|
Name |
Accession |
Description |
Interval |
E-value |
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
7-1422 |
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: 2891.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 7 CSADGSDPLWDWNVTWNTSNPDFTKCFQNTVLVWVPCFYLWACFPFYFLYLSRHDRGYIQMTPLNKTKTALGFLLWIVCW 86
Cdd:TIGR00957 1 CSADGSDPLWDWNVTWHTSNPDFTKCFQNTVLAWVPCFYLWVCFPCYFLYLSRHDRGYIQMTHLNKTKTALGFLLWIVCW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 87 ADLFYSFWERSRGIFLAPVFLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVALVCALAILRSKIMTALKEDAQ 166
Cdd:TIGR00957 81 ADLFYSFWERSHGRAPAPVFLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVALVCALAILRSKILLALKEDAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 167 VDLFRDITFYVYFSLLLIQLVLSCFSDRSPLFSETIHDPNPCPESSASFLSRITFWWITGLIVRGYRQPLEGSDLWSLNK 246
Cdd:TIGR00957 161 VDPFRDTTFYIYFALVLSQLVLSCFSDKSPLFSETNHDPNPCPESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 247 EDTSEQVVPVLVKNWKKECAKTRKQPVKVVYSSKDPAQPKESSKVDANEEVEALIVKSPQKEWNPSLFKVLYKTFGPYFL 326
Cdd:TIGR00957 241 EDTSEMVVPVLVENWKKECKKTRKQPVSAVYGKKDPSKPKGSSQLDANEEVEALIVKSPHKPRKPSLFKVLYKTFGPYFL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 327 MSFFFKAIHDLMMFSGPQILKLLIKFVNDTKAPDWQGYFYTVLLFVTACLQTLVLHQYFHICFVSGMRIKTAVIGAVYRK 406
Cdd:TIGR00957 321 MSFCFKAIHDLMMFIGPQILSLLIRFVNDPMAPDWQGYFYTGLLFVCACLQTLILHQYFHICFVSGMRIKTAVMGAVYRK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 407 ALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMVLMVPVNAVMAMK 486
Cdd:TIGR00957 401 ALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMK 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 487 TKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLSAVGTFTWVCTPFL------- 559
Cdd:TIGR00957 481 TKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLvalitfa 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 560 ------------------------------------------ASVSLKRLRIFLSHEELEPDSIERRPVKDGGGtNSITV 597
Cdd:TIGR00957 561 vyvtvdennildaekafvslalfnilrfplnilpmvissivqASVSLKRLRIFLSHEELEPDSIERRTIKPGEG-NSITV 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 598 RNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG-------------------- 657
Cdd:TIGR00957 640 HNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGsvayvpqqawiqndslreni 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 658 ---------------------------------------VNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI 698
Cdd:TIGR00957 720 lfgkalnekyyqqvleacallpdleilpsgdrteigekgVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 699 FENVIGPKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAEFLRTYASTEQEQDAEENGVTGV 778
Cdd:TIGR00957 800 FEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEQQGHLEDSWTALV 879
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 779 SGPGKEAKQMENGMLVTDSAGKQLQRQLSSSSSYSGDISRHHNSTAELQKAEAKkEETWKLMEADKAQTGQVKLSVYWDY 858
Cdd:TIGR00957 880 SGEGKEAKLIENGMLVTDVVGKQLQRQLSASSSDSGDQSRHHGSSAELQKAEAK-EETWKLMEADKAQTGQVELSVYWDY 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 859 MKAIGLFISFLSIFLFMCNHVSALASNYWLSLWTDDPIVNGTQEHTKVRLSVYGALGISQGIAVFGYSMAVSIGGILASR 938
Cdd:TIGR00957 959 MKAIGLFITFLSIFLFVCNHVSALASNYWLSLWTDDPMVNGTQNNTSLRLSVYGALGILQGFAVFGYSMAVSIGGIQASR 1038
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 939 CLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPIAAIIIPPLGLIY 1018
Cdd:TIGR00957 1039 VLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLY 1118
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1019 FFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECV 1098
Cdd:TIGR00957 1119 FFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECV 1198
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1099 GNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSS 1178
Cdd:TIGR00957 1199 GNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAPPSG 1278
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1179 WPQVGRVEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDL 1258
Cdd:TIGR00957 1279 WPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL 1358
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1259 RFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLR 1338
Cdd:TIGR00957 1359 RFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLR 1438
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1339 KTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRGLFYSMAK 1418
Cdd:TIGR00957 1439 KTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSMAK 1518
|
....
gi 2462549096 1419 DAGL 1422
Cdd:TIGR00957 1519 DAGL 1522
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
29-1421 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 897.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 29 FTKCFQNTVLVWVPCFYLWAcFPFYFLYLSRHDRGYIQMTPLNKTKTALGFLLWIVCWADLFY------SFWERSRGIFL 102
Cdd:PLN03130 29 YTPCATDSLVINISHLVLLG-LCLYRIWLIKKDHKVQRFCLRSKWYNYFLALLAAYCTAEPLFrlvmgiSVLNLDGQTSL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 103 APVFLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVALVCALAILRSKIMTaLKedaqvDLFRDITFYVYFSLL 182
Cdd:PLN03130 108 PPFEIVSLIVEALTWCSMLVMIGVETKIYIREFRWYVRFAVIYVLVGDAVMLNLVLS-VK-----EYYSSFVLYLYISEV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 183 LIQLVLSCF-----------SDRSPLFSETIHD---------PNPCPESSASFLSRITFWWITGLIVRGYRQPLEGSDLW 242
Cdd:PLN03130 182 AAQVLFGILllvyfpnldpyPGYTPIGSESVDDyeyeelpggEQICPERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVW 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 243 SLNKEDTSEQVVPVLVKNWKKECAKTrkqpvkvvysskdpaqpkesskvdaneevealivkspqkewNPSLFKVLYKTFG 322
Cdd:PLN03130 262 KLDTWDQTETLYRSFQKCWDEELKKP-----------------------------------------KPWLLRALNNSLG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 323 PYFLMSFFFKAIHDLMMFSGPQILKLLIKFVNdTKAPDWQGYFYTVLLFVTACLQTLVLHQYFHICFVSGMRIKTAVIGA 402
Cdd:PLN03130 301 GRFWLGGFFKIGNDLSQFVGPLLLNLLLESMQ-NGEPAWIGYIYAFSIFVGVVLGVLCEAQYFQNVMRVGFRLRSTLVAA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 403 VYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMVLMVPVNAV 482
Cdd:PLN03130 380 VFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLVLMFPIQTF 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 483 MAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLSAV-------------- 548
Cdd:PLN03130 460 IISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFnsfilnsipvlvtv 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 549 ---GTFTW---VCTP-----------------FL----------ASVSLKRLRIFLSHEE--LEPDSierrPVKDGggTN 593
Cdd:PLN03130 540 vsfGVFTLlggDLTParaftslslfavlrfplFMlpnlitqavnANVSLKRLEELLLAEErvLLPNP----PLEPG--LP 613
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 594 SITVRNATFTW-ARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVE-GHVAIKG-------------- 657
Cdd:PLN03130 614 AISIKNGYFSWdSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGtvayvpqvswifna 693
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 658 ---------------------------------------------VNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 692
Cdd:PLN03130 694 tvrdnilfgspfdperyeraidvtalqhdldllpggdlteigergVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 693 HVGKHIFENVIgpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAEFLRTYASTEQEQdaEE 772
Cdd:PLN03130 774 HVGRQVFDKCI--KDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMENAGKMEEYV--EE 849
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 773 NGvtGVSGPGKEAKQMENGmlvtdsAGKQLQRqlsssssysgdisrhhNSTAELQKAEAKKeetwKLMEADKAQTGQVKL 852
Cdd:PLN03130 850 NG--EEEDDQTSSKPVANG------NANNLKK----------------DSSSKKKSKEGKS----VLIKQEERETGVVSW 901
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 853 SVYWDYMKAIGLFisFLSIFLFMC---NHVSALASNYWLSLWTDDpivNGTQEHTKV-RLSVYGALGISQGIAVFGYSMA 928
Cdd:PLN03130 902 KVLERYKNALGGA--WVVMILFLCyvlTEVFRVSSSTWLSEWTDQ---GTPKTHGPLfYNLIYALLSFGQVLVTLLNSYW 976
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 929 VSIGGILASRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPIAA 1008
Cdd:PLN03130 977 LIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVSTISL 1056
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1009 IIIPPLGLIYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVAN 1088
Cdd:PLN03130 1057 WAIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTLVNMSSN 1136
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1089 RWLAVRLECVGNCIVLFAALFAVI-----SRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYSETE 1163
Cdd:PLN03130 1137 RWLAIRLETLGGLMIWLTASFAVMqngraENQAAFASTMGLLLSYALNITSLLTAVLRLASLAENSLNAVERVGTYIDLP 1216
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1164 KEAPWQIQETAPPSSWPQVGRVEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEI 1243
Cdd:PLN03130 1217 SEAPLVIENNRPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRI 1296
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1244 IIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLS 1323
Cdd:PLN03130 1297 LIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFS 1376
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1324 VGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAP 1403
Cdd:PLN03130 1377 VGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTP 1456
|
1530
....*....|....*....
gi 2462549096 1404 SDLLQ-QRGLFYSMAKDAG 1421
Cdd:PLN03130 1457 ENLLSnEGSAFSKMVQSTG 1475
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
102-1421 |
0e+00 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 807.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 102 LAPVFLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVALVCALAILRSKIMT---ALKEDAQVDLFRDITFYVY 178
Cdd:PLN03232 107 LPPFEVASLMVEAFAWFSMLVLIGLETKQYVKEFRWYVRFGVVYVLVADAVLLDLVLPlknSINRTALYLCISSRCCQAL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 179 FSLLLIQLV--LSCFSDRSPLFSETIHD---------PNPCPESSASFLSRITFWWITGLIVRGYRQPLEGSDLWSLNKE 247
Cdd:PLN03232 187 FGILLLVYIpeLDPYPGYHILNNESLDNveydalrggENICPERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQW 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 248 DTSEQVVPVLVKNWKKECAKtrkqpvkvvysskdpaqPKesskvdaneevealivkspqkewnPSLFKVLYKTFGPYFLM 327
Cdd:PLN03232 267 DQTETLIKRFQRCWTEESRR-----------------PK------------------------PWLLRALNNSLGGRFWL 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 328 SFFFKAIHDLMMFSGPQILKLLIKFVNDTKaPDWQGYFYTVLLFVTACLQTLVLHQYFHICFVSGMRIKTAVIGAVYRKA 407
Cdd:PLN03232 306 GGIFKIGHDLSQFVGPVILSHLLQSMQEGD-PAWVGYVYAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLVAAIFHKS 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 408 LVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMVLMVPVNAVMAMKT 487
Cdd:PLN03232 385 LRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRKM 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 488 KTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLSAVGTFTWVCTPFL-------- 559
Cdd:PLN03232 465 RKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVvtlvsfgv 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 560 ---------------------------------------ASVSLKRLR-IFLSHEELEPDSIERRPvkdggGTNSITVRN 599
Cdd:PLN03232 545 fvllggdltparaftslslfavlrsplnmlpnllsqvvnANVSLQRIEeLLLSEERILAQNPPLQP-----GAPAISIKN 619
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 600 ATFTW-ARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVE-------GHVAI---------------- 655
Cdd:PLN03232 620 GYFSWdSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAEtssvvirGSVAYvpqvswifnatvreni 699
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 656 -------------------------------------KGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI 698
Cdd:PLN03232 700 lfgsdfeserywraidvtalqhdldllpgrdlteigeRGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQV 779
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 699 FENVIgpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAEFLRTYASTEQEQDAEENGVTGV 778
Cdd:PLN03232 780 FDSCM--KDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGKMDATQEVNTNDENIL 857
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 779 SGPGKEAKQMENGMLVTDSAGKQLQRQLSssssysgdisrhhnstaelqkaeaKKEETwklmeadkaQTGQVKLSVYWDY 858
Cdd:PLN03232 858 KLGPTVTIDVSERNLGSTKQGKRGRSVLV------------------------KQEER---------ETGIISWNVLMRY 904
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 859 MKAIG-LFISFLSIFLFMCNHVSALASNYWLSLWTDDPIVNGTQehTKVRLSVYGALGISQGIAVFGYSMAVSIGGILAS 937
Cdd:PLN03232 905 NKAVGgLWVVMILLVCYLTTEVLRVSSSTWLSIWTDQSTPKSYS--PGFYIVVYALLGFGQVAVTFTNSFWLISSSLHAA 982
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 938 RCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPIAAIIIPPLGLI 1017
Cdd:PLN03232 983 KRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLIL 1062
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1018 YFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLEC 1097
Cdd:PLN03232 1063 FYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLET 1142
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1098 VGNCIVLFAALFAVI-----SRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQE 1172
Cdd:PLN03232 1143 LGGVMIWLTATFAVLrngnaENQAGFASTMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIEN 1222
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1173 TAPPSSWPQVGRVEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAK 1252
Cdd:PLN03232 1223 NRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAK 1302
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1253 IGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCL 1332
Cdd:PLN03232 1303 FGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSL 1382
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1333 ARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRG- 1411
Cdd:PLN03232 1383 ARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTs 1462
|
1450
....*....|
gi 2462549096 1412 LFYSMAKDAG 1421
Cdd:PLN03232 1463 AFFRMVHSTG 1472
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
312-1421 |
0e+00 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 631.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 312 SLFKVLYKTFGPYFLMSFFFKAIHDLMMFSGPQILKLLIKFVNDTKAPDWQGYFYTVLLFVTACLQTLVLHQYFHICFVS 391
Cdd:PTZ00243 233 SLLRTLFAALPYYVWWQIPFKLLSDVCTLTLPVLLKYFVKFLDADNATWGRGLGLVLTLFLTQLIQSVCLHRFYYISIRC 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 392 GMRIKTAVIGAVYRKALVITNS--ARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAG 469
Cdd:PTZ00243 313 GLQYRSALNALIFEKCFTISSKslAQPDMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWCALMA 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 470 VAVMVLMVPVNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLSAVG 549
Cdd:PTZ00243 393 VAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLARVAT 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 550 TFTWVCTPFLA-----------------------------------------------SVSLKRLRIFLSHE-------- 574
Cdd:PTZ00243 473 SFVNNATPTLMiavvftvyyllgheltpevvfptiallgvlrmpffmipwvfttvlqfLVSIKRISTFLECDnatcstvq 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 575 ELEPDSIERR---------------------PVK---------------------------------------------- 587
Cdd:PTZ00243 553 DMEEYWREQRehstacqlaavlenvdvtafvPVKlprapkvktsllsralrmlcceqcrptkrhpspsvvvedtdygsps 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 588 ------DGGGTNSITVRNATFTWARSDPPT-------------LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDK 648
Cdd:PTZ00243 633 sasrhiVEGGTGGGHEATPTSERSAKTPKMktddffelepkvlLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEI 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 649 VEGHV-------------------------------------AI----------------------KGVNLSGGQKQRVS 669
Cdd:PTZ00243 713 SEGRVwaersiayvpqqawimnatvrgnilffdeedaarladAVrvsqleadlaqlgggleteigeKGVNLSGGQKARVS 792
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 670 LARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIgpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYqella 749
Cdd:PTZ00243 793 LARAVYANRDVYLLDDPLSALDAHVGERVVEECF--LGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSS----- 865
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 750 rdgafAEFLRTyaSTEQEQDAEENGVTGVSGPGKEAKQMENGML---VTDSAGKQLQRQlsssssysgdisrhhnSTAEL 826
Cdd:PTZ00243 866 -----ADFMRT--SLYATLAAELKENKDSKEGDADAEVAEVDAApggAVDHEPPVAKQE----------------GNAEG 922
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 827 QKAEAKKEETWKLMEADKAQTGQVKLSVYWDYMKAIG-LFISFLSIFLFMCNHVSALASNYWLSLWTddpiVNGTQEHTK 905
Cdd:PTZ00243 923 GDGAALDAAAGRLMTREEKASGSVPWSTYVAYLRFCGgLHAAGFVLATFAVTELVTVSSGVWLSMWS----TRSFKLSAA 998
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 906 VRLSVYgaLGIS-QGIAVFGYSMAVSIGGI-LASRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVI 983
