cd03230 87 ---------------------NLTVR----------------ENLklSGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6678848 1461 TDNLIQSTIRT-QFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEV 1502
Cdd:cd03230 130 SRREFWELLRElKKEGKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1306-1501 |
6.67e-24 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 100.34 E-value: 6.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHN--LRFKITIIPQDPVLFSG-SLR 1382
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIGMVFQDFALFPHlTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1383 MNLdpfsqysdeevwmalelahlkgfvsALPdklnhecaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD 1462
Cdd:cd03229 95 ENI-------------------------ALG-------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITR 136
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6678848 1463 NLIQSTIRTQFED--CTVLTIAHRLNTIMDYT-RVIVLDKGE 1501
Cdd:cd03229 137 REVRALLKSLQAQlgITVVLVTHDLDEAARLAdRVVVLRDGK 178
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
634-890 |
7.22e-24 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 108.27 E-value: 7.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 634 RSIKSGegnSITVKNATFTWaRGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG------- 706
Cdd:PRK10790 334 RPLQSG---RIDIDNVSFAY-RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplssls 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 707 ------SVAYVPQQAWIQNDSLRENILFGHPLQENYYKAVMEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLAR 780
Cdd:PRK10790 410 hsvlrqGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALAR 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 781 AVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVgpmGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDG 860
Cdd:PRK10790 490 VLVQTPQILILDEATANIDSGTEQAIQQALA---AVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQG 566
|
250 260 270
....*....|....*....|....*....|
gi 6678848 861 afaeflRTYANAEQDLASEDDSVSGSGKES 890
Cdd:PRK10790 567 ------RYWQMYQLQLAGEELAASVREEES 590
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
645-846 |
1.02e-23 |
|
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: 99.82 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 645 TVKNATFtwARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS-------------VAYV 711
Cdd:cd03214 1 EVENLSV--GYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKdlaslspkelarkIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 712 PQqawiqndslrenilfghplqenyykaVMEACALlpdleilpsgdrTEIGEKGVN-LSGGQKQRVSLARAVYSNSDIYL 790
Cdd:cd03214 79 PQ--------------------------ALELLGL------------AHLADRPFNeLSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6678848 791 FDDPLSAVDAHVGKHIFEKVVGpMGLLKNKTRILVTHGISYLPQV-DVIIVMSGGKI 846
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRR-LARERGKTVVMVLHDLNLAARYaDRVILLKDGRI 176
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
644-860 |
1.13e-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: 101.47 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWarGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG------------SVAYV 711
Cdd:COG4555 2 IEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearrQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 712 PQQAWI-QNDSLRENILFGHPLQENYYKAVMEACA-LLPDLEILPSGDRteigeKGVNLSGGQKQRVSLARAVYSNSDIY 789
Cdd:COG4555 80 PDERGLyDRLTVRENIRYFAELYGLFDEELKKRIEeLIELLGLEEFLDR-----RVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6678848 790 LFDDPLSAVDAhVGKHIFEKVvgpMGLLKN--KTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLDRDG 860
Cdd:COG4555 155 LLDEPTNGLDV-MARRLLREI---LRALKKegKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
644-858 |
1.18e-23 |
|
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: 101.80 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKN--ATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS-------------V 708
Cdd:COG1124 2 LEVRNlsVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRpvtrrrrkafrrrV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 709 AYVPQQA-------WIQNDSLREnilfghPLQENYYKAVME-ACALLPDLEiLPSGDRTEIGEKgvnLSGGQKQRVSLAR 780
Cdd:COG1124 82 QMVFQDPyaslhprHTVDRILAE------PLRIHGLPDREErIAELLEQVG-LPPSFLDRYPHQ---LSGGQRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 781 AVYSNSDIYLFDDPLSAVDAHVGKHIfekvvgpMGLLK------NKTRILVTHG---ISYLpqVDVIIVMSGGKISEMGS 851
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQAEI-------LNLLKdlreerGLTYLFVSHDlavVAHL--CDRVAVMQNGRIVEELT 222
|
....*..
gi 6678848 852 YQELLDR 858
Cdd:COG1124 223 VADLLAG 229
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
643-858 |
1.20e-23 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 104.07 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 643 SITVKNATFTWarGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMDkvEGHVTLKGSVAYV---PQQAWI 717
Cdd:COG1118 2 SIEVRNISKRF--GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIagLETPD--SGRIVLNGRDLFTnlpPRERRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 718 ----QNDSL------RENILFGhplqenyykavmeacallpdLEILPSgDRTEIGEKgV------------------NLS 769
Cdd:COG1118 78 gfvfQHYALfphmtvAENIAFG--------------------LRVRPP-SKAEIRAR-VeellelvqlegladrypsQLS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 770 GGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIfEKVVgpMGLLK--NKTRILVTH------GISylpqvDVIIVM 841
Cdd:COG1118 136 GGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKEL-RRWL--RRLHDelGGTTVFVTHdqeealELA-----DRVVVM 207
|
250
....*....|....*..
gi 6678848 842 SGGKISEMGSYQELLDR 858
Cdd:COG1118 208 NQGRIEQVGTPDEVYDR 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
651-827 |
2.43e-23 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 99.51 E-value: 2.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 651 FTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAYVPQQAWI 717
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplsampppewrrQVAYVPQEPAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 718 QNDSLRENILFghPLQENYYKAVME-ACALLPDLEiLPsgdrTEIGEKGV-NLSGGQKQRVSLARAVYSNSDIYLFDDPL 795
Cdd:COG4619 86 WGGTVRDNLPF--PFQLRERKFDRErALELLERLG-LP----PDILDKPVeRLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190
....*....|....*....|....*....|..
gi 6678848 796 SAVDAHvGKHIFEKVVGPMGLLKNKTRILVTH 827
Cdd:COG4619 159 SALDPE-NTRRVEELLREYLAEEGRAVLWVSH 189
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1290-1506 |
2.85e-23 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 99.52 E-value: 2.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLtL----GLFRInesAEGEIIIDGVNIAKIGLHnlRF 1365
Cdd:cd03259 1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTL-LrliaGLERP---DSGEILIDGRDVTGVPPE--RR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1366 KITIIPQDPVLF----------SGsLRMNLDPFSQySDEEVWMALELAHLKGFVSALPDKLnhecaeggenlSVGQRQLV 1435
Cdd:cd03259 73 NIGMVFQDYALFphltvaeniaFG-LKLRGVPKAE-IRARVRELLELVGLEGLLNRYPHEL-----------SGGQQQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6678848 1436 CLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFE--DCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECG 1506
Cdd:cd03259 140 ALARALAREPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEEALALAdRIAVMNEGRIVQVG 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1290-1510 |
3.49e-23 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 99.74 E-value: 3.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDYCLRYREDLDlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKI---GLHNLRFK 1366
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1367 ITIIPQDP-----------VLFsgSLR-MNLDPfsQYSDEEVWMALELAHLKGFVSALPdklnHEcaeggenLSVGQRQL 1434
Cdd:COG2884 81 IGVVFQDFrllpdrtvyenVAL--PLRvTGKSR--KEIRRRVREVLDLVGLSDKAKALP----HE-------LSGGEQQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1435 VCLARALLRKTKILVLDEATAAVDLET-DNLIQstirtQFED-----CTVLtIA-HRLNTIMDY-TRVIVLDKGEVRECG 1506
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPETsWEIME-----LLEEinrrgTTVL-IAtHDLELVDRMpKRVLELEDGRLVRDE 219
|
....
gi 6678848 1507 APSE 1510
Cdd:COG2884 220 ARGV 223
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1290-1524 |
5.65e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 100.45 E-value: 5.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITI 1369
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1370 IPQDP-VLFSGSLRMNLDPFS----QYSDEEVW-MALELAHLKGfvsaLPDKLNHEcaegGENLSVGQRQLVCLARALLR 1443
Cdd:PRK13632 88 IFQNPdNQFIGATVEDDIAFGlenkKVPPKKMKdIIDDLAKKVG----MEDYLDKE----PQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1444 KTKILVLDEATAAVDLETDNLIQSTIRT--QFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIFYSM 1521
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKEILEKA 239
|
...
gi 6678848 1522 AKD 1524
Cdd:PRK13632 240 KID 242
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
644-850 |
8.04e-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: 98.73 E-value: 8.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKN--ATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG--------------- 706
Cdd:cd03257 2 LEVKNlsVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 707 -SVAYVPQQAW--------IQnDSLRENILF---GHPLQENYYKAVMEACALLPDLEILpsgDR--TEigekgvnLSGGQ 772
Cdd:cd03257 82 kEIQMVFQDPMsslnprmtIG-EQIAEPLRIhgkLSKKEARKEAVLLLLVGVGLPEEVL---NRypHE-------LSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 773 KQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIfekvvgpMGLLK------NKTRILVTHGISYLPQV-DVIIVMSGGK 845
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQI-------LDLLKklqeelGLTLLFITHDLGVVAKIaDRVAVMYAGK 223
|
....*
gi 6678848 846 ISEMG 850
Cdd:cd03257 224 IVEEG 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
643-858 |
1.97e-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: 100.56 E-value: 1.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 643 SITVKNATFTWarGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVTLKG-----------SVAY 710
Cdd:COG3842 5 ALELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLR-MIAGFETPdSGRILLDGrdvtglppekrNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 711 VPQqawiqNDSL------RENILFGhpL-QENYYKA-----VMEACAL--LPDLEilpsgDRtEIGEkgvnLSGGQKQRV 776
Cdd:COG3842 82 VFQ-----DYALfphltvAENVAFG--LrMRGVPKAeirarVAELLELvgLEGLA-----DR-YPHQ----LSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 777 SLARAVYSNSDIYLFDDPLSAVDAHVG-------KHIFEKVvgpmgllkNKTRILVTH------GISylpqvDVIIVMSG 843
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLReemreelRRLQREL--------GITFIYVTHdqeealALA-----DRIAVMND 211
|
250
....*....|....*
gi 6678848 844 GKISEMGSYQELLDR 858
Cdd:COG3842 212 GRIEQVGTPEEIYER 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1307-1514 |
2.84e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 98.97 E-value: 2.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1307 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIA--KIGLHNLRFKITIIPQDP--VLFS---- 1378
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQYPeyQLFEetie 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1379 -----GSLRMNLdpfsqySDEEVWM----ALELAHLKgfVSALPDKLNHEcaeggenLSVGQRQLVCLARALLRKTKILV 1449
Cdd:PRK13637 103 kdiafGPINLGL------SEEEIENrvkrAMNIVGLD--YEDYKDKSPFE-------LSGGQKRRVAIAGVVAMEPKILI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6678848 1450 LDEATAAVDLETDNLIQSTIRTQFE--DCTVLTIAHRLNTIMDY-TRVIVLDKGEVRECGAPSELLQQ 1514
Cdd:PRK13637 168 LDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKLaDRIIVMNKGKCELQGTPREVFKE 235
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
644-855 |
3.04e-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: 96.87 E-value: 3.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFtwARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL-----LAEMDKVEGHVTLKGS----------- 707
Cdd:cd03260 1 IELRDLNV--YYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKdiydldvdvle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 708 ----VAYVPQQAWIQNDSLRENILFGHPLQ----ENYYKAVMEAC---ALLPDLEilpsGDRTeigeKGVNLSGGQKQRV 776
Cdd:cd03260 79 lrrrVGMVFQKPNPFPGSIYDNVAYGLRLHgiklKEELDERVEEAlrkAALWDEV----KDRL----HALGLSGGQQQRL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 777 SLARAVYSNSDIYLFDDPLSAVDAhVGKHIFEKVVgpMGLLKNKTRILVTHGisyLPQV----DVIIVMSGGKISEMGSY 852
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDP-ISTAKIEELI--AELKKEYTIVIVTHN---MQQAarvaDRTAFLLNGRLVEFGPT 224
|
...
gi 6678848 853 QEL 855
Cdd:cd03260 225 EQI 227
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
643-851 |
3.36e-22 |
|
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: 96.33 E-value: 3.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 643 SITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVA 709
Cdd:cd03369 6 EIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 710 YVPQQAWIQNDSLRENI-LFGHPLQENYYKAVmeacallpdleilpsgdrtEIGEKGVNLSGGQKQRVSLARAVYSNSDI 788
Cdd:cd03369 86 IIPQDPTLFSGTIRSNLdPFDEYSDEEIYGAL-------------------RVSEGGLNLSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6678848 789 YLFDDPLSAVDAHVgKHIFEKVVgpMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGS 851
Cdd:cd03369 147 LVLDEATASIDYAT-DALIQKTI--REEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1290-1515 |
4.90e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 98.00 E-value: 4.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDYCLRYrEDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--VNIAKIGLHNLRFKI 1367
Cdd:PRK13636 6 LKVEELNYNY-SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1368 TIIPQDP--VLFSGSLR-------MNLdpfsQYSDEEVWMALELAHLKGFVSALPDKLNHEcaeggenLSVGQRQLVCLA 1438
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYqdvsfgaVNL----KLPEDEVRKRVDNALKRTGIEHLKDKPTHC-------LSFGQKKRVAIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1439 RALLRKTKILVLDEATAAVD-LETDNLIQSTIRTQFE-DCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELLQQR 1515
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDpMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCdNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
661-858 |
1.22e-21 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 95.52 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG------------SVAYVPQQAWIQND-SLRENI- 726
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGYVPQEPALYPDlTVRENLr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 727 ----LFGHPLQENYyKAVMEACALLpdlEILPSGDRteigeKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHV 802
Cdd:COG1131 96 ffarLYGLPRKEAR-ERIDELLELF---GLTDAADR-----KVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 803 GKHIFEkvvgpmgLLK-----NKTRILVTHgisYLPQV----DVIIVMSGGKISEMGSYQELLDR 858
Cdd:COG1131 167 RRELWE-------LLRelaaeGKTVLLSTH---YLEEAerlcDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1290-1483 |
1.27e-21 |
|
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: 94.85 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDYCLRYREDLD--LVLKHINVTIEGGEKVGIVGRTGAGKSSL---TLGLFRInesAEGEIIIDGVNIAKIGLHnlr 1364
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLlriIAGLERP---TSGEVLVDGEPVTGPGPD--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1365 fkITIIPQDPVLF---------SGSLRMNLDPFSQySDEEVWMALELAHLKGFVSALPdklnHEcaeggenLSVGQRQLV 1435
Cdd:cd03293 75 --RGYVFQQDALLpwltvldnvALGLELQGVPKAE-ARERAEELLELVGLSGFENAYP----HQ-------LSGGMRQRV 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6678848 1436 CLARALLRKTKILVLDEATAAVDLETDNLIQSTI-----RTQFedcTVLTIAH 1483
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDALTREQLQEELldiwrETGK---TVLLVTH 190
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1307-1515 |
1.53e-21 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 95.21 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1307 LKHINVTIEGGEKVGIVGRTGAGKSSLtLGL---FRinESAEGEIIIDGVNIAKIGLHNlRfKITIIPQDPVLFSG-SLR 1382
Cdd:COG3840 15 PLRFDLTIAAGERVAILGPSGAGKSTL-LNLiagFL--PPDSGRILWNGQDLTALPPAE-R-PVSMLFQENNLFPHlTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1383 MN----LDPFSQYSDEE---VWMALELAHLKGFVSALPdklnhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATA 1455
Cdd:COG3840 90 QNiglgLRPGLKLTAEQraqVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVALARCLVRKRPILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 1456 AVD----LETDNLIQSTIRTQfeDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELLQQR 1515
Cdd:COG3840 159 ALDpalrQEMLDLVDELCRER--GLTVLMVTHDPEDAARIAdRVLLVADGRIAADGPTAALLDGE 221
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
338-617 |
1.75e-21 |
|
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: 96.47 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 338 LMMFAGPKILELIINFVndREAPDWQGYFYTALLFVSAC-LQTLALHQYFHICFVSGMRIKTAVVGAVYRKALLITNAAR 416
Cdd:cd07346 13 ALGLALPLLTKLLIDDV--IPAGDLSLLLWIALLLLLLAlLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 417 KSSTVGEIVNLMSVDAQRFMDLATY-INMIWSAPLQVILALYFLwLSLGPSV-LAGVAVMILMVPLNAVMAMKTKTYQVA 494
Cdd:cd07346 91 DRNRTGDLMSRLTSDVDAVQNLVSSgLLQLLSDVLTLIGALVIL-FYLNWKLtLVALLLLPLYVLILRYFRRRIRKASRE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 495 HMKSKDNRIKLMNEILNGIKVLKLYAWELAFQDKVMSIRQEELKVLKKSAYLAAvgtFTWVCTPFLVALSTFAVFV---- 570
Cdd:cd07346 170 VRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSA---LFSPLIGLLTALGTALVLLyggy 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 6678848 571 -TVDERniLDAKKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRL 617
Cdd:cd07346 247 lVLQGS--LTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
644-858 |
2.04e-21 |
|
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: 99.98 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTW---ARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------- 706
Cdd:COG1123 261 LEVRNLSKRYpvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGkdltklsrrslrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 707 --SVAYVPQQAwiqNDSL------RENILFGHPLQENYYKA--------VMEACALLPD-LEILPSGdrteigekgvnLS 769
Cdd:COG1123 341 rrRVQMVFQDP---YSSLnprmtvGDIIAEPLRLHGLLSRAerrervaeLLERVGLPPDlADRYPHE-----------LS 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 770 GGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIfekvvgpMGLLK------NKTRILVTHGISYLPQV-DVIIVMS 842
Cdd:COG1123 407 GGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQI-------LNLLRdlqrelGLTYLFISHDLAVVRYIaDRVAVMY 479
|
250
....*....|....*.
gi 6678848 843 GGKISEMGSYQELLDR 858
Cdd:COG1123 480 DGRIVEDGPTEEVFAN 495
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1290-1502 |
3.00e-21 |
|
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: 93.63 E-value: 3.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDYCLRYREDLdLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKI---GLHNLRFK 1366
Cdd:cd03292 1 IEFINVTKTYPNGT-AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1367 ITIIPQDPVLFSG---------SLRMNLDPfSQYSDEEVWMALELAHLKGFVSALPdklnhecaeggENLSVGQRQLVCL 1437
Cdd:cd03292 80 IGVVFQDFRLLPDrnvyenvafALEVTGVP-PREIRKRVPAALELVGLSHKHRALP-----------AELSGGEQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6678848 1438 ARALLRKTKILVLDEATAAVDLETDNLIqSTIRTQFED--CTVLTIAHRLNTIMDYT-RVIVLDKGEV 1502
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEI-MNLLKKINKagTTVVVATHAKELVDTTRhRVIALERGKL 214
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
644-859 |
3.51e-21 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 94.11 E-value: 3.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFtwARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS---------------- 707
Cdd:cd03261 1 IELRGLTK--SFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisglseaelyrlrrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 708 VAYVPQQAWIQND-SLRENILFghPLQENY----------YKAVMEACALLPDLEILPSgdrteigekgvNLSGGQKQRV 776
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVAF--PLREHTrlseeeireiVLEKLEAVGLRGAEDLYPA-----------ELSGGMKKRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 777 SLARAVYSNSDIYLFDDPLSAVDAhVGKHIFEKVVGPMGLLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQEL 855
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLDP-IASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPEEL 224
|
....
gi 6678848 856 LDRD 859
Cdd:cd03261 225 RASD 228
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1289-1514 |
3.61e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 95.47 E-value: 3.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1289 RVEFRDYclRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLT---LGLFRineSAEGEIIIDGVNIAKIGLHNLRF 1365
Cdd:PRK13635 7 RVEHISF--RYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAkllNGLLL---PEAGTITVGGMVLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1366 KITIIPQDP------------VLFSgsLRMNLDPFSQYSdEEVWMALELAHLKGFvsalpdkLNHECAeggeNLSVGQRQ 1433
Cdd:PRK13635 82 QVGMVFQNPdnqfvgatvqddVAFG--LENIGVPREEMV-ERVDQALRQVGMEDF-------LNREPH----RLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1434 LVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRT--QFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSEL 1511
Cdd:PRK13635 148 RVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
...
gi 6678848 1512 LQQ 1514
Cdd:PRK13635 228 FKS 230
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
643-857 |
5.40e-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: 93.94 E-value: 5.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 643 SITVKNATFTWarGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVTLKG-----------SVAY 710
Cdd:cd03296 2 SIEVRNVSKRF--GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLR-LIAGLERPdSGTILFGGedatdvpvqerNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 711 VPQQ-AWIQNDSLRENILFG---HPLQENYYKAVMEA--CALLPDLEILPSGDRTEigekgVNLSGGQKQRVSLARAVYS 784
Cdd:cd03296 79 VFQHyALFRHMTVFDNVAFGlrvKPRSERPPEAEIRAkvHELLKLVQLDWLADRYP-----AQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6678848 785 NSDIYLFDDPLSAVDAHVGKHI---FEKVVGPMGLlknkTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLD 857
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELrrwLRRLHDELHV----TTVFVTHDQEEALEVaDRVVVMNKGRIEQVGTPDEVYD 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
645-846 |
7.97e-21 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 92.32 E-value: 7.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 645 TVKNATFTWARGePPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG----------SVAYVPQQ 714
Cdd:cd03226 1 RIENISFSYKKG-TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpikakerrkSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 715 AWIQ--NDSLRENILFGHPlqeNYYKAVMEACALLPDLEILPSGDRTEIgekgvNLSGGQKQRVSLARAVYSNSDIYLFD 792
Cdd:cd03226 80 VDYQlfTDSVREELLLGLK---ELDAGNEQAETVLKDLDLYALKERHPL-----SLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6678848 793 DPLSAVDAH----VGKhIFEKVVGpmgllKNKTRILVTHGISYLPQV-DVIIVMSGGKI 846
Cdd:cd03226 152 EPTSGLDYKnmerVGE-LIRELAA-----QGKAVIVITHDYEFLAKVcDRVLLLANGAI 204
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
313-848 |
1.30e-20 |
|
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: 97.95 E-value: 1.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 313 SLFKVLYKTFGPYFLMSFLYKALHDLMMfAGpkilelIINFVND---REAPDWQGYFytaLLFVSACLQTLALHqyfhic 389
Cdd:COG4615 2 NLLRLLLRESRWLLLLALLLGLLSGLAN-AG------LIALINQalnATGAALARLL---LLFAGLLVLLLLSR------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 390 FVSGMRIKTAVVGAVY--RKALL--ITNA----------ARKSSTVGEIVNLMSVDAQRFMDLATYINMIwsaplqVILA 455
Cdd:COG4615 66 LASQLLLTRLGQHAVArlRLRLSrrILAAplerlerigaARLLAALTEDVRTISQAFVRLPELLQSVALV------LGCL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 456 LYFLWLSLgPSVLAGVAVMILMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKL-YAWELAFQDKVMSIRQ 534
Cdd:COG4615 140 AYLAWLSP-PLFLLTLVLLGLGVAGYRLLVRRARRHLRRAREAEDRLFKHFRALLEGFKELKLnRRRRRAFFDEDLQPTA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 535 EELKVLKKSAYLAAVGTFTWVCTPFLVAL-STFAVFVTVDERNILDAKKaFVSLALFniLRFPLNILPMVISSIVQASVS 613
Cdd:COG4615 219 ERYRDLRIRADTIFALANNWGNLLFFALIgLILFLLPALGWADPAVLSG-FVLVLLF--LRGPLSQLVGALPTLSRANVA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 614 LKRL-RIFLSHEELEPDSIERRSIKSGEG-NSITVKNATFTWAR--GEPP-TLNGITFSIPEGALVAVVGQVGCGKSSLL 688
Cdd:COG4615 296 LRKIeELELALAAAEPAAADAAAPPAPADfQTLELRGVTYRYPGedGDEGfTLGPIDLTIRRGELVFIVGGNGSGKSTLA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 689 SALLAEMDKVEGHVTLKGSVayVPQQAWiqnDSLRENI--------LFGHPLQENYYKAVMEACALLPDLEIlpsGDRTE 760
Cdd:COG4615 376 KLLTGLYRPESGEILLDGQP--VTADNR---EAYRQLFsavfsdfhLFDRLLGLDGEADPARARELLERLEL---DHKVS 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 761 IgEKG----VNLSGGQKQRVSLARAVYSNSDIYLFD------DPlsavdahVGKHIFEKVVGPMglLK--NKTRILVTHG 828
Cdd:COG4615 448 V-EDGrfstTDLSQGQRKRLALLVALLEDRPILVFDewaadqDP-------EFRRVFYTELLPE--LKarGKTVIAISHD 517
|
570 580
....*....|....*....|
gi 6678848 829 ISYLPQVDVIIVMSGGKISE 848
Cdd:COG4615 518 DRYFDLADRVLKMDYGKLVE 537
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1306-1502 |
1.38e-20 |
|
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: 90.18 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--VNIAKIGlHNLRFKITIIPQdpvlfsgslrm 1383
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGkeVSFASPR-DARRAGIAMVYQ----------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1384 nldpfsqysdeevwmalelahlkgfvsalpdklnhecaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDL-ETD 1462
Cdd:cd03216 83 -------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPaEVE 119
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6678848 1463 NLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEV 1502
Cdd:cd03216 120 RLFKVIRRLRAQGVAVIFISHRLDEVFEIAdRVTVLRDGRV 160
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
644-856 |
3.10e-20 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 91.59 E-value: 3.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWaRGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL-----------------LAEMDKVEghvtLKG 706
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMInrlieptsgeifidgedIREQDPVE----LRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 707 SVAYVPQQAWI-QNDSLRENI-----LFGHPlQENYYKAVMEACALLpDLEILPSGDRTEiGEkgvnLSGGQKQRVSLAR 780
Cdd:cd03295 76 KIGYVIQQIGLfPHMTVEENIalvpkLLKWP-KEKIRERADELLALV-GLDPAEFADRYP-HE----LSGGQQQRVGVAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6678848 781 AVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVGPMGLLkNKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQELL 856
Cdd:cd03295 149 ALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQEL-GKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1306-1514 |
4.64e-20 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 93.22 E-value: 4.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSltlgLFR-IN--ESA-EGEIIIDGVNIAKI---GLHNLRFKITIIPQDpvlFs 1378
Cdd:COG1135 20 ALDDVSLTIEKGEIFGIIGYSGAGKST----LIRcINllERPtSGSVLVDGVDLTALserELRAARRKIGMIFQH---F- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1379 gslrmNLdpFSQYSDEE-VWMALELAHLKG------------FVSaLPDKLNHECAEggenLSVGQRQLVCLARALLRKT 1445
Cdd:COG1135 92 -----NL--LSSRTVAEnVALPLEIAGVPKaeirkrvaelleLVG-LSDKADAYPSQ----LSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6678848 1446 KILVLDEATAAVDLETD----NLIQStIRTQFeDCTVLTIAHRLN---TIMDytRVIVLDKGEVRECGAPSELLQQ 1514
Cdd:COG1135 160 KVLLCDEATSALDPETTrsilDLLKD-INREL-GLTIVLITHEMDvvrRICD--RVAVLENGRIVEQGPVLDVFAN 231
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
644-845 |
5.90e-20 |
|
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: 88.78 E-value: 5.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTwaRGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG---------------SV 708
Cdd:cd03229 1 LELKNVSKR--YGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltdledelpplrrRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 709 AYVPQQ-AWIQNDSLRENILFGhplqenyykavmeacallpdleilpsgdrteigekgvnLSGGQKQRVSLARAVYSNSD 787
Cdd:cd03229 79 GMVFQDfALFPHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6678848 788 IYLFDDPLSAVDAHVGKHI---FEKVVGPMGllknKTRILVTHGISYLPQV-DVIIVMSGGK 845
Cdd:cd03229 121 VLLLDEPTSALDPITRREVralLKSLQAQLG----ITVVLVTHDLDEAARLaDRVVVLRDGK 178
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1306-1513 |
1.25e-19 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 89.42 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHN-LRFKITIIPQDPVLFSG----- 1379
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPEltvee 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1380 SLRMNLDPFSQYSDEEVW-MALELahlkgFvSALPDKLNHEcaegGENLSVGQRQLVCLARALLRKTKILVLDEATAAvd 1458
Cdd:cd03224 95 NLLLGAYARRRAKRKARLeRVYEL-----F-PRLKERRKQL----AGTLSGGEQQMLAIARALMSRPKLLLLDEPSEG-- 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 1459 letdnlIQSTIRTQFEDC---------TVLTIAHRLNTIMDY-TRVIVLDKGEVRECGAPSELLQ 1513
Cdd:cd03224 163 ------LAPKIVEEIFEAirelrdegvTILLVEQNARFALEIaDRAYVLERGRVVLEGTAAELLA 221
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1290-1511 |
1.44e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 90.58 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITI 1369
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1370 IPQDPV-LFSGSL-----RMNLDPFSQYSDEevwMALELAHLKGFVSALpDKLNHEcaegGENLSVGQRQLVCLARALLR 1443
Cdd:PRK13648 88 VFQNPDnQFVGSIvkydvAFGLENHAVPYDE---MHRRVSEALKQVDML-ERADYE----PNALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1444 KTKILVLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSEL 1511
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRkvKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1307-1514 |
1.70e-19 |
|
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: 93.98 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1307 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESaEGEIIIDGVNIAKIG---LHNLRFKITIIPQDPvlFsGSL-- 1381
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--F-GSLsp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1382 RMN-----------LDPfsQYSDEE----VWMALELAHLKgfvsalPDKLN---HEcaeggenLSVGQRQLVCLARALLR 1443
Cdd:COG4172 378 RMTvgqiiaeglrvHGP--GLSAAErrarVAEALEEVGLD------PAARHrypHE-------FSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1444 KTKILVLDEATAAVDLetdnliqsTIRTQfedctVLT---------------IAHRLN---TIMDytRVIVLDKGEVREC 1505
Cdd:COG4172 443 EPKLLVLDEPTSALDV--------SVQAQ-----ILDllrdlqrehglaylfISHDLAvvrALAH--RVMVMKDGKVVEQ 507
|
....*....
gi 6678848 1506 GAPSELLQQ 1514
Cdd:COG4172 508 GPTEQVFDA 516
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
644-846 |
2.13e-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: 87.07 E-value: 2.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTwaRGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLkgsvayvpqqawiqndslr 723
Cdd:cd03230 1 IEVRNLSKR--YGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 724 enilFGHPLQENYyKAVMEACALLPDLEILPsGDRTeiGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVG 803
Cdd:cd03230 60 ----LGKDIKKEP-EEVKRRIGYLPEEPSLY-ENLT--VRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESR 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6678848 804 KHIFEkvvgpmgLLK-----NKTRILVTHgisYLPQV----DVIIVMSGGKI 846
Cdd:cd03230 132 REFWE-------LLRelkkeGKTILLSSH---ILEEAerlcDRVAILNNGRI 173
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
1001-1261 |
2.26e-19 |
|
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: 90.30 E-value: 2.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1001 VVNGTQANRNFRLSVYGALGILqgaAIFGYSMAVSIGGIFASRRLHLDLLYN--------VLRSPMSFFERTPSGNLVNR 1072
Cdd:cd07346 25 LIDDVIPAGDLSLLLWIALLLL---LLALLRALLSYLRRYLAARLGQRVVFDlrrdlfrhLQRLSLSFFDRNRTGDLMSR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1073 FSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATP----IAAVIIPPLGLVYFFVQRFYVASSRQLKrlESVSRspV 1148
Cdd:cd07346 102 LTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWkltlVALLLLPLYVLILRYFRRRIRKASREVR--ESLAE--L 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1149 YSHFNETLLGVSVIRAF----EEQERFIHQSDLKVDENQKAYYPSIVANRWLAVrLECVGNCIVLFAALFAVIsRHSLSA 1224
Cdd:cd07346 178 SAFLQESLSGIRVVKAFaaeeREIERFREANRDLRDANLRAARLSALFSPLIGL-LTALGTALVLLYGGYLVL-QGSLTI 255
|
250 260 270
....*....|....*....|....*....|....*..
gi 6678848 1225 GLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERL 1261
Cdd:cd07346 256 GELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1289-1470 |
2.62e-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: 87.92 E-value: 2.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1289 RVEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSL--TL-GLFRInesAEGEIIIDGVNIAKIGLHnLRF 1365
Cdd:COG4133 2 MLEAENLSCRRGERL--LFSGLSFTLAAGEALALTGPNGSGKTTLlrILaGLLPP---SAGEVLWNGEPIRDARED-YRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1366 KITIIPQDPVLFSG-SLRMNLDpFSQ------YSDEEVWMALELAHLKGFvsalpdkLNHECAeggeNLSVGQRQLVCLA 1438
Cdd:COG4133 76 RLAYLGHADGLKPElTVRENLR-FWAalyglrADREAIDEALEAVGLAGL-------ADLPVR----QLSAGQKRRVALA 143
|
170 180 190
....*....|....*....|....*....|..
gi 6678848 1439 RALLRKTKILVLDEATAAVDLETDNLIQSTIR 1470
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALDAAGVALLAELIA 175
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
644-801 |
2.82e-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: 87.92 E-value: 2.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFtwARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG------------SVAYV 711
Cdd:COG4133 3 LEAENLSC--RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaredyrrRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 712 PQQ-AWIQNDSLRENILF-----GHPLQENYYKAVMEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSN 785
Cdd:COG4133 81 GHAdGLKPELTVRENLRFwaalyGLRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLLSP 149
|
170
....*....|....*.
gi 6678848 786 SDIYLFDDPLSAVDAH 801
Cdd:COG4133 150 APLWLLDEPFTALDAA 165
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
644-846 |
2.87e-19 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 88.96 E-value: 2.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWArGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG----------------S 707
Cdd:COG3638 3 LELRNLSKRYP-GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGqdvtalrgralrrlrrR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 708 VAYVPQQ-AWIQNDSLRENILFG----HPLQEN----YYKA-VMEACALLPDLEILP-SGDRTEigekgvNLSGGQKQRV 776
Cdd:COG3638 82 IGMIFQQfNLVPRLSVLTNVLAGrlgrTSTWRSllglFPPEdRERALEALERVGLADkAYQRAD------QLSGGQQQRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 777 SLARAVYSNSDIYLFDDPLSAVDAHVGKHIfekvvgpMGLLK------NKTRILVTHgisylpQVDV-------IIVMSG 843
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTARQV-------MDLLRriaredGITVVVNLH------QVDLarryadrIIGLRD 222
|
...
gi 6678848 844 GKI 846
Cdd:COG3638 223 GRV 225
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1307-1500 |
3.29e-19 |
|
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: 88.16 E-value: 3.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1307 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNL----RFKITIIPQDPVLFSGSLR 1382
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1383 MNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE-T 1461
Cdd:cd03290 97 ENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6678848 1462 DNLIQSTIRTQFED--CTVLTIAHRLNTIMDYTRVIVLDKG 1500
Cdd:cd03290 177 DHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
644-855 |
4.78e-19 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 87.56 E-value: 4.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG------------SVAYV 711
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaarqSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 712 PQqawiqNDSL------RENILF-----GHPLQENyyKAVMEAcaLLPDLEILPSGDRteigeKGVNLSGGQKQRVSLAR 780
Cdd:cd03263 81 PQ-----FDALfdeltvREHLRFyarlkGLPKSEI--KEEVEL--LLRVLGLTDKANK-----RARTLSGGMKRKLSLAI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6678848 781 AVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVgpmGLLKNKTRILVTHG---ISYLpqVDVIIVMSGGKISEMGSYQEL 855
Cdd:cd03263 147 ALIGGPSVLLLDEPTSGLDPASRRAIWDLIL---EVRKGRSIILTTHSmdeAEAL--CDRIAIMSDGKLRCIGSPQEL 219
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1306-1504 |
6.46e-19 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 87.41 E-value: 6.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSL--TLGLFrinESA-EGEIIIDGVNIAKIG---LHNLRF-KITIIPQDPvlfs 1378
Cdd:COG1136 23 ALRGVSLSIEAGEFVAIVGPSGSGKSTLlnILGGL---DRPtSGEVLIDGQDISSLSereLARLRRrHIGFVFQFF---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1379 gslrmNLDPFsqYSDEE-VWMALELAHLKGFVSA-----------LPDKLNHECAEggenLSVGQRQLVCLARALLRKTK 1446
Cdd:COG1136 96 -----NLLPE--LTALEnVALPLLLAGVSRKERRerarellervgLGDRLDHRPSQ----LSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6678848 1447 ILVLDEATAAVDLETD----NLIQSTIRTQfeDCTVLTIAH--RLNTIMDytRVIVLDKGEVRE 1504
Cdd:COG1136 165 LILADEPTGNLDSKTGeevlELLRELNREL--GTTIVMVTHdpELAARAD--RVIRLRDGRIVS 224
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
644-856 |
1.07e-18 |
|
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: 87.87 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSL---LSALL-AEmdkvEGHVTLKGSVAYVPQQAW--- 716
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLaklLNGLLlPT----SGKVTVDGLDTLDEENLWeir 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 717 ------IQN-D------SLRENILFGhplQENY-------YKAVMEACALLpDLEIL----PSgdrteigekgvNLSGGQ 772
Cdd:TIGR04520 77 kkvgmvFQNpDnqfvgaTVEDDVAFG---LENLgvpreemRKRVDEALKLV-GMEDFrdrePH-----------LLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 773 KQRVSLARAVYSNSDIYLFDDPLSAVDAhVGKhifEKVVGPMGLLK---NKTRILVTHGISYLPQVDVIIVMSGGKISEM 849
Cdd:TIGR04520 142 KQRVAIAGVLAMRPDIIILDEATSMLDP-KGR---KEVLETIRKLNkeeGITVISITHDMEEAVLADRVIVMNKGKIVAE 217
|
....*..
gi 6678848 850 GSYQELL 856
Cdd:TIGR04520 218 GTPREIF 224
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1307-1510 |
1.12e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 89.47 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1307 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKI---GLHNLRFKITIIPQDPVLFSgslrm 1383
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALsekELRKARRQIGMIFQHFNLLS----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1384 nldpfSQYSDEEVWMALELAHL-KGFVSA----------LPDKLNHECAeggeNLSVGQRQLVCLARALLRKTKILVLDE 1452
Cdd:PRK11153 96 -----SRTVFDNVALPLELAGTpKAEIKArvtellelvgLSDKADRYPA----QLSGGQKQRVAIARALASNPKVLLCDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 1453 ATAAVDLETDNLIQSTIRTQFED--CTVLTIAHRlntiMDYT-----RVIVLDKGEVRECGAPSE 1510
Cdd:PRK11153 167 ATSALDPATTRSILELLKDINRElgLTIVLITHE----MDVVkricdRVAVIDAGRLVEQGTVSE 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1290-1512 |
1.31e-18 |
|
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: 87.06 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLtLGLF--RINESAEGEIII-----DGVNI----AKI 1358
Cdd:COG1119 4 LELRNVTVRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTL-LSLItgDLPPTYGNDVRLfgerrGGEDVwelrKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1359 GL------HNLRFKITIIpqDPVL--FSGSLrmnlDPFSQYSDEEV-----WMA-LELAHLKgfvsalpDKLNHEcaegg 1424
Cdd:COG1119 81 GLvspalqLRFPRDETVL--DVVLsgFFDSI----GLYREPTDEQRerareLLElLGLAHLA-------DRPFGT----- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1425 enLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRT--QFEDCTVLTIAHRLNTIMD-YTRVIVLDKGE 1501
Cdd:COG1119 143 --LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEEIPPgITHVLLLKDGR 220
|
250
....*....|.