Cdd:PTZ00243 999 TYLYVY--LGIVlLGTFSVPLRFFLSYEAMrRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSY 1076
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 984 KMFMGSLFNVIGACIVILLATPIAAIIIPPLGLIYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQ 1063
Cdd:PTZ00243 1077 LYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKA 1156
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1064 ERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVI------SRHSLsaGLVGLSVSYSLQVTTYLN 1137
Cdd:PTZ00243 1157 HLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIALIGVIgtmlraTSQEI--GLVSLSLTMAMQTTATLN 1234
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1138 WLVRMSSEMETNIVAVERLKEYS-ETEKEAPWQ-----------------------IQETAPPSSWP---QVGRVEFRNY 1190
Cdd:PTZ00243 1235 WLVRQVATVEADMNSVERLLYYTdEVPHEDMPEldeevdalerrtgmaadvtgtvvIEPASPTSAAPhpvQAGSLVFEGV 1314
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1191 CLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPV 1270
Cdd:PTZ00243 1315 QMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPV 1394
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1271 LFSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRK-TKILVLDEAT 1349
Cdd:PTZ00243 1395 LFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKgSGFILMDEAT 1474
|
1290 1300 1310 1320 1330 1340 1350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462549096 1350 AAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQR-GLFYSMAKDAG 1421
Cdd:PTZ00243 1475 ANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRqSIFHSMVEALG 1547
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
867-1160 |
4.07e-170 |
|
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: 509.71 E-value: 4.07e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 867 SFLSIFLFMCNHVSALASNYWLSLWTDDPIVNGTQ--EHTKVRLSVYGALGISQGIAVFGYSMAVSIGGILASRCLHVDL 944
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSDDPALNGTQdtEQRDYRLGVYGALGLGQAIFVFLGSLALALGCVRASRNLHNKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 945 LHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPIAAIIIPPLGLIYFFVQRF 1024
Cdd:cd18603 81 LHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAILYFFIQRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1025 YVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVL 1104
Cdd:cd18603 161 YVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEFLGNLIVL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462549096 1105 FAALFAVISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYS 1160
Cdd:cd18603 241 FAALFAVLSRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIKEYS 296
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1183-1403 |
1.96e-135 |
|
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: 414.97 E-value: 1.96e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1183 GRVEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKI 1262
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1263 TIIPQDPVLFSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKI 1342
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462549096 1343 LVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAP 1403
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
209-1413 |
3.39e-134 |
|
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: 450.52 E-value: 3.39e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 209 PESSASFLSRITFWWITGLIVRGYRQPLEGSDLWSLNKEDTSEQVVPVLVKNWKKECAKTRKqpvkvvysskdpaqpkes 288
Cdd:TIGR01271 5 PVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELASAKK------------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 289 skvdaneevealivkspqkewNPSLFKVLYKTFGPYFLMSFFFKAIHDLMMFSGPQILKLLIKFVNDTKAPDW-QGYFYT 367
Cdd:TIGR01271 67 ---------------------NPKLLNALRRCFFWRFVFYGILLYFGEATKAVQPLLLGRIIASYDPFNAPEReIAYYLA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 368 V---LLFVtacLQTLVLHQYFHICFVSGMRIKTAVIGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMI 444
Cdd:TIGR01271 126 LglcLLFI---VRTLLLHPAIFGLHHLGMQMRIALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFV 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 445 WSAPLQVILALYLLWLNLGPSVLAGVAVMVLMVPVNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAF 524
Cdd:TIGR01271 203 WIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAM 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 525 KDKVLAIRQEELKVLKKSAYL----SAVGTFTWVCTPFLASVS--------LKRL---------------RIFLSHEELE 577
Cdd:TIGR01271 283 EKIIKNIRQDELKLTRKIAYLryfySSAFFFSGFFVVFLSVVPyalikgiiLRRIfttisycivlrmtvtRQFPGAIQTW 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 578 PDSI-------------ERRPVKDGGGTNSITVRNATFTW----------------ARSDP----------------PTL 612
Cdd:TIGR01271 363 YDSLgaitkiqdflckeEYKTLEYNLTTTEVEMVNVTASWdegigelfekikqnnkARKQPngddglffsnfslyvtPVL 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 613 NGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV------------------AIK------------------ 656
Cdd:TIGR01271 443 KNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIkhsgrisfspqtswimpgTIKdniifglsydeyrytsvi 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 657 -----------------------GVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPkgMLKNKT 713
Cdd:TIGR01271 523 kacqleedialfpekdktvlgegGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCK--LMSNKT 600
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 714 RILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAEFLRTYASTEQEQDAEENGV--------------TGVS 779
Cdd:TIGR01271 601 RILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLLGLEAFDNFSAERRNSIltetlrrvsidgdsTVFS 680
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 780 GP------------------------------------GKEAKQME-NGM-------------LVTDS------------ 797
Cdd:TIGR01271 681 GPetikqsfkqpppefaekrkqsiilnpiasarkfsfvQMGPQKAQaTTIedavrepserkfsLVPEDeqgeeslprgnq 760
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 798 --AGKQLQ---RQ--LSSSSSYSGDISRHHNSTAELQKAEAKKEETWKLMEAD-----KAQTGQVKLS----------VY 855
Cdd:TIGR01271 761 yhHGLQHQaqrRQsvLQLMTHSNRGENRREQLQTSFRKKSSITQQNELASELDiysrrLSKDSVYEISeeineedlkeCF 840
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 856 WDYMKAIGLFIS---------------FLSIFLFMCNHVSALASNYWLSLWTDDPIVNG--TQEHTKVR--LSVYGAL-- 914
Cdd:TIGR01271 841 ADERENVFETTTwntylryittnrnlvFVLIFCLVIFLAEVAASLLGLWLITDNPSAPNyvDQQHANASspDVQKPVIit 920
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 915 ------------GISQGIAVFGYSMAVSIGGIL--ASRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIP 980
Cdd:TIGR01271 921 ptsayyifyiyvGTADSVLALGFFRGLPLVHTLltVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLP 1000
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 981 EVIKMFMGSLFNVIGACIVILLATPIAAIIIPPLGLIYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAF 1060
Cdd:TIGR01271 1001 LTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAF 1080
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1061 EEQ---ERFIHQSdlkVDENQKAYYPSIVANRWLAVRLECVgncIVLF--AALFAVISRHSLSAGLVGLSVSYSLQVTTY 1135
Cdd:TIGR01271 1081 GRQsyfETLFHKA---LNLHTANWFLYLSTLRWFQMRIDII---FVFFfiAVTFIAIGTNQDGEGEVGIILTLAMNILST 1154
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1136 LNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETAP--PSS------------WPQVGRVEFRNYCLRYREDLDFV 1201
Cdd:TIGR01271 1155 LQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEPRPSGGGGKyqLSTvlvienphaqkcWPSGGQMDVQGLTAKYTEAGRAV 1234
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1202 LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRInESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLD 1281
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD 1313
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1282 PFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQ 1361
Cdd:TIGR01271 1314 PYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIR 1393
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|..
gi 2462549096 1362 STIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRGLF 1413
Cdd:TIGR01271 1394 KTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLF 1445
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
328-563 |
1.98e-124 |
|
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: 388.37 E-value: 1.98e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 328 SFFFKAIHDLMMFSGPQILKLLIKFVNDTKAPDWQGYFYTVLLFVTACLQTLVLHQYFHICFVSGMRIKTAVIGAVYRKA 407
Cdd:cd18595 2 AALLKLLSDILLFASPQLLKLLINFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIYRKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 408 LVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMVLMVPVNAVMAMKT 487
Cdd:cd18595 82 LRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLARKI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462549096 488 KTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLSAVGTFTWVCTPFLASVS 563
Cdd:cd18595 162 KKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLNAVSSFLWTCAPFLVSLA 237
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
840-1418 |
3.75e-123 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 396.07 E-value: 3.75e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 840 MEADKAQTGQVKLSVYWDYMKAIglfisFLSIFLFMCNHVSALASNYWLSLWTDDPIVNGTQEHTKVRLSVYGALGISQG 919
Cdd:COG1132 1 MSKSPRKLLRRLLRYLRPYRGLL-----ILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 920 IAVFGYSMAVSIGGILASRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIV 999
Cdd:COG1132 76 LLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1000 ILLATPIAAIIIPPLGLIYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQK 1079
Cdd:COG1132 156 LFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1080 AYYPSIVANRWLAVRLECVGNCIVLFAALFAV--ISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLK 1157
Cdd:COG1132 236 ANLRAARLSALFFPLMELLGNLGLALVLLVGGllVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1158 EYSETEKEAPWQIQETAPPsswPQVGRVEFRNYCLRYREDlDFVLRHINVTINGGEKVGIVGRTGAGKSSLT---LGLFR 1234
Cdd:COG1132 316 ELLDEPPEIPDPPGAVPLP---PVRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGKSTLVnllLRFYD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1235 INEsaeGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL---DPfsQYSDEEVWTSLELAHLKDFVSALPDKL 1311
Cdd:COG1132 392 PTS---GRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRP--DATDEEVEEAAKAAQAHEFIEALPDGY 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1312 DHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIV 1391
Cdd:COG1132 467 DTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILV 546
|
570 580
....*....|....*....|....*..
gi 2462549096 1392 LDKGEIQEYGAPSDLLQQRGLFYSMAK 1418
Cdd:COG1132 547 LDDGRIVEQGTHEELLARGGLYARLYR 573
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
867-1160 |
3.00e-121 |
|
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: 379.64 E-value: 3.00e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 867 SFLSIFLFMCNHVSALASNYWLSLWTDDPiVNGTQEHTKVRLSVYGALGISQGIAVFGYSMAVSIGGILASRCLHVDLLH 946
Cdd:cd18559 1 SFLLIKLVLCNHVFSGPSNLWLLLWFDDP-VNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 947 SILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPIAAIIIpPLGLIYFFVQRFYV 1026
Cdd:cd18559 80 KALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGI-PLGLLYVPVNRVYA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1027 ASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDeNQKAYYPSIVANRWLAVRLECVGNCIVLFA 1106
Cdd:cd18559 159 ASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRD-NELAYLPSIVYLRALAVRLWCVGPCIVLFA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2462549096 1107 ALFAVISRHSLsAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYS 1160
Cdd:cd18559 238 SFFAYVSRHSL-AGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
867-1160 |
1.26e-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: 361.82 E-value: 1.26e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 867 SFLSIFLFMCNHVSALASNYWLSLWTDDpIVNGTQEHTKVRLSVYGALGI-SQGIAVFGYSMAVSIGGILASRCLHVDLL 945
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSD-WSSSPNSSSGYYLGVYAALLVlASVLLVLLRWLLFVLAGLRASRRLHDKLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 946 HSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPIAAIIIPPLGLIYFFVQRFY 1025
Cdd:cd18580 80 RSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1026 VASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLF 1105
Cdd:cd18580 160 LRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGLRLDLLGALLALV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2462549096 1106 AALFAVISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYS 1160
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 ... |
862-1160 |
1.28e-106 |
|
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: 339.84 E-value: 1.28e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 862 IGLFISFLSIFLFmcnhvSALASNYWLSLWTDDpivngtqehtKVRLS------VYGALGISQGIAVFGYSMAVSIGGIL 935
Cdd:cd18606 1 LPLLLLLLILSQF-----AQVFTNLWLSFWTED----------FFGLSqgfyigIYAGLGVLQAIFLFLFGLLLAYLGIR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 936 ASRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPIAAIIIPPLG 1015
Cdd:cd18606 66 ASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1016 LIYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRL 1095
Cdd:cd18606 146 VLYYFIANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRL 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549096 1096 ECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYS 1160
Cdd:cd18606 226 DLLGSLLVLIVALLCVTRRFSISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLLHYA 290
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1179-1403 |
1.22e-99 |
|
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: 317.05 E-value: 1.22e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1179 WPQVGRVEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDL 1258
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1259 RFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWTSLELahlkdfvsalpdkldhecAEGGENLSVGQRQLVCLARALLR 1338
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALRV------------------SEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549096 1339 KTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAP 1403
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
327-563 |
2.04e-99 |
|
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: 319.93 E-value: 2.04e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 327 MSFFFKAIHDLMMFSGPQILKLLIKFVNDTKAPDWQGYFYTVLLFVTACLQTLVLHQYFHICFVSGMRIKTAVIGAVYRK 406
Cdd:cd18559 1 SFLLIKLVLCNHVFSGPSNLWLLLWFDDPVNGPQEHGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 407 ALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMVLMVPVNAVMAMK 486
Cdd:cd18559 81 ALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAAS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549096 487 TKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLSAVGTFTWVCTPFLASVS 563
Cdd:cd18559 161 SRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFA 237
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
943-1418 |
1.08e-95 |
|
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: 324.48 E-value: 1.08e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 943 DLLHSILRSPMSFFERTPSGNLVNRFSkELDTVDSMIPEVIKMFMGSLFNVIGACIVILL----ATPIAAIIIPPLGLIY 1018
Cdd:COG2274 234 RFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSLLTALLDLLFVLIFLIVLFFysppLALVVLLLIPLYVLLG 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1019 FFVQRFYVASSRQlkrlESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDE----NQKAYYPSIVANRWLAVr 1094
Cdd:COG2274 313 LLFQPRLRRLSRE----ESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKylnaRFKLRRLSNLLSTLSGL- 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1095 LECVGNCIVLFAALFAVISRHsLSAG-LVGlSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPwqiqET 1173
Cdd:COG2274 388 LQQLATVALLWLGAYLVIDGQ-LTLGqLIA-FNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPERE----EG 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1174 APPSSWPQV-GRVEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLT---LGLFRINEsaeGEIIIDGIN 1249
Cdd:COG2274 462 RSKLSLPRLkGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLkllLGLYEPTS---GRILIDGID 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1250 IAKIGLHDLRFKITIIPQDPVLFSGSLRMNL---DPfsQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQ 1326
Cdd:COG2274 539 LRQIDPASLRRQIGVVLQDVFLFSGTIRENItlgDP--DATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQ 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1327 RQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDL 1406
Cdd:COG2274 617 RQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEEL 696
|
490
....*....|..
gi 2462549096 1407 LQQRGLFYSMAK 1418
Cdd:COG2274 697 LARKGLYAELVQ 708
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
868-1160 |
3.13e-91 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 297.46 E-value: 3.13e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 868 FLSIFLFMCNHVSALASNYWLSLWT---DDPIVNGTQEHTKVR-LSVYGALGISQGIAVFGYSMAVSIGGILASRCLHVD 943
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIWAsayETSSALPPSEVSVLYyLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 944 LLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPIAAIIIPPLGLIYFFVQR 1023
Cdd:cd18604 82 LLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1024 FYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIV 1103
Cdd:cd18604 162 LYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALFS 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549096 1104 LFAALFAViSRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYS 1160
Cdd:cd18604 242 FATAALLV-YGPGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
328-563 |
1.35e-87 |
|
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: 286.69 E-value: 1.35e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 328 SFFFKAIHDLMMFSGPQILKLLIKFVNDTKAPD-WQGYFYTVLLFVTACLQTLVLHQYFHICFVSGMRIKTAVIGAVYRK 406
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPlSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 407 ALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMVLMVPVNAVMAMK 486
Cdd:cd18579 82 ALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549096 487 TKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLSAVGTFTWVCTPFLASVS 563
Cdd:cd18579 162 ISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLA 238
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
865-1159 |
1.68e-87 |
|
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: 287.12 E-value: 1.68e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 865 FISFLsIFLFMCnHVSALASNYWLSLWTD---DPIVNGTQEHTKVRLSVYGALGISQGIAVFGYSMAVSIGGILASRCLH 941
Cdd:cd18605 1 LILIL-LSLILM-QASRNLIDFWLSYWVShsnNSFFNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 942 VDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPIAAIIIPPLGLIYFFV 1021
Cdd:cd18605 79 NKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1022 QRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNC 1101
Cdd:cd18605 159 QRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSIRLQLLGVL 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462549096 1102 IVLFAALFAVISRH---SLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEY 1159
Cdd:cd18605 239 IVTFVALTAVVQHFfglSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQY 299
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
868-1160 |
2.85e-86 |
|
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: 283.73 E-value: 2.85e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 868 FLSIFLFMCNHVSALASNYWLSLWTD-----------DPIVNGTQEHTKVRLSVYGALGISQGIAVFGYSMAVSIGGILA 936
Cdd:cd18602 2 ALVLALALLKQGLRVATDFWLADWTEanhdvasvvfnITSSSLEDDEVSYYISVYAGLSLGAVILSLVTNLAGELAGLRA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 937 SRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPIAAIIIPPLGL 1016
Cdd:cd18602 82 ARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIII 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1017 IYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLE 1096
Cdd:cd18602 162 VYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRLD 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462549096 1097 CVGNCIVLFAALFAVISRH--SLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYS 1160
Cdd:cd18602 242 YLGAVIVFLAALSSLTAALagYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVLEYT 307
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1183-1418 |
6.88e-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: 275.25 E-value: 6.88e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1183 GRVEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKI 1262
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1263 TIIPQDPVLFSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKI 1342
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549096 1343 LVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLL-QQRGLFYSMAK 1418
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLVR 254
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
923-1411 |
1.12e-74 |
|
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: 259.69 E-value: 1.12e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 923 FGYSMAVSIGGILASRclhvdLLHSILRSPMSFFERTPSGNLVNRFskeLDTVDSMIPEVIKmFMGSLFNVIGACIVILL 1002
Cdd:COG4988 81 AAFRAAARVKRRLRRR-----LLEKLLALGPAWLRGKSTGELATLL---TEGVEALDGYFAR-YLPQLFLAALVPLLILV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1003 AT----PIAAIII----PplgLIYFFV----QRFYVASSRQLKRLESVSrspvySHFNETLLGVSVIRAF----EEQERF 1066
Cdd:COG4988 152 AVfpldWLSGLILlvtaP---LIPLFMilvgKGAAKASRRQWRALARLS-----GHFLDRLRGLTTLKLFgrakAEAERI 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1067 IHQSD---------LKVdenqkAYYPSIVanrwlavrLECVGnciVLFAALFAVISRHSLSAGLVGLSVSYSL------- 1130
Cdd:COG4988 224 AEASEdfrkrtmkvLRV-----AFLSSAV--------LEFFA---SLSIALVAVYIGFRLLGGSLTLFAALFVlllapef 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1131 -----QVTTYlnWLVRMSsemetNIVAVERLKEYSETEKEAPWQIQETAPpssWPQVGRVEFRNYCLRYrEDLDFVLRHI 1205
Cdd:COG4988 288 flplrDLGSF--YHARAN-----GIAAAEKIFALLDAPEPAAPAGTAPLP---AAGPPSIELEDVSFSY-PGGRPALDGL 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1206 NVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL---DP 1282
Cdd:COG4988 357 SLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLrlgRP 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1283 fsQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQS 1362
Cdd:COG4988 437 --DASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQ 514
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2462549096 1363 TIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRG 1411
Cdd:COG4988 515 ALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1183-1411 |
1.60e-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: 247.14 E-value: 1.60e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1183 GRVEFRNYCLRYREDlDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKI 1262
Cdd:cd03254 1 GEIEFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1263 TIIPQDPVLFSGSLRMNLDPFSQYSDEEVWT-SLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTK 1341
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIeAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1342 ILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRG 1411
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
914-1416 |
1.52e-73 |
|
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: 256.95 E-value: 1.52e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 914 LGISQGIAVFGYSMAVSIGGILASRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNV 993
Cdd:TIGR02203 63 LAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 994 IGACIVILLA----TPIAAIIIPPLGLIyffvqrfyvaSSRQLKRLESVSRSPVYSH------FNETLLGVSVIRAF--- 1060
Cdd:TIGR02203 143 IGLFIVLLYYswqlTLIVVVMLPVLSIL----------MRRVSKRLRRISKEIQNSMgqvttvAEETLQGYRVVKLFggq 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1061 -EEQERFIHQSD------LKVDENQKAYYPSI--VANRWLAVrlecvgnciVLFAALFAVISRHSLSAGLVGLSVSySLQ 1131
Cdd:TIGR02203 213 aYETRRFDAVSNrnrrlaMKMTSAGSISSPITqlIASLALAV---------VLFIALFQAQAGSLTAGDFTAFITA-MIA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1132 VTTYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPwqiQETAPPsswPQV-GRVEFRNYCLRYREDLDFVLRHINVTIN 1210
Cdd:TIGR02203 283 LIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKD---TGTRAI---ERArGDVEFRNVTFRYPGRDRPALDSISLVIE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1211 GGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL---DPfSQYS 1287
Cdd:TIGR02203 357 PGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRT-EQAD 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1288 DEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQ 1367
Cdd:TIGR02203 436 RAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERL 515
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2462549096 1368 FEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRGLF---YSM 1416
Cdd:TIGR02203 516 MQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYaqlHNM 567
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
934-1418 |
1.11e-71 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 251.22 E-value: 1.11e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 934 ILASrcLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIkmfmgslFNVIGACIVILLATPIAAIIIPP 1013
Cdd:COG4987 86 LLAD--LRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVL-------LPLLVALLVILAAVAFLAFFSPA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1014 LGLIYF------------FVQRFYVASSRQLKRLesvsRSPVYSHFNETLLGVSVIRAFEEQERFIHQsdlkVDENQKAY 1081
Cdd:COG4987 157 LALVLAlglllaglllplLAARLGRRAGRRLAAA----RAALRARLTDLLQGAAELAAYGALDRALAR----LDAAEARL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1082 ypsiVANRWLAVRLECVGNCIVLFAALFAVI----------SRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIV 1151
Cdd:COG4987 229 ----AAAQRRLARLSALAQALLQLAAGLAVVavlwlaaplvAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1152 AVERLKEYSETEKeapwQIQETAPPSSWPQVGRVEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLG 1231
Cdd:COG4987 305 AARRLNELLDAPP----AVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLAL 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1232 LFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL---DPfsQYSDEEVWTSLELAHLKDFVSALP 1308
Cdd:COG4987 381 LLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLrlaRP--DATDEELWAALERVGLGDWLAALP 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1309 DKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTR 1388
Cdd:COG4987 459 DGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDR 538
|
490 500 510
....*....|....*....|....*....|
gi 2462549096 1389 VIVLDKGEIQEYGAPSDLLQQRGLFYSMAK 1418
Cdd:COG4987 539 ILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
863-1160 |
1.80e-71 |
|
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: 242.08 E-value: 1.80e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 863 GLFISFLSIFLFMCNHVSALASNYWLSLW---TDDPIVNGTQEHTKVRLSVYGALGISQGIAVFGYSMAVSIGGIL---- 935
Cdd:cd18599 1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWlkqGSGNTTNNVDNSTVDSGNISDNPDLNFYQLVYGGSILVILLLSLirgf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 936 --------ASRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPIA 1007
Cdd:cd18599 81 vfvkvtlrASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1008 AIIIPPLGLIYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVA 1087
Cdd:cd18599 161 LIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462549096 1088 NRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYS 1160
Cdd:cd18599 241 MRWLAVRLDILAVLITLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
595-737 |
1.17e-67 |
|
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: 226.58 E-value: 1.17e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTWARSD---PPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAI---------------- 655
Cdd:cd03250 1 ISVEDASFTWDSGEqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVpgsiayvsqepwiqng 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 656 -------------------------------------------KGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 692
Cdd:cd03250 81 tirenilfgkpfdeeryekvikacalepdleilpdgdlteigeKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462549096 693 HVGKHIFENVIGPKGMlKNKTRILVTHSMSYLPQVDVIIVMSGGK 737
Cdd:cd03250 161 HVGRHIFENCILGLLL-NNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1185-1416 |
1.08e-66 |
|
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: 225.19 E-value: 1.08e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITI 1264
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1265 IPQDPVLFSGSLRMNLdpfsQY-----SDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRK 1339
Cdd:cd03251 81 VSQDVFLFNDTVAENI----AYgrpgaTREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549096 1340 TKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRGLFYSM 1416
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
863-1160 |
2.52e-63 |
|
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: 218.73 E-value: 2.52e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 863 GLFISFLSIFLFMCNHVSALASNYWLSLWTDDPIVNGTQEHT----------------KVRLSVYGALGISQGIAVFGYS 926
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWANLEEKLNDTTDRvqgenstnvdiedldrDFNLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 927 MAVSIGGILASRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPI 1006
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1007 AAIIIPPLGLIYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIV 1086
Cdd:cd18601 161 VLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFLA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549096 1087 ANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYS 1160
Cdd:cd18601 241 TSRWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERVLEYS 314
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1185-1396 |
9.08e-63 |
|
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: 211.09 E-value: 9.08e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITI 1264
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1265 IPQDPVLFSGSLRMNLdpfsqysdeevwtslelahlkdfvsalpdkldhecaeggenLSVGQRQLVCLARALLRKTKILV 1344
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462549096 1345 LDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGE 1396
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1185-1416 |
1.63e-62 |
|
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: 213.25 E-value: 1.63e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYrEDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITI 1264
Cdd:cd03253 1 IEFENVTFAY-DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1265 IPQDPVLFSGSLRMNLdpfsQY-----SDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRK 1339
Cdd:cd03253 80 VPQDTVLFNDTIGYNI----RYgrpdaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549096 1340 TKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRGLFYSM 1416
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
940-1416 |
4.29e-62 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 223.83 E-value: 4.29e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 940 LHVDLLHSILRSPMSFFERTPSGNLVNRFSKelDTvdsmipEVIK----MFMGSLFN---VIGACIVILLATP-----IA 1007
Cdd:PRK10790 100 LRTDVMDAALRQPLSAFDTQPVGQLISRVTN--DT------EVIRdlyvTVVATVLRsaaLIGAMLVAMFSLDwrmalVA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1008 AIIIPPLGLIYFFVQRFyvaSSRQLKRLESVsRSPVYSHFNETLLGVSVIRAFEEQERFihqsDLKVDENQKAYYPSiva 1087
Cdd:PRK10790 172 IMIFPAVLVVMVIYQRY---STPIVRRVRAY-LADINDGFNEVINGMSVIQQFRQQARF----GERMGEASRSHYMA--- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1088 nRWLAVRLE--CVGNCIVLFAALF--AVISRHSLSA-GLVGLSVSYSlqvttYLNWLVRMS----------SEMETNIVA 1152
Cdd:PRK10790 241 -RMQTLRLDgfLLRPLLSLFSALIlcGLLMLFGFSAsGTIEVGVLYA-----FISYLGRLNeplielttqqSMLQQAVVA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1153 VERLKEYseteKEAPWQI--QETAPPSSwpqvGRVEFRNYCLRYREDlDFVLRHINVTINGGEKVGIVGRTGAGKSSLTL 1230
Cdd:PRK10790 315 GERVFEL----MDGPRQQygNDDRPLQS----GRIDIDNVSFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTLAS 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1231 GLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSALPDK 1310
Cdd:PRK10790 386 LLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDG 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1311 LDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVI 1390
Cdd:PRK10790 466 LYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTIL 545
|
490 500
....*....|....*....|....*.
gi 2462549096 1391 VLDKGEIQEYGAPSDLLQQRGLFYSM 1416
Cdd:PRK10790 546 VLHRGQAVEQGTHQQLLAAQGRYWQM 571
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1185-1418 |
1.30e-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: 1.30e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRY--REDLDfVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKI 1262
Cdd:cd03249 1 IEFKNVSFRYpsRPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1263 TIIPQDPVLFSGSLRMNL-----DPfsqySDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALL 1337
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIrygkpDA----TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1338 RKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRGLFYSMA 1417
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLV 235
|
.
gi 2462549096 1418 K 1418
Cdd:cd03249 236 K 236
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1112-1416 |
6.63e-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: 214.68 E-value: 6.63e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1112 ISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYSETEKEapwqIQET--APPSSwPQVGRVEFRN 1189
Cdd:COG5265 288 VVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPE----VADApdAPPLV-VGGGEVRFEN 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1190 YCLRYREDLDfVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDP 1269
Cdd:COG5265 363 VSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDT 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1270 VLFSGSLRMNLdpfsQY-----SDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILV 1344
Cdd:COG5265 442 VLFNDTIAYNI----AYgrpdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILI 517
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462549096 1345 LDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRGLFYSM 1416
Cdd:COG5265 518 FDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
908-1416 |
8.74e-58 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 213.82 E-value: 8.74e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 908 LSVYGALGISQGIAVFGYSMAvsiggiLASRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFM 987
Cdd:TIGR00958 210 LSIASSVSAGLRGGSFNYTMA------RINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 988 GSLFNVIGACIVILLATP----IAAIIIPPLGLIYFFVQRFYVASSRQLKrlESVSRSPVYSHfnETLLGVSVIRAF--E 1061
Cdd:TIGR00958 284 RNLVMLLGLLGFMLWLSPrltmVTLINLPLVFLAEKVFGKRYQLLSEELQ--EAVAKANQVAE--EALSGMRTVRSFaaE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1062 EQE--RFIHQSDLKVDENQK---AYYPSIVANRWLAVRLECvgncIVLFAALFAVISRHSLSAGLVGLsVSYSLQVTTYL 1136
Cdd:TIGR00958 360 EGEasRFKEALEETLQLNKRkalAYAGYLWTTSVLGMLIQV----LVLYYGGQLVLTGKVSSGNLVSF-LLYQEQLGEAV 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1137 NWLVRMSSEMETNIVAVERLKEYSETEKEAPwQIQETAPPsswPQVGRVEFRNYCLRY--REDLDfVLRHINVTINGGEK 1214
Cdd:TIGR00958 435 RVLSYVYSGMMQAVGASEKVFEYLDRKPNIP-LTGTLAPL---NLEGLIEFQDVSFSYpnRPDVP-VLKGLTFTLHPGEV 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1215 VGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLD-PFSQYSDEEVWT 1293
Cdd:TIGR00958 510 VALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAyGLTDTPDEEIMA 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1294 SLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTirTQFEDCTV 1373
Cdd:TIGR00958 590 AAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTV 667
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2462549096 1374 LTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRGLFYSM 1416
Cdd:TIGR00958 668 LLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1183-1413 |
3.80e-56 |
|
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: 196.61 E-value: 3.80e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1183 GRVEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRInESAEGEIIIDGINIAKIGLHDLRFKI 1262
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1263 TIIPQDPVLFSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKI 1342
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462549096 1343 LVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRGLF 1413
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
327-562 |
5.54e-56 |
|
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: 196.52 E-value: 5.54e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 327 MSFFFKAIHDLMMFSGPQILKLLIKFVNDTKA-----PDWQGYFYTVLLFVTACLQTLVLHQYFHICFVSGMRIKTAVIG 401
Cdd:cd18597 1 LAGLLKLLADVLQVLSPLLLKYLINFVEDAYLggpppSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 402 AVYRKALVITNSARKSSTVGEIVNLMSVDAQRfMDLA-TYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMVLMVPVN 480
Cdd:cd18597 81 AIYRKSLRLSGKSRHEFPNGKITNLMSTDLSR-IDFAlGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 481 AVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLSAVGTFTWVCTPFLA 560
Cdd:cd18597 160 GFLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLA 239
|
..
gi 2462549096 561 SV 562
Cdd:cd18597 240 SM 241
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
330-563 |
8.67e-56 |
|
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: 195.85 E-value: 8.67e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 330 FFKAIHDLMMFSGPQILKLLIKFVNDTKAPDWQGYFYTVLLFVTACLQTLVLHQY-FHICFVSgMRIKTAVIGAVYRKAL 408
Cdd:cd18598 4 LLKLLADVLGFAGPLLLNKLVEFLEDSSEPLSDGYLYALGLVLSSLLGALLSSHYnFQMNKVS-LKVRAALVTAVYRKAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 409 VITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMVLMVPVNAVMAMKTK 488
Cdd:cd18598 83 RVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAKRIG 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549096 489 TYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLSAVGTFTWVCTPFLASVS 563
Cdd:cd18598 163 ALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKYLDALCVYFWATTPVLISIL 237
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1183-1397 |
1.76e-54 |
|
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: 189.34 E-value: 1.76e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1183 GRVEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLT---LGLFRineSAEGEIIIDGINIAKIGLHDLR 1259
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLkllAGLYK---PTSGSVLLDGTDIRQLDPADLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1260 FKITIIPQDPVLFSGSLRMNLDPFSQY-SDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLR 1338
Cdd:cd03245 78 RNIGYVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549096 1339 KTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEI 1397
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
329-562 |
4.77e-54 |
|
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: 191.55 E-value: 4.77e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 329 FFFKAIHDLMMFSGPQILKLLIKFV-NDTKAPDWQGYFYTVLLFVTACLQTLVLHQYFHICFVSGMRIKTAVIGAVYRKA 407
Cdd:cd18596 3 ALLAVLSSVLSFAPPFFLNRLLRYLeDPGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFEKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 408 LVITNSA-------------------RKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLA 468
Cdd:cd18596 83 LRRRDKSgssksseskkkdkeededeKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSALV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 469 GVAVMVLMVPVNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLSAV 548
Cdd:cd18596 163 GLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLLDLL 242
|
250
....*....|....
gi 2462549096 549 GTFTWVCTPFLASV 562
Cdd:cd18596 243 LSLLWFLIPILVTV 256
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
868-1136 |
6.93e-54 |
|
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: 189.78 E-value: 6.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 868 FLSIFLFMCNHVSALASNYWLSLWTDDPIVNGTQE--HTKVRLSVYGALGISQGIAVFGYSMAVSIGGILASRCLHVDLL 945
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLGRILDVLLPDGDPEtqALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 946 HSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPIAAIIIPPLGLIYFFVQRFY 1025
Cdd:pfam00664 82 KKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1026 VASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLF 1105
Cdd:pfam00664 162 AKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYAL 241
|
250 260 270
....*....|....*....|....*....|...