gi 6678848 1502 VRECGAPSELL 1512
Cdd:COG1119 221 VVAAGPKEEVL 231
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1285-1504 |
1.38e-18 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 87.07 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1285 PHSGRVEFRDYCLRYREDLD--LVLKHINVTIEGGEKVGIVGRTGAGKSSLtlglFRI----NESAEGEIIIDGVNIAKI 1358
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGgvTALDDVSLTVAAGEFVALVGPSGCGKSTL----LRLiaglEKPTSGEVLVDGKPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1359 GLhnlrfKITIIPQDPVLF----------SGsLRMNLDPFSQYsDEEVWMALELAHLKGFVSALPdklnHEcaeggenLS 1428
Cdd:COG1116 79 GP-----DRGVVFQEPALLpwltvldnvaLG-LELRGVPKAER-RERARELLELVGLAGFEDAYP----HQ-------LS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1429 VGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRT--QFEDCTVLTIAH------RLNtimdyTRVIVLDK- 1499
Cdd:COG1116 141 GGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFLA-----DRVVVLSAr 215
|
....*.
gi 6678848 1500 -GEVRE 1504
Cdd:COG1116 216 pGRIVE 221
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
644-856 |
1.59e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 87.35 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLlSALLAEMDK-VEGHVTLKGSVayvpqqawIQNDSL 722
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTI-SKILTGLLKpQSGEIKIDGIT--------ISKENL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 723 RE-----NILFGHPLQENYYKAVMEACALlpDLE------------ILPSGDRTEIGE----KGVNLSGGQKQRVSLARA 781
Cdd:PRK13632 79 KEirkkiGIIFQNPDNQFIGATVEDDIAF--GLEnkkvppkkmkdiIDDLAKKVGMEDyldkEPQNLSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 782 VYSNSDIYLFDDPLSAVDAHvGKHIFEKVVGPMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELL 856
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPK-GKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
644-856 |
1.98e-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: 86.10 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNAT--FTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVTLKG-------------- 706
Cdd:cd03258 2 IELKNVSkvFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIR-CINGLERpTSGSVLVDGtdltllsgkelrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 707 --SVAYVPQQ-AWIQNDSLRENILFghPLQ-ENYYKAVMEAcALLPDLEILPSGDRTEIgeKGVNLSGGQKQRVSLARAV 782
Cdd:cd03258 81 rrRIGMIFQHfNLLSSRTVFENVAL--PLEiAGVPKAEIEE-RVLELLELVGLEDKADA--YPAQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 783 YSNSDIYLFDDPLSAVDAHVGKHIFEkvvgpmgLLK--NK----TRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQEL 855
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILA-------LLRdiNRelglTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEEV 228
|
.
gi 6678848 856 L 856
Cdd:cd03258 229 F 229
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1290-1527 |
2.01e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 87.16 E-value: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSS---LTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFK 1366
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1367 ITIIPQDP-VLFSGSLRMNLDPFS----QYSDEE----VWMALELAHLKGFVSALPdklnhecaeggENLSVGQRQLVCL 1437
Cdd:PRK13640 86 VGIVFQNPdNQFVGATVGDDVAFGlenrAVPRPEmikiVRDVLADVGMLDYIDSEP-----------ANLSGGQKQRVAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1438 ARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFED--CTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQR 1515
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnnLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
250
....*....|..
gi 6678848 1516 gifySMAKDAGL 1527
Cdd:PRK13640 235 ----EMLKEIGL 242
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1306-1511 |
2.22e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 90.46 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSslTL-----GLFRINEsaeGEIIIDGvniAKIGLHN----LRFKITIIPQDPVL 1376
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKS--TLmkilsGVYQPDS---GEILLDG---EPVRFRSprdaQAAGIAIIHQELNL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1377 FSgslrmNLdpfsqySDEE-VWMALELAHlKGFVSalPDKLNHECAE-----G--------GENLSVGQRQLVCLARALL 1442
Cdd:COG1129 91 VP-----NL------SVAEnIFLGREPRR-GGLID--WRAMRRRAREllarlGldidpdtpVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6678848 1443 RKTKILVLDEATAAVDL-ETDNLIQsTIRT-QFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSEL 1511
Cdd:COG1129 157 RDARVLILDEPTASLTErEVERLFR-IIRRlKAQGVAIIYISHRLDEVFEIAdRVTVLRDGRLVGTGPVAEL 227
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1290-1513 |
4.73e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 85.14 E-value: 4.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--VNIAKIGLHNLRFKI 1367
Cdd:PRK09493 2 IEFKNVSKHFGPTQ--VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkVNDPKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1368 TIIPQDPVLFS----------GSLRMNldpfSQYSDEEVWMALELAHLKGfvsaLPDKLNHECAEggenLSVGQRQLVCL 1437
Cdd:PRK09493 80 GMVFQQFYLFPhltalenvmfGPLRVR----GASKEEAEKQARELLAKVG----LAERAHHYPSE----LSGGQQQRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6678848 1438 ARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFED-CTVLTIAHRLNTIMDY-TRVIVLDKGEVRECGAPSELLQ 1513
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIK 225
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1306-1514 |
5.78e-18 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 86.65 E-value: 5.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLT---LGLFRINESAEGEIIIDGVNIAKIG---LHNLRFK-ITIIPQDPvlfs 1378
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLAraiLGLLPPPGITSGEILFDGEDLLKLSekeLRKIRGReIQMIFQDP---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1379 gslrMN-LDP--------------FSQYSDEEVW-MALELAHLKGFVSAlPDKLN---HEcaeggenLSVGQRQLVCLAR 1439
Cdd:COG0444 96 ----MTsLNPvmtvgdqiaeplriHGGLSKAEAReRAIELLERVGLPDP-ERRLDrypHE-------LSGGMRQRVMIAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1440 ALLRKTKILVLDEATAAVD-------LetdNLIQStIRTQFeDCTVLTIAHRLNT---IMDytRVIVLDKGEVRECGAPS 1509
Cdd:COG0444 164 ALALEPKLLIADEPTTALDvtiqaqiL---NLLKD-LQREL-GLAILFITHDLGVvaeIAD--RVAVMYAGRIVEEGPVE 236
|
....*
gi 6678848 1510 ELLQQ 1514
Cdd:COG0444 237 ELFEN 241
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
644-846 |
6.41e-18 |
|
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: 84.93 E-value: 6.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWARGEPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMDKVEGHV------TLKGS-------- 707
Cdd:cd03256 1 IEVENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLngLVEPTSGSVLIdgtdinKLKGKalrqlrrq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 708 VAYVPQQ-AWIQNDSLRENILFG----HP----LQENYYKA-VMEACALLPDLEILPSGDRteigeKGVNLSGGQKQRVS 777
Cdd:cd03256 80 IGMIFQQfNLIERLSVLENVLSGrlgrRStwrsLFGLFPKEeKQRALAALERVGLLDKAYQ-----RADQLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 778 LARAVYSNSDIYLFDDPLSAVDAHVGKHIfekvvgpMGLLK------NKTRILVTHgisylpQVDV-------IIVMSGG 844
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQV-------MDLLKrinreeGITVIVSLH------QVDLareyadrIVGLKDG 221
|
..
gi 6678848 845 KI 846
Cdd:cd03256 222 RI 223
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
660-846 |
8.30e-18 |
|
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: 83.88 E-value: 8.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 660 TLNgITFSIPEGaLVAVVGQVGCGKSSLLSaLLAEMDKVE-GHVTLKGS-----------------VAYVPQQ-AWIQND 720
Cdd:cd03297 14 TLK-IDFDLNEE-VTGIFGASGAGKSTLLR-CIAGLEKPDgGTIVLNGTvlfdsrkkinlppqqrkIGLVFQQyALFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 721 SLRENILFGHPLQENYYKAVMEAcallpdlEILPSGDRTEIGEKGV-NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVD 799
Cdd:cd03297 91 NVRENLAFGLKRKRNREDRISVD-------ELLDLLGLDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6678848 800 AHVgKHIFEKVVGPMGLLKNKTRILVTHGISYLPQV-DVIIVMSGGKI 846
Cdd:cd03297 164 RAL-RLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLaDRIVVMEDGRL 210
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1304-1484 |
9.04e-18 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 82.20 E-value: 9.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1304 DLVLKHINVTIEGGEKVGIVGRTGAGKSSLtlglFR-INE---SAEGEIIIDGVNiakiglhnlrfKITIIPQDPVLFSG 1379
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSL----FRaLAGlwpWGSGRIGMPEGE-----------DLLFLPQRPYLPLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1380 SLRmnldpfsqysdEEV---WMalelahlkgfvsalpdklnhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAA 1456
Cdd:cd03223 79 TLR-----------EQLiypWD--------------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSA 121
|
170 180
....*....|....*....|....*...
gi 6678848 1457 VDLETDNLIQSTIRTQFedCTVLTIAHR 1484
Cdd:cd03223 122 LDEESEDRLYQLLKELG--ITVISVGHR 147
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
661-858 |
9.12e-18 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 84.28 E-value: 9.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMDkvEGHVTLKGSVAYVPQQAWIQndsLRENI--------LFGH 730
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCInlLEEPD--SGTITVDGEDLTDSKKDINK---LRRKVgmvfqqfnLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 731 ----------PLQ---ENYYKAVMEACALLpdleilpsgDRTEIGEKG----VNLSGGQKQRVSLARAVYSNSDIYLFDD 793
Cdd:COG1126 92 ltvlenvtlaPIKvkkMSKAEAEERAMELL---------ERVGLADKAdaypAQLSGGQQQRVAIARALAMEPKVMLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6678848 794 PLSAVDAH-VGkhifEkVVGPMGLLKNK--TRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLDR 858
Cdd:COG1126 163 PTSALDPElVG----E-VLDVMRDLAKEgmTMVVVTHEMGFAREVaDRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
642-855 |
1.01e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 86.70 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 642 NSITVKNATFTWarGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVTLKGSvaYVPQQAWIQND 720
Cdd:PRK11432 5 NFVVLKNITKRF--GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLR-LVAGLEKpTEGQIFIDGE--DVTHRSIQQRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 721 --------------SLRENILFGHPLQ----ENYYKAVMEACALLpDLEILpsGDRTeigekgVN-LSGGQKQRVSLARA 781
Cdd:PRK11432 80 icmvfqsyalfphmSLGENVGYGLKMLgvpkEERKQRVKEALELV-DLAGF--EDRY------VDqISGGQQQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 782 VYSNSDIYLFDDPLSAVDAHVGKHIFEKVVGPMGLLkNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQEL 855
Cdd:PRK11432 151 LILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQF-NITSLYVTHDQSEAFAVsDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
644-850 |
1.06e-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: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWarGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLS--ALLAEMDKveGHVTLKG-----------SVAY 710
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRmiAGLEEPTS--GRIYIGGrdvtdlppkdrDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 711 VPQQ-AWIQNDSLRENILFGHPL----QENYYKAVMEACALLPDLEILpsgDRteigeKGVNLSGGQKQRVSLARAVYSN 785
Cdd:cd03301 77 VFQNyALYPHMTVYDNIAFGLKLrkvpKDEIDERVREVAELLQIEHLL---DR-----KPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6678848 786 SDIYLFDDPLSAVDAHVGKHIFEKVVGPMGLLKnKTRILVTHG-ISYLPQVDVIIVMSGGKISEMG 850
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLG-TTTIYVTHDqVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1290-1512 |
1.10e-17 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 84.27 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDYCLRYREDLDLVlKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITI 1369
Cdd:cd03295 1 IEFENVTKRYGGGKKAV-NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1370 IPQDPVLFSG-SLRMN--LDP-FSQYSDEEV-WMALELAHLKGFVSA-LPDKLNHEcaeggenLSVGQRQLVCLARALLR 1443
Cdd:cd03295 80 VIQQIGLFPHmTVEENiaLVPkLLKWPKEKIrERADELLALVGLDPAeFADRYPHE-------LSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6678848 1444 KTKILVLDEATAAVDLET-DNLIQSTIRTQFE-DCTVLTIAHRLN-TIMDYTRVIVLDKGEVRECGAPSELL 1512
Cdd:cd03295 153 DPPLLLMDEPFGALDPITrDQLQEEFKRLQQElGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
639-857 |
1.45e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 84.42 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 639 GEGNSITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVtlkgsvaYVPQQAwIQ 718
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI-------FYNNQA-IT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 719 NDSLRE-----NILFGHPLQ---------------EN----YYKAVMEACALLPDLEILPSGDrteigEKGVNLSGGQKQ 774
Cdd:PRK13648 75 DDNFEKlrkhiGIVFQNPDNqfvgsivkydvafglENhavpYDEMHRRVSEALKQVDMLERAD-----YEPNALSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 775 RVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEkVVGPMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQE 854
Cdd:PRK13648 150 RVAIAGVLALNPSVIILDEATSMLDPDARQNLLD-LVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTE 228
|
...
gi 6678848 855 LLD 857
Cdd:PRK13648 229 IFD 231
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
656-846 |
1.45e-17 |
|
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: 82.96 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 656 GEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMDkvEGHVTLKGSVAYVPQQAWIQndsLRENI------- 726
Cdd:cd03262 11 GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCInlLEEPD--SGTIIIDGLKLTDDKKNINE---LRQKVgmvfqqf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 727 -LFGHplqenyyKAVMEACALLP--------------DLEILpsgDRTEIGEKG----VNLSGGQKQRVSLARAVYSNSD 787
Cdd:cd03262 86 nLFPH-------LTVLENITLAPikvkgmskaeaeerALELL---EKVGLADKAdaypAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6678848 788 IYLFDDPLSAVDAHVGKhifeKVVGPMGLL--KNKTRILVTHGISYLPQV-DVIIVMSGGKI 846
Cdd:cd03262 156 VMLFDEPTSALDPELVG----EVLDVMKDLaeEGMTMVVVTHEMGFAREVaDRVIFMDDGRI 213
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1307-1502 |
1.49e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 87.77 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1307 LKHINVTIEGGEKVGIVGRTGAGKSslTL-----GLFRINEsaeGEIIIDG--VNI--------AKIGLhnlrfkitiIP 1371
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKS--TLmkilyGLYQPDS---GEILIDGkpVRIrsprdaiaLGIGM---------VH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1372 QDPVLFsgslrmnlDPFSQYsdEEVWMALElaHLKGFVSALpDKLNHE----CAEGG---------ENLSVGQRQLVCLA 1438
Cdd:COG3845 87 QHFMLV--------PNLTVA--ENIVLGLE--PTKGGRLDR-KAARARirelSERYGldvdpdakvEDLSVGEQQRVEIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6678848 1439 RALLRKTKILVLDEATaAV--DLETDNLIQsTIRtQF--EDCTVLTIAHRLNTIMDYT-RVIVLDKGEV 1502
Cdd:COG3845 154 KALYRGARILILDEPT-AVltPQEADELFE-ILR-RLaaEGKSIIFITHKLREVMAIAdRVTVLRRGKV 219
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
639-868 |
1.68e-17 |
|
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: 84.19 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 639 GEGNSITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-SVAYVPQQAWI 717
Cdd:cd03288 15 GLGGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGiDISKLPLHTLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 718 QNDS--LRENILFGHPLQENY-----------YKAvMEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYS 784
Cdd:cd03288 95 SRLSiiLQDPILFSGSIRFNLdpeckctddrlWEA-LEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 785 NSDIYLFDDPLSAVDAHVgKHIFEKVVgpMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELL-DRDGAFA 863
Cdd:cd03288 174 KSSILIMDEATASIDMAT-ENILQKVV--MTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFA 250
|
....*
gi 6678848 864 EFLRT 868
Cdd:cd03288 251 SLVRT 255
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1306-1502 |
2.22e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 83.98 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLtL----GLFRINEsaeGEIIIDGVNIAKIGLHNlRFK-ITIIPQDPVL---F 1377
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTL-LnaiaGSLPPDS---GSILIDGKDVTKLPEYK-RAKyIGRVFQDPMMgtaP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1378 SGSLRMNLDpfsqysdeevwMALELAHLKGFVSALPDKLNHECAE-------GGEN--------LSVGQRQLVCLARALL 1442
Cdd:COG1101 96 SMTIEENLA-----------LAYRRGKRRGLRRGLTKKRRELFREllatlglGLENrldtkvglLSGGQRQALSLLMATL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6678848 1443 RKTKILVLDEATAAVD-------LE-TDNLIQStirtqfEDCTVLTIAHRLNTIMDY-TRVIVLDKGEV 1502
Cdd:COG1101 165 TKPKLLLLDEHTAALDpktaalvLElTEKIVEE------NNLTTLMVTHNMEQALDYgNRLIMMHEGRI 227
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
656-846 |
2.31e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 83.57 E-value: 2.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 656 GEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKVEGHVTLKGSVAYvpqqAWIQND--------------S 721
Cdd:PRK11247 23 GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLR-LLAGLETPSAGELLAGTAPL----AEAREDtrlmfqdarllpwkK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 722 LRENILFGhpLQENYYKAVMEAcallpdLEILPSGDRTeiGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAH 801
Cdd:PRK11247 98 VIDNVGLG--LKGQWRDAALQA------LAAVGLADRA--NEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6678848 802 VG---KHIFEKVVGPMGLlknkTRILVTHGISYLPQV-DVIIVMSGGKI 846
Cdd:PRK11247 168 TRiemQDLIESLWQQHGF----TVLLVTHDVSEAVAMaDRVLLIEEGKI 212
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1306-1502 |
3.06e-17 |
|
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: 82.19 E-value: 3.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNI--AKIGLHNLRFKITIIPQDPVLFSgslRM 1383
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLFP---HL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1384 N------LDP---FSQYSDEEVWMALELAHLKGfvsaLPDKLNHECAEggenLSVGQRQLVCLARALLRKTKILVLDEAT 1454
Cdd:cd03262 92 TvlenitLAPikvKGMSKAEAEERALELLEKVG----LADKADAYPAQ----LSGGQQQRVAIARALAMNPKVMLFDEPT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6678848 1455 AAVDLETDNLIQSTIRTQFED-CTVLTIAHRlntiMDY-----TRVIVLDKGEV 1502
Cdd:cd03262 164 SALDPELVGEVLDVMKDLAEEgMTMVVVTHE----MGFarevaDRVIFMDDGRI 213
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
1015-1193 |
3.34e-17 |
|
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: 83.98 E-value: 3.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1015 VYGALGILQGAAIFGYSMAVSIGGIFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGS 1094
Cdd:cd18544 46 LYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1095 LFSVIGAVIIIL-----LATpIAAVIIPPLGLVYFFVQRFYVASSRQLKrlESVSRspVYSHFNETLLGVSVIRAFEEQE 1169
Cdd:cd18544 126 LLLLIGILIAMFllnwrLAL-ISLLVLPLLLLATYLFRKKSRKAYREVR--EKLSR--LNAFLQESISGMSVIQLFNREK 200
|
170 180
....*....|....*....|....
gi 6678848 1170 RFIHQSDLKVDENQKAYYPSIVAN 1193
Cdd:cd18544 201 REFEEFDEINQEYRKANLKSIKLF 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1290-1511 |
3.60e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 83.63 E-value: 3.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDYCLRYREDLD-LVLKHINVTIEGGEKVGIVGRTGAGKSS---LTLGLFrinESAEGEIIIDGVNIAKIGLHNLRF 1365
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGLL---EAESGQIIIDGDLLTEENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1366 KITIIPQDP-VLFSGSLRMNLDPFS--------QYSDEEVWMALELAHLKGFVSALPDKLnhecaeggenlSVGQRQLVC 1436
Cdd:PRK13650 82 KIGMVFQNPdNQFVGATVEDDVAFGlenkgiphEEMKERVNEALELVGMQDFKEREPARL-----------SGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6678848 1437 LARALLRKTKILVLDEATAAVD----LETDNLIQStIRTQFeDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSEL 1511
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDpegrLELIKTIKG-IRDDY-QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1303-1512 |
3.68e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 85.47 E-value: 3.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1303 LDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIG---LHNLRFK--------ITIIP 1371
Cdd:PRK10070 40 LSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaeLREVRRKkiamvfqsFALMP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1372 QDPVLFSGSLRMNLDPF-SQYSDEEVWMALELAHLKGFVSALPDKlnhecaeggenLSVGQRQLVCLARALLRKTKILVL 1450
Cdd:PRK10070 120 HMTVLDNTAFGMELAGInAEERREKALDALRQVGLENYAHSYPDE-----------LSGGMRQRVGLARALAINPDILLM 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6678848 1451 DEATAAVDletdnliqSTIRTQFED----------CTVLTIAHRLNTIMDY-TRVIVLDKGEVRECGAPSELL 1512
Cdd:PRK10070 189 DEAFSALD--------PLIRTEMQDelvklqakhqRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEIL 253
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1313-1496 |
8.46e-17 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 83.24 E-value: 8.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1313 TIEGGEKVGIVGRTGAGKSslTLG--LFRINESAEGEIIIDGVNIAKIG---LHNLRFKITIIPQDPvlfSGSL--RMN- 1384
Cdd:COG4608 40 DIRRGETLGLVGESGCGKS--TLGrlLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP---YASLnpRMTv 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1385 -------LDPFSQYS----DEEVWMALELAHLKgfvsalPDKLN---HEcaeggenLSVGQRQLVCLARALLRKTKILVL 1450
Cdd:COG4608 115 gdiiaepLRIHGLASkaerRERVAELLELVGLR------PEHADrypHE-------FSGGQRQRIGIARALALNPKLIVC 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 1451 DEATAAVDLEtdnlIQSTIRTQFED------CTVLTIAHRLNT---IMDytRVIV 1496
Cdd:COG4608 182 DEPVSALDVS----IQAQVLNLLEDlqdelgLTYLFISHDLSVvrhISD--RVAV 230
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1306-1510 |
8.77e-17 |
|
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: 81.33 E-value: 8.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSslTL-----GLFRINEsaeGEIIIDGVNI--------AKIGLHnlR-FKITIIP 1371
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKT--TLfnlisGFLRPTS---GSVLFDGEDItglppheiARLGIG--RtFQIPRLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1372 QD---------PVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGfvsaLPDKLNHECAeggeNLSVGQRQLVCLARALL 1442
Cdd:cd03219 88 PEltvlenvmvAAQARTGSGLLLARARREEREARERAEELLERVG----LADLADRPAG----ELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1443 RKTKILVLDEATAAVDL-ETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVRECGAPSE 1510
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPeETEELAELIRELRERGITVLLVEHDMDVVMSLaDRVTVLDQGRVIAEGTPDE 229
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1289-1512 |
9.02e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 82.34 E-value: 9.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1289 RVEFRDYCLryrEDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIG-LHNLRFKI 1367
Cdd:PRK13644 3 RLENVSYSY---PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1368 TIIPQDPV-----------LFSGSLRMNLDPFSqySDEEVWMALELAHLKGFVSALPdklnhecaeggENLSVGQRQLVC 1436
Cdd:PRK13644 80 GIVFQNPEtqfvgrtveedLAFGPENLCLPPIE--IRKRVDRALAEIGLEKYRHRSP-----------KTLSGGQGQCVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6678848 1437 LARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDC-TVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELL 1512
Cdd:PRK13644 147 LAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGkTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1290-1512 |
1.09e-16 |
|
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: 81.23 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDYCLRYREdldLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAkiGLHNLRFKITI 1369
Cdd:cd03299 1 LKVENLSKDWKE---FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1370 IPQDPVLF---------SGSLRMNLDPFSQySDEEVwmaLELAHLKGFVSALPDKlnhecaegGENLSVGQRQLVCLARA 1440
Cdd:cd03299 76 VPQNYALFphmtvykniAYGLKKRKVDKKE-IERKV---LEIAEMLGIDHLLNRK--------PETLSGGEQQRVAIARA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6678848 1441 LLRKTKILVLDEATAAVDLET-DNLIQ--STIRTQFeDCTVLTIAHRLNTI-MDYTRVIVLDKGEVRECGAPSELL 1512
Cdd:cd03299 144 LVVNPKILLLDEPFSALDVRTkEKLREelKKIRKEF-GVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
644-859 |
1.32e-16 |
|
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: 80.79 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFtwARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-SVAYVPQQAWI----- 717
Cdd:COG1127 6 IEVRNLTK--SFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqDITGLSEKELYelrrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 718 -----QN----DSL--RENILFghPLQENY-------YKAVMEACAL--LPDLEIL-PSgdrteigEkgvnLSGGQKQRV 776
Cdd:COG1127 84 igmlfQGgalfDSLtvFENVAF--PLREHTdlseaeiRELVLEKLELvgLPGAADKmPS-------E----LSGGMRKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 777 SLARAVYSNSDIYLFDDPLSAVDAHVGKHIFE---KVVGPMGLlknkTRILVTHGISYLPQV-DVIIVMSGGKISEMGSY 852
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDPITSAVIDElirELRDELGL----TSVVVTHDLDSAFAIaDRVAVLADGKIIAEGTP 226
|
....*..
gi 6678848 853 QELLDRD 859
Cdd:COG1127 227 EELLASD 233
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1306-1510 |
1.64e-16 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 81.24 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSL----TlGLFRINEsaeGEIIIDGVNI--------AKIGLhnLR-FKIT-IIP 1371
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLfnliT-GFYRPTS---GRILFDGRDItglpphriARLGI--ARtFQNPrLFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1372 QDPVL----------FSGSLRMNLDPFSQYSDEEVWM---ALELAHLKGfvsaLPDKLNHECAeggeNLSVGQRQLVCLA 1438
Cdd:COG0411 93 ELTVLenvlvaaharLGRGLLAALLRLPRARREEREArerAEELLERVG----LADRADEPAG----NLSYGQQRRLEIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6678848 1439 RALLRKTKILVLDEATAAVDL-ETDNLIQsTIRT--QFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSE 1510
Cdd:COG0411 165 RALATEPKLLLLDEPAAGLNPeETEELAE-LIRRlrDERGITILLIEHDMDLVMGLAdRIVVLDFGRVIAEGTPAE 239
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1306-1511 |
2.00e-16 |
|
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: 84.47 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLtLGLFRINESAE---GEII--------------------------------- 1349
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMDQYEptsGRIIyhvalcekcgyverpskvgepcpvcggtlepee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1350 IDGVNIAKIGLHNLRFKITIIPQDPVLFSGSLR-----MNLDPFSQYS-DEEVWMALELAHLKgfvsalpdKLNHECAEG 1423
Cdd:TIGR03269 94 VDFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTvldnvLEALEEIGYEgKEAVGRAVDLIEMV--------QLSHRITHI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1424 GENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDYT-RVIVLDKG 1500
Cdd:TIGR03269 166 ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEeaVKASGISMVLTSHWPEVIEDLSdKAIWLENG 245
|
250
....*....|.
gi 6678848 1501 EVRECGAPSEL 1511
Cdd:TIGR03269 246 EIKEEGTPDEV 256
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
644-827 |
2.16e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 80.85 E-value: 2.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWarGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL-----LAEMDKVEGHVTLKG------------ 706
Cdd:COG1117 12 IEVRNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndLIPGARVEGEILLDGediydpdvdvve 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 707 ---SVAYVPQQAwiqN---DSLRENILFGHPLQENYYKAVMEA--------CALLPDLEilpsgDRteIGEKGVNLSGGQ 772
Cdd:COG1117 90 lrrRVGMVFQKP---NpfpKSIYDNVAYGLRLHGIKSKSELDEiveeslrkAALWDEVK-----DR--LKKSALGLSGGQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 773 KQRVSLARAVYSNSDIYLFDDPLSAVD----AHVGKHIFEkvvgpmglLKNK-TRILVTH 827
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDpistAKIEELILE--------LKKDyTIVIVTH 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
661-858 |
2.74e-16 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 79.97 E-value: 2.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVTLKG-SVAYVP----------QQ-AWIQNDSLRENIL 727
Cdd:cd03300 16 LDGVSLDIKEGEFFTLLGPSGCGKTTLLR-LIAGFETPtSGEILLDGkDITNLPphkrpvntvfQNyALFPHLTVFENIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 728 FGHPLQ---ENYYKA-VMEACAL--LPDLEilpsgdRTEIGEkgvnLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAH 801
Cdd:cd03300 95 FGLRLKklpKAEIKErVAEALDLvqLEGYA------NRKPSQ----LSGGQQQRVAIARALVNEPKVLLLDEPLGALDLK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 802 VGKHIFEKVvgpMGLLKN--KTRILVTHGIS-YLPQVDVIIVMSGGKISEMGSYQELLDR 858
Cdd:cd03300 165 LRKDMQLEL---KRLQKElgITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
666-858 |
3.15e-16 |
|
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: 82.07 E-value: 3.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 666 FSIPEGALVAVVGQVGCGKSSLLSAL--LAEMDkvEGHVTLKGSV-----------------AYVPQQAwiqndSL---- 722
Cdd:COG4148 20 FTLPGRGVTALFGPSGSGKTTLLRAIagLERPD--SGRIRLGGEVlqdsargiflpphrrriGYVFQEA-----RLfphl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 723 --RENILFGH---PLQENYYK--AVMEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNSDIYLFDDPL 795
Cdd:COG4148 93 svRGNLLYGRkraPRAERRISfdEVVELLGIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6678848 796 SAVDAHVGKHI---FEKvvgpmglLKNKTRI---LVTHGisyLPQV----DVIIVMSGGKISEMGSYQELLDR 858
Cdd:COG4148 162 AALDLARKAEIlpyLER-------LRDELDIpilYVSHS---LDEVarlaDHVVLLEQGRVVASGPLAEVLSR 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
644-856 |
3.33e-16 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 80.18 E-value: 3.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWaRGEPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSA--LLAEMD----KVeGHVTLKGSVAYVPQQAWI 717
Cdd:PRK11264 4 IEVKNLVKKF-HGQT-VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCinLLEQPEagtiRV-GDITIDTARSLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 718 QNdsLRENI--------LFGH----------PLQ---ENYYKAVMEACALLPDLEIlpSGDRTEIGEKgvnLSGGQKQRV 776
Cdd:PRK11264 81 RQ--LRQHVgfvfqnfnLFPHrtvleniiegPVIvkgEPKEEATARARELLAKVGL--AGKETSYPRR---LSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 777 SLARAVYSNSDIYLFDDPLSAVDAH-VGkhifeKVVGPMGLL--KNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSY 852
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSALDPElVG-----EVLNTIRQLaqEKRTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGPA 228
|
....
gi 6678848 853 QELL 856
Cdd:PRK11264 229 KALF 232
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
644-848 |
3.63e-16 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 79.40 E-value: 3.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWARGEPPT--LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVTLKG-------------- 706
Cdd:COG4181 9 IELRGLTKTVGTGAGELtiLKGISLEVEAGESVAIVGASGSGKSTLLG-LLAGLDRPtSGTVRLAGqdlfaldedararl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 707 ---SVAYVpQQAW--IQNDSLRENI-----LFGHPLQENYYKAVMEACALLPDLEILPSGdrteigekgvnLSGGQKQRV 776
Cdd:COG4181 88 rarHVGFV-FQSFqlLPTLTALENVmlpleLAGRRDARARARALLERVGLGHRLDHYPAQ-----------LSGGEQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6678848 777 SLARAVYSNSDIYLFDDPLSAVDAHVGKHIfekvvgpMGLL--KNKTR----ILVTHGISYLPQVDVIIVMSGGKISE 848
Cdd:COG4181 156 ALARAFATEPAILFADEPTGNLDAATGEQI-------IDLLfeLNRERgttlVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
643-867 |
3.80e-16 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 79.67 E-value: 3.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 643 SITVKNATFTWarGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL-LAEMDK-----VEGH-------------VT 703
Cdd:COG4161 2 SIQLKNINCFY--GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnLLETPDsgqlnIAGHqfdfsqkpsekaiRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 704 LKGSVAYVPQQ--AWiQNDSLRENiLFGHP---LQENYYKAVMEACALLPDLEILPSGDRTEIgekgvNLSGGQKQRVSL 778
Cdd:COG4161 80 LRQKVGMVFQQynLW-PHLTVMEN-LIEAPckvLGLSKEQAREKAMKLLARLRLTDKADRFPL-----HLSGGQQQRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 779 ARAVYSNSDIYLFDDPLSAVDAHVGKHIFE--KVVGPMGLlknkTRILVTHGISYLPQV-DVIIVMSGGKISEMGSyQEL 855
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDPEITAQVVEiiRELSQTGI----TQVIVTHEVEFARKVaSQVVYMEKGRIIEQGD-ASH 227
|
250
....*....|....
gi 6678848 856 LD--RDGAFAEFLR 867
Cdd:COG4161 228 FTqpQTEAFAHYLS 241
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
1015-1261 |
3.98e-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: 80.68 E-value: 3.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1015 VYGALGILQGAAIFGYSMAVSIGGIFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGS 1094
Cdd:cd18557 41 ILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1095 LFSVIGAVIIILLA----TPIAAVIIPPLGLVYFFVQRFYVASSRQLkrLESVSRSPvySHFNETLLGVSVIRAFEEQER 1170
Cdd:cd18557 121 ILQVIGGLIILFILswklTLVLLLVIPLLLIASKIYGRYIRKLSKEV--QDALAKAG--QVAEESLSNIRTVRSFSAEEK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1171 FIHQSDLKVDENQKAYYPSIVAN---RWLAVRLECVGNCIVLFAALFAVISRHsLSAGLVGLSVSYSLQITAYLNWLVRM 1247
Cdd:cd18557 197 EIRRYSEALDRSYRLARKKALANalfQGITSLLIYLSLLLVLWYGGYLVLSGQ-LTVGELTSFILYTIMVASSVGGLSSL 275
|
250
....*....|....
gi 6678848 1248 SSEMETNIVAVERL 1261
Cdd:cd18557 276 LADIMKALGASERV 289
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
656-867 |
4.38e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 79.37 E-value: 4.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 656 GEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMDK----VEGHVTLKGSV---------AYVPQQAWI--Q 718
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEITSgdliVDGLKVNDPKVderlirqeaGMVFQQFYLfpH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 719 NDSLrENILFGhPLQ-ENYYKAVMEACALlpdlEILpsgDRTEIGEKG----VNLSGGQKQRVSLARAVYSNSDIYLFDD 793
Cdd:PRK09493 92 LTAL-ENVMFG-PLRvRGASKEEAEKQAR----ELL---AKVGLAERAhhypSELSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6678848 794 PLSAVDAHVgKHIFEKVvgpMGLLKNK--TRILVTHGISYLPQVDV-IIVMSGGKISEMGSYQELLDR--DGAFAEFLR 867
Cdd:PRK09493 163 PTSALDPEL-RHEVLKV---MQDLAEEgmTMVIVTHEIGFAEKVASrLIFIDKGRIAEDGDPQVLIKNppSQRLQEFLQ 237
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
661-866 |
4.83e-16 |
|
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: 79.30 E-value: 4.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS-----------VAYVPQQ-AWIQNDSLRENILF 728
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQNyALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 729 GHPLQ----ENYYKAVMEACALLPDLEILpsgDRteigeKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAhvgk 804
Cdd:cd03299 95 GLKKRkvdkKEIERKVLEIAEMLGIDHLL---NR-----KPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV---- 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6678848 805 HIFEKVVGPMGLLKNK---TRILVTHGIS-YLPQVDVIIVMSGGKISEMGSYQELLDR--DGAFAEFL 866
Cdd:cd03299 163 RTKEKLREELKKIRKEfgvTVLHVTHDFEeAWALADKVAIMLNGKLIQVGKPEEVFKKpkNEFVAEFL 230
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1307-1514 |
5.94e-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: 79.61 E-value: 5.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1307 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIG---LHNLRFK--------ITIIPQDPV 1375
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRKkismvfqsFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1376 LFSGSLRMNLDPFSQYSDEEVWM-ALELAHLKGFVSALPDKLnhecaeggenlSVGQRQLVCLARALLRKTKILVLDEAT 1454
Cdd:cd03294 120 LENVAFGLEVQGVPRAEREERAAeALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6678848 1455 AAVDletdnliqSTIRTQFEDC----------TVLTIAHRLNTIM---DytRVIVLDKGEVRECGAPSELLQQ 1514
Cdd:cd03294 189 SALD--------PLIRREMQDEllrlqaelqkTIVFITHDLDEALrlgD--RIAIMKDGRLVQVGTPEEILTN 251
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1289-1511 |
6.56e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 79.31 E-value: 6.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1289 RVEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINE-----SAEGEIIIDGVNI--AKIGLH 1361
Cdd:COG1117 11 KIEVRNLNVYYGDKQ--ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDlipgaRVEGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1362 NLRFKITIIPQDPVLFSGS--------LRMNLDPFSQYSDEEVWMALELAHL----KgfvsalpDKLNhecaEGGENLSV 1429
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSiydnvaygLRLHGIKSKSELDEIVEESLRKAALwdevK-------DRLK----KSALGLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1430 GQRQLVCLARALLRKTKILVLDEATAAVD-LETDNlIQSTIRTQFEDCTVLTIAHRLNT---IMDYTrvIVLDKGEVREC 1505
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDpISTAK-IEELILELKKDYTIVIVTHNMQQaarVSDYT--AFFYLGELVEF 234
|
....*.