gi 2462549096 1106 AALFAV--ISRHSLSAGLVGLSVSYSLQVTTYL 1136
Cdd:pfam00664 242 ALWFGAylVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1185-1416 |
2.00e-53 |
|
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: 187.31 E-value: 2.00e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITI 1264
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1265 IPQDPVLFSGSLRMNL---DPfsQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTK 1341
Cdd:cd03252 81 VLQENVLFNRSIRDNIalaDP--GMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549096 1342 ILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRGLFYSM 1416
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
944-1413 |
6.90e-53 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 196.39 E-value: 6.90e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 944 LLHSILRSPMSFFERTPSGNLVNRFskeldTVDSmiPEVIKMFMGSLFNVI--GACIVILLAT--------PIAAIIIPP 1013
Cdd:PRK11176 104 LFGHMMGMPVSFFDKQSTGTLLSRI-----TYDS--EQVASSSSGALITVVreGASIIGLFIMmfyyswqlSLILIVIAP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1014 L--GLIYFFVQRFyvassRQLKRLESVSRSPVYSHFNETLLGVSVIRAF----EEQERF------IHQSDLKVDENQKAY 1081
Cdd:PRK11176 177 IvsIAIRVVSKRF-----RNISKNMQNTMGQVTTSAEQMLKGHKEVLIFggqeVETKRFdkvsnrMRQQGMKMVSASSIS 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1082 YPSI--VANRWLAVrlecvgnciVLFAALFAVIsRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEY 1159
Cdd:PRK11176 252 DPIIqlIASLALAF---------VLYAASFPSV-MDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAI 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1160 --SETEKEAPWQIQETAPpsswpqvGRVEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINE 1237
Cdd:PRK11176 322 ldLEQEKDEGKRVIERAK-------GDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYD 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1238 SAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFS--QYSDEEVWTSLELAHLKDFVSALPDKLDHEC 1315
Cdd:PRK11176 395 IDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARteQYSREQIEEAARMAYAMDFINKMDNGLDTVI 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1316 AEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKG 1395
Cdd:PRK11176 475 GENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDG 554
|
490
....*....|....*...
gi 2462549096 1396 EIQEYGAPSDLLQQRGLF 1413
Cdd:PRK11176 555 EIVERGTHAELLAQNGVY 572
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
307-765 |
3.82e-50 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 188.06 E-value: 3.82e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 307 KEWNPSLFKVLYKTFGPY---FLMSFFFKAIHDLMMFSGPQILKLLIKFVndTKAPDWQG-YFYTVLLFVTACLQTLVLH 382
Cdd:COG1132 2 SKSPRKLLRRLLRYLRPYrglLILALLLLLLSALLELLLPLLLGRIIDAL--LAGGDLSAlLLLLLLLLGLALLRALLSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 383 QYFHICFVSGMRIKTAVIGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMD-LATYINMIWSAPLQVILALYLLWLN 461
Cdd:COG1132 80 LQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQfLAHGLPQLVRSVVTLIGALVVLFVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 462 LGPSVLAGVAVMVLMVPVNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYA---WELA-FKDKVLAIRQEELK 537
Cdd:COG1132 160 DWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGreeRELErFREANEELRRANLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 538 VLKKS-------------------------------------AYLSAVGTFTWVCTPFL--------ASVSLKRLRIFLS 572
Cdd:COG1132 240 AARLSalffplmellgnlglalvllvggllvlsgsltvgdlvAFILYLLRLFGPLRQLAnvlnqlqrALASAERIFELLD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 573 HEELEPDSIERRPVKDGGGtnSITVRNATFTWArSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGH 652
Cdd:COG1132 320 EPPEIPDPPGAVPLPPVRG--EIEFENVSFSYP-GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 653 VAI-------------------------------------------------------------------------KGVN 659
Cdd:COG1132 397 ILIdgvdirdltleslrrqigvvpqdtflfsgtirenirygrpdatdeeveeaakaaqahefiealpdgydtvvgeRGVN 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKIS 739
Cdd:COG1132 477 LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEAL---ERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIV 553
|
570 580
....*....|....*....|....*.
gi 2462549096 740 EMGSYQELLARDGAFAEFLRTYASTE 765
Cdd:COG1132 554 EQGTHEELLARGGLYARLYRLQFGEE 579
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
948-1423 |
7.77e-50 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 187.48 E-value: 7.77e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 948 ILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEvikmFMGSLFNVIGAcIVILLATPIA-----AIIIPPLGLIYFFVQ 1022
Cdd:PRK13657 99 IIQLPLAWHSQRGSGRALHTLLRGTDALFGLWLE----FMREHLATLVA-LVVLLPLALFmnwrlSLVLVVLGIVYTLIT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1023 RFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAF---EEQERFIHQSdlkVDENQKAYYPsiVANRW-LAVRLECV 1098
Cdd:PRK13657 174 TLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYnriEAETQALRDI---ADNLLAAQMP--VLSWWaLASVLNRA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1099 GNCIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPwQIQETAPPSS 1178
Cdd:PRK13657 249 ASTITMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQVFMAAPKLEEFFEVEDAVP-DVRDPPGAID 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1179 WPQV-GRVEFRNYCLRYR------EDLDFvlrhinvTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIA 1251
Cdd:PRK13657 328 LGRVkGAVEFDDVSFSYDnsrqgvEDVSF-------EAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIR 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1252 KIGLHDLRFKITIIPQDPVLFSGSLRMNL-----DPfsqySDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQ 1326
Cdd:PRK13657 401 TVTRASLRRNIAVVFQDAGLFNRSIEDNIrvgrpDA----TDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGE 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1327 RQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDL 1406
Cdd:PRK13657 477 RQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDEL 556
|
490
....*....|....*..
gi 2462549096 1407 LQQRGLFYSMAKDAGLV 1423
Cdd:PRK13657 557 VARGGRFAALLRAQGML 573
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
330-581 |
8.68e-50 |
|
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: 179.35 E-value: 8.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 330 FFKAIHDLMMFSGPQILKLLIKFVNDTKAPDWQ------------------GYFYTVLLFVTACLQTLVLHQYFHICFVS 391
Cdd:cd18591 4 ILKLLGDLLGFVGPLCISGIVDYVEENTYSSSNstdklsvsyvtveeffsnGYVLAVILFLALLLQATFSQASYHIVIRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 392 GMRIKTAVIGAVYRKALVIT--NSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAG 469
Cdd:cd18591 84 GIRLKTALQAMIYEKALRLSswNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSALIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 470 VAVMVLMVPVNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLSAVG 549
Cdd:cd18591 164 AALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYWSLM 243
|
250 260 270
....*....|....*....|....*....|..
gi 2462549096 550 TFTWVCTPFLASVSLKRLRIFLSHEELEPDSI 581
Cdd:cd18591 244 TFLTQASPILVTLVTFGLYPYLEGEPLTAAKA 275
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
945-1416 |
5.98e-49 |
|
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: 187.25 E-value: 5.98e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 945 LHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMG-SLFNVIGACIV---------ILLATPIAAIIIppl 1014
Cdd:TIGR01193 236 IKHLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDmWILVIVGLFLVrqnmllfllSLLSIPVYAVII--- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1015 gliYFFVQRFYVASSRQLKrlesvSRSPVYSHFNETLLGVSVIRAF-EEQERFIHQSDLKVDENQKA--YYPSIVANRWL 1091
Cdd:TIGR01193 313 ---ILFKRTFNKLNHDAMQ-----ANAVLNSSIIEDLNGIETIKSLtSEAERYSKIDSEFGDYLNKSfkYQKADQGQQAI 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1092 AVRLECVGNCIVLFAALFAVIsRHSLSAGLVglsVSYSLQVTTYLNWL---VRMSSEMETNIVAVERLKE--YSETEKEA 1166
Cdd:TIGR01193 385 KAVTKLILNVVILWTGAYLVM-RGKLTLGQL---ITFNALLSYFLTPLeniINLQPKLQAARVANNRLNEvyLVDSEFIN 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1167 PWQIQETAPPSSWPQVGRVEFR-NYClryredlDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII 1245
Cdd:TIGR01193 461 KKKRTELNNLNGDIVINDVSYSyGYG-------SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILL 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1246 DGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQ--YSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLS 1323
Cdd:TIGR01193 534 NGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKenVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSIS 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1324 VGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIrTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAP 1403
Cdd:TIGR01193 614 GGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNL-LNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSH 692
|
490
....*....|...
gi 2462549096 1404 SDLLQQRGLFYSM 1416
Cdd:TIGR01193 693 DELLDRNGFYASL 705
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
869-1380 |
1.68e-47 |
|
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: 179.09 E-value: 1.68e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 869 LSIFLFMCNHVSALA----SNYWLS-LWTDDPIVNGTQEHTKVRlsvygALGISQgiAVFGY-SMAVSIGGILASRC-LH 941
Cdd:TIGR02868 17 LAVLLGALALGSAVAllgvSAWLISrAAEMPPVLYLSVAAVAVR-----AFGIGR--AVFRYlERLVGHDAALRSLGaLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 942 VDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIkmfmgslFNVIGACIVILLATPIAAIIIPPLGLI---- 1017
Cdd:TIGR02868 90 VRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVI-------VPAGVALVVGAAAVAAIAVLSVPAALIlaag 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1018 ----YFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRW--- 1090
Cdd:TIGR02868 163 lllaGFVAPLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALgaa 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1091 ---LAVRLECVGNcivLFAALFAVISrHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERLKEYSETEKEAP 1167
Cdd:TIGR02868 243 ltlLAAGLAVLGA---LWAGGPAVAD-GRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAGPVA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1168 WQIQETAPPSSwPQVGRVEFRNYCLRYrEDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG 1247
Cdd:TIGR02868 319 EGSAPAAGAVG-LGKPTLELRDLSAGY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1248 INIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL---DPfsQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSV 1324
Cdd:TIGR02868 397 VPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLrlaRP--DATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSG 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462549096 1325 GQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRL 1380
Cdd:TIGR02868 475 GERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
343-564 |
2.22e-47 |
|
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent.
Pssm-ID: 350038 [Multi-domain] Cd Length: 291 Bit Score: 171.66 E-value: 2.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 343 PQILKLLIK-FVNDTKAPDWQGYFYTVLLFVTACLQTLVLHQYFHICFVSGMRIKTAVIGAVYRKALVITNSARKSSTVG 421
Cdd:cd18594 17 PLLLGRLVAyFVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYKKTLKLSSSALSKITTG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 422 EIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMVLMVPVNAVMAMKTKTYQVAHMKSKDNR 501
Cdd:cd18594 97 HIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGKLFAKYRRKTAGLTDER 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549096 502 IKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLSAVG-TFTWVCTPFLASVSL 564
Cdd:cd18594 177 VKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNmAFFFFSPTLVSFATF 240
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
949-1418 |
5.47e-45 |
|
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: 174.76 E-value: 5.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 949 LRSPMSFFERTPSGNLVNRFSKeLDTVDSMIPEV-IKMFMGSLFNVIG-----------ACIVILLATPIAAIIippLGL 1016
Cdd:TIGR03797 220 LRLPVSFFRQYSTGDLASRAMG-ISQIRRILSGStLTTLLSGIFALLNlglmfyyswklALVAVALALVAIAVT---LVL 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1017 IYFFVQRfyvasSRQLKRLESVSRSPVYSHFNetllGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLe 1096
Cdd:TIGR03797 296 GLLQVRK-----ERRLLELSGKISGLTVQLIN----GISKLRVAGAENRAFARWAKLFSRQRKLELSAQRIENLLTVFN- 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1097 cVGNCIVLFAALFAVISRHSLSAGL-VGLSVSYSLQVTTYLNWLVRMSSEMeTNIVAV----ERLKEYSETEKEAPwqiQ 1171
Cdd:TIGR03797 366 -AVLPVLTSAALFAAAISLLGGAGLsLGSFLAFNTAFGSFSGAVTQLSNTL-ISILAViplwERAKPILEALPEVD---E 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1172 ETAPPSswPQVGRVEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSL---TLGlFRINESaeGEIIIDGI 1248
Cdd:TIGR03797 441 AKTDPG--KLSGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLlrlLLG-FETPES--GSVFYDGQ 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1249 NIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQ 1328
Cdd:TIGR03797 516 DLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQ 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1329 LVCLARALLRKTKILVLDEATAAVDLETDDLI-QSTIRTQfedCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLL 1407
Cdd:TIGR03797 596 RLLIARALVRKPRILLFDEATSALDNRTQAIVsESLERLK---VTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELM 672
|
490
....*....|.
gi 2462549096 1408 QQRGLFYSMAK 1418
Cdd:TIGR03797 673 AREGLFAQLAR 683
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
354-548 |
1.00e-44 |
|
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: 163.93 E-value: 1.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 354 NDTKAPDWQGYFYTVLLFVTACLQTLVLHQYFHICFVSGMRIKTAVIGAVYRKALVITNSARKSSTVGEIVNLMSVDAQR 433
Cdd:cd18593 30 NGSSISLTEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLIYRKALRLSQAALGKTTVGQIVNLLSNDVNR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 434 FMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMVLMVPVNAVMAmktktYQVAHMKSK-----DNRIKLMNEI 508
Cdd:cd18593 110 FDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFG-----KLFSKLRRKtaartDKRIRIMNEI 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2462549096 509 LNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLSAV 548
Cdd:cd18593 185 INGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRAL 224
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1205-1416 |
5.67e-44 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 170.03 E-value: 5.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1205 INVTINGGEKVGIVGRTGAGKSSLT---LGLFrineSAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL- 1280
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLnalLGFL----PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVl 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1281 --DPfsQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDD 1358
Cdd:PRK11174 445 lgNP--DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQ 522
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549096 1359 LIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRGLFYSM 1416
Cdd:PRK11174 523 LVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1183-1397 |
7.15e-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: 159.17 E-value: 7.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1183 GRVEFRNYCLRYREDLD-FVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFK 1261
Cdd:cd03248 10 GIVKFQNVTFAYPTRPDtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1262 ITIIPQDPVLFSGSLRMNLD-PFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKT 1340
Cdd:cd03248 90 VSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549096 1341 KILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEI 1397
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
920-1392 |
1.21e-42 |
|
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: 164.77 E-value: 1.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 920 IAVFGYSMAVSIGGILASRC-------LHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDS----MIPEVIKMFMG 988
Cdd:TIGR02857 52 LVLLLRALLGWLQERAAARAaaavksqLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGyfarYLPQLVLAVIV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 989 SLfnVIGAciVILLATPIAAIII---PPLgLIYFFVQRFYVASSRQLKRLESVSRspVYSHFNETLLGVSVIRAF----E 1061
Cdd:TIGR02857 132 PL--AILA--AVFPQDWISGLILlltAPL-IPIFMILIGWAAQAAARKQWAALSR--LSGHFLDRLRGLPTLKLFgrakA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1062 EQERFIHQSD---------LKVdenqkAYYPS------------IVAnRWLAVRLecVGNCIVLFAALFAVISRHSLSAG 1120
Cdd:TIGR02857 205 QAAAIRRSSEeyrertmrvLRI-----AFLSSavlelfatlsvaLVA-VYIGFRL--LAGDLDLATGLFVLLLAPEFYLP 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1121 LVGLSVSY--SLQVTTylnwlvrmSSEMETNIVAVERLKEYSETEKEApwqiqetAPPSSwpqvgrVEFRNYCLRYrEDL 1198
Cdd:TIGR02857 277 LRQLGAQYhaRADGVA--------AAEALFAVLDAAPRPLAGKAPVTA-------APASS------LEFSGVSVAY-PGR 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1199 DFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRM 1278
Cdd:TIGR02857 335 RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAE 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1279 NL---DPFSqySDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1355
Cdd:TIGR02857 415 NIrlaRPDA--SDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAE 492
|
490 500 510
....*....|....*....|....*....|....*..