gi 6678848 1506 GAPSEL 1511
Cdd:COG1117 235 GPTEQI 240
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
648-829 |
6.63e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 79.52 E-value: 6.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 648 NATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSV--------AYVpqqawIQN 719
Cdd:COG4525 10 SVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgadrGVV-----FQK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 720 DSL------RENILFGHPLQeNYYKAVMEACALlpdlEILPSGDRTEIGEKGV-NLSGGQKQRVSLARAVYSNSDIYLFD 792
Cdd:COG4525 85 DALlpwlnvLDNVAFGLRLR-GVPKAERRARAE----ELLALVGLADFARRRIwQLSGGMRQRVGIARALAADPRFLLMD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6678848 793 DPLSAVDAHVGKHIFEKvvgpmgLLK-----NKTRILVTHGI 829
Cdd:COG4525 160 EPFGALDALTREQMQEL------LLDvwqrtGKGVFLITHSV 195
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1306-1520 |
6.79e-16 |
|
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: 79.90 E-value: 6.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGvniakiglhnlrfKITIIPQDPVLFSGSLRMNL 1385
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1386 DPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLI 1465
Cdd:cd03291 119 IFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6678848 1466 qstirtqFEDC--------TVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIFYS 1520
Cdd:cd03291 199 -------FESCvcklmankTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSS 254
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1290-1514 |
6.99e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 79.74 E-value: 6.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDYCLRYREDlDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIA--KIGLHNLRFKI 1367
Cdd:PRK13639 2 LETRDLKYSYPDG-TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1368 TIIPQDP--VLFSGSLR-------MNLDPFSQYSDEEVWMALELAHLKGFVSALPdklnhecaeggENLSVGQRQLVCLA 1438
Cdd:PRK13639 81 GIVFQNPddQLFAPTVEedvafgpLNLGLSKEEVEKRVKEALKAVGMEGFENKPP-----------HHLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6678848 1439 RALLRKTKILVLDEATAAVD-LETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELLQQ 1514
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDpMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYAdKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1306-1512 |
8.90e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 81.43 E-value: 8.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLtlgLFRINES---AEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVL---FSG 1379
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTL---LRAINGTltpTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsfeFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1380 S--LRMNLDP----FSQYSDEEVwMALELAHLKGFVSALPDKlnhecaeGGENLSVGQRQLVCLARALLRKTKILVLDEA 1453
Cdd:PRK09536 95 RqvVEMGRTPhrsrFDTWTETDR-AAVERAMERTGVAQFADR-------PVTSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6678848 1454 TAAVDLETDNLIQSTIRTQFEDC-TVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELL 1512
Cdd:PRK09536 167 TASLDINHQVRTLELVRRLVDDGkTAVAAIHDLDLAARYCdELVLLADGRVRAAGPPADVL 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1309-1502 |
9.11e-16 |
|
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: 77.92 E-value: 9.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1309 HINVTIEGGEKVGIVGRTGAGKSSLtLGLFRINESAE-GEIIIDGVNIAkiGLHNLRFKITIIPQDPVLFSG-------- 1379
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTL-LNLIAGFETPQsGRVLINGVDVT--AAPPADRPVSMLFQENNLFAHltveqnvg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1380 ---SLRMNLDPFSQysdEEVWMALELAHLKGFVSALPDKLnhecaeggenlSVGQRQLVCLARALLRKTKILVLDEATAA 1456
Cdd:cd03298 93 lglSPGLKLTAEDR---QAIEVALARVGLAGLEKRLPGEL-----------SGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6678848 1457 VD--LETDNL-IQSTIRTQfEDCTVLTIAHRLNTIMD-YTRVIVLDKGEV 1502
Cdd:cd03298 159 LDpaLRAEMLdLVLDLHAE-TKMTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
640-864 |
9.74e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 79.29 E-value: 9.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 640 EGNSITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVaYVPQQAW--- 716
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV-LSEETVWdvr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 717 ------IQN-------DSLRENILFGhplqenyykavMEACALlPDLEILPsgdRTEIGEKGVN-----------LSGGQ 772
Cdd:PRK13635 81 rqvgmvFQNpdnqfvgATVQDDVAFG-----------LENIGV-PREEMVE---RVDQALRQVGmedflnrephrLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 773 KQRVSLARAVYSNSDIYLFDDPLSAVDAhVGKhifEKVVGPMGLLKNKTRILV---THGISYLPQVDVIIVMSGGKISEM 849
Cdd:PRK13635 146 KQRVAIAGVLALQPDIIILDEATSMLDP-RGR---REVLETVRQLKEQKGITVlsiTHDLDEAAQADRVIVMNKGEILEE 221
|
250
....*....|....*
gi 6678848 850 GSYQELLDRDGAFAE 864
Cdd:PRK13635 222 GTPEEIFKSGHMLQE 236
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
643-855 |
1.18e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 80.51 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 643 SITVKNATFTWARGEppTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS-----------VAYV 711
Cdd:PRK10851 2 SIEIANIKKSFGRTQ--VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrlhardrkVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 712 PQQ-AWIQNDSLRENILFG---HPLQENYYKAVM--EACALLPDLEILPSGDRTEigekgVNLSGGQKQRVSLARAVYSN 785
Cdd:PRK10851 80 FQHyALFRHMTVFDNIAFGltvLPRRERPNAAAIkaKVTQLLEMVQLAHLADRYP-----AQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6678848 786 SDIYLFDDPLSAVDAHVGKHIFEKVVGPMGLLKNkTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQEL 855
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKF-TSVFVTHDQEEAMEVaDRVVVMSQGNIEQAGTPDQV 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
643-835 |
1.55e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 78.54 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 643 SITVKNATFTWARGEppTLNGITFSIPEGALVAVVGQVGCGKSSLLSALlAEMDKVEGHVTLKGSVAYVPQQAW---IQN 719
Cdd:PRK14258 7 AIKVNNLSFYYDTQK--ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVEFFNQNIYerrVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 720 DSLRENILFGHP----LQENYYKAVMEACALL---PDLEI-------LPSGD-----RTEIGEKGVNLSGGQKQRVSLAR 780
Cdd:PRK14258 84 NRLRRQVSMVHPkpnlFPMSVYDNVAYGVKIVgwrPKLEIddivesaLKDADlwdeiKHKIHKSALDLSGGQQQRLCIAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 781 AVYSNSDIYLFDDPLSAVDAHVGKHIfEKVVGPMGLLKNKTRILVTHGisyLPQV 835
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKV-ESLIQSLRLRSELTMVIVSHN---LHQV 214
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
644-851 |
1.66e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 79.74 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNA--TFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLS--ALLAEMDkvEGHVTLKG------------- 706
Cdd:COG1135 2 IELENLskTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRciNLLERPT--SGSVLVDGvdltalserelra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 707 ---SVAYVPQQAwiqndSL------RENILFghPLQ-ENYYKA-----VMEacaLLpdleilpsgDRTEIGEKG----VN 767
Cdd:COG1135 80 arrKIGMIFQHF-----NLlssrtvAENVAL--PLEiAGVPKAeirkrVAE---LL---------ELVGLSDKAdaypSQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 768 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEkvvgpmgLLK--NK----TRILVTHgisylpQVDVI--I 839
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILD-------LLKdiNRelglTIVLITH------EMDVVrrI 207
|
250
....*....|....*..
gi 6678848 840 -----VMSGGKISEMGS 851
Cdd:COG1135 208 cdrvaVLENGRIVEQGP 224
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
644-857 |
1.67e-15 |
|
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: 77.72 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWARGEPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG----------------S 707
Cdd:TIGR02315 2 LEVENLSKVYPNGKQ-ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGtditklrgkklrklrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 708 VAYVPQQ-AWIQNDSLRENILFGhplQENYYKAVMEACALLPDLEI---LPSGDRTEIGEKGV----NLSGGQKQRVSLA 779
Cdd:TIGR02315 81 IGMIFQHyNLIERLTVLENVLHG---RLGYKPTWRSLLGRFSEEDKeraLSALERVGLADKAYqradQLSGGQQQRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 780 RAVYSNSDIYLFDDPLSAVDAHVGKHIfekvvgpMGLLKnktRILVTHGISY---LPQVDV-------IIVMSGGKISEM 849
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKQV-------MDYLK---RINKEDGITViinLHQVDLakkyadrIVGLKAGEIVFD 227
|
....*...
gi 6678848 850 GSYQELLD 857
Cdd:TIGR02315 228 GAPSELDD 235
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1306-1506 |
1.84e-15 |
|
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: 76.85 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGeKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIaKIGLHNLRFKITIIPQDpvlFSGSLRMNL 1385
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV-LKQPQKLRRRIGYLPQE---FGVYPNFTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1386 DPFSQY-----------SDEEVWMALELAHLKGFVSalpDKLNhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEAT 1454
Cdd:cd03264 90 REFLDYiawlkgipskeVKARVDEVLELVNLGDRAK---KKIG--------SLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6678848 1455 AAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMD-YTRVIVLDKGEVRECG 1506
Cdd:cd03264 159 AGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1306-1514 |
2.23e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 77.89 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLtLGLFrineSAE-----GEIIIDGVNIAKIGLHNLRFKITIIPQDPVL-FSG 1379
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTL-LRAL----SGElspdsGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1380 S----LRMNLDPFSQYSDE-----EVWMAL-ELAHLKGfvsalpdKLNHEcaeggenLSVGQRQLVCLARALLR------ 1443
Cdd:PRK13548 92 TveevVAMGRAPHGLSRAEddalvAAALAQvDLAHLAG-------RDYPQ-------LSGGEQQRVQLARVLAQlwepdg 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6678848 1444 KTKILVLDEATAAVDL----ETDNLIQStiRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELLQQ 1514
Cdd:PRK13548 158 PPRWLLLDEPTSALDLahqhHVLRLARQ--LAHERGLAVIVVLHDLNLAARYAdRIVLLHQGRLVADGTPAEVLTP 231
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
642-858 |
2.63e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 78.30 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 642 NSITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSS---LLSALLAEMDKVEGHVTLKGsVAYVPQQAWiq 718
Cdd:PRK13640 4 NIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDG-ITLTAKTVW-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 719 ndSLREN--ILFGHPLQENYYKAVMEACALLPDLEILPSGDRTEIGEKGV--------------NLSGGQKQRVSLARAV 782
Cdd:PRK13640 81 --DIREKvgIVFQNPDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLadvgmldyidsepaNLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6678848 783 YSNSDIYLFDDPLSAVDAHvGKHIFEKVVGPMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDR 858
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPA-GKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1306-1514 |
2.83e-15 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 79.37 E-value: 2.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLtL----GLFRINEsaeGEIIIDGVNIAKIGLHNlRfKITIIPQDPVLFS--- 1378
Cdd:COG3842 20 ALDDVSLSIEPGEFVALLGPSGCGKTTL-LrmiaGFETPDS---GRILLDGRDVTGLPPEK-R-NVGMVFQDYALFPhlt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1379 -------GsLRM-NLDPfsQYSDEEVWMALELAHLKGFVSALPdklnHEcaeggenLSVGQRQLVCLARALLRKTKILVL 1450
Cdd:COG3842 94 vaenvafG-LRMrGVPK--AEIRARVAELLELVGLEGLADRYP----HQ-------LSGGQQQRVALARALAPEPRVLLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6678848 1451 DEATAAVDLETdnliqsTIRTQFEdctVLTIAHRLN--TIM------------DytRVIVLDKGEVRECGAPSELLQQ 1514
Cdd:COG3842 160 DEPLSALDAKL------REEMREE---LRRLQRELGitFIYvthdqeealalaD--RIAVMNDGRIEQVGTPEEIYER 226
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
661-854 |
3.23e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 79.22 E-value: 3.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVTLKG-SVAYVPQQ-----------AWIQNDSLRENIL 727
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLR-LIAGFETPdSGRIMLDGqDITHVPAEnrhvntvfqsyALFPHMTVFENVA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 728 FGHPLQ----ENYYKAVMEACALLpDLEILpsGDRteigeKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVG 803
Cdd:PRK09452 109 FGLRMQktpaAEITPRVMEALRMV-QLEEF--AQR-----KPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6678848 804 KHifekvvgpMGL-LK------NKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQE 854
Cdd:PRK09452 181 KQ--------MQNeLKalqrklGITFVFVTHDQeEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
590-800 |
4.09e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 80.24 E-value: 4.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 590 FNILRFPLNILPMVISSIVQASVSLKRLRIFLSH-EELEPDSIERRSIKSGEGNSITVKNATFTWARGEPpTLNGITFSI 668
Cdd:COG4178 308 FGQVQGALSWFVDNYQSLAEWRATVDRLAGFEEAlEAADALPEAASRIETSEDGALALEDLTLRTPDGRP-LLEDLSLSL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 669 PEGALVAVVGQVGCGKSSLLSAlLAEM-DKVEGHVTL--KGSVAYVPQQAWIQNDSLRENILFGHPlQENY----YKAVM 741
Cdd:COG4178 387 KPGERLLITGPSGSGKSTLLRA-IAGLwPYGSGRIARpaGARVLFLPQRPYLPLGTLREALLYPAT-AEAFsdaeLREAL 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6678848 742 EAC---ALLPDLEILPSGDRTeigekgvnLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDA 800
Cdd:COG4178 465 EAVglgHLAERLDEEADWDQV--------LSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1290-1511 |
4.35e-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: 76.51 E-value: 4.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDYCLRYreDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHnlRFKITI 1369
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1370 IPQDPVLF---------SGSLRMNLDPfSQYSDEEVWMALELAHLKGFVSALPDKLnhecaeggenlSVGQRQLVCLARA 1440
Cdd:cd03300 77 VFQNYALFphltvfeniAFGLRLKKLP-KAEIKERVAEALDLVQLEGYANRKPSQL-----------SGGQQQRVAIARA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1441 LLRKTKILVLDEATAAVD--------LETDNLIQSTirtqfeDCTVLTIAHRLN---TIMDytRVIVLDKGEVRECGAPS 1509
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDlklrkdmqLELKRLQKEL------GITFVFVTHDQEealTMSD--RIAVMNKGKIQQIGTPE 216
|
..
gi 6678848 1510 EL 1511
Cdd:cd03300 217 EI 218
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
643-850 |
5.13e-15 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 75.28 E-value: 5.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 643 SITVKNATFT----WARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMDKVEGHV----------TLKG 706
Cdd:cd03213 3 TLSFRNLTVTvkssPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVlingrpldkrSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 707 SVAYVPQqawiqndslrENILFGH-PLQEN-YYKAVMeacallpdleilpsgdrteigeKGvnLSGGQKQRVSLARAVYS 784
Cdd:cd03213 83 IIGYVPQ----------DDILHPTlTVRETlMFAAKL----------------------RG--LSGGERKRVSIALELVS 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6678848 785 NSDIYLFDDPLSAVDAHVGKHIfekvvgpMGLLK-----NKTRILVTHGISYL--PQVDVIIVMSGGKISEMG 850
Cdd:cd03213 129 NPSLLFLDEPTSGLDSSSALQV-------MSLLRrladtGRTIICSIHQPSSEifELFDKLLLLSQGRVIYFG 194
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
644-864 |
5.66e-15 |
|
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: 76.82 E-value: 5.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLaEMDKVEGHVTLKG-------------SVAY 710
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvswnsvplqkwrkAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 711 VPQQAWIQNDSLRENI-LFGHPLQENYYKaVMEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIY 789
Cdd:cd03289 82 IPQKVFIFSGTFRKNLdPYGKWSDEEIWK-VAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 790 LFDDPLSAVDAhVGKHIFEKVVGPMglLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAE 864
Cdd:cd03289 161 LLDEPSAHLDP-ITYQVIRKTLKQA--FADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQ 232
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1306-1515 |
7.97e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 76.21 E-value: 7.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSG-SLR-- 1382
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRel 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1383 --------MNL-DPFSQYSDEEVWMALELAHlkgfVSALPDKLnhecaegGENLSVGQRQLVCLARALLRKTKILVLDEA 1453
Cdd:PRK11231 97 vaygrspwLSLwGRLSAEDNARVNQAMEQTR----INHLADRR-------LTDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6678848 1454 TAAVDL----ETDNLIQstiRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELLQQR 1515
Cdd:PRK11231 166 TTYLDInhqvELMRLMR---ELNTQGKTVVTVLHDLNQASRYCdHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
643-881 |
8.06e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 76.46 E-value: 8.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 643 SITVKNATFTWARGEPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS----------VAYVP 712
Cdd:PRK15056 6 GIVVNDVTVTWRNGHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 713 QQAWIQND--SLRENIL----FGHPLQENYYKAVMEAC--ALLPDLEILPSGDRtEIGEkgvnLSGGQKQRVSLARAVYS 784
Cdd:PRK15056 85 QSEEVDWSfpVLVEDVVmmgrYGHMGWLRRAKKRDRQIvtAALARVDMVEFRHR-QIGE----LSGGQKKRVFLARAIAQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 785 NSDIYLFDDPLSAVDAHVGKhifeKVVGPMGLLKN--KTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQ-----ELLD 857
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEA----RIISLLRELRDegKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTEttftaENLE 235
|
250 260
....*....|....*....|....*.
gi 6678848 858 RdgAFAEFLR--TYANAEQDLASEDD 881
Cdd:PRK15056 236 L--AFSGVLRhvALNGSEESIITDDE 259
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
634-850 |
1.52e-14 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 74.49 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 634 RSIKSGEGNSITVKNATFTWARGEPPT---LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVTLKGSVA 709
Cdd:cd03220 8 KSYPTYKGGSSSLKKLGILGRKGEVGEfwaLKDVSFEVPRGERIGLIGRNGAGKSTLLR-LLAGIYPPdSGTVTVRGRVS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 710 YVPQ-QAWIQND-SLRENILFG---HPLQENYYKAVMEacallpdlEILpsgDRTEIGEKG----VNLSGGQKQRVSLAR 780
Cdd:cd03220 87 SLLGlGGGFNPElTGRENIYLNgrlLGLSRKEIDEKID--------EII---EFSELGDFIdlpvKTYSSGMKARLAFAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 781 AVYSNSDIYLFDDPLSAVDAH----VGKHIFEKVvgpmglLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMG 850
Cdd:cd03220 156 ATALEPDILLIDEVLAVGDAAfqekCQRRLRELL------KQGKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
664-858 |
1.58e-14 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 77.07 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 664 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-----------------SVAYVPQQAWI-QNDSLREN 725
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrkgiflppekrRIGYVFQEARLfPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 726 ILFGH-----PLQENYYKAVMEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDA 800
Cdd:TIGR02142 96 LRYGMkrarpSERRISFERVIELLGIGHLLGRLPG-----------RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 801 HVGKHIfekvvgpMGLLKNKTR------ILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLDR 858
Cdd:TIGR02142 165 PRKYEI-------LPYLERLHAefgipiLYVSHSLQEVLRLaDRVVVLEDGRVAAAGPIAEVWAS 222
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
644-845 |
2.08e-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: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWarGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTL--KGSVAYVPQqawiqnds 721
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWgsTVKIGYFEQ-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 722 lrenilfghplqenyykavmeacallpdleilpsgdrteigekgvnLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAH 801
Cdd:cd03221 71 ----------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE 104
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6678848 802 vGKHIFEkvvgpmGLLKN--KTRILVTHGISYLPQV-DVIIVMSGGK 845
Cdd:cd03221 105 -SIEALE------EALKEypGTVILVSHDRYFLDQVaTKIIELEDGK 144
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
1000-1176 |
2.09e-14 |
|
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: 75.54 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1000 PVVNGTQANRNFRLSVYGALGI-----LQGAAIFGYSMAVSIGGIFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFS 1074
Cdd:cd18552 24 PLLDDIFVEKDLEALLLVPLAIiglflLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRIT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1075 KELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLA----TPIAAVIIPPLGL-VYFFVQRFYVASSRQLKRLESVSrspvy 1149
Cdd:cd18552 104 NDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLdwklTLIALVVLPLAALpIRRIGKRLRKISRRSQESMGDLT----- 178
|
170 180 190
....*....|....*....|....*....|.
gi 6678848 1150 SHFNETLLGVSVIRAF----EEQERFIHQSD 1176
Cdd:cd18552 179 SVLQETLSGIRVVKAFgaedYEIKRFRKANE 209
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
643-858 |
2.28e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 76.42 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 643 SITVKNATFTWArGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVTLKGSV-----------AY 710
Cdd:PRK11650 3 GLKLQAVRKSYD-GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLR-MVAGLERItSGEIWIGGRVvnelepadrdiAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 711 VpqqawIQNDSL------RENILFGhpL------QENYYKAVMEACALLpdlEILPSGDRteigeKGVNLSGGQKQRVSL 778
Cdd:PRK11650 81 V-----FQNYALyphmsvRENMAYG--LkirgmpKAEIEERVAEAARIL---ELEPLLDR-----KPRELSGGQRQRVAM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 779 ARAVYSNSDIYLFDDPLSAVDAhvgkhifeKVVGPMGL-LK------NKTRILVTHGisylpQV------DVIIVMSGGK 845
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLDA--------KLRVQMRLeIQrlhrrlKTTSLYVTHD-----QVeamtlaDRVVVMNGGV 212
|
250
....*....|...
gi 6678848 846 ISEMGSYQELLDR 858
Cdd:PRK11650 213 AEQIGTPVEVYEK 225
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
644-858 |
2.69e-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: 75.86 E-value: 2.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKN--ATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSA---LLAEMDKVEGHVTLKGS----------- 707
Cdd:COG0444 2 LEVRNlkVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAilgLLPPPGITSGEILFDGEdllklsekelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 708 ------VAYVPQQAwiQN---------DSLRENILFGHPLQEnyyKAVME-ACALLPDLEILPSGDRteigekgVN---- 767
Cdd:COG0444 82 kirgreIQMIFQDP--MTslnpvmtvgDQIAEPLRIHGGLSK---AEARErAIELLERVGLPDPERR-------LDryph 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 768 -LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIfekvvgpMGLLK------NKTRILVTHGISYLPQV-DVII 839
Cdd:COG0444 150 eLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQI-------LNLLKdlqrelGLAILFITHDLGVVAEIaDRVA 222
|
250
....*....|....*....
gi 6678848 840 VMSGGKISEMGSYQELLDR 858
Cdd:COG0444 223 VMYAGRIVEEGPVEELFEN 241
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1290-1512 |
3.10e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 74.74 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDYCLRYREDLDL-VLKHINVTIEGGEKVGIVGRTGAGKSS---LTLGLFrinESAEGEIIIDGVNIAKIGLHNLRF 1365
Cdd:PRK13642 5 LEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTtarLIDGLF---EEFEGKVKIDGELLTAENVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1366 KITIIPQDP-VLFSGSLRMNLDPFSQYSD----EEVWMALELAHLKgfVSALPDKLNHECaeggeNLSVGQRQLVCLARA 1440
Cdd:PRK13642 82 KIGMVFQNPdNQFVGATVEDDVAFGMENQgiprEEMIKRVDEALLA--VNMLDFKTREPA-----RLSGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 1441 LLRKTKILVLDEATAAVDLETDNLIQSTIRtQFED---CTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELL 1512
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIH-EIKEkyqLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
545-864 |
4.16e-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: 78.03 E-value: 4.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 545 YLAAVGTFTWVCTPFLVALSTFAVFVTVDERnilDAKKAFVSLalfnILRFPLNILPM----VISSIVQASVSLKRLRIF 620
Cdd:TIGR01271 1104 YLSTLRWFQMRIDIIFVFFFIAVTFIAIGTN---QDGEGEVGI----ILTLAMNILSTlqwaVNSSIDVDGLMRSVSRVF 1176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 621 ----LSHEELEPDS------------IERRSIKS--GEGNSITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGC 682
Cdd:TIGR01271 1177 kfidLPQEEPRPSGgggkyqlstvlvIENPHAQKcwPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGS 1256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 683 GKSSLLSALLaEMDKVEGHVTLKG-------------SVAYVPQQAWIQNDSLRENI-LFGHPLQENYYKaVMEACALLP 748
Cdd:TIGR01271 1257 GKSTLLSALL-RLLSTEGEIQIDGvswnsvtlqtwrkAFGVIPQKVFIFSGTFRKNLdPYEQWSDEEIWK-VAEEVGLKS 1334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 749 DLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAhVGKHIFEKVVGPMglLKNKTRILVTHG 828
Cdd:TIGR01271 1335 VIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDP-VTLQIIRKTLKQS--FSNCTVILSEHR 1411
|
330 340 350
....*....|....*....|....*....|....*.
gi 6678848 829 ISYLPQVDVIIVMSGGKISEMGSYQELLDRDGAFAE 864
Cdd:TIGR01271 1412 VEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQ 1447
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
643-866 |
4.16e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 73.51 E-value: 4.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 643 SITVKNATFTWarGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL-LAEMDKvEGHVTLKGS---VAYVPQQAWIQ 718
Cdd:PRK11124 2 SIQLNGINCFY--GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEMPR-SGTLNIAGNhfdFSKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 719 ndSLRENI--------LFGH-PLQENYYKAVM------------EACALLPDLEILPSGDRTEIgekgvNLSGGQKQRVS 777
Cdd:PRK11124 79 --ELRRNVgmvfqqynLWPHlTVQQNLIEAPCrvlglskdqalaRAEKLLERLRLKPYADRFPL-----HLSGGQQQRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 778 LARAVYSNSDIYLFDDPLSAVD----AHVGKHIFEkvVGPMGLlknkTRILVTHgisylpQVDV-------IIVMSGGKI 846
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDpeitAQIVSIIRE--LAETGI----TQVIVTH------EVEVarktasrVVYMENGHI 219
|
250 260
....*....|....*....|.
gi 6678848 847 SEMGSYQELLD-RDGAFAEFL 866
Cdd:PRK11124 220 VEQGDASCFTQpQTEAFKNYL 240
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
652-800 |
5.37e-14 |
|
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: 72.39 E-value: 5.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 652 TWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG------------SVAYVPQQAWIQN 719
Cdd:TIGR01189 7 ACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtplaeqrdepheNILYLGHLPGLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 720 D-SLRENILFGHPLQENYYKAVMEACAL--LPDLEILPSGdrteigekgvNLSGGQKQRVSLARAVYSNSDIYLFDDPLS 796
Cdd:TIGR01189 87 ElSALENLHFWAAIHGGAQRTIEDALAAvgLTGFEDLPAA----------QLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
....
gi 6678848 797 AVDA 800
Cdd:TIGR01189 157 ALDK 160
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
656-856 |
5.45e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 73.51 E-value: 5.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 656 GEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAYVPQQAWIQND-S 721
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarRLALLPQHHLTPEGiT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 722 LRENILFGHP--------LQENYYKAVMEAcalLPDLEIlpsgdrTEIGEKGV-NLSGGQKQRVSLARAVYSNSDIYLFD 792
Cdd:PRK11231 93 VRELVAYGRSpwlslwgrLSAEDNARVNQA---MEQTRI------NHLADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 793 DPLSAVDAHvgkHIFEkVVGPMGLLKN--KTRILVTHGIS----YlpqVDVIIVMSGGKISEMGSYQELL 856
Cdd:PRK11231 164 EPTTYLDIN---HQVE-LMRLMRELNTqgKTVVTVLHDLNqasrY---CDHLVVLANGHVMAQGTPEEVM 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1306-1512 |
5.61e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 73.41 E-value: 5.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINE-----SAEGEIIIDGVNIAKIGLHNLRFKITIIPQDP------ 1374
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnpipnl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1375 -VLFSGSLRMNLDPFSQYSDE---EVWMALELAHLKGFVSalpDKLNhecAEGGEnLSVGQRQLVCLARALLRKTKILVL 1450
Cdd:PRK14247 98 sIFENVALGLKLNRLVKSKKElqeRVRWALEKAQLWDEVK---DRLD---APAGK-LSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 1451 DEATAAVDLETDNLIQSTIRTQFEDCTVLTIAH---RLNTIMDYtrVIVLDKGEVRECGAPSELL 1512
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqQAARISDY--VAFLYKGQIVEWGPTREVF 233
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1306-1511 |
5.63e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 76.63 E-value: 5.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIG-LHNLRFKITIIPQDPVLFSG-SLRM 1383
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQLGIYLVPQEPLLFPNlSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1384 NLD---PFSQYSDEEvwmalelahLKGFVSALPDKLNHECAEGgeNLSVGQRQLVCLARALLRKTKILVLDEATAAVD-L 1459
Cdd:PRK15439 106 NILfglPKRQASMQK---------MKQLLAALGCQLDLDSSAG--SLEVADRQIVEILRGLMRDSRILILDEPTASLTpA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6678848 1460 ETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSEL 1511
Cdd:PRK15439 175 ETERLFSRIRELLAQGVGIVFISHKLPEIRQLAdRISVMRDGTIALSGKTADL 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1306-1503 |
6.27e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.26 E-value: 6.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSltlgLFRI----NESAEGEIIIDGvniakiglhnlRFKITIIPQDPVLFSG-S 1380
Cdd:COG0488 13 LLDDVSLSINPGDRIGLVGRNGAGKST----LLKIlageLEPDSGEVSIPK-----------GLRIGYLPQEPPLDDDlT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1381 LRmnldpfsqysdEEVWMAL-----------ELAHLKGFVSALPDK---LNHECAEGGE--------------------- 1425
Cdd:COG0488 78 VL-----------DTVLDGDaelraleaeleELEAKLAEPDEDLERlaeLQEEFEALGGweaearaeeilsglgfpeedl 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1426 -----NLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTqfEDCTVLTIAH-R--LNTIMdyTRVIVL 1497
Cdd:COG0488 147 drpvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKN--YPGTVLVVSHdRyfLDRVA--TRILEL 222
|
....*.
gi 6678848 1498 DKGEVR 1503
Cdd:COG0488 223 DRGKLT 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
652-794 |
6.38e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.26 E-value: 6.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 652 TWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG--SVAYVPQQAWIQND-SLRENILF 728
Cdd:COG0488 5 SKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLDDDlTVLDTVLD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 729 GHP----LQENYYKAVM-----------------------------EACALLPDLEILPSGDRTEIGEkgvnLSGGQKQR 775
Cdd:COG0488 85 GDAelraLEAELEELEAklaepdedlerlaelqeefealggweaeaRAEEILSGLGFPEEDLDRPVSE----LSGGWRRR 160
|
170
....*....|....*....
gi 6678848 776 VSLARAVYSNSDIYLFDDP 794
Cdd:COG0488 161 VALARALLSEPDLLLLDEP 179
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
661-855 |
7.57e-14 |
|
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: 72.50 E-value: 7.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVTLKGSVAYVP---QQAWIQNDSLreniLFGHPLQENY 736
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLN-LISGLAQpTSGGVILEGKQITEPgpdRMVVFQNYSL----LPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 737 YKAVMEAcalLPDLeilPSGDRTEIGEKGVNL--------------SGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHV 802
Cdd:TIGR01184 76 ALAVDRV---LPDL---SKSERRAIVEEHIALvglteaadkrpgqlSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6678848 803 GKHIFEKVvgpMGLLKNK--TRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQEL 855
Cdd:TIGR01184 150 RGNLQEEL---MQIWEEHrvTVLMVTHDVdEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1305-1527 |
7.71e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 73.58 E-value: 7.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1305 LVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIG-LHNLRFKITIIPQDP--------- 1374
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIRNKAGMVFQNPdnqivativ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1375 ---VLFsGSLRMNLDPfsqysdEEVWMALELAHLKGFVSALPDKLNHEcaeggenLSVGQRQLVCLARALLRKTKILVLD 1451
Cdd:PRK13633 104 eedVAF-GPENLGIPP------EEIRERVDESLKKVGMYEYRRHAPHL-------LSGGQKQRVAIAGILAMRPECIIFD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6678848 1452 EATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQrgifYSMAKDAGL 1527
Cdd:PRK13633 170 EPTAMLDPSGRREVVNTIKelNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE----VEMMKKIGL 243
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
656-794 |
9.37e-14 |
|
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: 72.08 E-value: 9.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 656 GEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS--------------VAYVPQ-QAWIQND 720
Cdd:cd03224 11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEgRRIFPEL 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6678848 721 SLRENILFG-HPLQENYYKAVME-ACALLPDLEilpsgDRteIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDP 794
Cdd:cd03224 91 TVEENLLLGaYARRRAKRKARLErVYELFPRLK-----ER--RKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEP 159
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
661-846 |
1.04e-13 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 72.30 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSAL---LAEMDKVEGHVTLKG----------SVAYVPQQ-AWIQNDSLRENI 726
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNGqprkpdqfqkCVAYVRQDdILLPGLTVRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 727 LF-----GHPLQENYYKAVMEACALLPDLEILPSGdrteiGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAH 801
Cdd:cd03234 103 TYtailrLPRKSSDAIRKKRVEDVLLRDLALTRIG-----GNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6678848 802 VGKHIfekvvgpMGLLK-----NKTRILVTH--GISYLPQVDVIIVMSGGKI 846
Cdd:cd03234 178 TALNL-------VSTLSqlarrNRIVILTIHqpRSDLFRLFDRILLLSSGEI 222
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
654-801 |
1.21e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.44 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 654 ARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLL---SALLAemdKVEGHVTLKG----------SVAYV-PQQAWIQN 719
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLrliAGLLP---PAAGTIKLDGgdiddpdvaeACHYLgHRNAMKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 720 DSLRENILFGHPLQENYYKAVMEA-CAL-LPDLEILPSGdrteigekgvNLSGGQKQRVSLARAVYSNSDIYLFDDPLSA 797
Cdd:PRK13539 88 LTVAENLEFWAAFLGGEELDIAAAlEAVgLAPLAHLPFG----------YLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
....
gi 6678848 798 VDAH 801
Cdd:PRK13539 158 LDAA 161
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
644-856 |
1.64e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 72.71 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWARGEPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQQawIQNDSLR 723
Cdd:PRK13644 2 IRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSK--LQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 724 ENILFGHPLQENYYKAVMEACAL------LPDLEILPSGDRT--EIG-EK-----GVNLSGGQKQRVSLARAVYSNSDIY 789
Cdd:PRK13644 79 VGIVFQNPETQFVGRTVEEDLAFgpenlcLPPIEIRKRVDRAlaEIGlEKyrhrsPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6678848 790 LFDDPLSAVDAHVGKHIFEKVVGPMGllKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELL 856
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHE--KGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
661-846 |
1.72e-13 |
|
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: 69.76 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSvayvPQQAWIQNDSLRENILFGHplQenyykav 740
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK----EVSFASPRDARRAGIAMVY--Q------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 741 meacallpdleilpsgdrteigekgvnLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKvvgpMGLLKN- 819
Cdd:cd03216 83 ---------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKV----IRRLRAq 131
|
170 180 190
....*....|....*....|....*....|..
gi 6678848 820 -KTRILVTHgisYLPQV----DVIIVMSGGKI 846
Cdd:cd03216 132 gVAVIFISH---RLDEVfeiaDRVTVLRDGRV 160
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1306-1514 |
1.75e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 73.60 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSS---LTLGLfriNESAEGEIIIDGVNIAKIGLHNLrfKITIIPQDPVLFSG--- 1379
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTvlrLVAGL---EKPTEGQIFIDGEDVTHRSIQQR--DICMVFQSYALFPHmsl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1380 ------SLRMNLDPFSQYSdEEVWMALELAHLKGFVSALPDKLnhecaeggenlSVGQRQLVCLARALLRKTKILVLDEA 1453
Cdd:PRK11432 96 genvgyGLKMLGVPKEERK-QRVKEALELVDLAGFEDRYVDQI-----------SGGQQQRVALARALILKPKVLLFDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6678848 1454 TAAVDLETDNLIQSTIR---TQFeDCTVLTIAHrlntimDYTR-------VIVLDKGEVRECGAPSELLQQ 1514
Cdd:PRK11432 164 LSNLDANLRRSMREKIRelqQQF-NITSLYVTH------DQSEafavsdtVIVMNKGKIMQIGSPQELYRQ 227
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1306-1512 |
1.85e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 72.00 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGV------NIAKIGLHNLRFKITIIPQDPVLFSG 1379
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1380 -SLRMNLD-PFSQY---SDEEVWMALELAHLK-GFVSALPDKLNHECAEggenLSVGQRQLVCLARALLRKTKILVLDEA 1453
Cdd:PRK14246 105 lSIYDNIAyPLKSHgikEKREIKKIVEECLRKvGLWKEVYDRLNSPASQ----LSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6678848 1454 TAAVDLETDNLIQSTIRTQFEDCTVLTIAH---RLNTIMDYtrVIVLDKGEVRECGAPSELL 1512
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEIAIVIVSHnpqQVARVADY--VAFLYNGELVEWGSSNEIF 240
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1305-1506 |
1.94e-13 |
|
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: 71.24 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1305 LVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRfKITIIPQDPVLFSG-SLRM 1383
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARR-RLGFVSDSTGLYDRlTARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1384 NLDPFSQYsdeevwMALELAHLKGFVSALPDKL--NHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET 1461
Cdd:cd03266 98 NLEYFAGL------YGLKGDELTARLEELADRLgmEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 6678848 1462 DNLIQSTIRTQFED-CTVLTIAHRLNTIMDYT-RVIVLDKGEVRECG 1506
Cdd:cd03266 172 TRALREFIRQLRALgKCILFSTHIMQEVERLCdRVVVLHRGRVVYEG 218
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1306-1512 |
1.96e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 72.41 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAK--------------------IGLHNLRF 1365
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnraqrkafrrdiqmvfqdsISAVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1366 KITIIPQDPvlfsgsLR--MNLDPFSQYSdeevwMALELAHLKGFVSALPDKLNHEcaeggenLSVGQRQLVCLARALLR 1443
Cdd:PRK10419 107 TVREIIREP------LRhlLSLDKAERLA-----RASEMLRAVDLDDSVLDKRPPQ-------LSGGQLQRVCLARALAV 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6678848 1444 KTKILVLDEATAAVDLetdnLIQSTI-------RTQFeDCTVLTIAHRLNTIMDY-TRVIVLDKGEVRECGAPSELL 1512
Cdd:PRK10419 169 EPKLLILDEAVSNLDL----VLQAGVirllkklQQQF-GTACLFITHDLRLVERFcQRVMVMDNGQIVETQPVGDKL 240
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1044-1452 |
2.14e-13 |
|
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: 74.83 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1044 RLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVdSMIPQVIKMFMGSLFSVIGAVI-IILLATPIAAVIIPPLGLV 1122
Cdd:COG4615 82 RLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTI-SQAFVRLPELLQSVALVLGCLAyLAWLSPPLFLLTLVLLGLG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1123 yFFVQRFYVASSRQLKRLESVSRSPVYSHFNetllgvSVIRAFEE----QER--FIHQSDLKV------DENQKAYYPSI 1190
Cdd:COG4615 161 -VAGYRLLVRRARRHLRRAREAEDRLFKHFR------ALLEGFKElklnRRRrrAFFDEDLQPtaeryrDLRIRADTIFA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1191 VANRWlavrlecvGNCIVLFA---ALFAVISRHSLSAGLVglsVSYSL----------QITAYLNWLVRMSsemetniVA 1257
Cdd:COG4615 234 LANNW--------GNLLFFALiglILFLLPALGWADPAVL---SGFVLvllflrgplsQLVGALPTLSRAN-------VA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1258 VERLKEYSETEKEAPWQIQETAPPSTWPHSGRVEFRDYCLRYREDLD---LVLKHINVTIEGGEKVGIVGRTGAGKSSLT 1334
Cdd:COG4615 296 LRKIEELELALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGdegFTLGPIDLTIRRGELVFIVGGNGSGKSTLA 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1335 ---LGLFRineSAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSGslrmNLDPFSQYSDEEV--WMA-LELAHLKGF 1408
Cdd:COG4615 376 kllTGLYR---PESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDR----LLGLDGEADPARAreLLErLELDHKVSV 448
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 6678848 1409 vsalpdklnhecaEGGE----NLSVGQRQLVCLARALLRKTKILVLDE 1452
Cdd:COG4615 449 -------------EDGRfsttDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1306-1521 |
2.18e-13 |
|
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: 75.72 E-value: 2.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGvniakiglhnlrfKITIIPQDPVLFSGSLRMNL 1385
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1386 DPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLI 1465
Cdd:TIGR01271 508 IFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI 587
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6678848 1466 qstirtqFEDC--------TVLTIAHRLNTIMDYTRVIVLDKGEVRECGAPSELLQQRGIFYSM 1521
Cdd:TIGR01271 588 -------FESClcklmsnkTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSL 644
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1272-1506 |
2.21e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 74.74 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1272 PWQIQETAPPSTWPHSGRVEF--RDYCLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESaEGEII 1349
Cdd:PRK15134 265 PVPLPEPASPLLDVEQLQVAFpiRKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-QGEIW 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1350 IDGVNiakigLHNL--------RFKITIIPQDPvlfSGSL--RMNLDPF-------------SQYSDEEVWMALELAHLK 1406
Cdd:PRK15134 344 FDGQP-----LHNLnrrqllpvRHRIQVVFQDP---NSSLnpRLNVLQIieeglrvhqptlsAAQREQQVIAVMEEVGLD 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1407 gfvsalPDKLNHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRT--QFEDCTVLTIAHR 1484
Cdd:PRK15134 416 ------PETRHRYPAE----FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSlqQKHQLAYLFISHD 485
|
250 260
....*....|....*....|...
gi 6678848 1485 LNTIMDYT-RVIVLDKGEVRECG 1506
Cdd:PRK15134 486 LHVVRALChQVIVLRQGEVVEQG 508
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
658-846 |
2.46e-13 |
|
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: 69.77 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 658 PPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS--------------VAYVPQqawiqnDSLR 723
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtrrsprdairagIAYVPE------DRKR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 724 ENILFGHPLQENyykavmeacALLPDLeilpsgdrteigekgvnLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDahVG 803
Cdd:cd03215 87 EGLVLDLSVAEN---------IALSSL-----------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVD--VG 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6678848 804 --KHIFEKVVgpmgLL--KNKTRILVThgiSYLPQV----DVIIVMSGGKI 846
Cdd:cd03215 139 akAEIYRLIR----ELadAGKAVLLIS---SELDELlglcDRILVMYEGRI 182
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
644-848 |
2.49e-13 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 70.85 E-value: 2.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWARGePPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG---------SVAY---- 710
Cdd:COG2884 2 IRFENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsrlkrrEIPYlrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 711 ---VPQQAW-IQNDSLRENILFghPLQ------ENYYKAVMEACALLpdleilpsgdrtEIGEKG----VNLSGGQKQRV 776
Cdd:COG2884 81 igvVFQDFRlLPDRTVYENVAL--PLRvtgksrKEIRRRVREVLDLV------------GLSDKAkalpHELSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6678848 777 SLARAVYSNSDIYLFDDPLSAVDAHVGKHIfekvvgpMGLLK--NK---TRILVTHGISYLPQVDV-IIVMSGGKISE 848
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETSWEI-------MELLEeiNRrgtTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
642-867 |
3.00e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 71.69 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 642 NSITVKNATFTWARGEPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQQAWIQNds 721
Cdd:PRK13647 3 NIIEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRS-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 722 lRENILFGHPLQENYYKAVMEACALLP-DLEILPS--GDRTEIGEKGVN-----------LSGGQKQRVSLARAVYSNSD 787
Cdd:PRK13647 80 -KVGLVFQDPDDQVFSSTVWDDVAFGPvNMGLDKDevERRVEEALKAVRmwdfrdkppyhLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 788 IYLFDDPLSAVDAHVGKHIFEKVVGpmglLKN--KTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQELLDRDGAFAE 864
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDR----LHNqgKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDEDIVEQA 234
|
...
gi 6678848 865 FLR 867
Cdd:PRK13647 235 GLR 237
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
642-855 |
3.40e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 71.66 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 642 NSITVKNATFTWARGE----PPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQQAW- 716
Cdd:PRK13633 3 EMIKCKNVSYKYESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 717 IQNdslRENILFGHPLQENYYKAVMEACALLPD-LEILPSGDRTEIGE--KGVN-----------LSGGQKQRVSLARAV 782
Cdd:PRK13633 83 IRN---KAGMVFQNPDNQIVATIVEEDVAFGPEnLGIPPEEIRERVDEslKKVGmyeyrrhaphlLSGGQKQRVAIAGIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6678848 783 YSNSDIYLFDDPLSAVDAhVGKhifEKVVGPMGLLKNK---TRILVTHGISYLPQVDVIIVMSGGKISEMGSYQEL 855
Cdd:PRK13633 160 AMRPECIIFDEPTAMLDP-SGR---REVVNTIKELNKKygiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
644-862 |
3.51e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 73.34 E-value: 3.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTwaRGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-------------SVAY 710
Cdd:PRK09536 4 IDVSDLSVE--FGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraasrRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 711 VPQQAWIQND-SLRENILFGH--------PLQENYYKAVMEAcallpdleiLPSGDRTEIGEKGV-NLSGGQKQRVSLAR 780
Cdd:PRK09536 82 VPQDTSLSFEfDVRQVVEMGRtphrsrfdTWTETDRAAVERA---------MERTGVAQFADRPVtSLSGGERQRVLLAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 781 AVYSNSDIYLFDDPLSAVDAHVGKHIFEKVvgpMGLLKN-KTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQELLDR 858
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQVRTLELV---RRLVDDgKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLTA 229
|
....*..
gi 6678848 859 D---GAF 862
Cdd:PRK09536 230 DtlrAAF 236
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1290-1512 |
3.82e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 71.69 E-value: 3.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDYCLRYREDLDlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITI 1369
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1370 IPQDP--VLFS---------GSLRMNLDPfsQYSDEEVWMALELAHLKgfvsALPDKLNHecaeggeNLSVGQRQLVCLA 1438
Cdd:PRK13647 84 VFQDPddQVFSstvwddvafGPVNMGLDK--DEVERRVEEALKAVRMW----DFRDKPPY-------HLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6678848 1439 RALLRKTKILVLDEATAAVDLE-TDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELL 1512
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRgQETLMEILDRLHNQGKTVIVATHDVDLAAEWAdQVIVLKEGRVLAEGDKSLLT 226
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
972-1260 |
3.99e-13 |
|
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: 71.67 E-value: 3.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 972 FLSIFLFLCNHVSALASNYWLSLWTDDPPVVNGTQANRNFRlSVYGALGILQG----AAIFGYSMAVSIGGI--FASRRL 1045
Cdd:cd18547 2 ILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGVDFS-GLLRILLLLLGlyllSALFSYLQNRLMARVsqRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1046 HLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATP----IAAVIIPPLGL 1121
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPlltlIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1122 VYFFV----QRFYVASSRQLKRLEsvsrspvySHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWL- 1196
Cdd:cd18547 161 VTKFIakrsQKYFRKQQKALGELN--------GYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLm 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6678848 1197 -AVRLecVGN----CIVLFAALFAVisRHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVER 1260
Cdd:cd18547 233 pIMNF--INNlgyvLVAVVGGLLVI--NGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAER 297
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1290-1514 |
4.53e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 71.37 E-value: 4.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDYCLRYREDLDlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITI 1369
Cdd:PRK13652 4 IETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1370 IPQDP--VLFSGSLRMNL--DPFSQYSDEEV--WMALELAHLKGfVSALPDKLNHecaeggeNLSVGQRQLVCLARALLR 1443
Cdd:PRK13652 83 VFQNPddQIFSPTVEQDIafGPINLGLDEETvaHRVSSALHMLG-LEELRDRVPH-------HLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6678848 1444 KTKILVLDEATAAVDLETDNLIQSTIRTQFED--CTVLTIAHRLNTI---MDYtrVIVLDKGEVRECGAPSELLQQ 1514
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVpemADY--IYVMDKGRIVAYGTVEEIFLQ 228
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
661-856 |
4.72e-13 |
|
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: 71.14 E-value: 4.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-----------------SVAYVPQQ-AWIQNDSL 722
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaamsrkelrelrrkKISMVFQSfALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 723 RENILF-----GHPLQENYYKA--VMEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNSDIYLFDDPL 795
Cdd:cd03294 120 LENVAFglevqGVPRAEREERAaeALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6678848 796 SAVDAHVGKHIFEKVVGPMGLLKnKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELL 856
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAELQ-KTIVFITHDLDEALRLgDRIAIMKDGRLVQVGTPEEIL 249
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1306-1506 |
4.76e-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: 70.25 E-value: 4.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLhNLRFKITIIPQDPVLFSGSLrMNL 1385
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGL-GGGFNPELTGRENIYLNGRL-LGL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1386 DPfsQYSDEEVWMALELAHLKGFVSaLPDKlnhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLI 1465
Cdd:cd03220 115 SR--KEIDEKIDEIIEFSELGDFID-LPVK----------TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKC 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6678848 1466 QSTIRTQFEDC-TVLTIAHRLNTIMDY-TRVIVLDKGEVRECG 1506
Cdd:cd03220 182 QRRLRELLKQGkTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1306-1512 |
4.83e-13 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 70.40 E-value: 4.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNL-RFKITIIPQDPVLFSG-SLRM 1383
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSlTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1384 NLD--PFSQYSDEEVWMALELAH-----LKgfvsalpDKLNHEcaeGGeNLSVGQRQLVCLARALLRKTKILVLDEATAA 1456
Cdd:COG0410 98 NLLlgAYARRDRAEVRADLERVYelfprLK-------ERRRQR---AG-TLSGGEQQMLAIGRALMSRPKLLLLDEPSLG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6678848 1457 -----VDletdnLIQSTIRT-QFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELL 1512
Cdd:COG0410 167 lapliVE-----EIFEIIRRlNREGVTILLVEQNARFALEIAdRAYVLERGRIVLEGTAAELL 224
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1306-1502 |
5.01e-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: 69.50 E-value: 5.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSL--TLGLFRINESAEGEIIIDGVNIakiGLHNLRFKITIIPQDPVLFSgslrm 1383
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLlnALAGRRTGLGVSGEVLINGRPL---DKRSFRKIIGYVPQDDILHP----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1384 NLDPFsqysdEEVWMAlelAHLKGfvsalpdklnhecaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDN 1463
Cdd:cd03213 96 TLTVR-----ETLMFA---AKLRG-------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6678848 1464 LIQSTIRtQFED--CTVLTIAHRLNTIMDYT--RVIVLDKGEV 1502
Cdd:cd03213 149 QVMSLLR-RLADtgRTIICSIHQPSSEIFELfdKLLLLSQGRV 190
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1288-1511 |
5.31e-13 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 72.41 E-value: 5.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1288 GRVEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLtL----GLFRINEsaeGEIIIDGVNIAkiGLHNL 1363
Cdd:COG3839 2 ASLELENVSKSYGGVE--ALKDIDLDIEDGEFLVLLGPSGCGKSTL-LrmiaGLEDPTS---GEILIGGRDVT--DLPPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1364 RFKITIIPQDPVLF----------SGsLRMnldpfSQYSDEEV-----WMA--LELAHLkgfvsalpdkLNHECAEggen 1426
Cdd:COG3839 74 DRNIAMVFQSYALYphmtvyeniaFP-LKL-----RKVPKAEIdrrvrEAAelLGLEDL----------LDRKPKQ---- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1427 LSVGQRQLVCLARALLRKTKILVLDEATAAVD----LETdnliqstiRTQfedctvltIA---HRLNTIMDY-------- 1491
Cdd:COG3839 134 LSGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrVEM--------RAE--------IKrlhRRLGTTTIYvthdqvea 197
|
250 260
....*....|....*....|....
gi 6678848 1492 ----TRVIVLDKGEVRECGAPSEL 1511
Cdd:COG3839 198 mtlaDRIAVMNDGRIQQVGTPEEL 221
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
661-885 |
5.37e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 70.97 E-value: 5.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSAL-----LAEMDKVEGHVTLKGSVAYVP---------------QQAWIQND 720
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrlndLIPGFRVEGKVTFHGKNLYAPdvdpvevrrrigmvfQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 721 SLRENILFGHPLqeNYYKAVMEAC-------ALLPDlEIlpsgdRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDD 793
Cdd:PRK14243 106 SIYDNIAYGARI--NGYKGDMDELverslrqAALWD-EV-----KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 794 PLSAVDAHVGKHIFEKvvgpMGLLKNK-TRILVTHGISYLPQVDVIIVMSGGKISEMGSyqelldRDGAFAEFLRTYA-- 870
Cdd:PRK14243 178 PCSALDPISTLRIEEL----MHELKEQyTIIIVTHNMQQAARVSDMTAFFNVELTEGGG------RYGYLVEFDRTEKif 247
|
250
....*....|....*
gi 6678848 871 NAEQDLASEdDSVSG 885
Cdd:PRK14243 248 NSPQQQATR-DYVSG 261
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
656-854 |
5.37e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 70.13 E-value: 5.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 656 GEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS-------------VAYVPQQAWIQNDSL 722
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdistlkpeiyrqqVSYCAQTPTLFGDTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 723 RENILFghPLQENYYKAVMEAcaLLPDLEI--LPSgdrtEIGEKGVN-LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVD 799
Cdd:PRK10247 98 YDNLIF--PWQIRNQQPDPAI--FLDDLERfaLPD----TILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 800 AHvGKHIFEKVVGPMGLLKNKTRILVTHGISYLPQVDVIIVMSggkiSEMGSYQE 854
Cdd:PRK10247 170 ES-NKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQ----PHAGEMQE 219
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
643-855 |
5.79e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 72.37 E-value: 5.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 643 SITVKNATFTWarGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLS--ALLAE------------MDKVEghvTLKGSV 708
Cdd:PRK11000 3 SVTLRNVTKAY--GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRmiAGLEDitsgdlfigekrMNDVP---PAERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 709 AYVPQQ-AWIQNDSLRENILFGHPL----QENYYKAVMEACALLPDLEILpsgDRteigeKGVNLSGGQKQRVSLARAVY 783
Cdd:PRK11000 78 GMVFQSyALYPHLSVAENMSFGLKLagakKEEINQRVNQVAEVLQLAHLL---DR-----KPKALSGGQRQRVAIGRTLV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6678848 784 SNSDIYLFDDPLSAVDA--HVGKHI----FEKVVGpmgllknKTRILVTHG-ISYLPQVDVIIVMSGGKISEMGSYQEL 855
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDAalRVQMRIeisrLHKRLG-------RTMIYVTHDqVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
642-858 |
6.12e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 70.33 E-value: 6.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 642 NSITVKNATFTWarGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEM---DKVEGHVTLKGS--------- 707
Cdd:PRK14247 2 NKIEIRDLKVSF--GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELypeARVSGEVYLDGQdifkmdvie 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 708 -------VAYVPQQawIQNDSLRENILFGHPLQ---------ENYYKAVMEACALLPDLEilpsgDRteIGEKGVNLSGG 771
Cdd:PRK14247 80 lrrrvqmVFQIPNP--IPNLSIFENVALGLKLNrlvkskkelQERVRWALEKAQLWDEVK-----DR--LDAPAGKLSGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 772 QKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVvgpMGLLKNKTRILVTHgisYLPQV----DVIIVMSGGKIS 847
Cdd:PRK14247 151 QQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLF---LELKKDMTIVLVTH---FPQQAarisDYVAFLYKGQIV 224
|
250
....*....|.
gi 6678848 848 EMGSYQELLDR 858
Cdd:PRK14247 225 EWGPTREVFTN 235
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
1018-1261 |
6.18e-13 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 71.31 E-value: 6.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1018 ALGILQGAAIFGYSMAVSIGGIFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFS 1097
Cdd:cd18542 47 GVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1098 VIGAVIIIL-----LATpIAAVIIPPLGLV-YFF---VQRFYVASSRQLKRLESVsrspvyshFNETLLGVSVIRAF--- 1165
Cdd:cd18542 127 FIGALIIMFsinwkLTL-ISLAIIPFIALFsYVFfkkVRPAFEEIREQEGELNTV--------LQENLTGVRVVKAFare 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1166 -EEQERFIHQSDLKVDENQKA------YYPSIVAnrwlavrLECVGNCIVLFAALFAVIsRHSLSAG-LVGLSvSYslqi 1237
Cdd:cd18542 198 dYEIEKFDKENEEYRDLNIKLakllakYWPLMDF-------LSGLQIVLVLWVGGYLVI-NGEITLGeLVAFI-SY---- 264
|
250 260
....*....|....*....|....*...
gi 6678848 1238 TAYLNWLVRMS----SEMETNIVAVERL 1261
Cdd:cd18542 265 LWMLIWPVRQLgrliNDMSRASASAERI 292
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1297-1470 |
7.04e-13 |
|
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: 68.92 E-value: 7.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1297 LRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSL--TL-GLFRineSAEGEIIIDGVNIAKIglhnlrfkiTIIPQD 1373
Cdd:TIGR01189 6 LACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLlrILaGLLR---PDSGEVRWNGTPLAEQ---------RDEPHE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1374 PVLFSG---------SLRMNLD---PFSQYSDEEVWMALELAHLKGFvSALPdklnheCAEggenLSVGQRQLVCLARAL 1441
Cdd:TIGR01189 74 NILYLGhlpglkpelSALENLHfwaAIHGGAQRTIEDALAAVGLTGF-EDLP------AAQ----LSAGQQRRLALARLW 142
|
170 180
....*....|....*....|....*....
gi 6678848 1442 LRKTKILVLDEATAAVDLETDNLIQSTIR 1470
Cdd:TIGR01189 143 LSRRPLWILDEPTTALDKAGVALLAGLLR 171
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1307-1458 |
7.62e-13 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 69.05 E-value: 7.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1307 LKHINVTIEGGEKVGIVGRTGAGKSSL---TLGLFRINESAEGEIIIDGVNIAKIGLHnlRFKITIIPQDPVLFS----- 1378
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLlaaIAGTLSPAFSASGEVLLNGRRLTALPAE--QRRIGILFQDDLLFPhlsvg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1379 GSLRMNLDPFSQYSD--EEVWMALELAHLKGFVSALPDklnhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEATAA 1456
Cdd:COG4136 95 ENLAFALPPTIGRAQrrARVEQALEEAGLAGFADRDPA-----------TLSGGQRARVALLRALLAEPRALLLDEPFSK 163
|
..
gi 6678848 1457 VD 1458
Cdd:COG4136 164 LD 165
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
659-827 |
9.33e-13 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 68.97 E-value: 9.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 659 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-SVAYVPQQA----------------WIQNDS 721
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqDVSDLRGRAipylrrkigvvfqdfrLLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 722 LRENILF-----GHPLQEnYYKAVMEACALLpdleilpsGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLS 796
Cdd:cd03292 95 VYENVAFalevtGVPPRE-IRKRVPAALELV--------GLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 6678848 797 AVDAHVGKHIfekvvgpMGLLK--NK---TRILVTH 827
Cdd:cd03292 166 NLDPDTTWEI-------MNLLKkiNKagtTVVVATH 194
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
656-856 |
9.37e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 70.00 E-value: 9.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 656 GEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAY----------VPQQAWIQNDSLREN 725
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkVADKNQLRLLRTRLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 726 ILFGH-------PLQENyykaVMEACALLPDLEILPSGDRTE-------IGEKG-----VNLSGGQKQRVSLARAVYSNS 786
Cdd:PRK10619 96 MVFQHfnlwshmTVLEN----VMEAPIQVLGLSKQEARERAVkylakvgIDERAqgkypVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6678848 787 DIYLFDDPLSAVDAH-VGK--HIFEKVVGpmgllKNKTRILVTHGISYLPQVDV-IIVMSGGKISEMGSYQELL 856
Cdd:PRK10619 172 EVLLFDEPTSALDPElVGEvlRIMQQLAE-----EGKTMVVVTHEMGFARHVSShVIFLHQGKIEEEGAPEQLF 240
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
643-854 |
9.87e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 70.46 E-value: 9.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 643 SITVKNATFTWARGEP---PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG------------- 706
Cdd:PRK13637 2 SIKIENLTHIYMEGTPfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 707 --SVAYVPQQAWIQ--NDSLRENILFGhPLQ--------ENYYKAVMEACALlpdleilpsgDRTEIGEKG-VNLSGGQK 773
Cdd:PRK13637 82 rkKVGLVFQYPEYQlfEETIEKDIAFG-PINlglseeeiENRVKRAMNIVGL----------DYEDYKDKSpFELSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 774 QRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKvVGPMGLLKNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSY 852
Cdd:PRK13637 151 RRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNK-IKELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTP 229
|
..
gi 6678848 853 QE 854
Cdd:PRK13637 230 RE 231
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
656-857 |
1.03e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 69.87 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 656 GEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL-----LAEMDKVEGHVTLKGSVAYVPQQAWIQ------------ 718
Cdd:PRK14267 15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRNIYSPDVDPIEvrrevgmvfqyp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 719 ----NDSLRENILFGHPLQ---------ENYYKAVMEACALLPDLEilpsgDRteIGEKGVNLSGGQKQRVSLARAVYSN 785
Cdd:PRK14267 95 npfpHLTIYDNVAIGVKLNglvkskkelDERVEWALKKAALWDEVK-----DR--LNDYPSNLSGGQRQRLVIARALAMK 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6678848 786 SDIYLFDDPLSAVDAhVGKHIFEKVVgpMGLLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLD 857
Cdd:PRK14267 168 PKILLMDEPTANIDP-VGTAKIEELL--FELKKEYTIVLVTHSPAQAARVsDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1307-1485 |
1.05e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 69.80 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1307 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINE-----SAEGEIIIDGVNI--AKIGLHNLRFKITIIPQDPVLFSG 1379
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1380 S--------LRMNLDPFSQYSDEEVWMALELAHLKGFVSalpDKLnHECAEGgenLSVGQRQLVCLARALLRKTKILVLD 1451
Cdd:PRK14239 101 SiyenvvygLRLKGIKDKQVLDEAVEKSLKGASIWDEVK---DRL-HDSALG---LSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190
....*....|....*....|....*....|....
gi 6678848 1452 EATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRL 1485
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
656-827 |
1.14e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 69.80 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 656 GEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALlAEMDKVEGHVTLKGSVAY---------------------VPQQ 714
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSI-NRMNDLNPEVTITGSIVYnghniysprtdtvdlrkeigmVFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 715 AWIQNDSLRENILFGHPLQENYYKAVMEAcALLPDLEILPSGD--RTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFD 792
Cdd:PRK14239 95 PNPFPMSIYENVVYGLRLKGIKDKQVLDE-AVEKSLKGASIWDevKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 6678848 793 DPLSAVDAHVGKHIFEKVVGpmglLKNK-TRILVTH 827
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLG----LKDDyTMLLVTR 205
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
643-857 |
1.43e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 70.51 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 643 SITVKNATFtWARgePPTL---NGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-SVAYVPQQAW-- 716
Cdd:PRK15079 19 DIKDGKQWF-WQP--PKTLkavDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGkDLLGMKDDEWra 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 717 ----IQ---NDSL-----RENI--LFGHPLQeNYY------------KAVMEACALLPDLeilpsgdrteIGEKGVNLSG 770
Cdd:PRK15079 96 vrsdIQmifQDPLaslnpRMTIgeIIAEPLR-TYHpklsrqevkdrvKAMMLKVGLLPNL----------INRYPHEFSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 771 GQKQRVSLARAVYSNSDIYLFDDPLSAVDAhvgkHIFEKVVgpmGLLKNKTR------ILVTHGISYLPQV-DVIIVMSG 843
Cdd:PRK15079 165 GQCQRIGIARALILEPKLIICDEPVSALDV----SIQAQVV---NLLQQLQRemglslIFIAHDLAVVKHIsDRVLVMYL 237
|
250
....*....|....
gi 6678848 844 GKISEMGSYQELLD 857
Cdd:PRK15079 238 GHAVELGTYDEVYH 251
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1309-1514 |
1.44e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 68.84 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1309 HINVTIEGGEKVGIVGRTGAGKSSLtLGL---FRINESaeGEIIIDGVNiakiglHNL----RFKITIIPQDPVLFSG-S 1380
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTL-LNLiagFLTPAS--GSLTLNGQD------HTTtppsRRPVSMLFQENNLFSHlT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1381 LRMN----LDPFSQYSDEEVWMALELAHLKGfVSALPDKLNHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAA 1456
Cdd:PRK10771 88 VAQNiglgLNPGLKLNAAQREKLHAIARQMG-IEDLLARLPGQ-------LSGGQRQRVALARCLVREQPILLLDEPFSA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6678848 1457 VD----LETDNLIQSTIRTQfeDCTVLTIAHRLNTIMDY-TRVIVLDKGEVRECGAPSELLQQ 1514
Cdd:PRK10771 160 LDpalrQEMLTLVSQVCQER--QLTLLMVSHSLEDAARIaPRSLVVADGRIAWDGPTDELLSG 220
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1297-1492 |
1.46e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 69.68 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1297 LRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINEsAEGEIIIDG--------VNIAKIGLHNLRFKIT 1368
Cdd:PRK14258 13 LSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGrveffnqnIYERRVNLNRLRRQVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1369 IIPQDPVLFsgslrmnldPFSQYSDEEVWMALELAH----LKGFVSA------LPDKLNHECAEGGENLSVGQRQLVCLA 1438
Cdd:PRK14258 92 MVHPKPNLF---------PMSVYDNVAYGVKIVGWRpkleIDDIVESalkdadLWDEIKHKIHKSALDLSGGQQQRLCIA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6678848 1439 RALLRKTKILVLDEATAAVD----LETDNLIQS-TIRTQFEDCTVLTIAHRLNTIMDYT 1492
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDpiasMKVESLIQSlRLRSELTMVIVSHNLHQVSRLSDFT 221
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
614-857 |
1.58e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 70.63 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 614 LKRLRIFLSHEELEPDSIERRSI--------KSGEGNSITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKS 685
Cdd:PRK13536 2 LTRAVAEEAPRRLELSPIERKHQgiseakasIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 686 SLLSALLAEMDKVEGHVTLKGsvAYVPQQAWI---------QNDSL------RENIL-FGHplqenYYK-AVMEACALLP 748
Cdd:PRK13536 82 TIARMILGMTSPDAGKITVLG--VPVPARARLararigvvpQFDNLdleftvRENLLvFGR-----YFGmSTREIEAVIP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 749 DL---EILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVGPmgLLKNKTRILV 825
Cdd:PRK13536 155 SLlefARLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSL--LARGKTILLT 228
|
250 260 270
....*....|....*....|....*....|....
gi 6678848 826 THGISYLPQV-DVIIVMSGG-KISEmGSYQELLD 857
Cdd:PRK13536 229 THFMEEAERLcDRLCVLEAGrKIAE-GRPHALID 261
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
651-857 |
1.78e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 72.00 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 651 FTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL---LAEMDKVEGHVTLKGSVAYVPQQ----AWIQNDSL- 722
Cdd:TIGR00955 31 FCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALafrSPKGVKGSGSVLLNGMPIDAKEMraisAYVQQDDLf 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 723 ------RENILF-GH-PLQENYYKAV-MEAC-ALLPDLEILPSGDrTEIGEKGV--NLSGGQKQRVSLARAVYSNSDIYL 790
Cdd:TIGR00955 111 iptltvREHLMFqAHlRMPRRVTKKEkRERVdEVLQALGLRKCAN-TRIGVPGRvkGLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6678848 791 FDDPLSAVDAHVGKHifekVVGPMGLL--KNKTRILVTHGISY--LPQVDVIIVMSGGKISEMGSYQELLD 857
Cdd:TIGR00955 190 CDEPTSGLDSFMAYS----VVQVLKGLaqKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1308-1511 |
1.81e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 70.51 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1308 KHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIG---LHNLRFKITIIPQDPvLFSGSLRMN 1384
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKddeWRAVRSDIQMIFQDP-LASLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1385 L-----DPFSQY----SDEEVWMALELAHLKgfVSALPDKLN---HEcaeggenLSVGQRQLVCLARALLRKTKILVLDE 1452
Cdd:PRK15079 117 IgeiiaEPLRTYhpklSRQEVKDRVKAMMLK--VGLLPNLINrypHE-------FSGGQCQRIGIARALILEPKLIICDE 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6678848 1453 ATAAVDLETD----NLIQSTIRTQfeDCTVLTIAHRLNT---IMDytRVIVLDKGEVRECGAPSEL 1511
Cdd:PRK15079 188 PVSALDVSIQaqvvNLLQQLQREM--GLSLIFIAHDLAVvkhISD--RVLVMYLGHAVELGTYDEV 249
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1306-1503 |
1.94e-12 |
|
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: 68.08 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIA-----KIGL----HNLRFKITIIPQdpVL 1376
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDiaarnRIGYlpeeRGLYPKMKVIDQ--LV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1377 FSGSLR-MNLDPFSQYSDEevWM-ALELAHLKGfvsalpDKLnhecaeggENLSVGQRQLVCLARALLRKTKILVLDEAT 1454
Cdd:cd03269 93 YLAQLKgLKKEEARRRIDE--WLeRLELSEYAN------KRV--------EELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6678848 1455 AAVDLETDNLIQSTIRTQFED-CTVLTIAHRLNTIMDY-TRVIVLDKGEVR 1503
Cdd:cd03269 157 SGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEELcDRVLLLNKGRAV 207
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
644-850 |
2.08e-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: 67.99 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWARGEppTLNGITFSIPEGaLVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS------------VAYV 711
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqpqklrrrIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 712 PQQ-AWIQNDSLRENIlfghplqenYYKAVM----------EACALLPDLEILPSGDRtEIGEkgvnLSGGQKQRVSLAR 780
Cdd:cd03264 78 PQEfGVYPNFTVREFL---------DYIAWLkgipskevkaRVDEVLELVNLGDRAKK-KIGS----LSGGMRRRVGIAQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6678848 781 AVYSNSDIYLFDDPLSAVDAhVGKHIFEKVVGPMGllKNKTRILVTHGISylpqvDV------IIVMSGGKISEMG 850
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDP-EERIRFRNLLSELG--EDRIVILSTHIVE-----DVeslcnqVAVLNKGKLVFEG 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
658-875 |
2.24e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.20 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 658 PPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS--------------VAYVP----QQAWIQN 719
Cdd:COG1129 265 GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprdairagIAYVPedrkGEGLVLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 720 DSLRENIL------FGHPLQENYYKAVMEACALLPDLEILPSGDRTEIGekgvNLSGGQKQRVSLARAVYSNSDIYLFDD 793
Cdd:COG1129 345 LSIRENITlasldrLSRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 794 PLSAVDahVG-KH-IFEKVvgpMGLLKNKTRILVthgIS-YLPQV----DVIIVMSGGKISEMgsyqelLDRDGAFAEFL 866
Cdd:COG1129 421 PTRGID--VGaKAeIYRLI---RELAAEGKAVIV---ISsELPELlglsDRILVMREGRIVGE------LDREEATEEAI 486
|
....*....
gi 6678848 867 RTYANAEQD 875
Cdd:COG1129 487 MAAATGGAA 495
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
659-800 |
3.14e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 68.57 E-value: 3.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 659 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVP---QQAWIQNDSL------RENILFG 729
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPgaeRGVVFQNEGLlpwrnvQDNVAFG 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6678848 730 HPLQeNYYKAVMEACALlpdlEILPSGDRTEIGEKGV-NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDA 800
Cdd:PRK11248 95 LQLA-GVEKMQRLEIAH----QMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1306-1513 |
3.20e-12 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 67.95 E-value: 3.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSL---TLGLFRINEsaeGEIIIDGVNIAKIGLHN-LRFKITIIPQDPVLFSG-S 1380
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTfymIVGLVKPDS---GKILLDGQDITKLPMHKrARLGIGYLPQEASIFRKlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1381 LRMNLDPF--SQYSDEEVWMA-----LELAHLkgfvSALPDKLnhecaegGENLSVGQRQLVCLARALLRKTKILVLDEA 1453
Cdd:cd03218 92 VEENILAVleIRGLSKKEREEkleelLEEFHI----THLRKSK-------ASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6678848 1454 TAAVDLETDNLIQSTIRTQFE-DCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELLQ 1513
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDrGIGVLITDHNVRETLSITdRAYIIYEGKVLAEGTPEEIAA 222
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1256-1458 |
3.66e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.77 E-value: 3.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1256 VAVERLKEYSETEKEAPWQIqeTAPPSTWPhsgRVEFRDYCLRYrEDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTL 1335
Cdd:PRK10522 294 VAFNKLNKLALAPYKAEFPR--PQAFPDWQ---TLELRNVTFAY-QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAM 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1336 GLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSgslRMnLDPFSQYSDEEV---WmaleLAHLKgfvsaL 1412
Cdd:PRK10522 368 LLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFD---QL-LGPEGKPANPALvekW----LERLK-----M 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6678848 1413 PDKLNHecaEGGE----NLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1458
Cdd:PRK10522 435 AHKLEL---EDGRisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQD 481
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
659-877 |
3.89e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.80 E-value: 3.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 659 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS--VAYVPQQ------AWIQNDSLRENILFGH 730
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHevVTRSPQDglangiVYISEDRKRDGLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 731 PLQENyykavMEACAL------------------LPDLEIL-----PSGDRTeIGekgvNLSGGQKQRVSLARAVYSNSD 787
Cdd:PRK10762 346 SVKEN-----MSLTALryfsraggslkhadeqqaVSDFIRLfniktPSMEQA-IG----LLSGGNQQKVAIARGLMTRPK 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 788 IYLFDDPLSAVDAHVGKHIFEkvvgpmglLKNKTR------ILVThgiSYLPQV----DVIIVMSGGKISemgsyqelld 857
Cdd:PRK10762 416 VLILDEPTRGVDVGAKKEIYQ--------LINQFKaeglsiILVS---SEMPEVlgmsDRILVMHEGRIS---------- 474
|
250 260
....*....|....*....|
gi 6678848 858 rdgafAEFLRTYANAEQDLA 877
Cdd:PRK10762 475 -----GEFTREQATQEKLMA 489
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1310-1520 |
4.73e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 69.48 E-value: 4.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1310 INVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHnlRFKITIIPQDPVLF---------SGS 1380
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY--QRPINMMFQSYALFphmtveqniAFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1381 LRMNLDPFSQYSDEEVWMaLELAHLKGFVSALPdklnHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1460
Cdd:PRK11607 116 LKQDKLPKAEIASRVNEM-LGLVHMQEFAKRKP----HQ-------LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6678848 1461 TDNLIQSTIRTQFE--DCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELLQQRGIFYS 1520
Cdd:PRK11607 184 LRDRMQLEVVDILErvGVTCVMVTHDQEEAMTMAgRIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1300-1512 |
5.24e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 67.89 E-value: 5.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1300 REDLDLVlKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGvniakiglHNLRF--------KITIIP 1371
Cdd:PRK15112 23 RQTVEAV-KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD--------HPLHFgdysyrsqRIRMIF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1372 QDPV-----------LFSGSLRMNLDPFSQYSDEEVWMALELahlkgfVSALPDKLNHEcaegGENLSVGQRQLVCLARA 1440
Cdd:PRK15112 94 QDPStslnprqrisqILDFPLRLNTDLEPEQREKQIIETLRQ------VGLLPDHASYY----PHMLAPGQKQRLGLARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1441 LLRKTKILVLDEATAAVDLetdnliqsTIRTQFEDCTV-LTIAHRLNTI--------MDYT--RVIVLDKGEVRECGAPS 1509
Cdd:PRK15112 164 LILRPKVIIADEALASLDM--------SMRSQLINLMLeLQEKQGISYIyvtqhlgmMKHIsdQVLVMHQGEVVERGSTA 235
|
...
gi 6678848 1510 ELL 1512
Cdd:PRK15112 236 DVL 238
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1307-1511 |
5.84e-12 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 67.36 E-value: 5.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1307 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAK-------IGL---HNLRFK-ITIIpqDPV 1375
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDvpvqernVGFvfqHYALFRhMTVF--DNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1376 LFSgsLRM---NLDPFSQYSDEEVWMALELAHLKGFVSALPdklnhecaeggENLSVGQRQLVCLARALLRKTKILVLDE 1452
Cdd:cd03296 96 AFG--LRVkprSERPPEAEIRAKVHELLKLVQLDWLADRYP-----------AQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6678848 1453 ATAAVDLETDNLIQSTIRTQFEDCTVLTI--AHRLNTIMDYT-RVIVLDKGEVRECGAPSEL 1511
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDELHVTTVfvTHDQEEALEVAdRVVVMNKGRIEQVGTPDEV 224
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
644-858 |
6.51e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 68.11 E-value: 6.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWARGEP---PTLNGITFSIPEGALVAVVGQVGCGKSSLLS------------------ALLAEMDKVEGHV 702
Cdd:PRK13645 7 IILDNVSYTYAKKTPfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQltngliisetgqtivgdyAIPANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 703 TLKGSVAYV---PQQAWIQnDSLRENILFGhPL-----QENYYKAVMEacalLPDLEILPsgdRTEIGEKGVNLSGGQKQ 774
Cdd:PRK13645 87 RLRKEIGLVfqfPEYQLFQ-ETIEKDIAFG-PVnlgenKQEAYKKVPE----LLKLVQLP---EDYVKRSPFELSGGQKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 775 RVSLARAVYSNSDIYLFDDPLSAVDAHvGKHIFEKVVGPMGLLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMG--- 850
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPK-GEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIaDEVIVMHEGKVISIGspf 236
|
250
....*....|.
gi 6678848 851 ---SYQELLDR 858
Cdd:PRK13645 237 eifSNQELLTK 247
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
626-846 |
6.55e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 70.14 E-value: 6.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 626 LEPDSIeRRSIKSGEGnSITVknatftwargepptLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKVeghvtlK 705
Cdd:PRK10535 5 LELKDI-RRSYPSGEE-QVEV--------------LKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDKP------T 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 706 GSVAYVPQQ--AWIQNDSL----RENilFGHPLQENY----------------YKAV------MEACALLPDLEIlpsGD 757
Cdd:PRK10535 62 SGTYRVAGQdvATLDADALaqlrREH--FGFIFQRYHllshltaaqnvevpavYAGLerkqrlLRAQELLQRLGL---ED 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 758 RteIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIfekvvgpMGLLKN-----KTRILVTHGISYL 832
Cdd:PRK10535 137 R--VEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEV-------MAILHQlrdrgHTVIIVTHDPQVA 207
|
250
....*....|....
gi 6678848 833 PQVDVIIVMSGGKI 846
Cdd:PRK10535 208 AQAERVIEIRDGEI 221
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1306-1512 |
7.22e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 67.08 E-value: 7.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSL--TLGLFRINESAE---GEIIIDG---VNIAKIGLHNLRFKITIIPQDPVLF 1377
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLlrCINLLEQPEAGTirvGDITIDTarsLSQQKGLIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1378 ----------SGSLRMNLDPfsqySDEEVWMALEL---AHLKGFVSALPDKLnhecaeggenlSVGQRQLVCLARALLRK 1444
Cdd:PRK11264 98 phrtvleniiEGPVIVKGEP----KEEATARARELlakVGLAGKETSYPRRL-----------SGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1445 TKILVLDEATAAVDLETDNLIQSTIRTQFEDC-TVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELL 1512
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDVAdRAIFMDQGRIVEQGPAKALF 232
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
652-800 |
7.91e-12 |
|
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: 65.98 E-value: 7.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 652 TWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG------------SVAYVPQQAWIQN 719
Cdd:cd03231 7 TCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGgpldfqrdsiarGLLYLGHAPGIKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 720 D-SLRENILFGHPLQENyyKAVMEACAL--LPDLEILPSGdrteigekgvNLSGGQKQRVSLARAVYSNSDIYLFDDPLS 796
Cdd:cd03231 87 TlSVLENLRFWHADHSD--EQVEEALARvgLNGFEDRPVA----------QLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
....