gi 2462549096 1356 TDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVL 1392
Cdd:TIGR02857 493 TEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
367-759 |
7.29e-42 |
|
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: 165.39 E-value: 7.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 367 TVLLFVTACLQTL--VLHQYF--HIcfvsGMRIKTAVIGAVYRKALVITNSARKSSTVGEIVNlmsvdaqRFMDLATYIN 442
Cdd:COG2274 199 AIGLLLALLFEGLlrLLRSYLllRL----GQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLAS-------RFRDVESIRE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 443 MIWSAPLQVILAlyllwlnlGPSVLAGVAVM-----------VLMVPVNAVMA------MKTKTYQVAHMKSKDNRikLM 505
Cdd:COG2274 268 FLTGSLLTALLD--------LLFVLIFLIVLffyspplalvvLLLIPLYVLLGllfqprLRRLSREESEASAKRQS--LL 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 506 NEILNGIKVLKLYA--------WELAFKDKVLAirqeELKVLKKSAYLSAVGTF---------TWVC------------- 555
Cdd:COG2274 338 VETLRGIETIKALGaesrfrrrWENLLAKYLNA----RFKLRRLSNLLSTLSGLlqqlatvalLWLGaylvidgqltlgq 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 556 ------------TPFL-----------ASVSLKRLRIFLSHEeLEPDSiERRPVKDGGGTNSITVRNATFTWARSDPPTL 612
Cdd:COG2274 414 liafnilsgrflAPVAqligllqrfqdAKIALERLDDILDLP-PEREE-GRSKLSLPRLKGDIELENVSFRYPGDSPPVL 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 613 NGITFSIPEGALVAVVGQVGCGKSSLLSAL-----------------LAEMDKVE-----GHV----------------- 653
Cdd:COG2274 492 DNISLTIKPGERVAIVGRSGSGKSTLLKLLlglyeptsgrilidgidLRQIDPASlrrqiGVVlqdvflfsgtirenitl 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 654 ------------AIK----------------------GVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIF 699
Cdd:COG2274 572 gdpdatdeeiieAARlaglhdfiealpmgydtvvgegGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIIL 651
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 700 ENVigpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAEFLR 759
Cdd:COG2274 652 ENL---RRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
327-573 |
1.75e-40 |
|
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: 151.56 E-value: 1.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 327 MSFFFKAIHDLMMFSGPQIL-KLLIKFVNDTKAPDWQGYFYTVLLFVTACLQTLVLHQYFHICFVSGMRIKTAVIGAVYR 405
Cdd:cd18592 1 FSILLLLISLIFGFIGPTILiRKLLEYLEDSDSSVWYGILLVLGLFLTELLRSLFFSLTWAISYRTGIRLRGAVLGLLYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 406 KALVITNSARKSstVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSVLAGVAVMVLMVPVNAVMAM 485
Cdd:cd18592 81 KILRLRSLGDKS--VGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 486 KTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKVLKKSAYLSAVGTFTWVCTPFLASVSLk 565
Cdd:cd18592 159 LTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVT- 237
|
....*...
gi 2462549096 566 rlriFLSH 573
Cdd:cd18592 238 ----FLAH 241
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1150-1416 |
2.91e-40 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 158.45 E-value: 2.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1150 IVAVERLKEYSETEKEAPWQIQETAPPSSwpqvGRVEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLT 1229
Cdd:PRK11160 308 IASARRINEITEQKPEVTFPTTSTAAADQ----VSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1230 LGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL---DPfsQYSDEEVWTSLELAHLKDFVSA 1306
Cdd:PRK11160 384 QLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGLEKLLED 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1307 lPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTI--M 1384
Cdd:PRK11160 462 -DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLeqF 540
|
250 260 270
....*....|....*....|....*....|..
gi 2462549096 1385 DytRVIVLDKGEIQEYGAPSDLLQQRGLFYSM 1416
Cdd:PRK11160 541 D--RICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
595-737 |
1.32e-39 |
|
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: 144.83 E-value: 1.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN--------------- 659
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDlrdldleslrkniay 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 ----------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRILVTHSMSY 723
Cdd:cd03228 81 vpqdpflfsgtireniLSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEAL---RALAKGKTVIVIAHRLST 157
|
170
....*....|....
gi 2462549096 724 LPQVDVIIVMSGGK 737
Cdd:cd03228 158 IRDADRIIVLDDGR 171
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1185-1410 |
3.98e-39 |
|
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: 145.55 E-value: 3.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDlDFVLRHINVTINGGEKVGIVGRTGAGKSSLTL---GLFRINEsaeGEIIIDGINIAKIGLHDLRFK 1261
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRllnGLLKPTS---GEVLVDGKDITKKNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1262 ITIIPQDPV--LFSGSLR-------MNLdpfsQYSDEE----VWTSLELAHLKDFvsalpdkLDHECAEggenLSVGQRQ 1328
Cdd:COG1122 77 VGLVFQNPDdqLFAPTVEedvafgpENL----GLPREEirerVEEALELVGLEHL-------ADRPPHE----LSGGQKQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1329 LVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRT-QFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDL 1406
Cdd:COG1122 142 RVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAELAdRVIVLDDGRIVADGTPREV 221
|
....
gi 2462549096 1407 LQQR 1410
Cdd:COG1122 222 FSDY 225
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
325-564 |
4.80e-35 |
|
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: 135.46 E-value: 4.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 325 FLMSFFFKAIHDLMMFSGPQILKLLIKFVNDTKAPDWQ-GYFYTVLLFVTACLQTLVLHQYFHICFVSGMRIKTAVIGAV 403
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQaLNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 404 YRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMIWSAPLQVILALYLLWLNLGPSV-LAGVAVMVLMVPVNAV 482
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLtLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 483 MAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFKDKVLAIRQEELKV-LKKSAYLSAVGTFTWVCTPFLAS 561
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAgIKKAVANGLSFGITQFIGYLSYA 240
|
...
gi 2462549096 562 VSL 564
Cdd:pfam00664 241 LAL 243
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1186-1396 |
3.90e-34 |
|
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: 130.66 E-value: 3.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1186 EFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITII 1265
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1266 PQDP------------VLFsgSLRmNLdpfsQYSDEEVWTSLELAhLKDFvsALPDKLDHECAEggenLSVGQRQLVCLA 1333
Cdd:cd03225 81 FQNPddqffgptveeeVAF--GLE-NL----GLPEEEIEERVEEA-LELV--GLEGLRDRSPFT----LSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549096 1334 RALLRKTKILVLDEATAAVDLETDDLIQSTIRT-QFEDCTVLTIAHRLNTIMDY-TRVIVLDKGE 1396
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1185-1401 |
4.14e-33 |
|
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: 128.39 E-value: 4.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDLDFV--LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRF-- 1260
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1261 -KITIIPQDPvlfSGSL--RMN-----LDPF------SQYSDEEVWTSLELAHLKDfVSALPDKLDHEcaeggenLSVGQ 1326
Cdd:cd03257 82 kEIQMVFQDP---MSSLnpRMTigeqiAEPLrihgklSKKEARKEAVLLLLVGVGL-PEEVLNRYPHE-------LSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549096 1327 RQLVCLARALLRKTKILVLDEATAAVDLETDDLIQST---IRTQFeDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYG 1401
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLlkkLQEEL-GLTLLFITHDLGVVAKIAdRVAVMYAGKIVEEG 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1186-1397 |
6.79e-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: 125.79 E-value: 6.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1186 EFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLT---LGLFRineSAEGEIIIDGINIAKIGLHDLRFKI 1262
Cdd:cd03246 2 EVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLArliLGLLR---PTSGRVRLDGADISQWDPNELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1263 TIIPQDPVLFSGSLRMNLdpfsqysdeevwtslelahlkdfvsalpdkldhecaeggenLSVGQRQLVCLARALLRKTKI 1342
Cdd:cd03246 79 GYLPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462549096 1343 LVLDEATAAVDLETDDLIQSTI-RTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEI 1397
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIaALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1186-1396 |
1.33e-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: 124.28 E-value: 1.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1186 EFRNYCLRYREDldFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITII 1265
Cdd:cd00267 1 EIENLSFRYGGR--TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1266 PQdpvlfsgslrmnldpfsqysdeevwtslelahlkdfvsalpdkldhecaeggenLSVGQRQLVCLARALLRKTKILVL 1345
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462549096 1346 DEATAAVDLETDDLIQSTIRTQFED-CTVLTIAHRLNTIMDYT-RVIVLDKGE 1396
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAAdRVIVLKDGK 157
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
563-759 |
1.45e-32 |
|
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: 134.89 E-value: 1.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 563 SLKRLRIFLSHEELEPDSIERRPVKDGGgtnSITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL 642
Cdd:COG4987 305 AARRLNELLDAPPAVTEPAEPAPAPGGP---SLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 643 LAEMDKVEGHVAIKGV---------------------------------------------------------------- 658
Cdd:COG4987 382 LRFLDPQSGSITLGGVdlrdldeddlrrriavvpqrphlfdttlrenlrlarpdatdeelwaalervglgdwlaalpdgl 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 659 ---------NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPkgmLKNKTRILVTHSMSYLPQVDV 729
Cdd:COG4987 462 dtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA---LAGRTVLLITHRLAGLERMDR 538
|
250 260 270
....*....|....*....|....*....|
gi 2462549096 730 IIVMSGGKISEMGSYQELLARDGAFAEFLR 759
Cdd:COG4987 539 ILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1184-1407 |
3.37e-32 |
|
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: 126.70 E-value: 3.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1184 RVEFRNYCLRYREDldFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKIT 1263
Cdd:COG1120 1 MLEAENLSVGYGGR--PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1264 IIPQDPVL-FSGSLR----M----NLDPFSQYSDEE---VWTSLELAHLKDFVsalpdklDHECAEggenLSVGQRQLVC 1331
Cdd:COG1120 79 YVPQEPPApFGLTVRelvaLgrypHLGLFGRPSAEDreaVEEALERTGLEHLA-------DRPVDE----LSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1332 LARALLRKTKILVLDEATAAVDL----ETDDLIQSTIRTQfeDCTVLTIAHRLNTIMDY-TRVIVLDKGEIQEYGAPSDL 1406
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARER--GRTVVMVLHDLNLAARYaDRLVLLKDGRIVAQGPPEEV 225
|
.
gi 2462549096 1407 L 1407
Cdd:COG1120 226 L 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1185-1409 |
4.02e-32 |
|
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: 132.72 E-value: 4.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTL---GLFRINESAEGEIIIDGINIAKIGLHDLRFK 1261
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALalmGLLPHGGRISGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1262 ITIIPQDP------------VLFsgSLRMNLDPFSQySDEEVWTSLELAHLKDFVSALPdkldHEcaeggenLSVGQRQL 1329
Cdd:COG1123 85 IGMVFQDPmtqlnpvtvgdqIAE--ALENLGLSRAE-ARARVLELLEAVGLERRLDRYP----HQ-------LSGGQRQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1330 VCLARALLRKTKILVLDEATAAVDLETDDLIQSTIR--TQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDL 1406
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVAEIAdRVVVMDDGRIVEDGPPEEI 230
|
...
gi 2462549096 1407 LQQ 1409
Cdd:COG1123 231 LAA 233
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1185-1401 |
4.23e-32 |
|
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: 123.58 E-value: 4.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLtLGLFRINESA-EGEIIIDGINIAKIGlHDLRFKIT 1263
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTL-LQLLTGDLKPqQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1264 IIPQDPVLFSGSLRMNLdpfsqysdeevwtslelahlkdfvsalpdkldhecaegGENLSVGQRQLVCLARALLRKTKIL 1343
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549096 1344 VLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYG 1401
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
595-756 |
7.51e-32 |
|
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: 125.04 E-value: 7.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTWarsDP--PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAI----------------- 655
Cdd:cd03253 1 IEFENVTFAY---DPgrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIdgqdirevtldslrrai 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 656 --------------------------------------------------------KGVNLSGGQKQRVSLARAVYSNAD 679
Cdd:cd03253 78 gvvpqdtvlfndtigynirygrpdatdeevieaakaaqihdkimrfpdgydtivgeRGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549096 680 IYLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAE 756
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAAL---RDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAE 231
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
570-752 |
8.23e-32 |
|
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: 132.57 E-value: 8.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 570 FLSHEELEPDSIERRPVKDGGgtNSITVRNATFTWArSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKV 649
Cdd:COG4988 314 LLDAPEPAAPAGTAPLPAAGP--PSIELEDVSFSYP-GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPY 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 650 EGHVAI-------------------------------------------------------------------------K 656
Cdd:COG4988 391 SGSILIngvdlsdldpaswrrqiawvpqnpylfagtirenlrlgrpdasdeeleaaleaagldefvaalpdgldtplgeG 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 657 GVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGG 736
Cdd:COG4988 471 GRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQAL---RRLAKGRTVILITHRLALLAQADRILVLDDG 547
|
250
....*....|....*.
gi 2462549096 737 KISEMGSYQELLARDG 752
Cdd:COG4988 548 RIVEQGTHEELLAKNG 563
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
896-1416 |
1.94e-31 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 131.37 E-value: 1.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 896 IVNGTQEHTKVRLSVYGALGISQGIAV-------------FG--YSMAVSiggilasrcLHVDLLHSILRSPMSFFERTP 960
Cdd:PRK10789 21 IVDGVTEQHMTTGQILMWIGTMVLIAVvvyllryvwrvllFGasYQLAVE---------LREDFYRQLSRQHPEFYLRHR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 961 SGNLVNRFSKELDTVDSMIPEVIKMFMGSLfnVIGACIVILLAT--------------PIAAIIIPPLGLIYFfvQRFYV 1026
Cdd:PRK10789 92 TGDLMARATNDVDRVVFAAGEGVLTLVDSL--VMGCAVLIVMSTqiswqltllallpmPVMAIMIKRYGDQLH--ERFKL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1027 ASSrqlkrlesvSRSPVYSHFNETLLGVSVIRAFEEQErfiHQS----DLKVDENQKAYYPSIVANRWLAVRLECVGnci 1102
Cdd:PRK10789 168 AQA---------AFSSLNDRTQESLTSIRMIKAFGLED---RQSalfaADAEDTGKKNMRVARIDARFDPTIYIAIG--- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1103 vlFAALFAV------ISRHSLSAGlvglsvsyslQVTTYLNWLVRMSSEMET-----NIV-----AVERLKEYSEtekEA 1166
Cdd:PRK10789 233 --MANLLAIgggswmVVNGSLTLG----------QLTSFVMYLGLMIWPMLAlawmfNIVergsaAYSRIRAMLA---EA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1167 PWQIQETAPPSSWPQVGRVEFRNYClrYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIID 1246
Cdd:PRK10789 298 PVVKDGSEPVPEGRGELDVNIRQFT--YPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFH 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1247 GINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL---DPfsQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLS 1323
Cdd:PRK10789 376 DIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIalgRP--DATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLS 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1324 VGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAP 1403
Cdd:PRK10789 454 GGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNH 533
|
570
....*....|...
gi 2462549096 1404 SDLLQQRGLFYSM 1416
Cdd:PRK10789 534 DQLAQQSGWYRDM 546
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1202-1350 |
6.51e-31 |
|
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: 119.29 E-value: 6.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1202 LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSG-SLRMNL 1280
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549096 1281 -------DPFSQYSDEEVWTSLELAhlkdfvsALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATA 1350
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEKL-------GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
595-736 |
1.03e-30 |
|
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: 121.28 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTWArSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV--------------------- 653
Cdd:cd03290 1 VQVTNGYFSWG-SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsrnry 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 654 -------------------------------------------------------AIKGVNLSGGQKQRVSLARAVYSNA 678
Cdd:cd03290 80 svayaaqkpwllnatveenitfgspfnkqrykavtdacslqpdidllpfgdqteiGERGINLSGGQRQRICVARALYQNT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462549096 679 DIYLFDDPLSAVDAHVGKHIFEnvigpKGMLK-----NKTRILVTHSMSYLPQVDVIIVMSGG 736
Cdd:cd03290 160 NIVFLDDPFSALDIHLSDHLMQ-----EGILKflqddKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1185-1409 |
1.27e-30 |
|
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: 128.10 E-value: 1.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRN----YCLRYREDLDfVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIG---LHD 1257
Cdd:COG1123 261 LEVRNlskrYPVRGKGGVR-AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1258 LRFKITIIPQDPvlfSGSL--RMN--------LDPFSQYSDEEVW----TSLELAHL-KDFVSALPdkldHEcaeggenL 1322
Cdd:COG1123 340 LRRRVQMVFQDP---YSSLnpRMTvgdiiaepLRLHGLLSRAERRervaELLERVGLpPDLADRYP----HE-------L 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1323 SVGQRQLVCLARALLRKTKILVLDEATAAVDLetddLIQSTIRTQFED------CTVLTIAHRLNTIMDYT-RVIVLDKG 1395
Cdd:COG1123 406 SGGQRQRVAIARALALEPKLLILDEPTSALDV----SVQAQILNLLRDlqrelgLTYLFISHDLAVVRYIAdRVAVMYDG 481
|
250
....*....|....