gi 6678848 797 AVDA 800
Cdd:cd03231 155 ALDK 158
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1307-1510 |
8.28e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.60 E-value: 8.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1307 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLrfkITIIPQD-------PVLFSG 1379
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSeevdwsfPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1380 SLRMnldpfSQYSDEEvWMALELAHLKGFVS---ALPDKLNHECAEGGEnLSVGQRQLVCLARALLRKTKILVLDEATAA 1456
Cdd:PRK15056 100 VVMM-----GRYGHMG-WLRRAKKRDRQIVTaalARVDMVEFRHRQIGE-LSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 1457 VDLETDNLIQSTIRT-QFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVRECGaPSE 1510
Cdd:PRK15056 173 VDVKTEARIISLLRElRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG-PTE 226
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1306-1514 |
1.34e-11 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 67.86 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLtL----GLfrinESA-EGEIIIDGVNiAKIGLHNLRFKITIIPQDPVLFS-- 1378
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTL-LriiaGL----ETPdSGRIVLNGRD-LFTNLPPRERRVGFVFQHYALFPhm 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1379 --------GsLRMnLDPFSQYSDEEV--WmaLELAHLKGFVSALPDklnhecaeggeNLSVGQRQLVCLARALLRKTKIL 1448
Cdd:COG1118 91 tvaeniafG-LRV-RPPSKAEIRARVeeL--LELVQLEGLADRYPS-----------QLSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6678848 1449 VLDEATAAVD------LEtDNLIQSTIRTQFedcTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELLQQ 1514
Cdd:COG1118 156 LLDEPFGALDakvrkeLR-RWLRRLHDELGG---TTVFVTHDQEEALELAdRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
643-859 |
1.40e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 67.11 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 643 SITVKNATFTWARGEP---PTLNGITFSIPEGALVAVVGQVGCGKSSL---LSALL------AEMDKVEGHVTLK----- 705
Cdd:PRK13646 2 TIRFDNVSYTYQKGTPyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLiqnINALLkpttgtVTVDDITITHKTKdkyir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 706 ------GSVAYVPQQAWIQnDSLRENILFGhplQENYYKAVMEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLA 779
Cdd:PRK13646 82 pvrkriGMVFQFPESQLFE-DTVEREIIFG---PKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 780 RAVYSNSDIYLFDDPLSAVDAHvGKHIFEKVVGPMGLLKNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQELLDR 858
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQ-SKRQVMRLLKSLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKD 236
|
.
gi 6678848 859 D 859
Cdd:PRK13646 237 K 237
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1306-1512 |
1.54e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 66.55 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSGSLRMNL 1385
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1386 DPFSQYSDEEVWMALELAHLKGFVSAL-PDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD-- 1462
Cdd:PRK10253 102 VARGRYPHQPLFTRWRKEDEEAVTKAMqATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQid 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 6678848 1463 --NLIQSTIRTQfeDCTVLTIAHRLNTIMDY-TRVIVLDKGEVRECGAPSELL 1512
Cdd:PRK10253 182 llELLSELNREK--GYTLAAVLHDLNQACRYaSHLIALREGKIVAQGAPKEIV 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1291-1514 |
1.82e-11 |
|
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: 68.56 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1291 EFRDYCLRYREDLDL--VLKHINVTIEGGEKVGIVGRTGAGKS--SL-TLGLF-RINESAEGEIIIDGVNIAKIGLHNLR 1364
Cdd:COG4172 8 SVEDLSVAFGQGGGTveAVKGVSFDIAAGETLALVGESGSGKSvtALsILRLLpDPAAHPSGSILFDGQDLLGLSERELR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1365 ----FKITIIPQDPvlfsgslrMN-LDPF----SQ----------YSDEEVW-MALELAHLKGfvsaLPD---KLN---H 1418
Cdd:COG4172 88 rirgNRIAMIFQEP--------MTsLNPLhtigKQiaevlrlhrgLSGAAARaRALELLERVG----IPDperRLDaypH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1419 EcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLetdnliqsTIRTQF----------EDCTVLTIAHRLNTI 1488
Cdd:COG4172 156 Q-------LSGGQRQRVMIAMALANEPDLLIADEPTTALDV--------TVQAQIldllkdlqreLGMALLLITHDLGVV 220
|
250 260
....*....|....*....|....*..
gi 6678848 1489 MDYT-RVIVLDKGEVRECGAPSELLQQ 1514
Cdd:COG4172 221 RRFAdRVAVMRQGEIVEQGPTAELFAA 247
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
644-856 |
2.44e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 66.27 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWAR-GEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSvAYVPQQAWiqndSL 722
Cdd:PRK13642 5 LEVENLVFKYEKeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE-LLTAENVW----NL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 723 RENI--LFGHPLQENYYKAVMEACAL------LPDLEILPSGDRTEIG--------EKGVNLSGGQKQRVSLARAVYSNS 786
Cdd:PRK13642 80 RRKIgmVFQNPDNQFVGATVEDDVAFgmenqgIPREEMIKRVDEALLAvnmldfktREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 787 DIYLFDDPLSAVDAhVGKHIFEKVVGPMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELL 856
Cdd:PRK13642 160 EIIILDESTSMLDP-TGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1306-1506 |
2.52e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 65.42 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSL--TLGLFRINESAEgeiiidgVNIAkiglhNLRFKITIIPQDPVLFSgsLRM 1383
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLlrVLNLLEMPRSGT-------LNIA-----GNHFDFSKTPSDKAIRE--LRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1384 NLD-PFSQYS-----------------------DEEVWMALELA---HLKGFVSALPdklnhecaeggENLSVGQRQLVC 1436
Cdd:PRK11124 83 NVGmVFQQYNlwphltvqqnlieapcrvlglskDQALARAEKLLerlRLKPYADRFP-----------LHLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6678848 1437 LARALLRKTKILVLDEATAAVDLETDNLIQSTIRT-QFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVRECG 1506
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDPEITAQIVSIIRElAETGITQVIVTHEVEVARKTaSRVVYMENGHIVEQG 223
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1306-1513 |
2.95e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 65.30 E-value: 2.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLH-NLRFKITIIPQDPVLFS------ 1378
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaRARRGIGYLPQEASIFRrlsvyd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1379 ---GSLRMNLDPFSQYSDEEVWMALELAHlkgfVSALPDKLnhecaegGENLSVGQRQLVCLARALLRKTKILVLDEATA 1455
Cdd:PRK10895 98 nlmAVLQIRDDLSAEQREDRANELMEEFH----IEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6678848 1456 AVD----LETDNLIQStIRTQfeDCTVLTIAHRLNTIMDY-TRVIVLDKGEVRECGAPSELLQ 1513
Cdd:PRK10895 167 GVDpisvIDIKRIIEH-LRDS--GLGVLITDHNVRETLAVcERAYIVSQGHLIAHGTPTEILQ 226
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
1018-1251 |
3.31e-11 |
|
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: 65.97 E-value: 3.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1018 ALGILQGAAIFGYSMAVSIGGIFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVD---SMIPqvikMFMGS 1094
Cdd:cd18543 47 ALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQrflAFGP----FLLGN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1095 LFSVIGAVIIILLATP----IAAVIIPPLGLV-YFFVQRFYVASSRQLKRLESVSrspvySHFNETLLGVSVIRAF---- 1165
Cdd:cd18543 123 LLTLVVGLVVMLVLSPplalVALASLPPLVLVaRRFRRRYFPASRRAQDQAGDLA-----TVVEESVTGIRVVKAFgrer 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1166 EEQERFIHQSD-LKVDENQKAyypSIVANRWLAVR-LECVGNCIVLFAALFAVIsRHSLSAG-LVGLSvSYSLQitayLN 1242
Cdd:cd18543 198 RELDRFEAAARrLRATRLRAA---RLRARFWPLLEaLPELGLAAVLALGGWLVA-NGSLTLGtLVAFS-AYLTM----LV 268
|
....*....
gi 6678848 1243 WLVRMSSEM 1251
Cdd:cd18543 269 WPVRMLGWL 277
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
661-858 |
3.47e-11 |
|
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: 67.79 E-value: 3.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAeMDKVEGHVTLKG-SVAYVPQQAW------IQ------NDSL--REN 725
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGqDLDGLSRRALrplrrrMQvvfqdpFGSLspRMT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 726 I--LFGHPL-----------QENYYKAVMEACALLPDleilpSGDR--TEigekgvnLSGGQKQRVSLARAVYSNSDIYL 790
Cdd:COG4172 381 VgqIIAEGLrvhgpglsaaeRRARVAEALEEVGLDPA-----ARHRypHE-------FSGGQRQRIAIARALILEPKLLV 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6678848 791 FDDPLSAVDAHVGKHIFEkvvgpmgLLKnktRILVTHGISYL-----PQV-----DVIIVMSGGKISEMGSYQELLDR 858
Cdd:COG4172 449 LDEPTSALDVSVQAQILD-------LLR---DLQREHGLAYLfishdLAVvralaHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
614-794 |
4.38e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.40 E-value: 4.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 614 LKRLriflshEELEPDSIERRS------IKSGE--GNS-ITVKNATFTWarGEPPTLNGITFSIPEGALVAVVGQVGCGK 684
Cdd:COG0488 283 IKAL------EKLEREEPPRRDktveirFPPPErlGKKvLELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 685 SSLLSALLAEMDKVEGHVTLkGS---VAYVPQQawiqNDSLRENI-LFGHPLQENYYKAVMEACALLPDLeiLPSGDR-- 758
Cdd:COG0488 355 STLLKLLAGELEPDSGTVKL-GEtvkIGYFDQH----QEELDPDKtVLDELRDGAPGGTEQEVRGYLGRF--LFSGDDaf 427
|
170 180 190
....*....|....*....|....*....|....*.
gi 6678848 759 TEIGekgvNLSGGQKQRVSLARAVYSNSDIYLFDDP 794
Cdd:COG0488 428 KPVG----VLSGGEKARLALAKLLLSPPNVLLLDEP 459
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
644-862 |
4.81e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 65.49 E-value: 4.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWARGEP---PTLNGITFSIPEGALVAVVGQVGCGKSSL---LSALL--------------------AEMDK 697
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtelKALDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALLlpdtgtiewifkdeknkkktKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 698 VEGHVTLKGS--------------VAYVPQQAWIQ--NDSLRENILFGH-----PLQENYYKA--VMEACALlpDLEILP 754
Cdd:PRK13651 83 VLEKLVIQKTrfkkikkikeirrrVGVVFQFAEYQlfEQTIEKDIIFGPvsmgvSKEEAKKRAakYIELVGL--DESYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 755 sgdrteigEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGK---HIFEKVVgpmglLKNKTRILVTHGI-S 830
Cdd:PRK13651 161 --------RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKeilEIFDNLN-----KQGKTIILVTHDLdN 227
|
250 260 270
....*....|....*....|....*....|..
gi 6678848 831 YLPQVDVIIVMSGGKISEMGSYQELLdRDGAF 862
Cdd:PRK13651 228 VLEWTKRTIFFKDGKIIKDGDTYDIL-SDNKF 258
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1296-1498 |
5.12e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 63.67 E-value: 5.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1296 CLRyreDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSL--TL-GLFRineSAEGEIIIDGVNIAK-----------IG-- 1359
Cdd:PRK13538 9 CER---DERILFSGLSFTLNAGELVQIEGPNGAGKTSLlrILaGLAR---PDAGEVLWQGEPIRRqrdeyhqdllyLGhq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1360 ---------LHNLRFkitiipqdpvlfsgSLRMNldpfSQYSDEEVWMALELAHLKGFVSALpdklnheCAeggeNLSVG 1430
Cdd:PRK13538 83 pgikteltaLENLRF--------------YQRLH----GPGDDEALWEALAQVGLAGFEDVP-------VR----QLSAG 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1431 QRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFED--CTVLTIAHRLNTIMDYTRVIVLD 1498
Cdd:PRK13538 134 QQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQggMVILTTHQDLPVASDKVRKLRLG 203
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
661-827 |
5.49e-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: 67.47 E-value: 5.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKVEGHVTLK---GSVAYVPQQAWIQNDSLRENILFGHPLQENYY 737
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGGRLTKpakGKLFYVPQRPYMTLGTLRDQIIYPDSSEDMKR 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 738 KAVMEAcallpDLE-ILPSGDRTEIGEKGVN----------LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHI 806
Cdd:TIGR00954 547 RGLSDK-----DLEqILDNVQLTHILEREGGwsavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYM 621
|
170 180
....*....|....*....|...
gi 6678848 807 FEkvvgpmgLLKNK--TRILVTH 827
Cdd:TIGR00954 622 YR-------LCREFgiTLFSVSH 637
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1310-1514 |
6.02e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 65.14 E-value: 6.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1310 INVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIG----LHNLRFKITIIPQDP--VLFSGSLRM 1383
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKPVRKKVGVVFQFPesQLFEETVLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1384 NL----DPFSQYSDEEVWMALELAHLKGFVSALPDKLNHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVD- 1458
Cdd:PRK13643 105 DVafgpQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFE-------LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDp 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1459 ---LETDNLIQSTIRTqfeDCTVLTIAHRLNTIMDYTR-VIVLDKGEVRECGAPSELLQQ 1514
Cdd:PRK13643 178 karIEMMQLFESIHQS---GQTVVLVTHLMDDVADYADyVYLLEKGHIISCGTPSDVFQE 234
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1294-1517 |
6.45e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 64.64 E-value: 6.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1294 DYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--VNIAKIGLHNLRFKITIIP 1371
Cdd:PRK13638 6 DLWFRYQDEP--VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1372 QDP---VLFSG-------SLRmNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHecaeggenlsvGQRQLVCLARAL 1441
Cdd:PRK13638 84 QDPeqqIFYTDidsdiafSLR-NLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSH-----------GQKKRVAIAGAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1442 LRKTKILVLDEATAAVDLE-TDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAP------SELLQ 1513
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAgRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISdAVYVLRQGQILTHGAPgevfacTEAME 231
|
....
gi 6678848 1514 QRGI 1517
Cdd:PRK13638 232 QAGL 235
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1306-1513 |
6.73e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 64.48 E-value: 6.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLG---LFRINESA--EGEIIIDGVNI--AKIGLHNLRFKITIIPQDPVLF- 1377
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrLLELNEEArvEGEVRLFGRNIysPDVDPIEVRREVGMVFQYPNPFp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1378 --------SGSLRMN-LDPFSQYSDEEVWMALELAhlkgfvsALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKIL 1448
Cdd:PRK14267 99 hltiydnvAIGVKLNgLVKSKKELDERVEWALKKA-------ALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6678848 1449 VLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAH---RLNTIMDYTRVIVLdkGEVRECGAPSELLQ 1513
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHspaQAARVSDYVAFLYL--GKLIEVGPTRKVFE 237
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1299-1497 |
6.80e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 63.96 E-value: 6.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1299 YREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFS 1378
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1379 GSLRMNLDPFSQYSDEEVWMALELAHLKGFvsALPDK-LNHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAV 1457
Cdd:PRK10247 95 DTVYDNLIFPWQIRNQQPDPAIFLDDLERF--ALPDTiLTKNIAE----LSGGEKQRISLIRNLQFMPKVLLLDEITSAL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6678848 1458 D----LETDNLIQSTIRTQfeDCTVLTIAHRLNTIMDYTRVIVL 1497
Cdd:PRK10247 169 DesnkHNVNEIIHRYVREQ--NIAVLWVTHDKDEINHADKVITL 210
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
644-855 |
9.85e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 64.33 E-value: 9.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWARGEPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG--------SVAYVPQQA 715
Cdd:PRK13639 2 LETRDLKYSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikydkkSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 716 WI--QN--DSL-----RENILFGhPL-----QENYYKAVMEACAllpdleilpsgdrtEIGEKGV------NLSGGQKQR 775
Cdd:PRK13639 81 GIvfQNpdDQLfaptvEEDVAFG-PLnlglsKEEVEKRVKEALK--------------AVGMEGFenkpphHLSGGQKKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 776 VSLARAVYSNSDIYLFDDPLSAVDAHVGKHIfekvvgpMGLLK--NK---TRILVTHGISYLP-QVDVIIVMSGGKISEM 849
Cdd:PRK13639 146 VAIAGILAMKPEIIVLDEPTSGLDPMGASQI-------MKLLYdlNKegiTIIISTHDVDLVPvYADKVYVMSDGKIIKE 218
|
....*.
gi 6678848 850 GSYQEL 855
Cdd:PRK13639 219 GTPKEV 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1260-1504 |
1.03e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 66.24 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1260 RLKEYSETEKEAPWQIQETA----PPStwPHSGR--VEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSl 1333
Cdd:COG0488 282 RIKALEKLEREEPPRRDKTVeirfPPP--ERLGKkvLELEGLSKSYGDKT--LLDDLSLRIDRGDRIGLIGPNGAGKST- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1334 tlgLFRI----NESAEGEIiidgvniaKIGlHNLrfKITIIPQDPVLFSGSLRMnLDPFSQYSDEevwmaLELAHLKGFV 1409
Cdd:COG0488 357 ---LLKLlageLEPDSGTV--------KLG-ETV--KIGYFDQHQEELDPDKTV-LDELRDGAPG-----GTEQEVRGYL 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1410 SAL---PDKLNHECaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETdnliqstiRTQFEDC------TVLT 1480
Cdd:COG0488 417 GRFlfsGDDAFKPV----GVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET--------LEALEEAlddfpgTVLL 484
|
250 260
....*....|....*....|....*..
gi 6678848 1481 IAH-R--LNTIMDytRVIVLDKGEVRE 1504
Cdd:COG0488 485 VSHdRyfLDRVAT--RILEFEDGGVRE 509
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
644-856 |
1.11e-10 |
|
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: 63.57 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATftWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEG-HVT-------------LKGSVA 709
Cdd:COG1119 4 LELRNVT--VRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRlfgerrggedvweLRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 710 YV-P--QQAWIQNDSLRENIL---------FGHPLQENYYKAVmeacALLPDLEILPSGDRTeIGEkgvnLSGGQKQRVS 777
Cdd:COG1119 82 LVsPalQLRFPRDETVLDVVLsgffdsiglYREPTDEQRERAR----ELLELLGLAHLADRP-FGT----LSQGEQRRVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 778 LARAVYSNSDIYLFDDPLSAVDAHvGKHIFEKVVGPMGLLKNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQELL 856
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLG-ARELLLALLDKLAAEGAPTLVLVTHHVEEIPPgITHVLLLKDGRVVAAGPKEEVL 231
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1306-1513 |
1.26e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 63.65 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQD-PVLFSGSLRM- 1383
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQlPAAEGMTVREl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1384 ----------NLDPFSQYSDEEVWMALELAHLKGFVSALPDklnhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEA 1453
Cdd:PRK10575 106 vaigrypwhgALGRFGAADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWIAMLVAQDSRCLLLDEP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 1454 TAAVDL----ETDNLIQSTirTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELLQ 1513
Cdd:PRK10575 175 TSALDIahqvDVLALVHRL--SQERGLTVIAVLHDINMAARYCdYLVALRGGEMIAQGTPAELMR 237
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1300-1514 |
1.49e-10 |
|
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: 64.74 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1300 REDLDLvlkHINVTIEGGEKVGIVGRTGAGKSSLtL----GLFRineSAEGEIIIDG---------VNIA----KIGLhn 1362
Cdd:COG4148 11 RGGFTL---DVDFTLPGRGVTALFGPSGSGKTTL-LraiaGLER---PDSGRIRLGGevlqdsargIFLPphrrRIGY-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1363 lrfkitiIPQDPVLFSG-SLRMNLD--------PFSQYSDEEVWMALELAHLkgfvsalpdkLNHecaeGGENLSVGQRQ 1433
Cdd:COG4148 82 -------VFQEARLFPHlSVRGNLLygrkraprAERRISFDEVVELLGIGHL----------LDR----RPATLSGGERQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1434 LVCLARALLRKTKILVLDEATAAVDLETDNLIQ---STIRTQFeDCTVLTIAHRLNTIM---DytRVIVLDKGEVRECGA 1507
Cdd:COG4148 141 RVAIGRALLSSPRLLLMDEPLAALDLARKAEILpylERLRDEL-DIPILYVSHSLDEVArlaD--HVVLLEQGRVVASGP 217
|
....*..
gi 6678848 1508 PSELLQQ 1514
Cdd:COG4148 218 LAEVLSR 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
652-850 |
1.62e-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: 62.51 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 652 TWARGEPPTLNGITFsiPEGALVAVVGQVGCGKSSLLSaLLAEMDKVE-GHVTLKG-SVAYVPQQAWIQNDSLRENILFG 729
Cdd:cd03298 7 RFSYGEQPMHFDLTF--AQGEITAIVGPSGSGKSTLLN-LIAGFETPQsGRVLINGvDVTAAPPADRPVSMLFQENNLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 730 H-PLQENYykavmeACALLPDLEILPSgDRTEI----GEKGVN---------LSGGQKQRVSLARAVYSNSDIYLFDDPL 795
Cdd:cd03298 84 HlTVEQNV------GLGLSPGLKLTAE-DRQAIevalARVGLAglekrlpgeLSGGERQRVALARVLVRDKPVLLLDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6678848 796 SAVDAHVGKHIFEKVVGPMGLLKNkTRILVTHGISYLPQV-DVIIVMSGGKISEMG 850
Cdd:cd03298 157 AALDPALRAEMLDLVLDLHAETKM-TVLMVTHQPEDAKRLaQRVVFLDNGRIAAQG 211
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1307-1515 |
1.74e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 63.49 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1307 LKHINVTIEGGEKVGIVGRTGAGKSSLTL---GLFRINESAEGEIIIDGVNIAKIG------------------LHNLRF 1365
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsGLITGDKSAGSHIELLGRTVQREGrlardirksrantgyifqQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1366 KITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWMALELAHLKGFVsalpdklnHECAEGGENLSVGQRQLVCLARALLRKT 1445
Cdd:PRK09984 100 RLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALTRVGMV--------HFAHQRVSTLSGGQQQRVAIARALMQQA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6678848 1446 KILVLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVRECGAPSELLQQR 1515
Cdd:PRK09984 172 KVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDYALRYcERIVALRQGHVFYDGSSQQFDNER 244
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1307-1489 |
1.76e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 65.34 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1307 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRI--NESAEGEIIIDGvniAKIGLHNLR----FKITIIPQDPVL---- 1376
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEG---EELQASNIRdterAGIAIIHQELALvkel 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1377 ------FSGSL-----RMNLDpfSQYSDEEVWMAlELahlkgfvsalpdKLNHECAEGGENLSVGQRQLVCLARALLRKT 1445
Cdd:PRK13549 98 svleniFLGNEitpggIMDYD--AMYLRAQKLLA-QL------------KLDINPATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6678848 1446 KILVLDEATAAV-DLETDNLIqSTIRT-QFEDCTVLTIAHRLNTIM 1489
Cdd:PRK13549 163 RLLILDEPTASLtESETAVLL-DIIRDlKAHGIACIYISHKLNEVK 207
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1305-1513 |
1.84e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 63.89 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1305 LVLKHINVTIEGGEKVGIVGRTGAGKSSL----------TLGLFRINEsaegEIIIDGVNIAKigLHNLRFKITIIPQDP 1374
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLlqhlngllqpTSGTVTIGE----RVITAGKKNKK--LKPLRKKVGIVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1375 --VLFSGSLR-------MNldpFSQYSDEEVWMALELAHLKGFVSALPDKLNHEcaeggenLSVGQRQLVCLARALLRKT 1445
Cdd:PRK13634 95 ehQLFEETVEkdicfgpMN---FGVSEEDAKQKAREMIELVGLPEELLARSPFE-------LSGGQMRRVAIAGVLAMEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6678848 1446 KILVLDEATAAVD----LETDNLIQSTIRTQfeDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELLQ 1513
Cdd:PRK13634 165 EVLVLDEPTAGLDpkgrKEMMEMFYKLHKEK--GLTTVLVTHSMEDAARYAdQIVVMHKGTVFLQGTPREIFA 235
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
661-858 |
1.95e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 64.22 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQQAWIQNDSLRENILFGHPLQE-NYYKA 739
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNPYGSlNPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 740 VMeacALLPD-LEILPSGDRTEIGEKG------VNL------------SGGQKQRVSLARAVYSNSDIYLFDDPLSAVDA 800
Cdd:PRK11308 111 VG---QILEEpLLINTSLSAAERREKAlammakVGLrpehydryphmfSGGQRQRIAIARALMLDPDVVVADEPVSALDV 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6678848 801 HVGKHI---FEKVVGPMGLlknkTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLDR 858
Cdd:PRK11308 188 SVQAQVlnlMMDLQQELGL----SYVFISHDLSVVEHIaDEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
1018-1260 |
2.04e-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: 63.72 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1018 ALGILQG--AAIFGYSMAvsiggiFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSL 1095
Cdd:cd18572 48 LSGLFSGlrGGCFSYAGT------RLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1096 FSVIGAVIIILLATP----IAAVIIPPLGLVYFFVQRFYvassRQLKRLESVSRSPVYSHFNETLLGVSVIRAF--EEQE 1169
Cdd:cd18572 122 VQLVGGLAFMFSLSWrltlLAFITVPVIALITKVYGRYY----RKLSKEIQDALAEANQVAEEALSNIRTVRSFatEERE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1170 --RFIHQSDLKVDENQK---AYypsiVANRWLAVRLECVGNCIVLFAALFAVISrHSLSAGLVGLSVSYSLQITAYLNWL 1244
Cdd:cd18572 198 arRYERALDKALKLSVRqalAY----AGYVAVNTLLQNGTQVLVLFYGGHLVLS-GRMSAGQLVTFMLYQQQLGEAFQSL 272
|
250
....*....|....*.
gi 6678848 1245 VRMSSEMETNIVAVER 1260
Cdd:cd18572 273 GDVFSSLMQAVGAAEK 288
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1306-1514 |
2.16e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 61.77 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSL--TLGLFRINESAEGEIIIDGVNIAKIGLHNlRFK--ITIIPQDPVLFSGsl 1381
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLakTIMGHPKYEVTEGEILFKGEDITDLPPEE-RARlgIFLAFQYPPEIPG-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1382 rmnldpfsqysdeevwmaLELAHLKGFVsalpdklnhecaegGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET 1461
Cdd:cd03217 92 ------------------VKNADFLRYV--------------NEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6678848 1462 DNLIQSTIRT-QFEDCTVLTIAHRLNtIMDY---TRVIVLDKGEVRECGaPSELLQQ 1514
Cdd:cd03217 140 LRLVAEVINKlREEGKSVLIITHYQR-LLDYikpDRVHVLYDGRIVKSG-DKELALE 194
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
1015-1260 |
2.27e-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: 63.26 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1015 VYGALGILQGAAIFGYSMAVSIGG---IFASRRlhlDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMF 1091
Cdd:cd18545 45 LFLALNLVNWVASRLRIYLMAKVGqriLYDLRQ---DLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1092 MGSLFSVIGAVIIIL-----LATpIAAVIIPPLGLVYFFVQRFyvasSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFE 1166
Cdd:cd18545 122 IPDLLTLVGIVIIMFslnvrLAL-VTLAVLPLLVLVVFLLRRR----ARKAWQRVRKKISNLNAYLHESISGIRVIQSFA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1167 EQERFIHQSDLKVDENQKAYYPSIVANR--WLAVRL-ECVGNCIVLFAALFAVISrHSLSAGLVGLSVSYSLQITAYLNW 1243
Cdd:cd18545 197 REDENEEIFDELNRENRKANMRAVRLNAlfWPLVELiSALGTALVYWYGGKLVLG-GAITVGVLVAFIGYVGRFWQPIRN 275
|
250
....*....|....*..
gi 6678848 1244 LVRMSSEMETNIVAVER 1260
Cdd:cd18545 276 LSNFYNQLQSAMASAER 292
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1306-1497 |
2.30e-10 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 61.48 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVniAKIGLhnLRFKITIIPQDPVLFSGSLRMNL 1385
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG--ARVAY--VPQRSEVPDSLPLTVRDLVAMGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1386 ----DPFSQYSDE---EVWMALELAHLKGFvsalpdkLNHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1458
Cdd:NF040873 83 warrGLWRRLTRDdraAVDDALERVGLADL-------AGRQLGE----LSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6678848 1459 LETDNLIQSTIRTQFED-CTVLTIAHRLNTIMDYTRVIVL 1497
Cdd:NF040873 152 AESRERIIALLAEEHARgATVVVVTHDLELVRRADPCVLL 191
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
644-866 |
2.70e-10 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 62.08 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWargEPPTLNgITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKVE-GHVTLKG-SVAYVP--------- 712
Cdd:COG3840 2 LRLDDLTYRY---GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLN-LIAGFLPPDsGRILWNGqDLTALPpaerpvsml 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 713 -QQawiqND-----SLRENILFG-HP---LQENYYKAVMEACAllpdleilpsgdRTEIGEKG----VNLSGGQKQRVSL 778
Cdd:COG3840 77 fQE----NNlfphlTVAQNIGLGlRPglkLTAEQRAQVEQALE------------RVGLAGLLdrlpGQLSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 779 ARAVYSNSDIYLFDDPLSAVDahvgkhifekvvgP------MGLLK------NKTRILVTHGIS-YLPQVDVIIVMSGGK 845
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALD-------------PalrqemLDLVDelcrerGLTVLMVTHDPEdAARIADRVLLVADGR 207
|
250 260
....*....|....*....|...
gi 6678848 846 ISEMGSYQELLDRDG--AFAEFL 866
Cdd:COG3840 208 IAADGPTAALLDGEPppALAAYL 230
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
665-869 |
2.86e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 64.28 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 665 TFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSvayvpQQAWIQNDSLREnilfghpLQENYYKAVMEAC 744
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGV-----DIAKISDAELRE-------VRRKKIAMVFQSF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 745 ALLPDLEIL------------PSGDRTE-----IGEKGVN---------LSGGQKQRVSLARAVYSNSDIYLFDDPLSAV 798
Cdd:PRK10070 116 ALMPHMTVLdntafgmelagiNAEERREkaldaLRQVGLEnyahsypdeLSGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6678848 799 DAHVGKHIFEKVVgPMGLLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLDRDGafAEFLRTY 869
Cdd:PRK10070 196 DPLIRTEMQDELV-KLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNNPA--NDYVRTF 264
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1306-1502 |
3.14e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 62.39 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIdgvniAKIGLHNLRFKITIIPQDPVLF-------- 1377
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLA-----GTAPLAEAREDTRLMFQDARLLpwkkvidn 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1378 -SGSLRMNLDPFSQYSDEEVwmalelahlkgfvsALPDKLNHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAA 1456
Cdd:PRK11247 102 vGLGLKGQWRDAALQALAAV--------------GLADRANEWPAA----LSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6678848 1457 VD----LETDNLIQSTIRTQ-FedcTVLTIAHRLN---TIMDytRVIVLDKGEV 1502
Cdd:PRK11247 164 LDaltrIEMQDLIESLWQQHgF---TVLLVTHDVSeavAMAD--RVLLIEEGKI 212
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1307-1514 |
3.22e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 62.87 E-value: 3.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1307 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNI-AKIG---LHNLRFKITIIPQDP--VLFSGS 1380
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKdkyIRPVRKRIGMVFQFPesQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1381 L-----------RMNLDPFSQYSDEevwMALELAHLKGFVSALPDKlnhecaeggenLSVGQRQLVCLARALLRKTKILV 1449
Cdd:PRK13646 103 VereiifgpknfKMNLDEVKNYAHR---LLMDLGFSRDVMSQSPFQ-----------MSGGQMRKIAIVSILAMNPDIIV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6678848 1450 LDEATAAVDLETDNLIQSTIRT-QFEDC-TVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELLQQ 1514
Cdd:PRK13646 169 LDEPTAGLDPQSKRQVMRLLKSlQTDENkTIILVSHDMNEVARYAdEVIVMKEGSIVSQTSPKELFKD 236
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
656-866 |
3.55e-10 |
|
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: 61.92 E-value: 3.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 656 GEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS--------------VAYVPQQAWI-QND 720
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditglpphriarlgIGYVPEGRRIfPSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 721 SLRENIL---FGHPLQENYYKAVMEACALLPDLEilpsgDRteIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDP--- 794
Cdd:COG0410 94 TVEENLLlgaYARRDRAEVRADLERVYELFPRLK-----ER--RRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPslg 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 795 LSAVdahVGKHIFEKVvgpmgllknktRILVTHGIS------YLPQV----DVIIVMSGGKISEMGSYQELLDRDGAFAE 864
Cdd:COG0410 167 LAPL---IVEEIFEII-----------RRLNREGVTillveqNARFAleiaDRAYVLERGRIVLEGTAAELLADPEVREA 232
|
..
gi 6678848 865 FL 866
Cdd:COG0410 233 YL 234
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
644-851 |
3.57e-10 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 63.28 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKN--ATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSA--LLAEMDkvEGHVTLKG-SVAYVPQQAWIQ 718
Cdd:PRK11153 2 IELKNisKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCinLLERPT--SGRVLVDGqDLTALSEKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 719 ndsLRENI--LFGHplqenYY----KAVMEACALlPdLEIlpSG-DRTEIGEK--------GV---------NLSGGQKQ 774
Cdd:PRK11153 80 ---ARRQIgmIFQH-----FNllssRTVFDNVAL-P-LEL--AGtPKAEIKARvtellelvGLsdkadrypaQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 775 RVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEkvvgpmgLLK--NK----TRILVTHgisylpQVDVI-------IVM 841
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSILE-------LLKdiNRelglTIVLITH------EMDVVkricdrvAVI 214
|
250
....*....|
gi 6678848 842 SGGKISEMGS 851
Cdd:PRK11153 215 DAGRLVEQGT 224
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
655-801 |
3.91e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.97 E-value: 3.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 655 RGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG------------SVAYVPQQAWIQND-S 721
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGepirrqrdeyhqDLLYLGHQPGIKTElT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 722 LRENILFGHPLQENYYKAVMEAcAL----LPDLEILPSGdrteigekgvNLSGGQKQRVSLARAVYSNSDIYLFDDPLSA 797
Cdd:PRK13538 91 ALENLRFYQRLHGPGDDEALWE-ALaqvgLAGFEDVPVR----------QLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
....
gi 6678848 798 VDAH 801
Cdd:PRK13538 160 IDKQ 163
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1310-1519 |
4.03e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 63.20 E-value: 4.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1310 INVTIEGGEKVGIVGRTGAGKSSLT---LGLFRINESAEGEIIIDG---VNIAKIGLHNLRF-KITIIPQDPVlfsgslr 1382
Cdd:PRK09473 35 LNFSLRAGETLGIVGESGSGKSQTAfalMGLLAANGRIGGSATFNGreiLNLPEKELNKLRAeQISMIFQDPM------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1383 MNLDPFSQYSDE--EVWM-------------------ALELAHLKGFVSALPdklnHEcaeggenLSVGQRQLVCLARAL 1441
Cdd:PRK09473 108 TSLNPYMRVGEQlmEVLMlhkgmskaeafeesvrmldAVKMPEARKRMKMYP----HE-------FSGGMRQRVMIAMAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1442 LRKTKILVLDEATAAVDLEtdnlIQSTIRTQFED------CTVLTIAHRLNT---IMDytRVIVLDKGEVRECGapsell 1512
Cdd:PRK09473 177 LCRPKLLIADEPTTALDVT----VQAQIMTLLNElkrefnTAIIMITHDLGVvagICD--KVLVMYAGRTMEYG------ 244
|
....*..
gi 6678848 1513 QQRGIFY 1519
Cdd:PRK09473 245 NARDVFY 251
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1310-1514 |
4.03e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 62.45 E-value: 4.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1310 INVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIG----LHNLRFKITIIPQDP--VLFSGSLRM 1383
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQIRKKVGLVFQFPesQLFEETVLK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1384 NL----DPFSQYSDEEVWMALELAHLKGFVSALPDKLNHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1459
Cdd:PRK13649 106 DVafgpQNFGVSQEEAEALAREKLALVGISESLFEKNPFE-------LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6678848 1460 ETDNLIQSTIRTQFED-CTVLTIAHRLNTIMDY-TRVIVLDKGEVRECGAPSELLQQ 1514
Cdd:PRK13649 179 KGRKELMTLFKKLHQSgMTIVLVTHLMDDVANYaDFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
642-858 |
4.49e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 62.44 E-value: 4.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 642 NSITVKNATFTWARG-EPPTLNGITFSIPEGALVAVVGQVGCGKSS---LLSALL-AEMDK--VEGHVTLKGSVAYVPQQ 714
Cdd:PRK13650 3 NIIEVKNLTFKYKEDqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGLLeAESGQiiIDGDLLTEENVWDIRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 715 AWI--QND-------SLRENILFGH-----PLQEnYYKAVMEAcallpdLEILPSGDRTEigEKGVNLSGGQKQRVSLAR 780
Cdd:PRK13650 83 IGMvfQNPdnqfvgaTVEDDVAFGLenkgiPHEE-MKERVNEA------LELVGMQDFKE--REPARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6678848 781 AVYSNSDIYLFDDPLSAVDAHvGKHIFEKVVGPMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLDR 858
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPE-GRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
661-858 |
5.06e-10 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 62.83 E-value: 5.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-SVAYVPQQAWIQndsLREN--ILFghplQENY- 736
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGqDITGLSGRELRP---LRRRmqMVF----QDPYa 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 737 --------YKAVMEAcallpdLEILPSGDRTEIGEK--------GVN----------LSGGQKQRVSLARAVYSNSDIYL 790
Cdd:COG4608 107 slnprmtvGDIIAEP------LRIHGLASKAERRERvaellelvGLRpehadrypheFSGGQRQRIGIARALALNPKLIV 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6678848 791 FDDPLSAVDAHVGKHI---FEKVVGPMGLlknkTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLDR 858
Cdd:COG4608 181 CDEPVSALDVSIQAQVlnlLEDLQDELGL----TYLFISHDLSVVRHIsDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1304-1471 |
5.31e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 60.66 E-value: 5.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1304 DLVLKHINVTIEGGEKVGIVGRTGAGKSSL--TL-GLFRInesAEGEIIIDGVNiakIGLHNLRFKITII-PQD---PVL 1376
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLlrLIaGLLPP---AAGTIKLDGGD---IDDPDVAEACHYLgHRNamkPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1377 fsgSLRMNLDPFSQY---SDEEVWMALE------LAHLKgfvsalpdklnhecaegGENLSVGQRQLVCLARALLRKTKI 1447
Cdd:PRK13539 89 ---TVAENLEFWAAFlggEELDIAAALEavglapLAHLP-----------------FGYLSAGQKRRVALARLLVSNRPI 148
|
170 180
....*....|....*....|....
gi 6678848 1448 LVLDEATAAVDLETDNLIQSTIRT 1471
Cdd:PRK13539 149 WILDEPTAALDAAAVALFAELIRA 172
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1260-1514 |
5.42e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 62.93 E-value: 5.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1260 RLKEYSETEKEAPWQIQETAPPSTWPHSGRVEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFR 1339
Cdd:PRK13536 12 RRLELSPIERKHQGISEAKASIPGSMSTVAIDLAGVSKSYGDKA--VVNGLSFTVASGECFGLLGPNGAGKSTIARMILG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1340 INESAEGEIIIDGVNI-AKIGLhnLRFKITIIPQ-DPVLFSGSLRMNLDPFSQY-------SDEEVWMALELAHLKgfvs 1410
Cdd:PRK13536 90 MTSPDAGKITVLGVPVpARARL--ARARIGVVPQfDNLDLEFTVRENLLVFGRYfgmstreIEAVIPSLLEFARLE---- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1411 alpDKLNHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQF-EDCTVLTIAHrlntIM 1489
Cdd:PRK13536 164 ---SKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTH----FM 232
|
250 260 270
....*....|....*....|....*....|
gi 6678848 1490 DYT-----RVIVLDKGEVRECGAPSELLQQ 1514
Cdd:PRK13536 233 EEAerlcdRLCVLEAGRKIAEGRPHALIDE 262
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1317-1506 |
5.64e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 64.11 E-value: 5.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1317 GEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIG---LHNLRFKITIIPQDPVlfsgslrMNLDPFSQ--Y 1391
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPY-------ASLDPRQTvgD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1392 SDEEVWM----------ALELAHLKGFVSALPD---KLNHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1458
Cdd:PRK10261 423 SIMEPLRvhgllpgkaaAARVAWLLERVGLLPEhawRYPHE-------FSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6678848 1459 LET-DNLIQSTIRTQFE-DCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECG 1506
Cdd:PRK10261 496 VSIrGQIINLLLDLQRDfGIAYLFISHDMAVVERIShRVAVMYLGQIVEIG 546
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
1016-1187 |
5.86e-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: 62.11 E-value: 5.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1016 YGALGILQGAAIFGYSMAVSIGGIFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSL 1095
Cdd:cd18577 53 FVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1096 FSVIGAVII----------ILLATpiaaviIPPLGLVYFFVQRFYV-ASSRQLKRLESVSrspvySHFNETLLGVSVIRA 1164
Cdd:cd18577 133 STFIAGFIIafiyswkltlVLLAT------LPLIAIVGGIMGKLLSkYTKKEQEAYAKAG-----SIAEEALSSIRTVKA 201
|
170 180
....*....|....*....|...
gi 6678848 1165 FEEQERFIHQSDLKVDENQKAYY 1187
Cdd:cd18577 202 FGGEEKEIKRYSKALEKARKAGI 224
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
655-799 |
6.03e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 61.93 E-value: 6.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 655 RGEPPTL--------NGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS-------------VAYVPQ 713
Cdd:PRK10253 9 RGEQLTLgygkytvaENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiqhyaskevarrIGLLAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 714 QAWIQND-SLRENILFG----HPLQENYYKAVMEACAllpdlEILPSGDRTEIGEKGVN-LSGGQKQRVSLARAVYSNSD 787
Cdd:PRK10253 89 NATTPGDiTVQELVARGryphQPLFTRWRKEDEEAVT-----KAMQATGITHLADQSVDtLSGGQRQRAWIAMVLAQETA 163
|
170
....*....|..
gi 6678848 788 IYLFDDPLSAVD 799
Cdd:PRK10253 164 IMLLDEPTTWLD 175
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
629-855 |
6.59e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 62.93 E-value: 6.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 629 DSIERRSIKSGEGNS--ITVKNATFTWaRGEPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG 706
Cdd:PRK11607 3 DAIPRPQAKTRKALTplLEIRNLTKSF-DGQH-AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 707 -SVAYVP-----------QQAWIQNDSLRENILFGHPlQENYYKA-----VMEACALLPDLEIlpsgdrteIGEKGVNLS 769
Cdd:PRK11607 81 vDLSHVPpyqrpinmmfqSYALFPHMTVEQNIAFGLK-QDKLPKAeiasrVNEMLGLVHMQEF--------AKRKPHQLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 770 GGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVGPMGLLkNKTRILVTHGI-SYLPQVDVIIVMSGGKISE 848
Cdd:PRK11607 152 GGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERV-GVTCVMVTHDQeEAMTMAGRIAIMNRGKFVQ 230
|
....*..
gi 6678848 849 MGSYQEL 855
Cdd:PRK11607 231 IGEPEEI 237
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1306-1492 |
6.94e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 61.28 E-value: 6.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIidgvniakiglHNLRFKITIIPQ----DPVL-FSGS 1380
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-----------RNGKLRIGYVPQklylDTTLpLTVN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1381 LRMNLDPFSQYSDeeVWMALELAHLKGFVSALPDKLNhecaeGGENlsvgqrQLVCLARALLRKTKILVLDEATAAVD-- 1458
Cdd:PRK09544 88 RFLRLRPGTKKED--ILPALKRVQAGHLIDAPMQKLS-----GGET------QRVLLARALLNRPQLLVLDEPTQGVDvn 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 6678848 1459 --LETDNLIQStIRTQFeDCTVLTIAHRLNTIMDYT 1492
Cdd:PRK09544 155 gqVALYDLIDQ-LRREL-DCAVLMVSHDLHLVMAKT 188
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
661-850 |
7.03e-10 |
|
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: 59.64 E-value: 7.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEmdkvEGHVTLKGSVAYVPQQAWIQNDSLRENILFGhplqenyykav 740
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYA----SGKARLISFLPKFSRNKLIFIDQLQFLIDVG----------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 741 meacallpdLEILPsgdrteIGEKGVNLSGGQKQRVSLARAVYSNSD--IYLFDDPLSAVDaHVGKHIFEKVVGPMGLLK 818
Cdd:cd03238 76 ---------LGYLT------LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH-QQDINQLLEVIKGLIDLG 139
|
170 180 190
....*....|....*....|....*....|....*...
gi 6678848 819 NkTRILVTHGISYLPQVDVIIVM------SGGKISEMG 850
Cdd:cd03238 140 N-TVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
1015-1225 |
7.58e-10 |
|
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: 61.74 E-value: 7.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1015 VYGALGILQGAAIFGYsmAVSIGGIFASRRLHLDLLYN--------VLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQ 1086
Cdd:cd18546 38 LLLAAAAYLAVVLAGW--VAQRAQTRLTGRTGERLLYDlrlrvfahLQRLSLDFHERETSGRIMTRMTSDIDALSELLQT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1087 VIKMFMGSLFSVIGAVIIILLATP----IAAVIIPPLGLVYFFVQRfyvASSRQLKRL-ESVSRspVYSHFNETLLGVSV 1161
Cdd:cd18546 116 GLVQLVVSLLTLVGIAVVLLVLDPrlalVALAALPPLALATRWFRR---RSSRAYRRArERIAA--VNADLQETLAGIRV 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6678848 1162 IRAF----EEQERFIHQSDLKVDENQKA------YYPSIvanRWLAVrlecVGNCIVLFAALFAVIsRHSLSAG 1225
Cdd:cd18546 191 VQAFrrerRNAERFAELSDDYRDARLRAqrlvaiYFPGV---ELLGN----LATAAVLLVGAWRVA-AGTLTVG 256
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1306-1514 |
7.65e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 61.25 E-value: 7.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSL--TLGlfRINESAEGEIIIDGvNIAKI-----GLH-------NLRFKITII- 1370
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLlkLIA--GILEPTSGRVEVNG-RVSALlelgaGFHpeltgreNIYLNGRLLg 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1371 --PQDP-------VLFSGsLRMNLD-PFSQYSDEevwMALELA-----HLKgfvsalPDklnhecaeggenlsvgqrqlv 1435
Cdd:COG1134 118 lsRKEIdekfdeiVEFAE-LGDFIDqPVKTYSSG---MRARLAfavatAVD------PD--------------------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1436 clarallrktkILVLDEATAAVDLE----TDNLIQSTIRtqfEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVRECGAPSE 1510
Cdd:COG1134 167 -----------ILLVDEVLAVGDAAfqkkCLARIRELRE---SGRTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDGDPEE 232
|
....
gi 6678848 1511 LLQQ 1514
Cdd:COG1134 233 VIAA 236
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
643-855 |
7.69e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 61.77 E-value: 7.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 643 SITVKNATFTWARGEP---PTLNGITFSIPEGALVAVVGQVGCGKSSLL---SALL----AEMDKVEGHVT--------- 703
Cdd:PRK13641 2 SIKFENVDYIYSPGTPmekKGLDNISFELEEGSFVALVGHTGSGKSTLMqhfNALLkpssGTITIAGYHITpetgnknlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 704 -LKGSVAYVPQ--QAWIQNDSLRENILFGhPL------QENYYKAV--MEACALLPDLeilpsgdrteIGEKGVNLSGGQ 772
Cdd:PRK13641 82 kLRKKVSLVFQfpEAQLFENTVLKDVEFG-PKnfgfseDEAKEKALkwLKKVGLSEDL----------ISKSPFELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 773 KQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEkvvgpmgLLKN-----KTRILVTHGISYLPQ-VDVIIVMSGGKI 846
Cdd:PRK13641 151 MRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQ-------LFKDyqkagHTVILVTHNMDDVAEyADDVLVLEHGKL 223
|
....*....
gi 6678848 847 SEMGSYQEL 855
Cdd:PRK13641 224 IKHASPKEI 232
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1306-1502 |
7.79e-10 |
|
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: 60.81 E-value: 7.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGV--------NIAKIGLHnLRFKITIIPQDPVLf 1377
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvpwkrrkkFLRRIGVV-FGQKTQLWWDLPVI- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1378 sGSLRMNLD----PFSQYSdeevwmalelAHLKGFVSALpdKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEA 1453
Cdd:cd03267 114 -DSFYLLAAiydlPPARFK----------KRLDELSELL--DLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6678848 1454 TAAVDLETDNLIQSTIRTQFED--CTVLTIAHRLNTIMDY-TRVIVLDKGEV 1502
Cdd:cd03267 181 TIGLDVVAQENIRNFLKEYNRErgTTVLLTSHYMKDIEALaRRVLVIDKGRL 232
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
661-867 |
7.87e-10 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 61.36 E-value: 7.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSAL-LAEMDKvEGHVTLKG-SVAYVPQQA-------WIQNDSLR-------- 723
Cdd:COG4598 24 LKGVSLTARKGDVISIIGSSGSGKSTFLRCInLLETPD-SGEIRVGGeEIRLKPDRDgelvpadRRQLQRIRtrlgmvfq 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 724 -----------ENILFG--HPLQENYYKAVMEACALLpdleilpsgDRTEIGEKG----VNLSGGQKQRVSLARAVYSNS 786
Cdd:COG4598 103 sfnlwshmtvlENVIEApvHVLGRPKAEAIERAEALL---------AKVGLADKRdaypAHLSGGQQQRAAIARALAMEP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 787 DIYLFDDPLSAVDAH-VGkhifeKVVGPMGLLKN--KTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLD--RDG 860
Cdd:COG4598 174 EVMLFDEPTSALDPElVG-----EVLKVMRDLAEegRTMLVVTHEMGFARDVsSHVVFLHQGRIEEQGPPAEVFGnpKSE 248
|
....*..
gi 6678848 861 AFAEFLR 867
Cdd:COG4598 249 RLRQFLS 255
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1303-1502 |
9.32e-10 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 59.37 E-value: 9.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1303 LDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHN-LRFKITIIPQDPvlfsgsL 1381
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVPEDR------K 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1382 RMNLdpFSQYSdeeVWMALELAHLkgfvsalpdklnhecaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET 1461
Cdd:cd03215 86 REGL--VLDLS---VAENIALSSL---------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6678848 1462 DNLIQSTIRTQFED-CTVLTIAHRLNTIM---DytRVIVLDKGEV 1502
Cdd:cd03215 140 KAEIYRLIRELADAgKAVLLISSELDELLglcD--RILVMYEGRI 182
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
647-846 |
1.03e-09 |
|
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: 59.97 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 647 KNATFTWARGEP--PTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL---LAEMDKVEGHVTLKG------------SVA 709
Cdd:cd03233 7 RNISFTTGKGRSkiPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGipykefaekypgEII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 710 YVPQQAW-IQNDSLRENILFGHPLQENYYKavmeacallpdleilpsgdrteigeKGVnlSGGQKQRVSLARAVYSNSDI 788
Cdd:cd03233 87 YVSEEDVhFPTLTVRETLDFALRCKGNEFV-------------------------RGI--SGGERKRVSIAEALVSRASV 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6678848 789 YLFDDPLSAVDAHVGKHIFEKvvgpmglLKNKTRILVTHGISYLPQ--------VDVIIVMSGGKI 846
Cdd:cd03233 140 LCWDNSTRGLDSSTALEILKC-------IRTMADVLKTTTFVSLYQasdeiydlFDKVLVLYEGRQ 198
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
644-855 |
1.09e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 61.19 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWARGEP---PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLkGSVAYVPQQAWIQND 720
Cdd:PRK13634 3 ITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 721 SLREN--ILFGHP----LQENYYK---------AVMEACALLPDLEILP-SGDRTEIGEKG-VNLSGGQKQRVSLARAVY 783
Cdd:PRK13634 82 PLRKKvgIVFQFPehqlFEETVEKdicfgpmnfGVSEEDAKQKAREMIElVGLPEELLARSpFELSGGQMRRVAIAGVLA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6678848 784 SNSDIYLFDDPLSAVDAHVGKHIfekvvgpMGLL------KNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQEL 855
Cdd:PRK13634 162 MEPEVLVLDEPTAGLDPKGRKEM-------MEMFyklhkeKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
661-827 |
1.18e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 60.21 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVTLKG---SVAYVPQQAWIQNDSLRENILFGHplqeny 736
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLH-LLGGLDTpTSGDVIFNGqpmSKLSSAAKAELRNQKLGFIYQFHH------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 737 ykavmeacaLLPDLEILPS---------GDRTEIGEKGVN-----------------LSGGQKQRVSLARAVYSNSDIYL 790
Cdd:PRK11629 98 ---------LLPDFTALENvamplligkKKPAEINSRALEmlaavglehranhrpseLSGGERQRVAIARALVNNPRLVL 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 6678848 791 FDDPLSAVDAHVGKHIFEkVVGPMGLLKNKTRILVTH 827
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQ-LLGELNRLQGTAFLVVTH 204
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1290-1513 |
1.19e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 61.36 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGlHNLRFKITI 1369
Cdd:PRK13537 8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA-RHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1370 IPQ----DPVLfsgSLRMNLDPFSQY-------SDEEVWMALELAHLKgfvsalpdklNHECAEGGEnLSVGQRQLVCLA 1438
Cdd:PRK13537 85 VPQfdnlDPDF---TVRENLLVFGRYfglsaaaARALVPPLLEFAKLE----------NKADAKVGE-LSGGMKRRLTLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1439 RALLRKTKILVLDEATAAVDLETDNLIQSTIRTQF-EDCTVLTIAH------RLntimdYTRVIVLDKGEVRECGAPSEL 1511
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHfmeeaeRL-----CDRLCVIEEGRKIAEGAPHAL 225
|
..
gi 6678848 1512 LQ 1513
Cdd:PRK13537 226 IE 227
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
640-896 |
1.32e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 61.02 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 640 EGNSITVKNATFTWARGEPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQQAWIQn 719
Cdd:PRK13636 2 EDYILKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 720 dsLRENI--LFGHPLQENYYKAVMEACAL------LPDLEILPSGDRTeIGEKGVN---------LSGGQKQRVSLARAV 782
Cdd:PRK13636 80 --LRESVgmVFQDPDNQLFSASVYQDVSFgavnlkLPEDEVRKRVDNA-LKRTGIEhlkdkpthcLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 783 YSNSDIYLFDDPLSAVDAHVGKHIFEKVVG---PMGLlknkTRILVTHGISYLP-QVDVIIVMSGGK------ISEMGSY 852
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEmqkELGL----TIIIATHDIDIVPlYCDNVFVMKEGRvilqgnPKEVFAE 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 6678848 853 QEL-------LDRDGAFAEFLRTYANAEQDlaSEDDSVSGSGKESKPVENG 896
Cdd:PRK13636 233 KEMlrkvnlrLPRIGHLMEILKEKDGFVFD--ELDLTISQARKTLNSWKNK 281
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
656-859 |
1.38e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 61.36 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 656 GEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS------------VAYVPQQAWIQND-SL 722
Cdd:PRK13537 18 GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpvpsrarharqrVGVVPQFDNLDPDfTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 723 RENIL-FGHplqenYYKAVMEAC-ALLPDL---EILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNSDIYLFDDPLSA 797
Cdd:PRK13537 98 RENLLvFGR-----YFGLSAAAArALVPPLlefAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6678848 798 VDAHVGKHIFEKVVGPMGllKNKTRILVTHGISYLPQV--DVIIVMSGGKISEmGSYQELLDRD 859
Cdd:PRK13537 169 LDPQARHLMWERLRSLLA--RGKTILLTTHFMEEAERLcdRLCVIEEGRKIAE-GAPHALIESE 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1310-1514 |
1.54e-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: 62.51 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1310 INVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII----DGVNIAKIGLHNL-RFK--ITIIPQDPVLFSGslR 1382
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDGRgRAKryIGILHQEYDLYPH--R 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1383 MNLDPFSQYSDEEvwMALELAHLK--------GF-----VSALpDKLNHEcaeggenLSVGQRQLVCLARALLRKTKILV 1449
Cdd:TIGR03269 381 TVLDNLTEAIGLE--LPDELARMKavitlkmvGFdeekaEEIL-DKYPDE-------LSEGERHRVALAQVLIKEPRIVI 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6678848 1450 LDEATAAVDLETDNLIQSTI---RTQFEDcTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELLQQ 1514
Cdd:TIGR03269 451 LDEPTGTMDPITKVDVTHSIlkaREEMEQ-TFIIVSHDMDFVLDVCdRAALMRDGKIVKIGDPEEIVEE 518
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
643-856 |
1.55e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 60.62 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 643 SITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLlSALLAEMDK-------VEGHVTLKGSVAYVPQQa 715
Cdd:COG4167 11 SKTFKYRTGLFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTL-AKMLAGIIEptsgeilINGHKLEYGDYKYRCKH- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 716 wIQ------NDSLRENILFGH----PL----------QENYYKAVMEACALLPD-LEILPSgdrteigekgvNLSGGQKQ 774
Cdd:COG4167 89 -IRmifqdpNTSLNPRLNIGQileePLrlntdltaeeREERIFATLRLVGLLPEhANFYPH-----------MLSSGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 775 RVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIF-------EKvvgpMGLlknkTRILVTHG------ISylpqvDVIIVM 841
Cdd:COG4167 157 RVALARALILQPKIIIADEALAALDMSVRSQIInlmlelqEK----LGI----SYIYVSQHlgivkhIS-----DKVLVM 223
|
250
....*....|....*
gi 6678848 842 SGGKISEMGSYQELL 856
Cdd:COG4167 224 HQGEVVEYGKTAEVF 238
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1306-1514 |
1.58e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 60.37 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIA-------------KIGLHNLRFKITIIPQ 1372
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1373 DPVLFSgslRMNLDPFSQYSDEEVwMALELAHLKGFVSALPDKLNHECAEGGE---NLSVGQRQLVCLARALLRKTKILV 1449
Cdd:PRK10619 100 HFNLWS---HMTVLENVMEAPIQV-LGLSKQEARERAVKYLAKVGIDERAQGKypvHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6678848 1450 LDEATAAVDLEtdnLIQSTIRTQF----EDCTVLTIAHRlntiMDYTR-----VIVLDKGEVRECGAPSELLQQ 1514
Cdd:PRK10619 176 FDEPTSALDPE---LVGEVLRIMQqlaeEGKTMVVVTHE----MGFARhvsshVIFLHQGKIEEEGAPEQLFGN 242
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1317-1503 |
1.64e-09 |
|
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: 59.62 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1317 GEKVGIVGRTGAGKSSL---TLGLFRINEsaeGEIIIDGVNI----AKIGLHNLRFKITIIPQDPVLFSG-SLRMNL--- 1385
Cdd:cd03297 23 EEVTGIFGASGAGKSTLlrcIAGLEKPDG---GTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYALFPHlNVRENLafg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1386 -----DPFSQYSDEEVWMALELAHLKGfvsALPDKLnhecaeggenlSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1460
Cdd:cd03297 100 lkrkrNREDRISVDELLDLLGLDHLLN---RYPAQL-----------SGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6678848 1461 TDNLIQSTIRTQFED--CTVLTIAHRLNTIMDYT-RVIVLDKGEVR 1503
Cdd:cd03297 166 LRLQLLPELKQIKKNlnIPVIFVTHDLSEAEYLAdRIVVMEDGRLQ 211
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1306-1458 |
1.66e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 61.50 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLtLGLFRINESA-EGEIIIDGVNIAKIGLH----NLRFK-------ITIIpqD 1373
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTV-LRLIAGFETPdSGRIMLDGQDITHVPAEnrhvNTVFQsyalfphMTVF--E 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1374 PVLFSgsLRMNLDPFSQYsDEEVWMALELAHLKGFVSALPdklnhecaeggENLSVGQRQLVCLARALLRKTKILVLDEA 1453
Cdd:PRK09452 106 NVAFG--LRMQKTPAAEI-TPRVMEALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
....*
gi 6678848 1454 TAAVD 1458
Cdd:PRK09452 172 LSALD 176
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1305-1492 |
1.72e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 60.57 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1305 LVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINE-----SAEGEIIIDGVNI--AKIGLHNLRFKITIIPQDPVLF 1377
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1378 SGSLRMNL------DPFSQYSDEEVWMALELAHLKGFVSalpDKLNhecaEGGENLSVGQRQLVCLARALLRKTKILVLD 1451
Cdd:PRK14243 104 PKSIYDNIaygariNGYKGDMDELVERSLRQAALWDEVK---DKLK----QSGLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6678848 1452 EATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNT---IMDYT 1492
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQaarVSDMT 220
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1290-1506 |
1.74e-09 |
|
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: 59.58 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGV----------NIAKI- 1358
Cdd:cd03301 1 VELENVTKRFGNVT--ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtdlppkdrDIAMVf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1359 ----------GLHNLRF--KITIIPQDPVlfsgslrmnldpfsqysDEEVWMALELAHLKGFVSALPDKlnhecaeggen 1426
Cdd:cd03301 79 qnyalyphmtVYDNIAFglKLRKVPKDEI-----------------DERVREVAELLQIEHLLDRKPKQ----------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1427 LSVGQRQLVCLARALLRKTKILVLDEATAAVDLetdnLIQSTIRTQFEdctvlTIAHRLNTIMDY------------TRV 1494
Cdd:cd03301 131 LSGGQRQRVALGRAIVREPKVFLMDEPLSNLDA----KLRVQMRAELK-----RLQQRLGTTTIYvthdqveamtmaDRI 201
|
250
....*....|..
gi 6678848 1495 IVLDKGEVRECG 1506
Cdd:cd03301 202 AVMNDGQIQQIG 213
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1308-1502 |
1.98e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.99 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1308 KHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHN-LRFKITIIPQD---PVLF-SGSLR 1382
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEDrqsSGLYlDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1383 MNLDPFSqYSDEEVWM--ALELAHLKGFVSALPDKLNHECAEGGeNLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1460
Cdd:PRK15439 360 WNVCALT-HNRRGFWIkpARENAVLERYRRALNIKFNHAEQAAR-TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6678848 1461 TDNLIQSTIRTQFEDCT-VLTIAHRLNTIMDYT-RVIVLDKGEV 1502
Cdd:PRK15439 438 ARNDIYQLIRSIAAQNVaVLFISSDLEEIEQMAdRVLVMHQGEI 481
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1306-1513 |
3.00e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.84 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLtLGLF--RINESAE-------GEIIIDGVNIAKIGLHNLRFKITIIPQ--DP 1374
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTL-LKALagDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQaaQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1375 VL-FSGSLRMNLDPF---------SQYSDEEVWMALELAHLKGFVsalpdklnhecAEGGENLSVGQRQLVCLARAL--- 1441
Cdd:PRK13547 95 AFaFSAREIVLLGRYpharragalTHRDGEIAWQALALAGATALV-----------GRDVTTLSGGELARVQFARVLaql 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1442 ------LRKTKILVLDEATAAVDLETDNLIQSTIRTQFED--CTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELL 1512
Cdd:PRK13547 164 wpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwnLGVLAIVHDPNLAARHAdRIAMLADGAIVAHGAPADVL 243
|
.
gi 6678848 1513 Q 1513
Cdd:PRK13547 244 T 244
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
644-855 |
3.66e-09 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 58.54 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWarGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMDKVEGHV----------TLKGSVAYV 711
Cdd:cd03265 1 IEVENLVKKY--GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLttLLKPTSGRATVaghdvvreprEVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 712 PQQAWIQND-SLRENI-----LFGHPLQENYYKAvmeacallpdLEILPSGDRTEIGEKGV-NLSGGQKQRVSLARAVYS 784
Cdd:cd03265 79 FQDLSVDDElTGWENLyiharLYGVPGAERRERI----------DELLDFVGLLEAADRLVkTYSGGMRRRLEIARSLVH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 785 NSDIYLFDDPLSAVDAHVGKHIFEkVVGPMGLLKNKTRILVTHgisYLPQV----DVIIVMSGGKISEMGSYQEL 855
Cdd:cd03265 149 RPEVLFLDEPTIGLDPQTRAHVWE-YIEKLKEEFGMTILLTTH---YMEEAeqlcDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
975-1245 |
3.69e-09 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 59.73 E-value: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 975 IFLFLCNhVSALASNYWLSLWTDDppVVNGTQANRNFRLSVYGALGILQGAAIFGYSMAVSIGGifASRRLHLDL---LY 1051
Cdd:cd18541 6 LFLILVD-LLQLLIPRIIGRAIDA--LTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFG--ASRRIEYDLrndLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1052 N-VLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATP---IAAVIIPPL--GLVYFF 1125
Cdd:cd18541 81 AhLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPkltLIALLPLPLlaLLVYRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1126 VQRFYVASSRQLKRLESVSrspvySHFNETLLGVSVIRAF----EEQERFIHQSDLKVDENQK------AYYPSIVanrw 1195
Cdd:cd18541 161 GKKIHKRFRKVQEAFSDLS-----DRVQESFSGIRVIKAFvqeeAEIERFDKLNEEYVEKNLRlarvdaLFFPLIG---- 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 6678848 1196 LAVRLecvGNCIVLFAALFAVIsRHSLSAG-LVglsvsyslQITAYLNWLV 1245
Cdd:cd18541 232 LLIGL---SFLIVLWYGGRLVI-RGTITLGdLV--------AFNSYLGMLI 270
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1306-1461 |
5.33e-09 |
|
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: 58.21 E-value: 5.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLtLGLFRINESA-EGEIIIDGVNIAKI---GLHNLRF-KITIIPQDPVLFsGS 1380
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTL-LGLLAGLDRPtSGTVRLAGQDLFALdedARARLRArHVGFVFQSFQLL-PT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1381 LRMnLdpfsqysdEEVWMALELA-HLKGFVSA--------LPDKLNHECAEggenLSVGQRQLVCLARALLRKTKILVLD 1451
Cdd:COG4181 105 LTA-L--------ENVMLPLELAgRRDARARArallervgLGHRLDHYPAQ----LSGGEQQRVALARAFATEPAILFAD 171
|
170
....*....|
gi 6678848 1452 EATAAVDLET 1461
Cdd:COG4181 172 EPTGNLDAAT 181
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1313-1490 |
5.57e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 59.59 E-value: 5.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1313 TIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIA---KIGLHNLRFKITIIPQDPVlfsGS--------- 1380
Cdd:PRK11308 37 TLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadPEAQKLLRQKIQIVFQNPY---GSlnprkkvgq 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1381 -----LRMNLDPFSQYSDEEVWMALELAHLKgfvsalP---DKLNHEcaeggenLSVGQRQLVCLARALLRKTKILVLDE 1452
Cdd:PRK11308 114 ileepLLINTSLSAAERREKALAMMAKVGLR------PehyDRYPHM-------FSGGQRQRIAIARALMLDPDVVVADE 180
|
170 180 190
....*....|....*....|....*....|....*...
gi 6678848 1453 ATAAVDLetdnliqsTIRTQFedctvltiahrLNTIMD 1490
Cdd:PRK11308 181 PVSALDV--------SVQAQV-----------LNLMMD 199
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1307-1515 |
6.84e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 59.07 E-value: 6.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1307 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNI----AKIGLHNLRFKITIIPQDP--VLFSGS 1380
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKKLRKKVSLVFQFPeaQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1381 LRMNLD--P--FSQYSDEEVWMALELAHLKGFVSALPDKLNHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAA 1456
Cdd:PRK13641 103 VLKDVEfgPknFGFSEDEAKEKALKWLKKVGLSEDLISKSPFE-------LSGGQMRRVAIAGVMAYEPEILCLDEPAAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6678848 1457 VDLET-DNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTR-VIVLDKGEVRECGAPSELLQQR 1515
Cdd:PRK13641 176 LDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADdVLVLEHGKLIKHASPKEIFSDK 236
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
661-875 |
6.91e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 58.49 E-value: 6.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 661 LNGITFSIPEGALVAVVGQVGCGKSSLL---SALLAEMDKVEGHVTLKGSV------------------AYVPQQAWIQN 719
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLrhlSGLITGDKSAGSHIELLGRTvqregrlardirksrantGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 720 D-SLRENILFGHPLQENYYKAVMEACALLPDLEILPSGDRTEIG----EKGVNLSGGQKQRVSLARAVYSNSDIYLFDDP 794
Cdd:PRK09984 100 RlSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALTRVGMVhfahQRVSTLSGGQQQRVAIARALMQQAKVILADEP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 795 LSAVDAHVGKHIFEkVVGPMGLLKNKTRILVTHGISY-LPQVDVIIVMSGGKISEMGSYQElLDRDgAFAEFLRTYANAE 873
Cdd:PRK09984 180 IASLDPESARIVMD-TLRDINQNDGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGSSQQ-FDNE-RFDHLYRSINRVE 256
|
..
gi 6678848 874 QD 875
Cdd:PRK09984 257 EN 258
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
665-799 |
7.16e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 58.05 E-value: 7.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 665 TFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS--VAYVPQQAWI----QNDSL------RENILFG-HP 731
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhTTTPPSRRPVsmlfQENNLfshltvAQNIGLGlNP 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6678848 732 -LQENYY-KAVMEACA----LLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVD 799
Cdd:PRK10771 99 gLKLNAAqREKLHAIArqmgIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
661-856 |
7.18e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 58.52 E-value: 7.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMD----KVEGHV-------------TLKGSVAYVPQQA-WIQND 720
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLnrLIEIYdskiKVDGKVlyfgkdifqidaiKLRKEVGMVFQQPnPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 721 SLRENILF---GHPLQENY-YKAVMEACALLPDL--EILpsgDRteIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDP 794
Cdd:PRK14246 106 SIYDNIAYplkSHGIKEKReIKKIVEECLRKVGLwkEVY---DR--LNSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6678848 795 LSAVDAhVGKHIFEKVVGPmgLLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELL 856
Cdd:PRK14246 181 TSMIDI-VNSQAIEKLITE--LKNEIAIVIVSHNPQQVARVaDYVAFLYNGELVEWGSSNEIF 240
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
644-799 |
7.52e-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: 7.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWARGEPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSAlLAEM-DKVEGHVTL--KGSVAYVPQQAWIQND 720
Cdd:cd03223 1 IELENLSLATPDGRV-LLKDLSFEIKPGDRLLITGPSGTGKSSLFRA-LAGLwPWGSGRIGMpeGEDLLFLPQRPYLPLG 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6678848 721 SLRENIlfghplqenyykavmeacallpdleILPSGDRteigekgvnLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVD 799
Cdd:cd03223 79 TLREQL-------------------------IYPWDDV---------LSGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1306-1485 |
7.56e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 58.57 E-value: 7.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEG-----EIIIDGVNIAKI-GLHNLRFKITIIPQDPVLFSG 1379
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1380 SLRMN---------LDPFSQYSDEEVWMALELahlkGFVSALPDKLnhecAEGGENLSVGQRQLVCLARALLRKTKILVL 1450
Cdd:PRK14271 116 SIMDNvlagvrahkLVPRKEFRGVAQARLTEV----GLWDAVKDRL----SDSPFRLSGGQQQLLCLARTLAVNPEVLLL 187
|
170 180 190
....*....|....*....|....*....|....*
gi 6678848 1451 DEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRL 1485
Cdd:PRK14271 188 DEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNL 222
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
1001-1225 |
8.92e-09 |
|
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: 58.60 E-value: 8.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1001 VVNGTQANRNFRLSVYGALGILQGAAIFG----YSMAVSigGIFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKE 1076
Cdd:cd18551 25 LIDALSAGGSSGGLLALLVALFLLQAVLSalssYLLGRT--GERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTND 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1077 LDTVDSMIPQVIKMFMGSLFSVIGAVI-----------IILLATPIAAVIIPPLGlvyffvQRFYVASSRQLKRLESVSr 1145
Cdd:cd18551 103 TTLLRELITSGLPQLVTGVLTVVGAVVlmflldwvltlVTLAVVPLAFLIILPLG------RRIRKASKRAQDALGELS- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1146 spvySHFNETLLGVSVIRAF--EEQErfihqSDLKVDENQKAYYPSIVANRWLAVrLECVGNcIVLFAALFAVI------ 1217
Cdd:cd18551 176 ----AALERALSAIRTVKASnaEERE-----TKRGGEAAERLYRAGLKAAKIEAL-IGPLMG-LAVQLALLVVLgvggar 244
|
....*....
gi 6678848 1218 -SRHSLSAG 1225
Cdd:cd18551 245 vASGALTVG 253
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1306-1497 |
1.11e-08 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 56.73 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDPVLFSGSLRMNL 1385
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1386 DPFSQY-SDEEVWMALELAHLKGFVSALpdklnheCAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNL 1464
Cdd:cd03231 95 RFWHADhSDEQVEEALARVGLNGFEDRP-------VAQ----LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180 190
....*....|....*....|....*....|....*
gi 6678848 1465 IQSTIRTQFED--CTVLTIAHRLNTIMDYTRVIVL 1497
Cdd:cd03231 164 FAEAMAGHCARggMVVLTTHQDLGLSEAGARELDL 198
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
661-856 |
1.17e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 58.18 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHvTLKGSVAYVPQQAWIQNDSL----RENILFGHP----- 731
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGY-RYSGDVLLGGRSIFNYRDVLefrrRVGMLFQRPnpfpm 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 732 -LQENYYKAVmEACALLPDLEI--LPSGDRTEIG----------EKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAV 798
Cdd:PRK14271 116 sIMDNVLAGV-RAHKLVPRKEFrgVAQARLTEVGlwdavkdrlsDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSAL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6678848 799 DAHVGKHIFEKVvgpMGLLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELL 856
Cdd:PRK14271 195 DPTTTEKIEEFI---RSLADRLTVIIVTHNLAQAARIsDRAALFFDGRLVEEGPTEQLF 250
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
656-827 |
1.74e-08 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 56.52 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 656 GEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSvayvPQQAWIQNDslrenilFGH-PLQE 734
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK----PLDIAARNR-------IGYlPEER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 735 NYYK--AVMEACALLPDL------EILPSGD----RTEIGEKGV----NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAV 798
Cdd:cd03269 80 GLYPkmKVIDQLVYLAQLkglkkeEARRRIDewleRLELSEYANkrveELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190
....*....|....*....|....*....|
gi 6678848 799 DAhVGKHIFEKVVgpMGLL-KNKTRILVTH 827
Cdd:cd03269 160 DP-VNVELLKDVI--RELArAGKTVILSTH 186
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1019-1261 |
1.82e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 57.91 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1019 LGILQGAAIFGYS---MAVSIGGIFASRrLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSL 1095
Cdd:cd18564 61 VGIALLRGLASYAgtyLTALVGQRVVLD-LRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1096 FSVIGAVIIIL-----LATpIAAVIIPPLGLVYFFVQRFYVASSRQLKRLESVsrspVYSHFNETLLGVSVIRAF----E 1166
Cdd:cd18564 140 LTLVGMLGVMFwldwqLAL-IALAVAPLLLLAARRFSRRIKEASREQRRREGA----LASVAQESLSAIRVVQAFgreeH 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1167 EQERFIHQSDLKVDENQKAYYPSIVANRWLAVrLECVGNCIVLFAALFAVIsRHSLSAGlvGLSVsyslqITAYLNWL-- 1244
Cdd:cd18564 215 EERRFARENRKSLRAGLRAARLQALLSPVVDV-LVAVGTALVLWFGAWLVL-AGRLTPG--DLLV-----FLAYLKNLyk 285
|
250 260
....*....|....*....|..
gi 6678848 1245 -VRMSSEMETNI----VAVERL 1261
Cdd:cd18564 286 pVRDLAKLTGRIakasASAERV 307
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
661-799 |
1.98e-08 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 56.78 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG--------------SVAYVPQQAWIQND-SLREN 725
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditklpmhkrarlGIGYLPQEASIFRKlTVEEN 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 726 ILFGHPLQENYYKAVME-ACALLPDLEILPSGDRteigeKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVD 799
Cdd:cd03218 96 ILAVLEIRGLSKKEREEkLEELLEEFHITHLRKS-----KASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1297-1511 |
2.05e-08 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 56.61 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1297 LRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKiGLHNLRFKITIIPQDPVL 1376
Cdd:cd03265 6 LVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1377 fsgslrmnldpfsqysDEEV--WMALEL-AHLKGFVSALPDKLNHECAEGGE----------NLSVGQRQLVCLARALLR 1443
Cdd:cd03265 85 ----------------DDELtgWENLYIhARLYGVPGAERRERIDELLDFVGlleaadrlvkTYSGGMRRRLEIARSLVH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6678848 1444 KTKILVLDEATAAVDLETDNLIQSTIRTQFE--DCTVLTIAHRL---NTIMDytRVIVLDKGEVRECGAPSEL 1511
Cdd:cd03265 149 RPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMeeaEQLCD--RVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
660-843 |
2.17e-08 |
|
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: 56.65 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 660 TLNGITFSIPEGAL-----VAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-SVAYVPQQAWIQNDSLRENILFG---H 730
Cdd:cd03237 9 TLGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYIKADYEGTVRDLLSSitkD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 731 PLQENYYKAvmeacALLPDLEILPSGDRtEIGEkgvnLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHvGKHIFEKV 810
Cdd:cd03237 89 FYTHPYFKT-----EIAKPLQIEQILDR-EVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE-QRLMASKV 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 6678848 811 VGPMGLLKNKTRILVTHGI---SYLpqVDVIIVMSG 843
Cdd:cd03237 158 IRRFAENNEKTAFVVEHDIimiDYL--ADRLIVFEG 191
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
1020-1247 |
2.24e-08 |
|
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: 57.41 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1020 GILQGAAIFGYSMAVsIGGIFAS-------RRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFM 1092
Cdd:cd18548 43 LLMLLLALLGLIAGI-LAGYFAAkasqgfgRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1093 GSLFSVIGAVIIILLATP----IAAVIIPPLGLVYFFVQRF-YVASSRQLKRLESVSRSpvyshFNETLLGVSVIRAF-- 1165
Cdd:cd18548 122 RAPIMLIGAIIMAFRINPklalILLVAIPILALVVFLIMKKaIPLFKKVQKKLDRLNRV-----VRENLTGIRVIRAFnr 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1166 --EEQERFIhqsdlkvDENQKAYYPSIVANRWLAVR---LECVGN----CIVLFAALFavISRHSLSAG-LVGLsVSYSL 1235
Cdd:cd18548 197 edYEEERFD-------KANDDLTDTSLKAGRLMALLnplMMLIMNlaivAILWFGGHL--INAGSLQVGdLVAF-INYLM 266
|
250
....*....|..