gi 2462549096 1396 EIQEYGAPSDLLQQ 1409
Cdd:COG1123 482 RIVEDGPTEEVFAN 495
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1201-1409 |
2.50e-30 |
|
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: 127.85 E-value: 2.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL 1280
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1281 DPFSQYSD-EEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDD- 1358
Cdd:TIGR01842 413 ARFGENADpEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQa 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462549096 1359 LIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQ 1409
Cdd:TIGR01842 493 LANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
647-1420 |
7.28e-30 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 129.38 E-value: 7.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 647 DKVEGHVAIKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDaHVGKHIFENVIGPKGMLKNKTRILVTHSMSYLPQ 726
Cdd:PTZ00265 567 DKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINNLKGNENRITIIIAHRLSTIRY 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 727 VDVIIVMSGgkiSEMGSYQELlarDGAFAEFLRTYASTEQEQDAEENGVTGVS---------------GPGKEAKQMENG 791
Cdd:PTZ00265 646 ANTIFVLSN---RERGSTVDV---DIIGEDPTKDNKENNNKNNKDDNNNNNNNnnnkinnagsyiieqGTHDALMKNKNG 719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 792 MLVT----------DSAGKQLQRQLSSSSSYSGDISRHH-------NSTAELQKAEAKKEETWKLMEADKAQTGQvKLS- 853
Cdd:PTZ00265 720 IYYTminnqkvsskKSSNNDNDKDSDMKSSAYKDSERGYdpdemngNSKHENESASNKKSCKMSDENASENNAGG-KLPf 798
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 854 -----------------VY---WDYMKAIGlfISFLSIFLF--MCNHVSALASNYWLSLWTDDPIVNGTQEHTKVRLSVY 911
Cdd:PTZ00265 799 lrnlfkrkpkapnnlriVYreiFSYKKDVT--IIALSILVAggLYPVFALLYAKYVSTLFDFANLEANSNKYSLYILVIA 876
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 912 GALGISQGIAVFgYSMAVsigGILASRCLHVDLLHSILRSPMSFFER---TPsGNLVNRFSKELDTVDSMIPEVIKMFMG 988
Cdd:PTZ00265 877 IAMFISETLKNY-YNNVI---GEKVEKTMKRRLFENILYQEISFFDQdkhAP-GLLSAHINRDVHLLKTGLVNNIVIFTH 951
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 989 SLFNVIGACIVILLATPIAAIIippLGLIYFFVQRFYVASSR-------QLKRLESVSRSPVYSH-----------FNET 1050
Cdd:PTZ00265 952 FIVLFLVSMVMSFYFCPIVAAV---LTGTYFIFMRVFAIRARltankdvEKKEINQPGTVFAYNSddeifkdpsflIQEA 1028
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1051 LLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLFAALFA--VISRHSLSAGLVGLSVSY 1128
Cdd:PTZ00265 1029 FYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGsfLIRRGTILVDDFMKSLFT 1108
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1129 SLQVTTYLNWLVRMSSEMETNIVAVERL------KEYSETEKEAPWQIQETAPPSswpqvGRVEFRNYCLRY--REDLDf 1200
Cdd:PTZ00265 1109 FLFTGSYAGKLMSLKGDSENAKLSFEKYypliirKSNIDVRDNGGIRIKNKNDIK-----GKIEIMDVNFRYisRPNVP- 1182
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSL--------------------------------------TLGLFRINESA--- 1239
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVmsllmrfydlkndhhivfknehtndmtneqdyqgdeeqNVGMKNVNEFSltk 1262
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1240 -------------EGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDpFSQ--YSDEEVWTSLELAHLKDFV 1304
Cdd:PTZ00265 1263 eggsgedstvfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK-FGKedATREDVKRACKFAAIDEFI 1341
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1305 SALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIR--TQFEDCTVLTIAHRLNT 1382
Cdd:PTZ00265 1342 ESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdiKDKADKTIITIAHRIAS 1421
|
890 900 910 920
....*....|....*....|....*....|....*....|....
gi 2462549096 1383 IMDYTRVIVLDKGE-----IQEYGAPSDLLQ-QRGLFYSMAKDA 1420
Cdd:PTZ00265 1422 IKRSDKIVVFNNPDrtgsfVQAHGTHEELLSvQDGVYKKYVKLA 1465
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1180-1396 |
4.70e-29 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 127.07 E-value: 4.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1180 PQVGRVEFRNYCLRY--REDLDfVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII-DGINIAKIGLH 1256
Cdd:PTZ00265 378 KDIKKIQFKNVRFHYdtRKDVE-IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLK 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1257 DLRFKITIIPQDPVLFSGSLRMN----------LDPFSQYSDEE---------------------------VWTSLELAH 1299
Cdd:PTZ00265 457 WWRSKIGVVSQDPLLFSNSIKNNikyslyslkdLEALSNYYNEDgndsqenknkrnscrakcagdlndmsnTTDSNELIE 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1300 LK---------------------DFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDD 1358
Cdd:PTZ00265 537 MRknyqtikdsevvdvskkvlihDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2462549096 1359 LIQSTIRT--QFEDCTVLTIAHRLNTIMDYTRVIVLDKGE 1396
Cdd:PTZ00265 617 LVQKTINNlkGNENRITIIIAHRLSTIRYANTIFVLSNRE 656
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
596-737 |
6.98e-29 |
|
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: 113.88 E-value: 6.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 596 TVRNATFTWArsDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN---------------- 659
Cdd:cd00267 1 EIENLSFRYG--GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDiaklpleelrrrigyv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 --LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFENVIgpKGML-KNKTRILVTHSMSYLPQV-DVIIVMSG 735
Cdd:cd00267 79 pqLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA-SRERLLELL--RELAeEGRTVIIVTHDPELAELAaDRVIVLKD 155
|
..
gi 2462549096 736 GK 737
Cdd:cd00267 156 GK 157
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1186-1401 |
1.40e-28 |
|
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: 113.68 E-value: 1.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1186 EFRNYCLRYREDldFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITII 1265
Cdd:cd03214 1 EVENLSVGYGGR--TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1266 PQdpVLfsgslrmnldpfsqysdeevwTSLELAHLKD-FVSalpdkldhecaeggeNLSVGQRQLVCLARALLRKTKILV 1344
Cdd:cd03214 79 PQ--AL---------------------ELLGLAHLADrPFN---------------ELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462549096 1345 LDEATAAVDL----ETDDLIQSTIRTqfEDCTVLTIAHRLNTIMDY-TRVIVLDKGEIQEYG 1401
Cdd:cd03214 121 LDEPTSHLDIahqiELLELLRRLARE--RGKTVVMVLHDLNLAARYaDRVILLKDGRIVAQG 180
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1185-1396 |
1.46e-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: 1.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRY---REDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLfrINESA--EGEIIIDGiniakiglhdlr 1259
Cdd:cd03250 1 ISVEDASFTWdsgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL--LGELEklSGSVSVPG------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1260 fKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRK 1339
Cdd:cd03250 67 -SIAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462549096 1340 TKILVLDEATAAVDLETDDLIqstirtqFEDC---------TVLTIAHRLNTIMDYTRVIVLDKGE 1396
Cdd:cd03250 146 ADIYLLDDPLSAVDAHVGRHI-------FENCilglllnnkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1185-1408 |
2.14e-28 |
|
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: 115.29 E-value: 2.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDLD--FVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKI 1262
Cdd:COG1124 2 LEVRNLSVSYGQGGRrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1263 TIIPQDPvlfSGSL--RMNLD-----PFS----QYSDEEVWTSLELAHLKDfvsALPDKLDHEcaeggenLSVGQRQLVC 1331
Cdd:COG1124 82 QMVFQDP---YASLhpRHTVDrilaePLRihglPDREERIAELLEQVGLPP---SFLDRYPHQ-------LSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1332 LARALLRKTKILVLDEATAAVDL----ETDDLIQStIRTQfEDCTVLTIAHRLNTImDY--TRVIVLDKGEIQEYGAPSD 1405
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVsvqaEILNLLKD-LREE-RGLTYLFVSHDLAVV-AHlcDRVAVMQNGRIVEELTVAD 225
|
...
gi 2462549096 1406 LLQ 1408
Cdd:COG1124 226 LLA 228
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1185-1412 |
3.04e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 114.80 E-value: 3.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDLdfVLRHINVTINGGEKVGIVGRTGAGKSSL---TLGLFRInesAEGEIIIDGINIAK----IG--- 1254
Cdd:COG1121 7 IELENLTVSYGGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLlkaILGLLPP---TSGTVRLFGKPPRRarrrIGyvp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1255 ---LHDLRFKITIipQDPVLfsgslrMNLDP----FSQYSDEE---VWTSLELAHLKDF----VSALpdkldhecaegge 1320
Cdd:COG1121 82 qraEVDWDFPITV--RDVVL------MGRYGrrglFRRPSRADreaVDEALERVGLEDLadrpIGEL------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1321 nlSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRT-QFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEIq 1398
Cdd:COG1121 141 --SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREYfDRVLLLNRGLV- 217
|
250
....*....|....
gi 2462549096 1399 EYGAPSDLLQQRGL 1412
Cdd:COG1121 218 AHGPPEEVLTPENL 231
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
595-738 |
3.34e-28 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 112.31 E-value: 3.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN--------------- 659
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADisqwdpnelgdhvgy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 ----------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPKgmLKNKTRILVTHSMSY 723
Cdd:cd03246 81 lpqddelfsgsiaeniLSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALK--AAGATRIVIAHRPET 158
|
170
....*....|....*
gi 2462549096 724 LPQVDVIIVMSGGKI 738
Cdd:cd03246 159 LASADRILVLEDGRV 173
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1185-1406 |
2.13e-27 |
|
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: 111.89 E-value: 2.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDldFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINES-----AEGEIIIDGINIAKIGLHD-- 1257
Cdd:cd03260 1 IELRDLNVYYGDK--HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1258 LRFKITIIPQDPVLFSGSLRMNLDpfsqYS------------DEEVWTSLELAHLKDFVSalpDKLDhecaegGENLSVG 1325
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVA----YGlrlhgiklkeelDERVEEALRKAALWDEVK---DRLH------ALGLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1326 QRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNT---IMDYTrvIVLDKGEIQEYGA 1402
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQaarVADRT--AFLLNGRLVEFGP 223
|
....
gi 2462549096 1403 PSDL 1406
Cdd:cd03260 224 TEQI 227
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1201-1409 |
2.26e-27 |
|
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: 118.70 E-value: 2.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSL---TLGLFRineSAEGEIIIDGINIA-----KIGLHdlrfkITIIPQDPVLF 1272
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLarlLVGVWP---PTAGSVRLDGADLSqwdreELGRH-----IGYLPQDVELF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1273 SGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAV 1352
Cdd:COG4618 419 DGTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNL 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1353 DLETDDLIQSTIRTQFED-CTVLTIAHRLNTI--MDytRVIVLDKGEIQEYGAPSDLLQQ 1409
Cdd:COG4618 499 DDEGEAALAAAIRALKARgATVVVITHRPSLLaaVD--KLLVLRDGRVQAFGPRDEVLAR 556
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1131-1395 |
2.91e-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: 2.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1131 QVTTYLNWLVRMSSEMeTNIVA-VERLKEYSETEKEAPwQIQETAPPSSWPQVGRVEFRNYCLRyREDLDFVLRHINVTI 1209
Cdd:COG4178 310 QVQGALSWFVDNYQSL-AEWRAtVDRLAGFEEALEAAD-ALPEAASRIETSEDGALALEDLTLR-TPDGRPLLEDLSLSL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1210 NGGEKVGIVGRTGAGKSSLtlglFR----INESAEGEIIidginiakigLHDLRfKITIIPQDPVLFSGSLRMNL---DP 1282
Cdd:COG4178 387 KPGERLLITGPSGSGKSTL----LRaiagLWPYGSGRIA----------RPAGA-RVLFLPQRPYLPLGTLREALlypAT 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1283 FSQYSDEEVWTSLELAHLKDFVsalpDKLDHEcAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQS 1362
Cdd:COG4178 452 AEAFSDAELREALEAVGLGHLA----ERLDEE-ADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQ 526
|
250 260 270
....*....|....*....|....*....|....
gi 2462549096 1363 TIRTQFEDCTVLTIAHRlNTIMDY-TRVIVLDKG 1395
Cdd:COG4178 527 LLREELPGTTVISVGHR-STLAAFhDRVLELTGD 559
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
934-1156 |
7.02e-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: 113.36 E-value: 7.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 934 ILASRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPIAAIIIPP 1013
Cdd:cd18600 99 ITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIGAITVVSILQPYIFLATVP 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1014 LGLIYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERF---IHQSdlkVDENQKAYYPSIVANRW 1090
Cdd:cd18600 179 VIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFetlFHKA---LNLHTANWFLYLSTLRW 255
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549096 1091 LAVRLECVgncIVLF--AALFAVISRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERL 1156
Cdd:cd18600 256 FQMRIEMI---FVIFftAVTFISIGTTGDGEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSRI 320
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
595-759 |
8.21e-27 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 110.32 E-value: 8.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTW-ARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN-------------- 659
Cdd:cd03249 1 IEFKNVSFRYpSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDirdlnlrwlrsqig 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 -----------------------------------------------------------LSGGQKQRVSLARAVYSNADI 680
Cdd:cd03249 81 lvsqepvlfdgtiaenirygkpdatdeeveeaakkanihdfimslpdgydtlvgergsqLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549096 681 YLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAEFLR 759
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEAL---DRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVK 236
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1200-1411 |
1.01e-26 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 110.33 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1200 FVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRfKITIIPQDPVLFSG-SLRM 1278
Cdd:COG4555 15 PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARR-QIGVLPDERGLYDRlTVRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1279 NLD---PFSQYSDEEVWTSLE-LAHLKDfvsaLPDKLDHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1354
Cdd:COG4555 94 NIRyfaELYGLFDEELKKRIEeLIELLG----LEEFLDRRVGE----LSTGMKKKVALARALVHDPKVLLLDEPTNGLDV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549096 1355 ETDDLIQSTIRTQF-EDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLLQQRG 1411
Cdd:COG4555 166 MARRLLREILRALKkEGKTVLFSSHIMQEVEALCdRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
595-756 |
2.49e-26 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 108.86 E-value: 2.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAI------------------- 655
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdghdvrdytlaslrrqigl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 656 ------------------------------------------------------KGVNLSGGQKQRVSLARAVYSNADIY 681
Cdd:cd03251 81 vsqdvflfndtvaeniaygrpgatreeveeaaraanahefimelpegydtvigeRGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549096 682 LFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAE 756
Cdd:cd03251 161 ILDEATSALDTESERLVQAAL---ERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAK 232
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1186-1395 |
1.63e-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: 1.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1186 EFRNYCLRYREDLdfVLRHINVTINGGEKVGIVGRTGAGKSSLT---LGLFRineSAEGEIIIDGINIAKIglhdlRFKI 1262
Cdd:cd03235 1 EVEDLTVSYGGHP--VLEDVSFEVKPGEFLAIVGPNGAGKSTLLkaiLGLLK---PTSGSIRVFGKPLEKE-----RKRI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1263 TIIPQ----D---PVLFSGSLRMNLDP----FSQYSDEE---VWTSLELAHLKDFVSAlpdKLDHecaeggenLSVGQRQ 1328
Cdd:cd03235 71 GYVPQrrsiDrdfPISVRDVVLMGLYGhkglFRRLSKADkakVDEALERVGLSELADR---QIGE--------LSGGQQQ 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549096 1329 LVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRT-QFEDCTVLTIAHRLNTIMDYT-RVIVLDKG 1395
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYFdRVLLLNRT 208
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1201-1407 |
1.66e-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: 1.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKI---GLHDLRFKITIIPQDPVLFSG--- 1274
Cdd:cd03258 20 ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLsgkELRKARRRIGMIFQHFNLLSSrtv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1275 ----SLRMNLDPFSQ-YSDEEVWTSLELAHLKDFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEAT 1349
Cdd:cd03258 100 fenvALPLEIAGVPKaEIEERVLELLELVGLEDKADAYP-----------AQLSGGQKQRVGIARALANNPKVLLCDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462549096 1350 AAVDLETDDLIQSTIRT--QFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEIQEYGAPSDLL 1407
Cdd:cd03258 169 SALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEEVF 229
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1185-1397 |
2.31e-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: 105.65 E-value: 2.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDLD--FVLRHINVTINGGEKVGIVGRTGAGKSSL--TLGLfrINESAEGEIIIDGINIAKIGLHDL-- 1258
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLlnILGG--LDRPTSGEVRVDGTDISKLSEKELaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1259 --RFKITIIPQD---------------PVLFSGSLRMnldpfsqySDEEVWTSLeLAHLKdfvsaLPDKLDHECAEggen 1321
Cdd:cd03255 79 frRRHIGFVFQSfnllpdltalenvelPLLLAGVPKK--------ERRERAEEL-LERVG-----LGDRLNHYPSE---- 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549096 1322 LSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIR--TQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEI 1397
Cdd:cd03255 141 LSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRelNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1185-1397 |
7.27e-25 |
|
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: 102.86 E-value: 7.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDldFVLRHINVTINGGEKVGIVGRTGAGKSSLT---LGLFRINEsaeGEIIIDGINIAKIGlHDLRFK 1261
Cdd:cd03230 1 IEVRNLSKRYGKK--TALDDISLTVEKGEIYGLLGPNGAGKTTLIkiiLGLLKPDS---GEIKVLGKDIKKEP-EEVKRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1262 ITIIPQDPVLfsgslrmnldpfsqYSDEEVWTSLELahlkdfvsalpdkldhecaeggenlSVGQRQLVCLARALLRKTK 1341
Cdd:cd03230 75 IGYLPEEPSL--------------YENLTVRENLKL-------------------------SGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549096 1342 ILVLDEATAAVDLETDDLIQSTIRT-QFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEI 1397
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1186-1410 |
1.26e-24 |
|
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: 104.19 E-value: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1186 EFRNYCLRYREDLDfVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIG---LHDLRFKI 1262
Cdd:cd03256 2 EVENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1263 TIIPQDP-----------VLfSGSL-RMNLDP--FSQYSDEEVWTSLELahLKDFvsALPDKLDHECAEggenLSVGQRQ 1328
Cdd:cd03256 81 GMIFQQFnlierlsvlenVL-SGRLgRRSTWRslFGLFPKEEKQRALAA--LERV--GLLDKAYQRADQ----LSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1329 LVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIR--TQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSD 1405
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKriNREEGITVIVSLHQVDLAREYAdRIVGLKDGRIVFDGPPAE 231
|
....*
gi 2462549096 1406 LLQQR 1410
Cdd:cd03256 232 LTDEV 236
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1185-1407 |
1.30e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 105.07 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITI 1264
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1265 IPQDP-VLFSGSLRMNLDPFS----QYSDEEVWTS-LELAHlkdfVSALPDKLDHEcaegGENLSVGQRQLVCLARALLR 1338
Cdd:PRK13632 88 IFQNPdNQFIGATVEDDIAFGlenkKVPPKKMKDIiDDLAK----KVGMEDYLDKE----PQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462549096 1339 KTKILVLDEATAAVDLETDDLIQSTIRT--QFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLL 1407
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
594-759 |
1.72e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 109.91 E-value: 1.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 594 SITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN-------------- 659
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPiadyseaalrqais 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 ----------------------------------------------------------LSGGQKQRVSLARAVYSNADIY 681
Cdd:PRK11160 418 vvsqrvhlfsatlrdnlllaapnasdealievlqqvgleklleddkglnawlgeggrqLSGGEQRRLGIARALLHDAPLL 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549096 682 LFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAEFLR 759
Cdd:PRK11160 498 LLDEPTEGLDAETERQILELL---AEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQ 572
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1185-1408 |
2.05e-24 |
|
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: 103.35 E-value: 2.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDldFVLRHINVTINGGEKVGIVGRTGAGKSSLT---LGLFRineSAEGEIIIDGINIAK---IGLHDL 1258
Cdd:cd03261 1 IELRGLTKSFGGR--TVLKGVDLDVRRGEILAIIGPSGSGKSTLLrliVGLLR---PDSGEVLIDGEDISGlseAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1259 RFKITIIPQDPVLFSG-SLRMN----LDPFSQYSDEE----VWTSLELAHLKDFVSALPDkldhecaeggeNLSVGQRQL 1329
Cdd:cd03261 76 RRRMGMLFQSGALFDSlTVFENvafpLREHTRLSEEEireiVLEKLEAVGLRGAEDLYPA-----------ELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1330 VCLARALLRKTKILVLDEATAAVD----LETDDLIQSTIRTQfeDCTVLTIAHRLNTIM---DytRVIVLDKGEIQEYGA 1402
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDpiasGVIDDLIRSLKKEL--GLTSIMVTHDLDTAFaiaD--RIAVLYDGKIVAEGT 220
|
....*.