gi 6678848 1236 QITAYLNWLVRM 1247
Cdd:cd18548 267 QILMSLMMLSMV 278
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
661-859 |
2.49e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 57.55 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEM----------DKVEGHVTLKGSVAYVPQQAWIQN----------- 719
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIkskygtiqvgDIYIGDKKNNHELITNPYSKKIKNfkelrrrvsmv 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 720 ----------DSLRENILFGhP--LQENYYKAVMEACALLPDLEI-LPSGDRTEIGekgvnLSGGQKQRVSLARAVYSNS 786
Cdd:PRK13631 122 fqfpeyqlfkDTIEKDIMFG-PvaLGVKKSEAKKLAKFYLNKMGLdDSYLERSPFG-----LSGGQKRRVAIAGILAIQP 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 787 DIYLFDDPLSAVDAHvGKHIFekvvgpMGLLK-----NKTRILVTHGISYLPQV-DVIIVMSGGKISEMGS-YQELLDRD 859
Cdd:PRK13631 196 EILIFDEPTAGLDPK-GEHEM------MQLILdakanNKTVFVITHTMEHVLEVaDEVIVMDKGKILKTGTpYEIFTDQH 268
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
661-869 |
2.57e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 58.36 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 661 LNGITFSIPEGALVAVVGQVGCGKSSlLSALLAEMD-KVEGHVTLKGSVAYVPQQAWIQND-SLRENILFghplqenyyK 738
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKST-LSNLIAGVTmPNKGTVDIKGSAALIAISSGLNGQlTGIENIEL---------K 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 739 AVMEACALLPDLEILPSG-DRTEIGeKGVN-----LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKvvg 812
Cdd:PRK13545 110 GLMMGLTKEKIKEIIPEIiEFADIG-KFIYqpvktYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDK--- 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6678848 813 pMGLLKN--KTRILVTHGISylpQVDVI----IVMSGGKISEMGSYQELLDRdgaFAEFLRTY 869
Cdd:PRK13545 186 -MNEFKEqgKTIFFISHSLS---QVKSFctkaLWLHYGQVKEYGDIKEVVDH---YDEFLKKY 241
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1307-1488 |
2.67e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 58.30 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1307 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRI--NESAEGEIIIDGVNIAKIGLHNLRFK-ITIIPQDPVLFSgslrm 1383
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVP----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1384 NLDPFsqysdEEVWMALELAHlKGFVSALPdKLNHECAEGGENLSV--------------GQRQLVCLARALLRKTKILV 1449
Cdd:TIGR02633 92 ELSVA-----ENIFLGNEITL-PGGRMAYN-AMYLRAKNLLRELQLdadnvtrpvgdyggGQQQLVEIAKALNKQARLLI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6678848 1450 LDEATAAV-DLETDNLIQSTIRTQFEDCTVLTIAHRLNTI 1488
Cdd:TIGR02633 165 LDEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEV 204
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1305-1501 |
2.85e-08 |
|
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: 54.38 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1305 LVLKHINVTIEGGEKVGIVGRTGAGKSSLtlglfrinesaegeiiidgvniakiglhnlrfkITIIPQDPVLFSGSLRmn 1384
Cdd:cd03221 14 LLLKDISLTINPGDRIGLVGRNGAGKSTL---------------------------------LKLIAGELEPDEGIVT-- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1385 ldpfsqysdeevWMA-LELAHLkgfvsalpdklnhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDN 1463
Cdd:cd03221 59 ------------WGStVKIGYF-------------------EQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIE 107
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6678848 1464 LIQSTIRTQfeDCTVLTIAH-R--LNTIMdyTRVIVLDKGE 1501
Cdd:cd03221 108 ALEEALKEY--PGTVILVSHdRyfLDQVA--TKIIELEDGK 144
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1306-1458 |
3.69e-08 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 55.90 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIID----GVNIAKIG---LHNLRfKITI--------- 1369
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASpreILALR-RRTIgyvsqflrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1370 IPQ--------DPVLFSGslrmnldpfsqYSDEEvwmALE-----LAHLKgfvsaLPDKLNHecaeggenL-----SVGQ 1431
Cdd:COG4778 105 IPRvsaldvvaEPLLERG-----------VDREE---ARArarelLARLN-----LPERLWD--------LppatfSGGE 157
|
170 180
....*....|....*....|....*..
gi 6678848 1432 RQLVCLARALLRKTKILVLDEATAAVD 1458
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLD 184
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1307-1500 |
5.56e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.49 E-value: 5.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1307 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGlHNLRFK--ITIIPQD-PVLFSGSLRM 1383
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD-HKLAAQlgIGIIYQElSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1384 NLdPFSQYSDEEVW--MALELAHLKGFVSALPDK--LNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAV-D 1458
Cdd:PRK09700 100 NL-YIGRHLTKKVCgvNIIDWREMRVRAAMMLLRvgLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtN 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6678848 1459 LETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDY-TRVIVLDKG 1500
Cdd:PRK09700 179 KEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRIcDRYTVMKDG 221
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
668-843 |
7.36e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.13 E-value: 7.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 668 IPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQqaWIQNDS-------LRENilfGHPLQENYYKAv 740
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQ--YIKPDYdgtvedlLRSI---TDDLGSSYYKS- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 741 meacallpdlEILPSGDRTEIGEKGVN-LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVD-------AHVGKHIFEKvvg 812
Cdd:PRK13409 436 ----------EIIKPLQLERLLDKNVKdLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavAKAIRRIAEE--- 502
|
170 180 190
....*....|....*....|....*....|....
gi 6678848 813 pmgllKNKTRILVTHGIS---YLpqVDVIIVMSG 843
Cdd:PRK13409 503 -----REATALVVDHDIYmidYI--SDRLMVFEG 529
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
965-1260 |
8.15e-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: 55.59 E-value: 8.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 965 AIGLFITFLSIFLflcnhvsALASNYWLSLWTDDppVVNGTQANRNFRLsVYGALGILQGAAIFGYSMAVSIG--GIFAS 1042
Cdd:cd18563 2 ILGFLLMLLGTAL-------GLVPPYLTKILIDD--VLIQLGPGGNTSL-LLLLVLGLAGAYVLSALLGILRGrlLARLG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1043 RRLHLDL---LYNVL-RSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVIIIL-----LAtpiAA 1113
Cdd:cd18563 72 ERITADLrrdLYEHLqRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFslnwkLA---LL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1114 VIIP-PL--GLVYFFVQRFYVASSRQLKRlesvsRSPVYSHFNETLLGVSVIRAF----EEQERFIHQSDLKVDENQKA- 1185
Cdd:cd18563 149 VLIPvPLvvWGSYFFWKKIRRLFHRQWRR-----WSRLNSVLNDTLPGIRVVKAFgqekREIKRFDEANQELLDANIRAe 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1186 -----YYPSIVAnrwlavrLECVGNCIVLFAALFAVISRHsLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVER 1260
Cdd:cd18563 224 klwatFFPLLTF-------LTSLGTLIVWYFGGRQVLSGT-MTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAER 295
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1015-1260 |
9.12e-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: 349984 [Multi-domain] Cd Length: 295 Bit Score: 55.56 E-value: 9.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1015 VYGALGILQGAAIFGYSMAVSIGGIFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGS 1094
Cdd:cd18540 47 LYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1095 LFSVIGAVIIILLATP----IAAVIIPPLGLVYFFVQRFYVASSRQLKRLESVsrspVYSHFNETLLGVSVIRAF--EEQ 1168
Cdd:cd18540 127 ITYMIGILIVMLILNWklalIVLAVVPVLAVVSIYFQKKILKAYRKVRKINSR----ITGAFNEGITGAKTTKTLvrEEK 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1169 erfiHQSDLKVDeNQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLV---GLSV--SYSLQITAYLNW 1243
Cdd:cd18540 203 ----NLREFKEL-TEEMRRASVRAARLSALFLPIVLFLGSIATALVLWYGGILVLAGAItigTLVAfiSYATQFFEPIQQ 277
|
250
....*....|....*..
gi 6678848 1244 LVRMSSEMETNIVAVER 1260
Cdd:cd18540 278 LARVLAELQSAQASAER 294
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1317-1503 |
1.08e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.48 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1317 GEKVGIVGRTGAGKSSLTLGLFRINESA-EGEIIIDGvniAKIGLHN----LRFKITIIPQD-------PVLFSG--SLR 1382
Cdd:PRK13549 288 GEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDG---KPVKIRNpqqaIAQGIAMVPEDrkrdgivPVMGVGknITL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1383 MNLDPFSQYS--DEevwmALELAHLKGFVSALPDKLNHECAEGGeNLSVGQRQLVCLARALLRKTKILVLDEATAAVDL- 1459
Cdd:PRK13549 365 AALDRFTGGSriDD----AAELKTILESIQRLKVKTASPELAIA-RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVg 439
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6678848 1460 ---ETDNLIQSTIRtqfEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVR 1503
Cdd:PRK13549 440 akyEIYKLINQLVQ---QGVAIIVISSELPEVLGLSdRVLVMHEGKLK 484
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
1038-1164 |
1.57e-07 |
|
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: 54.91 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1038 GIFASRRLHLDLLYNV----LRSPMSFFERTPSGNLVNRFSkELDTV-DSMIPQVIKMFMGSLFSVIGAVIIILLATPIA 1112
Cdd:cd18782 66 FTDTANRIDLELGGTIidhlLRLPLGFFDKRPVGELSTRIS-ELDTIrGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLT 144
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 1113 AVI---IPPLGLVYFFVQRFYvasSRQLKRLESvSRSPVYSHFNETLLGVSVIRA 1164
Cdd:cd18782 145 LVVlatVPLQLLLTFLFGPIL---RRQIRRRAE-ASAKTQSYLVESLTGIQTVKA 195
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
661-859 |
1.60e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.41 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS-------------VAYVPQQ-AWIQNDSLRENI 726
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleswsskafarkVAYLPQQlPAAEGMTVRELV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 727 LFG-HPL--------QENYYKaVMEACALLpdleilpsgDRTEIGEKGVN-LSGGQKQRVSLARAVYSNSDIYLFDDPLS 796
Cdd:PRK10575 107 AIGrYPWhgalgrfgAADREK-VEEAISLV---------GLKPLAHRLVDsLSGGERQRAWIAMLVAQDSRCLLLDEPTS 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 797 AVD-AHVGKHIfeKVVGPMGLLKNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQELLDRD 859
Cdd:PRK10575 177 ALDiAHQVDVL--ALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
659-810 |
1.64e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.42 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 659 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS------VAYVPQQAWIQNDS-------LREN 725
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsikkdlCTYQKQLCFVGHRSginpyltLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 726 ILFG-HPLQENYykAVMEACAL--LPDLEILPSGdrteigekgvNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHV 802
Cdd:PRK13540 95 CLYDiHFSPGAV--GITELCRLfsLEHLIDYPCG----------LLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
....*...
gi 6678848 803 GKHIFEKV 810
Cdd:PRK13540 163 LLTIITKI 170
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1306-1458 |
1.91e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 55.41 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--VNI--------AKIGL-------------HN 1362
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIrsprdairAGIAYvpedrkgeglvldLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1363 LRFKITIipqdPVLFSGSLRMNLDPfsqysdeevwmALELAHLKGFVSAL---PDKLNHECAeggeNLSVGQRQLVCLAR 1439
Cdd:COG1129 347 IRENITL----ASLDRLSRGGLLDR-----------RRERALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAK 407
|
170
....*....|....*....
gi 6678848 1440 ALLRKTKILVLDEATAAVD 1458
Cdd:COG1129 408 WLATDPKVLILDEPTRGID 426
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
661-827 |
2.02e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 53.63 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-----------------SVAYVPQQ-AWIQNDSL 722
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGqplhqmdeearaklrakHVGFVFQSfMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 723 RENILFGHPLQ-ENYYKAVMEACALLPDLEIlpsGDRteIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAH 801
Cdd:PRK10584 106 LENVELPALLRgESSRQSRNGAKALLEQLGL---GKR--LDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
|
170 180
....*....|....*....|....*.
gi 6678848 802 VGKHIFEkVVGPMGLLKNKTRILVTH 827
Cdd:PRK10584 181 TGDKIAD-LLFSLNREHGTTLILVTH 205
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1306-1511 |
2.11e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 54.70 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLtlglFRI----NESAEGEIIIDGVNIA-------KIG--------------L 1360
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTL----LRIiaglEHQTSGHIRFHGTDVSrlhardrKVGfvfqhyalfrhmtvF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1361 HNLRFKITIIPQDPvlfsgslrmnlDPFSQYSDEEVWMALELAHLKGFVSALPDKLnhecaeggenlSVGQRQLVCLARA 1440
Cdd:PRK10851 93 DNIAFGLTVLPRRE-----------RPNAAAIKAKVTQLLEMVQLAHLADRYPAQL-----------SGGQKQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6678848 1441 LLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDC--TVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSEL 1511
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHDQEEAMEVAdRVVVMSQGNIEQAGTPDQV 224
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1296-1465 |
2.15e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 53.67 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1296 CLRYRED--LDLVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIG-------------- 1359
Cdd:PRK11629 12 CKRYQEGsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaakaelrnqklgf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1360 ---LHNLRFKITIIPQD--PVLFSGSLRMNldpfSQYSDEEVWMALELAHlkgfvsalpdKLNHECAEggenLSVGQRQL 1434
Cdd:PRK11629 92 iyqFHHLLPDFTALENVamPLLIGKKKPAE----INSRALEMLAAVGLEH----------RANHRPSE----LSGGERQR 153
|
170 180 190
....*....|....*....|....*....|.
gi 6678848 1435 VCLARALLRKTKILVLDEATAAVDLETDNLI 1465
Cdd:PRK11629 154 VAIARALVNNPRLVLADEPTGNLDARNADSI 184
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
644-875 |
2.59e-07 |
|
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: 55.19 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWarGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMDKVEGHVTLKgsVAYVPQQAWIQNDS 721
Cdd:TIGR03269 1 IEVKNLTKKF--DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIYH--VALCEKCGYVERPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 722 L-------------RENILFGHPlQENYYKAVMEACALLPDLEILPSGDRT----------EIGEKGV------------ 766
Cdd:TIGR03269 77 KvgepcpvcggtlePEEVDFWNL-SDKLRRRIRKRIAIMLQRTFALYGDDTvldnvlealeEIGYEGKeavgravdliem 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 767 ------------NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVVGpmGLLKNKTRILVThgiSYLPQ 834
Cdd:TIGR03269 156 vqlshrithiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEE--AVKASGISMVLT---SHWPE 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 6678848 835 V-----DVIIVMSGGKISEMGSYQELLDRdgafaeFLRTYANAEQD 875
Cdd:TIGR03269 231 ViedlsDKAIWLENGEIKEEGTPDEVVAV------FMEGVSEVEKE 270
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
667-843 |
2.66e-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: 55.18 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 667 SIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQqaWIQNDS-------LRENIlfGHPLQENYYKA 739
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQ--YISPDYdgtveefLRSAN--TDDFGSSYYKT 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 740 vmeacallpdlEILPSGDRTEIGEKGV-NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVD-------AHVGKHIFEKvv 811
Cdd:COG1245 438 -----------EIIKPLGLEKLLDKNVkDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavAKAIRRFAEN-- 504
|
170 180 190
....*....|....*....|....*....|...
gi 6678848 812 gpmgllKNKTRILVTHGISYLPQV-DVIIVMSG 843
Cdd:COG1245 505 ------RGKTAMVVDHDIYLIDYIsDRLMVFEG 531
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1306-1452 |
2.74e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 53.34 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNI-----AKIglhnLRFKITIIPQDPVLFSgs 1380
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItdwqtAKI----MREAVAIVPEGRRVFS-- 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6678848 1381 lRMNLDpfsqysdEEVWMALELAHLKGF------VSALPDKLNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDE 1452
Cdd:PRK11614 94 -RMTVE-------ENLAMGGFFAERDQFqerikwVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
631-847 |
2.83e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.03 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 631 IERRSIKSGEgNSITVKNATFTWARGEPPtLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS--- 707
Cdd:COG3845 246 VEKAPAEPGE-VVLEVENLSVRDDRGVPA-LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEdit 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 708 -----------VAYVPQ----QAWIQNDSLRENILFGHPLQENY-------YKAVMEACA-LLPDLEILPSGDRTEIGek 764
Cdd:COG3845 324 glsprerrrlgVAYIPEdrlgRGLVPDMSVAENLILGRYRRPPFsrggfldRKAIRAFAEeLIEEFDVRTPGPDTPAR-- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 765 gvNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVD----AHVGKHIFEkvvgpmglLKNK-TRILVthgISY-LPQV--- 835
Cdd:COG3845 402 --SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDvgaiEFIHQRLLE--------LRDAgAAVLL---ISEdLDEIlal 468
|
250
....*....|...
gi 6678848 836 -DVIIVMSGGKIS 847
Cdd:COG3845 469 sDRIAVMYEGRIV 481
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
1014-1169 |
3.03e-07 |
|
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: 54.06 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1014 SVYGALG---ILQGAAIFGYSMAVSIGGIFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKM 1090
Cdd:cd18573 42 TFALALLgvfVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSD 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1091 FMGSLFSVIGAVIIILLATP----IAAVIIPPLGLVYFFVQRFYVASSRQLkrLESVSRSpvySHF-NETLLGVSVIRAF 1165
Cdd:cd18573 122 GLRSLVSGVGGIGMMLYISPkltlVMLLVVPPIAVGAVFYGRYVRKLSKQV--QDALADA---TKVaEERLSNIRTVRAF 196
|
....*.
gi 6678848 1166 --EEQE 1169
Cdd:cd18573 197 aaERKE 202
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1021-1170 |
3.04e-07 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 54.03 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1021 ILQGAAIFGYSMAVSIGGIFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIG 1100
Cdd:cd18576 47 LLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIG 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6678848 1101 AVIIILLATP----IAAVIIPPLGLVYFFVQRFYVASSRQlkRLESVSRSPVysHFNETLLGVSVIRAF--EEQER 1170
Cdd:cd18576 127 GVVLLFFISWkltlLMLATVPVVVLVAVLFGRRIRKLSKK--VQDELAEANT--IVEETLQGIRVVKAFtrEDYEI 198
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1307-1488 |
3.05e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.92 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1307 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNiakiglhnLRFK---------ITIIPQDpvlf 1377
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE--------MRFAsttaalaagVAIIYQE---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1378 sgslrMNLDPfsQYSDEEVWMALELAHLKGFV--SALPDKLNHECAEGGEN---------LSVGQRQLVCLARALLRKTK 1446
Cdd:PRK11288 88 -----LHLVP--EMTVAENLYLGQLPHKGGIVnrRLLNYEAREQLEHLGVDidpdtplkyLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6678848 1447 ILVLDEATAAVDL-ETDNLIQSTIRTQFEDCTVLTIAHRLNTI 1488
Cdd:PRK11288 161 VIAFDEPTSSLSArEIEQLFRVIRELRAEGRVILYVSHRMEEI 203
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
644-850 |
3.11e-07 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 52.76 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNAT--FTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-SVAYVPQQAW---- 716
Cdd:cd03266 2 ITADALTkrFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfDVVKEPAEARrrlg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 717 IQND--------SLRENIL-FG--HPLQENYYKAVMEACALLpdLEILPSGDRteigeKGVNLSGGQKQRVSLARAVYSN 785
Cdd:cd03266 82 FVSDstglydrlTARENLEyFAglYGLKGDELTARLEELADR--LGMEELLDR-----RVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6678848 786 SDIYLFDDPLSAVDAHVGKHIFE-----KVVGpmgllknKTRILVTHGISYLPQV-DVIIVMSGGKISEMG 850
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREfirqlRALG-------KCILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1307-1514 |
3.94e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 53.94 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1307 LKHINVTIEGGEKVGIVGRTGAGKSS----LTlGLfrINESAeGEIIIDGVNIAKIGLHNLRfKITII------------ 1370
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTtikmLT-GI--LVPTS-GEVRVLGYVPFKRRKEFAR-RIGVVfgqrsqlwwdlp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1371 PQDpvlfsgSLRMN-----LDP--FSQYSDEEVWMaLELAH-LKGFVsalpdklnhecaeggENLSVGQRQLVCLARALL 1442
Cdd:COG4586 113 AID------SFRLLkaiyrIPDaeYKKRLDELVEL-LDLGElLDTPV---------------RQLSLGQRMRCELAAALL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 1443 RKTKILVLDEATAAVDLETDNLIQSTIRT--QFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVRECGAPSELLQQ 1514
Cdd:COG4586 171 HRPKILFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIEALcDRVIVIDHGRIIYDGSLEELKER 245
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
644-846 |
4.04e-07 |
|
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: 55.02 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG------------SVAYV 711
Cdd:TIGR01257 929 VCVKNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietnldavrqSLGMC 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 712 PQQAWI-QNDSLRENILFGHPLQ-ENYYKAVMEACALLPDleilpSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIY 789
Cdd:TIGR01257 1009 PQHNILfHHLTVAEHILFYAQLKgRSWEEAQLEMEAMLED-----TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVV 1083
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6678848 790 LFDDPLSAVDAHVGKHIFEKvvgpmgLLK---NKTRILVTHgisYLPQVDV----IIVMSGGKI 846
Cdd:TIGR01257 1084 VLDEPTSGVDPYSRRSIWDL------LLKyrsGRTIIMSTH---HMDEADLlgdrIAIISQGRL 1138
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1306-1502 |
4.09e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 54.73 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGLHNL----RFKITIIPQDPVLFSG-S 1380
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLSHlT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1381 LRMNLDPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1460
Cdd:PRK10535 103 AAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQ----LSGGQQQRVSIARALMNGGQVILADEPTGALDSH 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6678848 1461 TDNLIQSTIRtQFED--CTVLTIAHRLNTIMDYTRVIVLDKGEV 1502
Cdd:PRK10535 179 SGEEVMAILH-QLRDrgHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
655-827 |
5.65e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 52.27 E-value: 5.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 655 RGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGhvtlKGSVAyVPQQAWIQNDSLRENILFGHPLqe 734
Cdd:COG2401 40 VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPV----AGCVD-VPDNQFGREASLIDAIGRKGDF-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 735 nyyKAVME---ACALlpdleilpsGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVD---AHVGKHIFE 808
Cdd:COG2401 113 ---KDAVEllnAVGL---------SDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtAKRVARNLQ 180
|
170
....*....|....*....
gi 6678848 809 KVVGPMGllknKTRILVTH 827
Cdd:COG2401 181 KLARRAG----ITLVVATH 195
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
646-870 |
5.85e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.02 E-value: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 646 VKNATftwaRGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS--------------VAYV 711
Cdd:PRK09700 268 VRNVT----SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprspldavkkgMAYI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 712 PQQ----AWIQNDSLRENILFGHPLQENYYKAVM----------EACALLPDLEILPSGDRTEIGEkgvnLSGGQKQRVS 777
Cdd:PRK09700 344 TESrrdnGFFPNFSIAQNMAISRSLKDGGYKGAMglfhevdeqrTAENQRELLALKCHSVNQNITE----LSGGNQQKVL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 778 LARAVYSNSDIYLFDDPLSAVDAHVGKHIFeKVvgpMGLLKN--KTRILVThgiSYLPQV----DVIIVMSGGKISemgs 851
Cdd:PRK09700 420 ISKWLCCCPEVIIFDEPTRGIDVGAKAEIY-KV---MRQLADdgKVILMVS---SELPEIitvcDRIAVFCEGRLT---- 488
|
250
....*....|....*....
gi 6678848 852 yQELLDRDGAFAEFLRTYA 870
Cdd:PRK09700 489 -QILTNRDDMSEEEIMAWA 506
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1306-1512 |
6.61e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 52.78 E-value: 6.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLT--LGLFRINESAEGEIIIDGVNIAKIGLHNLRFKITIIPQDP----VLFSG 1379
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIehLNALLLPDTGTIEWIFKDEKNKKKTKEKEKVLEKLVIQKTrfkkIKKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1380 SLRMNLD---PFSQY--------------------SDEEvwmALELAhlKGFVS--ALPDKLnheCAEGGENLSVGQRQL 1434
Cdd:PRK13651 102 EIRRRVGvvfQFAEYqlfeqtiekdiifgpvsmgvSKEE---AKKRA--AKYIElvGLDESY---LQRSPFELSGGQKRR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1435 VCLARALLRKTKILVLDEATAAVDLE-TDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELL 1512
Cdd:PRK13651 174 VALAGILAMEPDFLVFDEPTAGLDPQgVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTkRTIFFKDGKIIKDGDTYDIL 253
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
1021-1225 |
6.77e-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: 6.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1021 ILQGAAIFGYSMAVSIGGIFASRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIG 1100
Cdd:cd18574 53 LLQSLLTFAYISLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1101 AVIIILLATP----IAAVIIPPLGLVYFFVQRFYVASSRQLKRLESVSRspvySHFNETLLGVSVIRAF----EEQERFI 1172
Cdd:cd18574 133 CVVSLYLISPkltlLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKAT----GVADEALGNIRTVRAFamedRELELYE 208
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6678848 1173 hqsdlkvDENQKAyypsIVANRWLAVRLEC-------VGNCIVLfAALFA---VISRHSLSAG 1225
Cdd:cd18574 209 -------EEVEKA----AKLNEKLGLGIGIfqglsnlALNGIVL-GVLYYggsLVSRGELTAG 259
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
644-859 |
6.97e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 52.50 E-value: 6.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWaRGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVayvpqqawIQNDSLR 723
Cdd:PRK13652 4 IETRDLCYSY-SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEP--------ITKENIR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 724 E-----NILFGHPLQENYYKAVMEACALLP-----DLEILPSGDRTEIGEKGV---------NLSGGQKQRVSLARAVYS 784
Cdd:PRK13652 75 EvrkfvGLVFQNPDDQIFSPTVEQDIAFGPinlglDEETVAHRVSSALHMLGLeelrdrvphHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6678848 785 NSDIYLFDDPLSAVDAHVGKHIFeKVVGPMGLLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLDRD 859
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELI-DFLNDLPETYGMTVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
444-859 |
7.11e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.82 E-value: 7.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 444 MIWSAPLQVILALYFLWLSlgPSVLAGVAVMILMVPLNAVMAMkTKTYQvaHMKS-KDNRIKLMNE---ILNGIKVLKL- 518
Cdd:PRK10522 128 LVQGIILTLGSAAYLAWLS--PKMLLVTAIWMAVTIWGGFVLV-ARVYK--HMATlRETEDKLYNDyqtVLEGRKELTLn 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 519 -----YAWELAFQD-----KVMSIRQEELKVL----KKSAYLAAVGTFTWVCTPFLVALSTFAvfvtvdernildakkAF 584
Cdd:PRK10522 203 reraeYVFENEYEPdaqeyRHHIIRADTFHLSavnwSNIMMLGAIGLVFYMANSLGWADTNVA---------------AT 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 585 VSLALFnILRFPL----NILPMVISsivqASVSLKRLRIFlsheELEPDSIE-RRSIKSGEGNSITVKNATFTWArGEPP 659
Cdd:PRK10522 268 YSLTLL-FLRTPLlsavGALPTLLS----AQVAFNKLNKL----ALAPYKAEfPRPQAFPDWQTLELRNVTFAYQ-DNGF 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 660 TLNGITFSIPEGALVAVVGQVGCGKSSLlSALLAEMDK-VEGHVTLKGS-VAYVPQQAWIQNDS--LRENILFGHPL-QE 734
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTL-AMLLTGLYQpQSGEILLDGKpVTAEQPEDYRKLFSavFTDFHLFDQLLgPE 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 735 NYykavmEACALLPD--LEILPSGDRTEIGEKGV---NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVgKHIFEK 809
Cdd:PRK10522 417 GK-----PANPALVEkwLERLKMAHKLELEDGRIsnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHF-RREFYQ 490
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 6678848 810 VVGPMGLLKNKTRILVTHGISYLPQVDVIIVMSGGKISEM-GSYQELLDRD 859
Cdd:PRK10522 491 VLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSELtGEERDAASRD 541
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
661-799 |
8.74e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.98 E-value: 8.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVT-LKGS-------------VAYVPQqawi---qndSL 722
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLS-LIAGARKIqQGRVEvLGGDmadarhrravcprIAYMPQglgknlyptlSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 723 RENI-----LFGHPLQENYYK--AVMEACALLPDLEiLPSGdrteigekgvNLSGGQKQRVSLARAVYSNSDIYLFDDPL 795
Cdd:NF033858 96 FENLdffgrLFGQDAAERRRRidELLRATGLAPFAD-RPAG----------KLSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
....
gi 6678848 796 SAVD 799
Cdd:NF033858 165 TGVD 168
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
661-858 |
9.90e-07 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 50.99 E-value: 9.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMD-KV-EGHVTLKGsvayvpqqawiqndslrENILFgHPLQENYYK 738
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyEVtEGEILFKG-----------------EDITD-LPPEERARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 739 AVMEACALLPDLEilpsGDRTEIGEKGVN--LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEKVvgpMGL 816
Cdd:cd03217 78 GIFLAFQYPPEIP----GVKNADFLRYVNegFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVI---NKL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6678848 817 L-KNKTRILVTH--GISYLPQVDVIIVMSGGKISEMGSyQELLDR 858
Cdd:cd03217 151 ReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD-KELALE 194
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1012-1191 |
1.05e-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: 52.15 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1012 RLSVYGALGILQGAAIFGYSMAVSIGGIFASR---RLHLDL---LYNVL-RSPMSFFERTPSGNLVNRFSKELDTVDSMI 1084
Cdd:cd18778 35 SLGLLLGLALLLLGAYLLRALLNFLRIYLNHVaeqKVVADLrsdLYDKLqRLSLRYFDDRQTGDLMSRVINDVANVERLI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1085 PQVIKMFMGSLFSVIGAVIIILLATPI-AAVIIPPLGLVYFFVqRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIR 1163
Cdd:cd18778 115 ADGIPQGITNVLTLVGVAIILFSINPKlALLTLIPIPFLALGA-WLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQ 193
|
170 180 190
....*....|....*....|....*....|....*...
gi 6678848 1164 AF----EEQERFIHQSDLKVDENQKA------YYPSIV 1191
Cdd:cd18778 194 AFgreeEEAKRFEALSRRYRKAQLRAmklwaiFHPLME 231
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
653-860 |
1.24e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 51.93 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 653 WAR-GEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQQAWIqndSLRENI--LFG 729
Cdd:PRK13638 8 WFRyQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLL---ALRQQVatVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 730 HPLQENYYKAVMEACAL------LPDLEILPSGDR--TEIGEKGVN------LSGGQKQRVSLARAVYSNSDIYLFDDPL 795
Cdd:PRK13638 85 DPEQQIFYTDIDSDIAFslrnlgVPEAEITRRVDEalTLVDAQHFRhqpiqcLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6678848 796 SAVDAhVGK----HIFEKVVGpmgllKNKTRILVTHGISYLPQV-DVIIVMSGGKI------SEMGSYQELLDRDG 860
Cdd:PRK13638 165 AGLDP-AGRtqmiAIIRRIVA-----QGNHVIISSHDIDLIYEIsDAVYVLRQGQIlthgapGEVFACTEAMEQAG 234
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
968-1225 |
1.61e-06 |
|
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: 51.69 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 968 LFITFLSIFLFLCnhvsALASNYWLSLWTDDppVVngTQANRNFrLSV----YGALGILQGAAifgySMAVSIGGIFASR 1043
Cdd:cd18567 5 LQILLLSLALELF----ALASPLYLQLVIDE--VI--VSGDRDL-LTVlaigFGLLLLLQALL----SALRSWLVLYLST 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1044 RLHLDLLYNV----LRSPMSFFERTPSGNLVNRFSkELDTVDSMIP-QVIKMFMGSLFSVIGAVIIILLATPIAAVIIPP 1118
Cdd:cd18567 72 SLNLQWTSNLfrhlLRLPLSYFEKRHLGDIVSRFG-SLDEIQQTLTtGFVEALLDGLMAILTLVMMFLYSPKLALIVLAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1119 LgLVYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAF-EEQERFIHQSDLKVDENQKayypSIVANRWLA 1197
Cdd:cd18567 151 V-ALYALLRLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFgREAEREARWLNLLVDAINA----DIRLQRLQI 225
|
250 260 270
....*....|....*....|....*....|....
gi 6678848 1198 VR------LECVGNCIVLFAALFAVISRHsLSAG 1225
Cdd:cd18567 226 LFsaanglLFGLENILVIYLGALLVLDGE-FTVG 258
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1285-1484 |
1.79e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 52.83 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1285 PHSGRVEFRDYCLRYrEDLDLV-------LKHINVTIEGGEKVGIVGRTGAGKSSLtlglFRInesaEGEI--IIDGVnI 1355
Cdd:TIGR00954 440 PGRGIVEYQDNGIKF-ENIPLVtpngdvlIESLSFEVPSGNNLLICGPNGCGKSSL----FRI----LGELwpVYGGR-L 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1356 AKiglhNLRFKITIIPQDPVLFSGSLR------MNLDPFSQ--YSDEEVWMALELAHLKGFVSAlpdklnhecaEGG--- 1424
Cdd:TIGR00954 510 TK----PAKGKLFYVPQRPYMTLGTLRdqiiypDSSEDMKRrgLSDKDLEQILDNVQLTHILER----------EGGwsa 575
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1425 -----ENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIqstirtqFEDC-----TVLTIAHR 1484
Cdd:TIGR00954 576 vqdwmDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYM-------YRLCrefgiTLFSVSHR 638
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1307-1513 |
2.54e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.17 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1307 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEI-------------IID-------------GVNIAKIgl 1360
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIElseqsaaqmrhvrGADMAMI-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1361 hnlrFKITIIPQDPVLFSG-----SLRMNLDPFSQYSDEEVWMALELAHL---KGFVSALPdklnHEcaeggenLSVGQR 1432
Cdd:PRK10261 110 ----FQEPMTSLNPVFTVGeqiaeSIRLHQGASREEAMVEAKRMLDQVRIpeaQTILSRYP----HQ-------LSGGMR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1433 QLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCT--VLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPS 1509
Cdd:PRK10261 175 QRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIAdRVLVMYQGEAVETGSVE 254
|
....
gi 6678848 1510 ELLQ 1513
Cdd:PRK10261 255 QIFH 258
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
661-846 |
2.59e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 51.94 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMDkvEGHVTLKGS--------------VAYVPQQ-AWIQNDSLR 723
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILsgVYQPD--SGEILLDGEpvrfrsprdaqaagIAIIHQElNLVPNLSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 724 ENILFGHPLQENY-------YKAVMEACALLpDLEILPsgdRTEIGEkgvnLSGGQKQRVSLARAVYSNSDIYLFDDPLS 796
Cdd:COG1129 98 ENIFLGREPRRGGlidwramRRRARELLARL-GLDIDP---DTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6678848 797 AVDAHVGKHIFEKvvgpMGLLKNK--TRILVTHgisYLPQV----DVIIVMSGGKI 846
Cdd:COG1129 170 SLTEREVERLFRI----IRRLKAQgvAIIYISH---RLDEVfeiaDRVTVLRDGRL 218
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
1018-1185 |
2.73e-06 |
|
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: 51.30 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1018 ALGILQGAAIFGYSMAVSIGGIFASRRLHLDLLYNVLRSPMSFFERTP--SGNLVNRFSKELDTVDSMIPQVIKMFMGSL 1095
Cdd:cd18578 60 VLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDDPEnsTGALTSRLSTDASDVRGLVGDRLGLILQAI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1096 FSVIGAVIIILLA----TPIAAVIIPPLGLVYFFVQRFYVASSRQLKR-LESVSRspvysHFNETLLGVSVIRAFEEQER 1170
Cdd:cd18578 140 VTLVAGLIIAFVYgwklALVGLATVPLLLLAGYLRMRLLSGFEEKNKKaYEESSK-----IASEAVSNIRTVASLTLEDY 214
|
170
....*....|....*
gi 6678848 1171 FIHQSDLKVDENQKA 1185
Cdd:cd18578 215 FLEKYEEALEEPLKK 229
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1427-1511 |
2.94e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 51.00 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1427 LSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRT-QFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRE 1504
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDaKANNKTVFVITHTMEHVLEVAdEVIVMDKGKILK 256
|
....*..
gi 6678848 1505 CGAPSEL 1511
Cdd:PRK13631 257 TGTPYEI 263
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
647-874 |
3.00e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.58 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 647 KNATFTwargeppTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSVAYVPQQAWIqNDSLR--E 724
Cdd:PRK13546 33 KNKTFF-------ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGL-SGQLTgiE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 725 NILFGHPLQENYYKavmEACALLPdlEILpsgDRTEIGE---KGV-NLSGGQKQRVSLARAVYSNSDIYLFDDPLSavda 800
Cdd:PRK13546 105 NIEFKMLCMGFKRK---EIKAMTP--KII---EFSELGEfiyQPVkKYSSGMRAKLGFSINITVNPDILVIDEALS---- 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6678848 801 hVGKHIF-EKVVGPMGLLK--NKTRILVTHGISYLPQVDVIIV-MSGGKISEMGSYQELLDRDGAFAEFLRTYANAEQ 874
Cdd:PRK13546 173 -VGDQTFaQKCLDKIYEFKeqNKTIFFVSHNLGQVRQFCTKIAwIEGGKLKDYGELDDVLPKYEAFLNDFKKKSKAEQ 249
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
1042-1261 |
5.80e-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: 49.75 E-value: 5.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1042 SRRLHLDLLYN----VLRSPMSFFERTPSGNLVNRFSkELDTVDSMIPQVIKMFMGSLFSVIGAVIIILLATP----IAA 1113
Cdd:cd18570 70 SQKLDIRLILGyfkhLLKLPLSFFETRKTGEIISRFN-DANKIREAISSTTISLFLDLLMVIISGIILFFYNWklflITL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1114 VIIPPLGLVYFFVQRFYvassRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPS---I 1190
Cdd:cd18570 149 LIIPLYILIILLFNKPF----KKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLgklS 224
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 1191 VANRWLAVRLECVGNCIVLFAALFAVISrHSLSaglVGLSVSYsLQITAY----LNWLVRMSSEMETNIVAVERL 1261
Cdd:cd18570 225 NLQSSIKGLISLIGSLLILWIGSYLVIK-GQLS---LGQLIAF-NALLGYflgpIENLINLQPKIQEAKVAADRL 294
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1290-1511 |
6.07e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 50.41 E-value: 6.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDYCLRYREDLdlVLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG-----VNIAKIGLHNLR 1364
Cdd:PRK11000 4 VTLRNVTKAYGDVV--ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEkrmndVPPAERGVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1365 FKITIIPQDPVLFSGSLRMNLDPFS----QYSDEEVWMALELAHLkgfVSALPdklnhecaeggENLSVGQRQLVCLARA 1440
Cdd:PRK11000 82 QSYALYPHLSVAENMSFGLKLAGAKkeeiNQRVNQVAEVLQLAHL---LDRKP-----------KALSGGQRQRVAIGRT 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6678848 1441 LLRKTKILVLDEATAAVD--LETDNLIQSTIRTQFEDCTVLTIAH---RLNTIMDytRVIVLDKGEVRECGAPSEL 1511
Cdd:PRK11000 148 LVAEPSVFLLDEPLSNLDaaLRVQMRIEISRLHKRLGRTMIYVTHdqvEAMTLAD--KIVVLDAGRVAQVGKPLEL 221
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
656-794 |
8.49e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 48.72 E-value: 8.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 656 GEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG--------------SVAYVPQQAWI-QND 720
Cdd:PRK11614 16 GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGkditdwqtakimreAVAIVPEGRRVfSRM 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6678848 721 SLRENILFGHPL--QENYYKAVMEACALLPDLEilpsgDRTEigEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDP 794
Cdd:PRK11614 96 TVEENLAMGGFFaeRDQFQERIKWVYELFPRLH-----ERRI--QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
652-799 |
9.00e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 48.31 E-value: 9.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 652 TWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGS----------VAYVPQQAWIQND- 720
Cdd:PRK13543 18 AFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatrgdrsrfMAYLGHLPGLKADl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 721 SLRENILFGHPLQENYYKAvmeacallpdleiLPSGDRTEIGEKGV------NLSGGQKQRVSLARAVYSNSDIYLFDDP 794
Cdd:PRK13543 98 STLENLHFLCGLHGRRAKQ-------------MPGSALAIVGLAGYedtlvrQLSAGQKKRLALARLWLSPAPLWLLDEP 164
|
....*
gi 6678848 795 LSAVD 799
Cdd:PRK13543 165 YANLD 169
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
659-801 |
1.20e-05 |
|
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: 48.48 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 659 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGsvaYVPqqaWIQNDSLRENI--LFGHPLQENY 736
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG---LVP---WKRRKKFLRRIgvVFGQKTQLWW 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6678848 737 YKAVMEACALLPDLEILPSG-------------DRTEIGEKGV-NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAH 801
Cdd:cd03267 109 DLPVIDSFYLLAAIYDLPPArfkkrldelsellDLEELLDTPVrQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
664-856 |
1.22e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 48.63 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 664 ITFSIPEGALVAVVGQVGCGKSSL---LSALLAEMDK---VEGHVTLKGSVAYVPQQAWI--QNDS-------------- 721
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLakmLAGMIEPTSGellIDDHPLHFGDYSYRSQRIRMifQDPStslnprqrisqild 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 722 --LRENILFGHPLQENYYKAVMEACALLPD-LEILPSGdrteigekgvnLSGGQKQRVSLARAVYSNSDIYLFDDPLSAV 798
Cdd:PRK15112 112 fpLRLNTDLEPEQREKQIIETLRQVGLLPDhASYYPHM-----------LAPGQKQRLGLARALILRPKVIIADEALASL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6678848 799 DAHVGKHIfekvVGPMGLLKNKtrilvtHGISYLPQV----------DVIIVMSGGKISEMGSYQELL 856
Cdd:PRK15112 181 DMSMRSQL----INLMLELQEK------QGISYIYVTqhlgmmkhisDQVLVMHQGEVVERGSTADVL 238
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
655-877 |
1.23e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.78 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 655 RGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG--SVAYVPQ------------------- 713
Cdd:PRK10636 11 RGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwQLAWVNQetpalpqpaleyvidgdre 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 714 ---------QAWIQNDSLRENILFGHPLQENYYKAVMEACALLPDLeilpsGDRTEIGEKGV-NLSGGQKQRVSLARAVY 783
Cdd:PRK10636 91 yrqleaqlhDANERNDGHAIATIHGKLDAIDAWTIRSRAASLLHGL-----GFSNEQLERPVsDFSGGWRMRLNLAQALI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 784 SNSDIYLFDDPLSAVDahvgkhiFEKVVGPMGLLKN--KTRILVTHGISYL-PQVDVIIVMSGGKISE-MGSYQEL-LDR 858
Cdd:PRK10636 166 CRSDLLLLDEPTNHLD-------LDAVIWLEKWLKSyqGTLILISHDRDFLdPIVDKIIHIEQQSLFEyTGNYSSFeVQR 238
|
250
....*....|....*....
gi 6678848 859 DGAFAEFLRTYANAEQDLA 877
Cdd:PRK10636 239 ATRLAQQQAMYESQQERVA 257
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1019-1190 |
1.26e-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: 49.10 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1019 LGILQGAAIFGYSMAVSIGGiFASRRLH---LDLLYNVLRSPMSFFERTPSGNL-------VNRFSKELDTvdsMIPQVI 1088
Cdd:cd18565 61 VAAFLLESLFQYLSGVLWRR-FAQRVQHdlrTDTYDHVQRLDMAFFEDRQTGDLmsvlnndVNQLERFLDD---GANSII 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1089 KMFmgSLFSVIGAVIIIL---LATpIAAVIIPPL-GLVYFFVQRfyvASSRQLKRLESVSRspVYSHFNETLLGVSVIRA 1164
Cdd:cd18565 137 RVV--VTVLGIGAILFYLnwqLAL-VALLPVPLIiAGTYWFQRR---IEPRYRAVREAVGD--LNARLENNLSGIAVIKA 208
|
170 180 190
....*....|....*....|....*....|....*.
gi 6678848 1165 F----EEQERFIHQSDLKVDENQKA------YYPSI 1190
Cdd:cd18565 209 FtaedFERERVADASEEYRDANWRAirlraaFFPVI 244
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
657-881 |
1.53e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 49.49 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 657 EPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAemdKVEGHvTLKGSVayVPQQAWIQNDSLR-------ENILFG 729
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAG---RIQGN-NFTGTI--LANNRKPTKQILKrtgfvtqDDILYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 730 HPLqenyYKAVMEACALLPDLEILPSGDRTEIGEKGVN-------------------LSGGQKQRVSLARAVYSNSDIYL 790
Cdd:PLN03211 154 HLT----VRETLVFCSLLRLPKSLTKQEKILVAESVISelgltkcentiignsfirgISGGERKRVSIAHEMLINPSLLI 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 791 FDDPLSAVDAHVGKhifeKVVGPMGLLKNKTRILVT--HGIS--YLPQVDVIIVMSGG------KISEMGSYQELLDRDG 860
Cdd:PLN03211 230 LDEPTSGLDATAAY----RLVLTLGSLAQKGKTIVTsmHQPSsrVYQMFDSVLVLSEGrclffgKGSDAMAYFESVGFSP 305
|
250 260
....*....|....*....|....*..
gi 6678848 861 AF----AEFLRTYANA--EQDLASEDD 881
Cdd:PLN03211 306 SFpmnpADFLLDLANGvcQTDGVSERE 332
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
1015-1174 |
1.62e-05 |
|
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: 48.66 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1015 VYGALGILQGA--AIFGYSMAVSIGGIFASRRLHLdllynvlrsPMSFFERTPSGNLVNRFSkELDTVDSMIP-QVIKMF 1091
Cdd:cd18555 54 LYGLFSFLRGYiiIKLQTKLDKSLMSDFFEHLLKL---------PYSFFENRSSGDLLFRAN-SNVYIRQILSnQVISLI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1092 MGSLFSVIGAVIIILLATPIAAVIIpPLGLVYFFvqrFYVASSRQLKRL---ESVSRSPVYSHFNETLLGVSVIRAFEEQ 1168
Cdd:cd18555 124 IDLLLLVIYLIYMLYYSPLLTLIVL-LLGLLIVL---LLLLTRKKIKKLnqeEIVAQTKVQSYLTETLYGIETIKSLGSE 199
|
....*.
gi 6678848 1169 ERFIHQ 1174
Cdd:cd18555 200 KNIYKK 205
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1317-1501 |
1.72e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 49.23 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1317 GEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAkiglhnlrFK---------ITIIPQDpvlfsgslrMNLDP 1387
Cdd:PRK10762 30 GRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT--------FNgpkssqeagIGIIHQE---------LNLIP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1388 fsQYS-DEEVWMALELAHLKGFV---------SALPDKLN--HECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATA 1455
Cdd:PRK10762 93 --QLTiAENIFLGREFVNRFGRIdwkkmyaeaDKLLARLNlrFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6678848 1456 AV-DLETDNLIqSTIRT-QFEDCTVLTIAHRLNTIMDYT-RVIVLDKGE 1501
Cdd:PRK10762 171 ALtDTETESLF-RVIRElKSQGRGIVYISHRLKEIFEICdDVTVFRDGQ 218
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
664-799 |
1.84e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 48.72 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 664 ITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMDkvEGHVTLKGSV-----------------AYVPQQAWI-QNDSLR 723
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAIsgLTRPQ--KGRIVLNGRVlfdaekgiclppekrriGYVFQDARLfPHYKVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 724 ENILFGhplqenyYKAVMEA-----CALL---PDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNSDIYLFDDPL 795
Cdd:PRK11144 95 GNLRYG-------MAKSMVAqfdkiVALLgiePLLDRYPG-----------SLSGGEKQRVAIGRALLTAPELLLMDEPL 156
|
....
gi 6678848 796 SAVD 799
Cdd:PRK11144 157 ASLD 160
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
644-869 |
1.84e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 48.19 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWARGEP---PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG-SVAYVPQQAWIQN 719
Cdd:PRK13643 2 IKFEKVNYTYQPNSPfasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDiVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 720 DSLRENILFGHPLQENYYKAVMEACALLPD----------------LEILpsGDRTEIGEKG-VNLSGGQKQRVSLARAV 782
Cdd:PRK13643 82 VRKKVGVVFQFPESQLFEETVLKDVAFGPQnfgipkekaekiaaekLEMV--GLADEFWEKSpFELSGGQMRRVAIAGIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 783 YSNSDIYLFDDPLSAVDAHVG---KHIFEKVVGpmgllKNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQELLDR 858
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKARiemMQLFESIHQ-----SGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQE 234
|
250
....*....|.
gi 6678848 859 dgafAEFLRTY 869
Cdd:PRK13643 235 ----VDFLKAH 241
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
754-869 |
1.94e-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: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 754 PSGDRTE-------IGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIfEKVVGPMGLLKNKTRILVT 826
Cdd:cd03222 51 PNGDNDEwdgitpvYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNA-ARAIRRLSEEGKKTALVVE 129
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 6678848 827 HGISYLPQV-DVIIVMSGgkisEMGSYQELLDRDG---AFAEFLRTY 869
Cdd:cd03222 130 HDLAVLDYLsDRIHVFEG----EPGVYGIASQPKGtreGINRFLRGY 172
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1305-1511 |
1.97e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 48.06 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1305 LVLKHINVTIEGGEKVGIVGRTGAGKSS----LTlGLFRineSAEGEIIIDGVN--------IAKIGL----HNLR-FK- 1366
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTvfncLT-GFYK---PTGGTILLRGQHieglpghqIARMGVvrtfQHVRlFRe 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1367 ITIIPQDPV---------LFSGSLRMnldPFSQYSDEEvwmALELAHLKGFVSALPDKLNHECAeggeNLSVGQRQLVCL 1437
Cdd:PRK11300 95 MTVIENLLVaqhqqlktgLFSGLLKT---PAFRRAESE---ALDRAATWLERVGLLEHANRQAG----NLAYGQQRRLEI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6678848 1438 ARALLRKTKILVLDEATAAVD-LETDNLIQ--STIRTQFeDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSEL 1511
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNpKETKELDEliAELRNEH-NVTVLLIEHDMKLVMGISdRIYVVNQGTPLANGTPEEI 241
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
1044-1164 |
1.99e-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: 48.35 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1044 RLHLDLLYNVLRSPMSFFERTPSGNLVNRFsKELDTV-DSMIPQVIKMFMGSLFSVIGAVIIILLATPIAAViipPLGLV 1122
Cdd:cd18566 76 RLSNAAFEHLLSLPLSFFEREPSGAHLERL-NSLEQIrEFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLV---PLVLL 151
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 6678848 1123 YFFVQRFYVASSRQLKRLESVSRSPV--YSHFNETLLGVSVIRA 1164
Cdd:cd18566 152 GLFVLVAILLGPILRRALKERSRADErrQNFLIETLTGIHTIKA 195
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1317-1501 |
2.22e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 46.21 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1317 GEKVGIVGRTGAGKSSLTLGLFR-INESAEGEIIIDGVNIAKIGLHNLRFKITiipqdpvlfsgslrmnldpfsqysdee 1395
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQLLLIIV--------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1396 vwmalelahlkgfvsalpdklnhecAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQF-- 1473
Cdd:smart00382 55 -------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLll 109
|
170 180 190
....*....|....*....|....*....|....*....
gi 6678848 1474 -----EDCTVLTIAHRLNTIMD------YTRVIVLDKGE 1501
Cdd:smart00382 110 llkseKNLTVILTTNDEKDLGPallrrrFDRRIVLLLIL 148
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1306-1512 |
2.44e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.93 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESA-----EGEIIIDGVNIAKIGLHNLRF----KITIIPQDPVL 1376
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1377 fsgslrmNLDPFSQYSDE--EVW-----MALELAhlKGFVSALPDKLNHECAEGGEN-----LSVGQRQLVCLARALLRK 1444
Cdd:PRK15134 104 -------SLNPLHTLEKQlyEVLslhrgMRREAA--RGEILNCLDRVGIRQAAKRLTdyphqLSGGERQRVMIAMALLTR 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6678848 1445 TKILVLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELL 1512
Cdd:PRK15134 175 PELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVRKLAdRVAVMQNGRCVEQNRAATLF 245
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
656-855 |
2.57e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.55 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 656 GEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLaEMDKVEGHVTLKGSvayvPQQAW-----------IQ------ 718
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALL-RLINSQGEIWFDGQ----PLHNLnrrqllpvrhrIQvvfqdp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 719 NDSL--RENIL--------FGHPL-----QENYYKAVMEACALLPDLEI-LPSgdrteigekgvNLSGGQKQRVSLARAV 782
Cdd:PRK15134 372 NSSLnpRLNVLqiieeglrVHQPTlsaaqREQQVIAVMEEVGLDPETRHrYPA-----------EFSGGQRQRIAIARAL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 783 YSNSDIYLFDDPLSAVDAHVGKHIFEkvvgpmgLLKNKTRilvTHGISYL-------------PQVdviIVMSGGKISEM 849
Cdd:PRK15134 441 ILKPSLIILDEPTSSLDKTVQAQILA-------LLKSLQQ---KHQLAYLfishdlhvvralcHQV---IVLRQGEVVEQ 507
|
....*.
gi 6678848 850 GSYQEL 855
Cdd:PRK15134 508 GDCERV 513
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1307-1502 |
2.62e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.79 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1307 LKHINVTIEGGEKVGIVGRTGAGKSSLTLGLfrinesaEGEIIIDG--VNIAKiglhnlRFKITIIPQDP------VLFS 1378
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDDgrIIYEQ------DLIVARLQQDPprnvegTVYD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1379 ---------GSL-----RMNLDPFSQYSDEevwMALELAHLKGFVS-----ALPDKLNHECAEGGEN-------LSVGQR 1432
Cdd:PRK11147 86 fvaegieeqAEYlkryhDISHLVETDPSEK---NLNELAKLQEQLDhhnlwQLENRINEVLAQLGLDpdaalssLSGGWL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6678848 1433 QLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTqFEDCTVLtIAHRLNTI--MdYTRVIVLDKGEV 1502
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKT-FQGSIIF-ISHDRSFIrnM-ATRIVDLDRGKL 231
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
648-855 |
3.69e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 48.31 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 648 NATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG--------SVAYVPQQAWIQN 719
Cdd:PRK10261 19 NIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrQVIELSEQSAAQM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 720 DSLREN---ILFGHPLQE---------------------NYYKAVMEACALLPDLEILPSgdRTEIGEKGVNLSGGQKQR 775
Cdd:PRK10261 99 RHVRGAdmaMIFQEPMTSlnpvftvgeqiaesirlhqgaSREEAMVEAKRMLDQVRIPEA--QTILSRYPHQLSGGMRQR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 776 VSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFE--KVVG---PMGLlknktrILVTHGISYLPQV-DVIIVMSGGKISEM 849
Cdd:PRK10261 177 VMIAMALSCRPAVLIADEPTTALDVTIQAQILQliKVLQkemSMGV------IFITHDMGVVAEIaDRVLVMYQGEAVET 250
|
....*.
gi 6678848 850 GSYQEL 855
Cdd:PRK10261 251 GSVEQI 256
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
1039-1261 |
3.84e-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: 47.55 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1039 IFASRRLHLDLL---YN-VLRSPMSFFERTPSGNLVNRFsKELDTVDSMI-PQVIKMFMGSLFSVIgaVIIILLA----- 1108
Cdd:cd18568 67 DYFANRIDLSLLsdfYKhLLSLPLSFFASRKVGDIITRF-QENQKIRRFLtRSALTTILDLLMVFI--YLGLMFYynlql 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1109 TPIAAVIIPPLGLvyffvqrFYVASSRQLKRLES---VSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKA 1185
Cdd:cd18568 144 TLIVLAFIPLYVL-------LTLLSSPKLKRNSReifQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNT 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1186 YYPSIVanrwLAVRLECV-------GNCIVLFAALFAVISrHSLSAG-LVGLSVSYSLQITAYLNwLVRMSSEMETNIVA 1257
Cdd:cd18568 217 RFRGQK----LSIVLQLIsslinhlGTIAVLWYGAYLVIS-GQLTIGqLVAFNMLFGSVINPLLA-LVGLWDELQETRIS 290
|
....
gi 6678848 1258 VERL 1261
Cdd:cd18568 291 VERL 294
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1307-1512 |
4.23e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 47.31 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1307 LKHINVTIEGGEKVGIVGRTGAGKSS---LTLGLFrINESaeGEIIIDG----VNIAKIG-LHNLRFKITIIPQDP--VL 1376
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTmiqLTNGLI-ISET--GQTIVGDyaipANLKKIKeVKRLRKEIGLVFQFPeyQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1377 FSGSLRMNL--DPFSQYSD-EEVWMalELAHLKGFVSALPDKLNHECAEggenLSVGQRQLVCLARALLRKTKILVLDEA 1453
Cdd:PRK13645 104 FQETIEKDIafGPVNLGENkQEAYK--KVPELLKLVQLPEDYVKRSPFE----LSGGQKRRVALAGIIAMDGNTLVLDEP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6678848 1454 TAAVDL--ETD--NLIQSTIRTQFEdcTVLTIAHRLNTIMDYT-RVIVLDKGEVRECGAPSELL 1512
Cdd:PRK13645 178 TGGLDPkgEEDfiNLFERLNKEYKK--RIIMVTHNMDQVLRIAdEVIVMHEGKVISIGSPFEIF 239
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
644-800 |
4.24e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 47.90 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKNATFTWarGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL--------------LAEMDKVEGHV--TLKGS 707
Cdd:TIGR02633 2 LEMKGIVKTF--GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILsgvyphgtwdgeiyWSGSPLKASNIrdTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 708 VAYVPQQ-AWIQNDSLRENILFGHPLQE-----NYYKAVMEACALLPDLEILPSGDRTEIGEKGvnlsGGQKQRVSLARA 781
Cdd:TIGR02633 80 IVIIHQElTLVPELSVAENIFLGNEITLpggrmAYNAMYLRAKNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKA 155
|
170
....*....|....*....
gi 6678848 782 VYSNSDIYLFDDPLSAVDA 800
Cdd:TIGR02633 156 LNKQARLLILDEPSSSLTE 174
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1305-1512 |
5.39e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 46.46 E-value: 5.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1305 LVLKHINV---------TIEGGEKVGIVGRTGAGKSSL---TLGLFrineSAEGEIIIDGVNIAKIGLHNL-RFKITIIP 1371
Cdd:PRK03695 1 MQLNDVAVstrlgplsaEVRAGEILHLVGPNGAGKSTLlarMAGLL----PGSGSIQFAGQPLEAWSAAELaRHRAYLSQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1372 QDPVLFSgslrMnldPFSQYSD---------EEVWMAL-ELAHLKGfvsaLPDKLnHECAeggENLSVGQRQLVCLARAL 1441
Cdd:PRK03695 77 QQTPPFA----M---PVFQYLTlhqpdktrtEAVASALnEVAEALG----LDDKL-GRSV---NQLSGGEWQRVRLAAVV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1442 LR-------KTKILVLDEATAAVDLETDNLIQSTIRtqfEDC----TVLTIAHRLNTIMDY-TRVIVLDKGEVRECGAPS 1509
Cdd:PRK03695 142 LQvwpdinpAGQLLLLDEPMNSLDVAQQAALDRLLS---ELCqqgiAVVMSSHDLNHTLRHaDRVWLLKQGKLLASGRRD 218
|
...
gi 6678848 1510 ELL 1512
Cdd:PRK03695 219 EVL 221
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
659-859 |
5.50e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 47.74 E-value: 5.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 659 PTLNGITFSIPEGALVAVVGQVGCGKSSLLS--ALLAEMD----KVEGHVTLKGSVA-------Y-VPQQAWI-QNDSLR 723
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKiiAGIVPPDsgtlEIGGNPCARLTPAkahqlgiYlVPQEPLLfPNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 724 ENILFGHPLQENYYKAVMEACALLP---DLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDA 800
Cdd:PRK15439 105 ENILFGLPKRQASMQKMKQLLAALGcqlDLDSSAG-----------SLEVADRQIVEILRGLMRDSRILILDEPTASLTP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6678848 801 HVGKHIFEKVvgpMGLLKNKTRIL-VTHGISYLPQV-DVIIVMSGGKISEMGSYQELLDRD 859
Cdd:PRK15439 174 AETERLFSRI---RELLAQGVGIVfISHKLPEIRQLaDRISVMRDGTIALSGKTADLSTDD 231
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1306-1511 |
6.20e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 47.15 E-value: 6.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1306 VLKHINVTIEGGEKVGIVGRTGAGKSSLtL----GLFRInesAEGEIIIDG--VN--------IAKI------------- 1358
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTL-LrmvaGLERI---TSGEIWIGGrvVNelepadrdIAMVfqnyalyphmsvr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1359 -----GLHNLRFKITIIPQdpvlfsgslRMnldpfsqysdEEVWMALELAHLkgfvsalpdkLNHECAEggenLSVGQRQ 1433
Cdd:PRK11650 95 enmayGLKIRGMPKAEIEE---------RV----------AEAARILELEPL----------LDRKPRE----LSGGQRQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1434 LVCLARALLRKTKILVLDEATAAVD--------LETDNLiQSTIRT--------QFEdctVLTIAHRLntimdytrvIVL 1497
Cdd:PRK11650 142 RVAMGRAIVREPAVFLFDEPLSNLDaklrvqmrLEIQRL-HRRLKTtslyvthdQVE---AMTLADRV---------VVM 208
|
250
....*....|....
gi 6678848 1498 DKGEVRECGAPSEL 1511
Cdd:PRK11650 209 NGGVAEQIGTPVEV 222
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
664-799 |
6.30e-05 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 46.43 E-value: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 664 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTL--------------KGSVAYVPQQAWI-QNDSLRENILF 728
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddedisllplharaRRGIGYLPQEASIfRRLSVYDNLMA 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6678848 729 GHPLQENYYKAVME--ACALLPDLEIlpSGDRTEIGEkgvNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVD 799
Cdd:PRK10895 102 VLQIRDDLSAEQREdrANELMEEFHI--EHLRDSMGQ---SLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
644-858 |
6.34e-05 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 47.37 E-value: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 644 ITVKN--ATFTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKS----SLLSALLAEMDKVEGHVTLKG-SVAYVPQQAW 716
Cdd:COG4172 7 LSVEDlsVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGqDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 717 IQndsLREN---ILFghplQE---------NYYKAVMEACAL---LPD-------LEILpsgDRTEI--GEKGVN----- 767
Cdd:COG4172 87 RR---IRGNriaMIF----QEpmtslnplhTIGKQIAEVLRLhrgLSGaaararaLELL---ERVGIpdPERRLDayphq 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 768 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEkvvgpmgLLKNKTR------ILVTH--GIsylpqV---- 835
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILD-------LLKDLQRelgmalLLITHdlGV-----Vrrfa 224
|
250 260
....*....|....*....|...
gi 6678848 836 DVIIVMSGGKISEMGSYQELLDR 858
Cdd:COG4172 225 DRVAVMRQGEIVEQGPTAELFAA 247
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
768-855 |
9.69e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 46.27 E-value: 9.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 768 LSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDAHVGKHIFEkvvgpmgLL------KNKTRILVTHGISYLPQV-DVIIV 840
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIE-------LLlelqqkENMALVLITHDLALVAEAaHKIIV 226
|
90
....*....|....*
gi 6678848 841 MSGGKISEMGSYQEL 855
Cdd:PRK11022 227 MYAGQVVETGKAHDI 241
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1313-1501 |
1.08e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 46.73 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1313 TIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDgVNIAkiglhnlrFK---ITIIPQDPVlfSGSLRMNLDPF- 1388
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKIS--------YKpqyIKPDYDGTV--EDLLRSITDDLg 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1389 SQYSDEEVWMALELAHLkgfvsaLPDKLNhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQST 1468
Cdd:PRK13409 430 SSYYKSEIIKPLQLERL------LDKNVK--------DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKA 495
|
170 180 190
....*....|....*....|....*....|....*..
gi 6678848 1469 IRTQFE--DCTVLTIAHRLnTIMDY--TRVIVLDkGE 1501
Cdd:PRK13409 496 IRRIAEerEATALVVDHDI-YMIDYisDRLMVFE-GE 530
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1426-1489 |
1.16e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.71 E-value: 1.16e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 1426 NLSVGQRQLVCLARALLRKTKILVLDEATAAV-DLETDNLIQSTIRTQFEDCTVLTIAHRLNTIM 1489
Cdd:NF040905 139 DIGVGKQQLVEIAKALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIR 203
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
661-844 |
1.27e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.32 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKG--------------SVAYVPQQAWIQND-SLREN 725
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynkldhklaaqlGIGIIYQELSVIDElTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 726 ILFG-HPLQENY------YKAVMEACALLpdleILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNSDIYLFDDPLSAV 798
Cdd:PRK09700 101 LYIGrHLTKKVCgvniidWREMRVRAAMM----LLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6678848 799 -DAHVgkhifEKVVGPMGLLKN--KTRILVTHGISYLPQV-DVIIVMSGG 844
Cdd:PRK09700 177 tNKEV-----DYLFLIMNQLRKegTAIVYISHKLAEIRRIcDRYTVMKDG 221
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1304-1503 |
2.14e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 45.25 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1304 DLVLKhINVTIEGGEKVGIVGRTGAGKSSLtlglfrINESA------EGEIIIDG---VNIAK-IGLHNLRFKITIIPQD 1373
Cdd:PRK11144 12 DLCLT-VNLTLPAQGITAIFGRSGAGKTSL------INAISgltrpqKGRIVLNGrvlFDAEKgICLPPEKRRIGYVFQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1374 PVLF-----SGSLRMNLDPFSQ-YSDEEVWMaLELAHLkgfVSALPdklnhecaeggENLSVGQRQLVCLARALLRKTKI 1447
Cdd:PRK11144 85 ARLFphykvRGNLRYGMAKSMVaQFDKIVAL-LGIEPL---LDRYP-----------GSLSGGEKQRVAIGRALLTAPEL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6678848 1448 LVLDEATAAVDL----ETDNLIQSTIRTQfeDCTVLTIAHRLNTIM---DytRVIVLDKGEVR 1503
Cdd:PRK11144 150 LLMDEPLASLDLprkrELLPYLERLAREI--NIPILYVSHSLDEILrlaD--RVVVLEQGKVK 208
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
661-797 |
2.53e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 45.31 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 661 LNGITFSIPEGALVAVVGQVGCGKSSL---LSA-----------LLAEMDKVEGHV--TLKGSVAYVPQQ-AWIQNDSLR 723
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLmkvLSGvyphgtyegeiIFEGEELQASNIrdTERAGIAIIHQElALVKELSVL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6678848 724 ENILFGHPLQE----NYYKAVMEACALLPDLEILPSGDrTEIGekgvNLSGGQKQRVSLARAVYSNSDIYLFDDPLSA 797
Cdd:PRK13549 101 ENIFLGNEITPggimDYDAMYLRAQKLLAQLKLDINPA-TPVG----NLGLGQQQLVEIAKALNKQARLLILDEPTAS 173
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
651-856 |
3.07e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.08 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 651 FTWARGEPPTLNGITFSIPEGALVAVVGQVGCGKS-SLLSAL-LAEMDKVE---GHVTLKG-SVAYVPQQAWIQndsLRE 724
Cdd:PRK15134 15 FRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILrLLPSPPVVypsGDIRFHGeSLLHASEQTLRG---VRG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 725 N---ILFGHPLQ-----ENYYKAVMEACALLPDL-------EILPSGDRTEI--GEKGVN-----LSGGQKQRVSLARAV 782
Cdd:PRK15134 92 NkiaMIFQEPMVslnplHTLEKQLYEVLSLHRGMrreaargEILNCLDRVGIrqAAKRLTdyphqLSGGERQRVMIAMAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 783 YSNSDIYLFDDPLSAVDAHVGKHIfekvvgpMGLLK------NKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQEL 855
Cdd:PRK15134 172 LTRPELLIADEPTTALDVSVQAQI-------LQLLRelqqelNMGLLFITHNLSIVRKLaDRVAVMQNGRCVEQNRAATL 244
|
.
gi 6678848 856 L 856
Cdd:PRK15134 245 F 245
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
661-799 |
3.45e-04 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 43.86 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 661 LNGITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMDkvEGHVTLKGS--------------VAYVPQQAWI-QNDSLR 723
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIvgLVKPD--SGRIFLDGEdithlpmhkrarlgIGYLPQEASIfRKLTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 724 ENILfghplqenyykAVMEacallpdLEILPSGDRTEIGE--------------KGVNLSGGQKQRVSLARAVYSNSDIY 789
Cdd:COG1137 97 DNIL-----------AVLE-------LRKLSKKEREERLEelleefgithlrksKAYSLSGGERRRVEIARALATNPKFI 158
|
170
....*....|
gi 6678848 790 LFDDPLSAVD 799
Cdd:COG1137 159 LLDEPFAGVD 168
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1052-1170 |
6.74e-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: 43.63 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1052 NVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMGSLFSVIGAVI-----------IILLATPIaaVIIPplg 1120
Cdd:cd18575 78 HLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVmlfitspkltlLVLLVIPL--VVLP--- 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 6678848 1121 lVYFFVQRFYVASSRQLKRLESVSrspvySHFNETLLGVSVIRAF--EEQER 1170
Cdd:cd18575 153 -IILFGRRVRRLSRASQDRLADLS-----AFAEETLSAIKTVQAFtrEDAER 198
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1310-1508 |
6.82e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 44.62 E-value: 6.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1310 INVTIEGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIaKIGLHNLRFKITIIPQDPVLFSG-SLRMNLDPF 1388
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1389 SQY---SDEEVWMALElahlkgfvSALPDK-LNHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNL 1464
Cdd:TIGR01257 1028 AQLkgrSWEEAQLEME--------AMLEDTgLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6678848 1465 IQSTIRTQFEDCTVLTIAHRLNTI-MDYTRVIVLDKGEVRECGAP 1508
Cdd:TIGR01257 1100 IWDLLLKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSGTP 1144
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
1060-1261 |
1.05e-03 |
|
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: 42.79 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1060 FFERTPSGNLVNRFskeLDTVDSMIPQVIKMFMGSLFSVIGAVIII-------LLATPIAAVIIPPLGL-VYFFVQRFyv 1131
Cdd:cd18554 96 YYANNRSGEIISRV---INDVEQTKDFITTGLMNIWLDMITIIIAIcimlvlnPKLTFVSLVIFPFYILaVKYFFGRL-- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1132 assRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDlkvDENQKAYYPSIVANRWLAVRLECV------GN 1205
Cdd:cd18554 171 ---RKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFD---KRNGHFLTRALKHTRWNAKTFSAVntitdlAP 244
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 6678848 1206 CIVLFAALFAVISrHSLSAGLVGLSVSYSLQITAYLNWLVRMSSEMETNIVAVERL 1261
Cdd:cd18554 245 LLVIGFAAYLVIE-GNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
1025-1171 |
1.23e-03 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 42.71 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1025 AAIFG---YSMAVSI-----GGIFA------SRRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKM 1090
Cdd:cd18590 37 SAIGLmclFSLGSSLsaglrGGLFMctlsrlNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1091 FMGSLFSVIGAVIIIL-----------LATPIAAVIipplglvyffvQRFYVASSRQLKR--LESVSRSPvySHFNETLL 1157
Cdd:cd18590 117 LLRSLVKTLGMLGFMLslswqltlltlIEMPLTAIA-----------QKVYNTYHQKLSQavQDSIAKAG--ELAREAVS 183
|
170
....*....|....*...
gi 6678848 1158 GVSVIRAF----EEQERF 1171
Cdd:cd18590 184 SIRTVRSFkaeeEEACRY 201
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
1021-1130 |
1.61e-03 |
|
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: 42.30 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1021 ILQGAAIFGYSMAVSI-GGIF--ASRRLHL---DLLY-NVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMFMG 1093
Cdd:cd18784 40 IIMGLLAIASSVAAGIrGGLFtlAMARLNIrirNLLFrSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLR 119
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 6678848 1094 SLFSVIGAVIIILLAT---PIAAVIIPPLGlvyFFVQRFY 1130
Cdd:cd18784 120 SLVKAIGVIVFMFKLSwqlSLVTLIGLPLI---AIVSKVY 156
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
670-799 |
1.80e-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: 41.97 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 670 EGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTLKGSvayvpqqaWiqNDSLREniLFGHPLQeNYYKAVMEA---CAL 746
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPD--------W--DEILDE--FRGSELQ-NYFTKLLEGdvkVIV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 747 LP---DL----------EILPSGDRTEIGEKGV--------------NLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVD 799
Cdd:cd03236 92 KPqyvDLipkavkgkvgELLKKKDERGKLDELVdqlelrhvldrnidQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
1026-1121 |
2.34e-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: 41.85 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1026 AIFGYSMAVSIGGIFAS--------------RRLHLDLLYNVLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPQVIKMF 1091
Cdd:cd18780 44 AVLILLGVVLIGSIATFlrswlftlagervvARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSML 123
|
90 100 110
....*....|....*....|....*....|....
gi 6678848 1092 MGSLFSVIGAVIIILLA----TPIAAVIIPPLGL 1121
Cdd:cd18780 124 LRYLVQIIGGLVFMFTTswklTLVMLSVVPPLSI 157
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
750-847 |
2.35e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.49 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 750 LEILPSGDRtEIGEkgvnLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVDahvgkhIFEKV-VGPM--GLLKNKTRILVT 826
Cdd:PRK13409 200 LGLENILDR-DISE----LSGGELQRVAIAAALLRDADFYFFDEPTSYLD------IRQRLnVARLirELAEGKYVLVVE 268
|
90 100
....*....|....*....|....*....
gi 6678848 827 HGIS---YLpqVDVIIVMSG-----GKIS 847
Cdd:PRK13409 269 HDLAvldYL--ADNVHIAYGepgayGVVS 295
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
750-799 |
3.83e-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: 41.69 E-value: 3.83e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 6678848 750 LEILPSGDRtEIGEkgvnLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVD 799
Cdd:COG1245 200 LGLENILDR-DISE----LSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
609-713 |
3.93e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.80 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 609 QASVSLKRL-RIFLshEELEPDSIERRSIKSGEG-----NSITVKNATFTWarGEPPTLNGITFSIPEGALVAVVGQVGC 682
Cdd:PRK15064 281 QATSRAKQIdKIKL--EEVKPSSRQNPFIRFEQDkklhrNALEVENLTKGF--DNGPLFKNLNLLLEAGERLAIIGENGV 356
|
90 100 110
....*....|....*....|....*....|...
gi 6678848 683 GKSSLLSALLAEMDKVEGHV--TLKGSVAYVPQ 713
Cdd:PRK15064 357 GKTTLLRTLVGELEPDSGTVkwSENANIGYYAQ 389
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1290-1452 |
3.95e-03 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 40.90 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1290 VEFRDycLRYREDLDLVLKHINVTIEGGEKVGIVGRTGAGKSSLtLGLFRINESAE-GEIIIDGVNIAKI---GLHNLRF 1365
Cdd:PRK11831 8 VDMRG--VSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTL-LRLIGGQIAPDhGEILFDGENIPAMsrsRLYTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1366 KITIIPQdpvlfSGSLRMNLDPF----------SQYSDE----EVWMALELAHLKGFVSALPDKlnhecaeggenLSVGQ 1431
Cdd:PRK11831 85 RMSMLFQ-----SGALFTDMNVFdnvayplrehTQLPAPllhsTVMMKLEAVGLRGAAKLMPSE-----------LSGGM 148
|
170 180
....*....|....*....|.
gi 6678848 1432 RQLVCLARALLRKTKILVLDE 1452
Cdd:PRK11831 149 ARRAALARAIALEPDLIMFDE 169
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
656-799 |
4.05e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.69 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 656 GEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVTL-KG-SVAYVPQQawiQNDSLRENilfGHPLQ 733
Cdd:PRK10636 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGiKLGYFAQH---QLEFLRAD---ESPLQ 396
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6678848 734 ENYYKAVMEACALLPDLeiLPS----GDR-TEIGEKgvnLSGGQKQRVSLARAVYSNSDIYLFDDPLSAVD 799
Cdd:PRK10636 397 HLARLAPQELEQKLRDY--LGGfgfqGDKvTEETRR---FSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
655-827 |
7.02e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 38.88 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 655 RGEPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEmdkveghVTLKGSVAYVPQQAwiqndslrenilfghplQE 734
Cdd:cd03227 5 GRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLA-------LGGAQSATRRRSGV-----------------KA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 735 NYYKAVMEACALLpdleILPSgdrteigekgvnLSGGQKQRVSLARAV----YSNSDIYLFDDPLSAVDAHVGKHIFEKV 810
Cdd:cd03227 61 GCIVAAVSAELIF----TRLQ------------LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAI 124
|
170
....*....|....*...
gi 6678848 811 vgpMGLLKNKTR-ILVTH 827
Cdd:cd03227 125 ---LEHLVKGAQvIVITH 139
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1322-1469 |
8.14e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.47 E-value: 8.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1322 IVGRTGAGKSSLTLGLFRINESAEGEIIIDGVNIAKIGL-------HNLRFKITIIPQDpvlfsgslrmNLDPFSQYSDE 1394
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKpyctyigHNLGLKLEMTVFE----------NLKFWSEIYNS 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6678848 1395 EVWMALELAHLKgfvsaLPDKLNHECAeggeNLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTI 1469
Cdd:PRK13541 101 AETLYAAIHYFK-----LHDLLDEKCY----SLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1308-1513 |
9.80e-03 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 40.42 E-value: 9.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1308 KHI--NVT--IEGGEKVGIVGRTGAGKSSLTLGL-FRINESAE--GEIIIDGVniaKIGLHNLRFKITIIPQDPVL---- 1376
Cdd:TIGR00955 38 KHLlkNVSgvAKPGELLAVMGSSGAGKTTLMNALaFRSPKGVKgsGSVLLNGM---PIDAKEMRAISAYVQQDDLFiptl 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1377 -------FSGSLRMnldPFSQYSDEEVWMALELAHLKGFVSALPDKLNHECAEGGenLSVGQRQLVCLARALLRKTKILV 1449
Cdd:TIGR00955 115 tvrehlmFQAHLRM---PRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRVKG--LSGGERKRLAFASELLTDPPLLF 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678848 1450 LDEATAAVDletDNLIQSTIRTQFEDCT-----VLTIAHRLNTIMD-YTRVIVLDKGEVRECGAPSELLQ 1513
Cdd:TIGR00955 190 CDEPTSGLD---SFMAYSVVQVLKGLAQkgktiICTIHQPSSELFElFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| |