gi 2462549096 1403 PSDLLQ 1408
Cdd:cd03261 221 PEELRA 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1185-1396 |
9.25e-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: 99.57 E-value: 9.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDldFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLH--DLRFKI 1262
Cdd:cd03229 1 LELKNVSKRYGQK--TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1263 TIIPQDPVLFSgslRMNldpfsqysdeeVWTSLELAhlkdfvsalpdkldhecaeggenLSVGQRQLVCLARALLRKTKI 1342
Cdd:cd03229 79 GMVFQDFALFP---HLT-----------VLENIALG-----------------------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549096 1343 LVLDEATAAVDLETDDLIQSTIRTQFED--CTVLTIAHRLNTIMDYT-RVIVLDKGE 1396
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARLAdRVVVLRDGK 178
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1185-1402 |
1.13e-23 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 100.90 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDLDfVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKI---GLHDLRFK 1261
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1262 ITIIPQDP-----------VLFsgSLR-MNLDPfsQYSDEEVWTSLELAHLKDFVSALPdkldHEcaeggenLSVGQRQL 1329
Cdd:COG2884 81 IGVVFQDFrllpdrtvyenVAL--PLRvTGKSR--KEIRRRVREVLDLVGLSDKAKALP----HE-------LSGGEQQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1330 VCLARALLRKTKILVLDEATAAVDLET-DDLIQstirtQFED-----CTVLtIA-HRLNTIMDY-TRVIVLDKGEIQEYG 1401
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPETsWEIME-----LLEEinrrgTTVL-IAtHDLELVDRMpKRVLELEDGRLVRDE 219
|
.
gi 2462549096 1402 A 1402
Cdd:COG2884 220 A 220
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
610-766 |
3.33e-23 |
|
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: 101.47 E-value: 3.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 610 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV------------------AIK--------------- 656
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIkhsgrisfssqfswimpgTIKeniifgvsydeyryk 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 657 --------------------------GVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPkgMLK 710
Cdd:cd03291 131 svvkacqleeditkfpekdntvlgegGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCK--LMA 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462549096 711 NKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAEFLRTYASTEQ 766
Cdd:cd03291 209 NKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLMGYDTFDQ 264
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
595-742 |
7.28e-23 |
|
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: 97.00 E-value: 7.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN--------------- 659
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPvsdlekalsslisvl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 ------------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIgpkGMLKNKTRILVTHSM 721
Cdd:cd03247 81 nqrpylfdttlrnnlgrrFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIF---EVLKDKTLIWITHHL 157
|
170 180
....*....|....*....|.
gi 2462549096 722 SYLPQVDVIIVMSGGKISEMG 742
Cdd:cd03247 158 TGIEHMDKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1184-1409 |
9.89e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 99.70 E-value: 9.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1184 RVEFRNYclRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLT---LGLFRineSAEGEIIIDGINIAKIGLHDLRF 1260
Cdd:PRK13635 7 RVEHISF--RYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAkllNGLLL---PEAGTITVGGMVLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1261 KITIIPQDP------------VLFSgsLRMNLDPFSQYSdEEVWTSLELAHLKDFvsalpdkLDHECAeggeNLSVGQRQ 1328
Cdd:PRK13635 82 QVGMVFQNPdnqfvgatvqddVAFG--LENIGVPREEMV-ERVDQALRQVGMEDF-------LNREPH----RLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1329 LVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRT--QFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDL 1406
Cdd:PRK13635 148 RVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
...
gi 2462549096 1407 LQQ 1409
Cdd:PRK13635 228 FKS 230
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1192-1410 |
1.88e-22 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 97.52 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1192 LRYREDlDFVLRhINVTINGGEKVGIVGRTGAGKSSLtLGL---FRinESAEGEIIIDGINIAKIGLHDlRfKITIIPQD 1268
Cdd:COG3840 7 LTYRYG-DFPLR-FDLTIAAGERVAILGPSGAGKSTL-LNLiagFL--PPDSGRILWNGQDLTALPPAE-R-PVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1269 PVLFSG-SLRMN----LDPFSQYSDEE---VWTSLELAHLKDFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKT 1340
Cdd:COG3840 80 NNLFPHlTVAQNiglgLRPGLKLTAEQraqVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549096 1341 KILVLDEATAAVD----LETDDLIQSTIRTQfeDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLLQQR 1410
Cdd:COG3840 149 PILLLDEPFSALDpalrQEMLDLVDELCRER--GLTVLMVTHDPEDAARIAdRVLLVADGRIAADGPTAALLDGE 221
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1185-1401 |
2.21e-22 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 96.82 E-value: 2.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDldFVLRHINVTINGGEKVGIVGRTGAGKSSLtL----GLFRInesAEGEIIIDGINIAKIGLHdlRF 1260
Cdd:cd03259 1 LELKGLSKTYGSV--RALDDLSLTVEPGEFLALLGPSGCGKTTL-LrliaGLERP---DSGEILIDGRDVTGVPPE--RR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1261 KITIIPQDPVLF----------SGsLRMNLDPFSQySDEEVWTSLELAHLKDFVSALPDKLdhecaeggenlSVGQRQLV 1330
Cdd:cd03259 73 NIGMVFQDYALFphltvaeniaFG-LKLRGVPKAE-IRARVRELLELVGLEGLLNRYPHEL-----------SGGQQQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549096 1331 CLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFE--DCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYG 1401
Cdd:cd03259 140 ALARALAREPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEEALALAdRIAVMNEGRIVQVG 213
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1202-1412 |
4.43e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 98.20 E-value: 4.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1202 LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIA--KIGLHDLRFKITIIPQDP--VLFS---- 1273
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQYPeyQLFEetie 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1274 -----GSLRMNLdpfsqySDEE----VWTSLELAHLKdfVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILV 1344
Cdd:PRK13637 103 kdiafGPINLGL------SEEEienrVKRAMNIVGLD--YEDYKDKSPFE-------LSGGQKRRVAIAGVVAMEPKILI 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549096 1345 LDEATAAVDLETDDLIQSTIRTQFE--DCTVLTIAHRLNTIMDY-TRVIVLDKGEIQEYGAPS------DLLQQRGL 1412
Cdd:PRK13637 168 LDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKLaDRIIVMNKGKCELQGTPRevfkevETLESIGL 244
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
594-738 |
4.61e-22 |
|
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: 96.12 E-value: 4.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 594 SITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAI------------------ 655
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLdgtdirqldpadlrrnig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 656 -------------------------------------------------------KGVNLSGGQKQRVSLARAVYSNADI 680
Cdd:cd03245 82 yvpqdvtlfygtlrdnitlgapladderilraaelagvtdfvnkhpngldlqigeRGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549096 681 YLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKI 738
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERL---RQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
597-737 |
6.27e-22 |
|
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: 95.61 E-value: 6.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 597 VRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN----------------- 659
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDltklslkelrrkvglvf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 -----------------------------------------------------LSGGQKQRVSLARAVYSNADIYLFDDP 686
Cdd:cd03225 82 qnpddqffgptveeevafglenlglpeeeieerveealelvgleglrdrspftLSGGQKQRVAIAGVLAMDPDILLLDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549096 687 LSAVDAHVGKHIFEnvigpkgMLK-----NKTRILVTHSMSYLPQV-DVIIVMSGGK 737
Cdd:cd03225 162 TAGLDPAGRRELLE-------LLKklkaeGKTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
595-752 |
1.45e-21 |
|
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: 94.98 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTWaRSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALL------------------------------- 643
Cdd:cd03254 3 IEFENVNFSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMrfydpqkgqilidgidirdisrkslrsmigv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 644 ----------------------AEMDKV--------------------EGHVAIKGVNLSGGQKQRVSLARAVYSNADIY 681
Cdd:cd03254 82 vlqdtflfsgtimenirlgrpnATDEEVieaakeagahdfimklpngyDTVLGENGGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462549096 682 LFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDG 752
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEAL---EKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
595-755 |
2.27e-21 |
|
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: 94.86 E-value: 2.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSL---------------------------------LSA 641
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLtkliqrfyvpengrvlvdghdlaladpawlrrqVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 642 LLAE--------------------MDKV-----------------EGH---VAIKGVNLSGGQKQRVSLARAVYSNADIY 681
Cdd:cd03252 81 VLQEnvlfnrsirdnialadpgmsMERVieaaklagahdfiselpEGYdtiVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549096 682 LFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFA 755
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNM---HDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYA 231
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
595-738 |
3.51e-21 |
|
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: 93.71 E-value: 3.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTWARSDPPT--LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVAIKGVN------------ 659
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVRVDGTDisklsekelaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 -------------------------------------------------------------LSGGQKQRVSLARAVYSNA 678
Cdd:cd03255 80 rrrhigfvfqsfnllpdltalenvelplllagvpkkerreraeellervglgdrlnhypseLSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462549096 679 DIYLFDDPLSAVDAHVGKHIFEnvigpkgMLK------NKTRILVTHSMSYLPQVDVIIVMSGGKI 738
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVME-------LLRelnkeaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
561-779 |
5.74e-21 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 99.02 E-value: 5.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 561 SVSLKRLRIFLSHEELEPDSIErrPVKDGGGTNSITVRnaTFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLS 640
Cdd:PRK10789 284 SAAYSRIRAMLAEAPVVKDGSE--PVPEGRGELDVNIR--QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLS 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 641 ALLAEMDKVEG--------------------------------------------------------------------- 651
Cdd:PRK10789 360 LIQRHFDVSEGdirfhdipltklqldswrsrlavvsqtpflfsdtvannialgrpdatqqeiehvarlasvhddilrlpq 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 652 ----HVAIKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRILVTHSMSYLPQV 727
Cdd:PRK10789 440 gydtEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNL---RQWGEGRTVIISAHRLSALTEA 516
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2462549096 728 DVIIVMSGGKISEMGSYQELLARDGAFAEFLRtYASTEQEQDAEENGVTGVS 779
Cdd:PRK10789 517 SEILVMQHGHIAQRGNHDQLAQQSGWYRDMYR-YQQLEAALDDAPEIREEAV 567
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
612-738 |
6.56e-21 |
|
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: 91.31 E-value: 6.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 612 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN-------------------------------- 659
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDikkepeevkrrigylpeepslyenltvrenlk 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGKHIFENVIgpKGMLK-NKTRILVTHSMSYLPQV-DVIIVMSGGK 737
Cdd:cd03230 96 LSGGMKQRLALAQALLHDPELLILDEPTSGLDP-ESRREFWELL--RELKKeGKTILLSSHILEEAERLcDRVAILNNGR 172
|
.
gi 2462549096 738 I 738
Cdd:cd03230 173 I 173
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1185-1409 |
7.64e-21 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 95.53 E-value: 7.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDLDFV--LRHINVTINGGEKVGIVGRTGAGKSSLtlglFR-IN--ESA-EGEIIIDGINIAKI---GL 1255
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTL----IRcINllERPtSGSVLVDGVDLTALserEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1256 HDLRFKITIIPQDPVLFSgslrmnldpfsqysdeevwtS----------LELAHLK------------DFVSaLPDKLDH 1313
Cdd:COG1135 78 RAARRKIGMIFQHFNLLS--------------------SrtvaenvalpLEIAGVPkaeirkrvaellELVG-LSDKADA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1314 ECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD----DLIQStIRTQFeDCTVLTIAHRLN---TIMDy 1386
Cdd:COG1135 137 YPSQ----LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTrsilDLLKD-INREL-GLTIVLITHEMDvvrRICD- 209
|
250 260
....*....|....*....|...
gi 2462549096 1387 tRVIVLDKGEIQEYGAPSDLLQQ 1409
Cdd:COG1135 210 -RVAVLENGRIVEQGPVLDVFAN 231
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
570-759 |
7.85e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 98.76 E-value: 7.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 570 FLSHEELEPDSIERRPVKDGGgtNSITVRNATFTwARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMdKV 649
Cdd:PRK11174 327 FLETPLAHPQQGEKELASNDP--VTIEAEDLEIL-SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PY 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 650 EGHVAIKGVNL--------------------------------------------------------------------- 660
Cdd:PRK11174 403 QGSLKINGIELreldpeswrkhlswvgqnpqlphgtlrdnvllgnpdasdeqlqqalenawvseflpllpqgldtpigdq 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 661 ----SGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGG 736
Cdd:PRK11174 483 aaglSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQAL---NAASRRQTTLMVTHQLEDLAQWDQIWVMQDG 559
|
250 260
....*....|....*....|...
gi 2462549096 737 KISEMGSYQELLARDGAFAEFLR 759
Cdd:PRK11174 560 QIVQQGDYAELSQAGGLFATLLA 582
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1185-1406 |
1.90e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 92.89 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITI 1264
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1265 IPQDPV-LFSGS---------LRMNLDPFSQYSdEEVWTSLELAHLKdfvsalpDKLDHEcaegGENLSVGQRQLVCLAR 1334
Cdd:PRK13648 88 VFQNPDnQFVGSivkydvafgLENHAVPYDEMH-RRVSEALKQVDML-------ERADYE----PNALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549096 1335 ALLRKTKILVLDEATAAVDLETDDLIQSTIR--TQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDL 1406
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRkvKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1201-1397 |
2.32e-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: 89.41 E-value: 2.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHD-LRFKITIIPQdpvlfsgslrmn 1279
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMVYQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1280 ldpfsqysdeevwtslelahlkdfvsalpdkldhecaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDL-ETDD 1358
Cdd:cd03216 83 ------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPaEVER 120
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2462549096 1359 LIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEI 1397
Cdd:cd03216 121 LFKVIRRLRAQGVAVIFISHRLDEVFEIAdRVTVLRDGRV 160
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1185-1410 |
2.46e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 92.99 E-value: 2.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYrEDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--INIAKIGLHDLRFKI 1262
Cdd:PRK13636 6 LKVEELNYNY-SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1263 TIIPQDP--VLFSGSLR-------MNLdpfsQYSDEEVWTSLELAHLKDFVSALPDKLDHEcaeggenLSVGQRQLVCLA 1333
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYqdvsfgaVNL----KLPEDEVRKRVDNALKRTGIEHLKDKPTHC-------LSFGQKKRVAIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1334 RALLRKTKILVLDEATAAVD-LETDDLIQSTIRTQFE-DCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLLQQR 1410
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDpMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCdNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
595-759 |
3.86e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 96.24 E-value: 3.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN--------------- 659
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDlrdytlaslrnqval 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 -----------------------------------------------------------LSGGQKQRVSLARAVYSNADI 680
Cdd:PRK11176 422 vsqnvhlfndtianniayarteqysreqieeaarmayamdfinkmdngldtvigengvlLSGGQRQRIAIARALLRDSPI 501
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549096 681 YLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAEFLR 759
Cdd:PRK11176 502 LILDEATSALDTESERAIQAAL---DELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHK 577
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1184-1365 |
4.44e-20 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 89.85 E-value: 4.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1184 RVEFRNYCLRYREDLdfVLRHINVTINGGEKVGIVGRTGAGKSSL--TL-GLFRInesAEGEIIIDGINIAKIGlHDLRF 1260
Cdd:COG4133 2 MLEAENLSCRRGERL--LFSGLSFTLAAGEALALTGPNGSGKTTLlrILaGLLPP---SAGEVLWNGEPIRDAR-EDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1261 KITIIPQDPVLFSG-SLRMNLDpFSQ------YSDEEVWTSLELAHLKDFvsalpdkLDHECAeggeNLSVGQRQLVCLA 1333
Cdd:COG4133 76 RLAYLGHADGLKPElTVRENLR-FWAalyglrADREAIDEALEAVGLAGL-------ADLPVR----QLSAGQKRRVALA 143
|
170 180 190
....*....|....*....|....*....|..
gi 2462549096 1334 RALLRKTKILVLDEATAAVDLETDDLIQSTIR 1365
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALDAAGVALLAELIA 175
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
595-761 |
4.69e-20 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 90.92 E-value: 4.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFtwARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN--------------- 659
Cdd:COG1121 7 IELENLTV--SYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPprrarrrigyvpqra 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 -------------------------------------------------------LSGGQKQRVSLARAVYSNADIYLFD 684
Cdd:COG1121 85 evdwdfpitvrdvvlmgrygrrglfrrpsradreavdealervgledladrpigeLSGGQQQRVLLARALAQDPDLLLLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 685 DPLSAVDAHVGKHIFEnvigpkgMLK-----NKTRILVTHSMSYLPQ-VDVIIVMSGGKISEmGSYQELLARDgafaEFL 758
Cdd:COG1121 165 EPFAGVDAATEEALYE-------LLRelrreGKTILVVTHDLGAVREyFDRVLLLNRGLVAH-GPPEEVLTPE----NLS 232
|
...
gi 2462549096 759 RTY 761
Cdd:COG1121 233 RAY 235
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1201-1408 |
7.47e-20 |
|
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: 89.80 E-value: 7.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHD-LRFKITIIPQDPVLFSG-SLRM 1278
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1279 NLD--PFSQYSDEEVWTsleLAHLKDFVSALPDKLDHEcaegGENLSVGQRQLVCLARALLRKTKILVLDEATAA----- 1351
Cdd:cd03224 95 NLLlgAYARRRAKRKAR---LERVYELFPRLKERRKQL----AGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGlapki 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549096 1352 VDlETDDLIQsTIRTqfEDCTVLTIAHRLNTIMDY-TRVIVLDKGEIQEYGAPSDLLQ 1408
Cdd:cd03224 168 VE-EIFEAIR-ELRD--EGVTILLVEQNARFALEIaDRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
596-738 |
9.66e-20 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 88.26 E-value: 9.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 596 TVRNATFtwARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN---------------- 659
Cdd:cd03214 1 EVENLSV--GYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDlaslspkelarkiayv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 -------------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPKGMlKNKTRILVTHS 720
Cdd:cd03214 79 pqalellglahladrpfneLSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARE-RGKTVVMVLHD 157
|
170
....*....|....*....
gi 2462549096 721 MSYLPQV-DVIIVMSGGKI 738
Cdd:cd03214 158 LNLAARYaDRVILLKDGRI 176
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1201-1416 |
1.24e-19 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 91.65 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLT---LGLFRINESAEGEIIIDGINIAKIG---LHDLRFK-ITIIPQDPvlfs 1273
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLAraiLGLLPPPGITSGEILFDGEDLLKLSekeLRKIRGReIQMIFQDP---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1274 gslrMN-LDP--------------FSQYSDEEVWT----SLELAHL---KDFVSALPdkldHEcaeggenLSVGQRQLVC 1331
Cdd:COG0444 96 ----MTsLNPvmtvgdqiaeplriHGGLSKAEAREraieLLERVGLpdpERRLDRYP----HE-------LSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1332 LARALLRKTKILVLDEATAAVDLetddLIQSTI-------RTQFeDCTVLTIAHRLNT---IMDytRVIVLDKGEIQEYG 1401
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDV----TIQAQIlnllkdlQREL-GLAILFITHDLGVvaeIAD--RVAVMYAGRIVEEG 233
|
250 260
....*....|....*....|.
gi 2462549096 1402 APSDLLQQ------RGLFYSM 1416
Cdd:COG0444 234 PVEELFENprhpytRALLSSI 254
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
595-737 |
2.25e-19 |
|
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: 87.24 E-value: 2.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTwaRSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN--------------- 659
Cdd:cd03229 1 LELKNVSKR--YGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDltdledelpplrrri 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 ----------------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPKGMLKnKTRILV 717
Cdd:cd03229 79 gmvfqdfalfphltvlenialgLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLG-ITVVLV 157
|
170 180
....*....|....*....|.
gi 2462549096 718 THSMSYLPQV-DVIIVMSGGK 737
Cdd:cd03229 158 THDLDEAARLaDRVVVLRDGK 178
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1202-1409 |
2.26e-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: 93.60 E-value: 2.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1202 LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESaEGEIIIDGINIAKIG---LHDLRFKITIIPQDPvlFsGSL-- 1276
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--F-GSLsp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1277 RMN-----------LDPfsQYSDEE----VWTSLELAHLKdfvsalPDKLD---HEcaeggenLSVGQRQLVCLARALLR 1338
Cdd:COG4172 378 RMTvgqiiaeglrvHGP--GLSAAErrarVAEALEEVGLD------PAARHrypHE-------FSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1339 KTKILVLDEATAAVDLetddliqsTIRTQfedctVLT---------------IAHRLN---TIMDytRVIVLDKGEIQEY 1400
Cdd:COG4172 443 EPKLLVLDEPTSALDV--------SVQAQ-----ILDllrdlqrehglaylfISHDLAvvrALAH--RVMVMKDGKVVEQ 507
|
....*....
gi 2462549096 1401 GAPSDLLQQ 1409
Cdd:COG4172 508 GPTEQVFDA 516
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1185-1378 |
2.88e-19 |
|
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: 87.91 E-value: 2.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDLDF--VLRHINVTINGGEKVGIVGRTGAGKSSL---TLGLFRInesAEGEIIIDGINIAKIGLHdlr 1259
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLlriIAGLERP---TSGEVLVDGEPVTGPGPD--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1260 fkITIIPQDPVLF---------SGSLRMNLDPFSQySDEEVWTSLELAHLKDFVSALPdkldHEcaeggenLSVGQRQLV 1330
Cdd:cd03293 75 --RGYVFQQDALLpwltvldnvALGLELQGVPKAE-ARERAEELLELVGLSGFENAYP----HQ-------LSGGMRQRV 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462549096 1331 CLARALLRKTKILVLDEATAAVDLETDDLIQSTI-----RTQFedcTVLTIAH 1378
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDALTREQLQEELldiwrETGK---TVLLVTH 190
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1185-1407 |
2.91e-19 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 88.51 E-value: 2.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYReDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITI 1264
Cdd:cd03295 1 IEFENVTKRYG-GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1265 IPQDPVLFSG-SLRMN--LDP-FSQYSDEEVWT-SLELAHLKDFVSA-LPDKLDHEcaeggenLSVGQRQLVCLARALLR 1338
Cdd:cd03295 80 VIQQIGLFPHmTVEENiaLVPkLLKWPKEKIRErADELLALVGLDPAeFADRYPHE-------LSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462549096 1339 KTKILVLDEATAAVDLETDDLIQSTIRTQFEDC--TVLTIAHRLN-TIMDYTRVIVLDKGEIQEYGAPSDLL 1407
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQELgkTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
595-737 |
3.62e-19 |
|
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: 85.58 E-value: 3.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTWarSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN-------LSGGQKQR 667
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVkigyfeqLSGGEKMR 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462549096 668 VSLARAVYSNADIYLFDDPLSAVDAHvGKHIFENvigpkgMLKN--KTRILVTHSMSYLPQV-DVIIVMSGGK 737
Cdd:cd03221 79 LALAKLLLENPNLLLLDEPTNHLDLE-SIEALEE------ALKEypGTVILVSHDRYFLDQVaTKIIELEDGK 144
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
868-1156 |
6.30e-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: 88.76 E-value: 6.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 868 FLSIFLFMCNHVSALASNYWLSLWTDDPIVNGTQEHTKVRLSVYGALGISQGIAVFGYSMAVSIGGILASRCLHVDLLHS 947
Cdd:cd07346 2 LLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 948 ILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATP----IAAIIIPPLGLIYFFVQR 1023
Cdd:cd07346 82 LQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWkltlVALLLLPLYVLILRYFRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1024 FYVASSRQLKrlESVSRspVYSHFNETLLGVSVIRAF----EEQERFIHQSDLKVDENQKAYYPSIVANRWLAVrLECVG 1099
Cdd:cd07346 162 RIRKASREVR--ESLAE--LSAFLQESLSGIRVVKAFaaeeREIERFREANRDLRDANLRAARLSALFSPLIGL-LTALG 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549096 1100 NCIVLFAALFAVIsRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERL 1156
Cdd:cd07346 237 TALVLLYGGYLVL-QGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
595-740 |
6.62e-19 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 87.02 E-value: 6.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTWARSDPPT--LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVAIKGVN------------ 659
Cdd:COG1136 5 LELRNLTKSYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLN-ILGGLDRPtSGEVLIDGQDisslserelarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 -------------------------------------------------------------LSGGQKQRVSLARAVYSNA 678
Cdd:COG1136 84 rrrhigfvfqffnllpeltalenvalplllagvsrkerrerarellervglgdrldhrpsqLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549096 679 DIYLFDDPLSAVDAHVGKHIFEnvigpkgMLK------NKTRILVTHSMSYLPQVDVIIVMSGGKISE 740
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLE-------LLRelnrelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
595-774 |
7.25e-19 |
|
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: 91.89 E-value: 7.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSA---LLAEMDKVEGHVAIKGVN------------ 659
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALAlmgLLPHGGRISGEVLLDGRDllelsealrgrr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 ----------------------------------------------------------LSGGQKQRVSLARAVYSNADIY 681
Cdd:COG1123 85 igmvfqdpmtqlnpvtvgdqiaealenlglsraeararvlelleavglerrldryphqLSGGQRQRVAIAMALALDPDLL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 682 LFDDPLSAVDAHVGKHIFEnVIGPKGMLKNKTRILVTHSMSYLPQV-DVIIVMSGGKISEMGSYQELLARDGAFAEFLRT 760
Cdd:COG1123 165 IADEPTTALDVTTQAEILD-LLRELQRERGTTVLLITHDLGVVAEIaDRVVVMDDGRIVEDGPPEEILAAPQALAAVPRL 243
|
250
....*....|....
gi 2462549096 761 YASTEQEQDAEENG 774
Cdd:COG1123 244 GAARGRAAPAAAAA 257
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1185-1399 |
9.07e-19 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 86.64 E-value: 9.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDLD--FVLRHINVTINGGEKVGIVGRTGAGKSSL--TLGLFrinESA-EGEIIIDGINIAKIG---LH 1256
Cdd:COG1136 5 LELRNLTKSYGTGEGevTALRGVSLSIEAGEFVAIVGPSGSGKSTLlnILGGL---DRPtSGEVLIDGQDISSLSereLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1257 DLRF-KITIIPQDPvlfsgslrmNLDPFsqYSDEE-VWTSLELAHLKDFVSA-----------LPDKLDHECAEggenLS 1323
Cdd:COG1136 82 RLRRrHIGFVFQFF---------NLLPE--LTALEnVALPLLLAGVSRKERRerarellervgLGDRLDHRPSQ----LS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1324 VGQRQLVCLARALLRKTKILVLDEATAAVDLETD----DLIQSTIRTQfeDCTVLTIAH--RLNTIMDytRVIVLDKGEI 1397
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGeevlELLRELNREL--GTTIVMVTHdpELAARAD--RVIRLRDGRI 222
|
..
gi 2462549096 1398 QE 1399
Cdd:COG1136 223 VS 224
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1185-1407 |
9.08e-19 |
|
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: 87.45 E-value: 9.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDLdfVLRHINVTINGGEKVGIVGRTGAGKSSLtLGLF--RINESAEGEIIIDGINIAKIGLHDLRFKI 1262
Cdd:COG1119 4 LELRNVTVRRGGKT--ILDDISWTVKPGEHWAILGPNGAGKSTL-LSLItgDLPPTYGNDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1263 ---------TIIPQDPVL------FSGSLrmnlDPFSQYSDEEV-----W-TSLELAHLKD--FVSalpdkldhecaegg 1319
Cdd:COG1119 81 glvspalqlRFPRDETVLdvvlsgFFDSI----GLYREPTDEQRerareLlELLGLAHLADrpFGT-------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1320 enLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRT--QFEDCTVLTIAHRLNTIMD-YTRVIVLDKGE 1396
Cdd:COG1119 143 --LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEEIPPgITHVLLLKDGR 220
|
250
....*....|.
gi 2462549096 1397 IQEYGAPSDLL 1407
Cdd:COG1119 221 VVAAGPKEEVL 231
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1185-1422 |
1.14e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 87.93 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSS---LTLGLFRINESAEGEIIIDGINIAKIGLHDLRFK 1261
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1262 ITIIPQDP-VLFSGSLRMNLDPFS----QYSDEE----VWTSLELAHLKDFVSALPdkldhecaeggENLSVGQRQLVCL 1332
Cdd:PRK13640 86 VGIVFQNPdNQFVGATVGDDVAFGlenrAVPRPEmikiVRDVLADVGMLDYIDSEP-----------ANLSGGQKQRVAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1333 ARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFED--CTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQR 1410
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnnLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
250
....*....|..
gi 2462549096 1411 glfySMAKDAGL 1422
Cdd:PRK13640 235 ----EMLKEIGL 242
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1202-1405 |
1.27e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 89.09 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1202 LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKI---GLHDLRFKITIIPQDPVLFSgslrm 1278
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALsekELRKARRQIGMIFQHFNLLS----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1279 nldpfSQYSDEEVWTSLELAHL-KDFVSA----------LPDKLDHECAeggeNLSVGQRQLVCLARALLRKTKILVLDE 1347
Cdd:PRK11153 96 -----SRTVFDNVALPLELAGTpKAEIKArvtellelvgLSDKADRYPA----QLSGGQKQRVAIARALASNPKVLLCDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549096 1348 ATAAVDLETDDLIQSTIRTQFED--CTVLTIAHRlntiMDYT-----RVIVLDKGEIQEYGAPSD 1405
Cdd:PRK11153 167 ATSALDPATTRSILELLKDINRElgLTIVLITHE----MDVVkricdRVAVIDAGRLVEQGTVSE 227
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
560-750 |
1.33e-18 |
|
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: 91.35 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 560 ASVSLKRLRIFLSHEELEPDSIER-RPvkdgggTNSITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSL 638
Cdd:COG4618 301 ARQAYRRLNELLAAVPAEPERMPLpRP------KGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 639 LSALL----------------------------------------------------AEMDKV----------------- 649
Cdd:COG4618 375 ARLLVgvwpptagsvrldgadlsqwdreelgrhigylpqdvelfdgtiaeniarfgdADPEKVvaaaklagvhemilrlp 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 650 EG---HVAIKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGKHIFENVIgpkGMLK--NKTRILVTHSMSYL 724
Cdd:COG4618 455 DGydtRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD-EGEAALAAAI---RALKarGATVVVITHRPSLL 530
|
250 260
....*....|....*....|....*.
gi 2462549096 725 PQVDVIIVMSGGKISEMGSYQELLAR 750
Cdd:COG4618 531 AAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1185-1397 |
1.36e-18 |
|
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: 85.92 E-value: 1.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDLdFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAkiGLHD-----LR 1259
Cdd:cd03292 1 IEFINVTKTYPNGT-AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS--DLRGraipyLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1260 FKITIIPQDPVLFSG---------SLRMNLDPfSQYSDEEVWTSLELAHLKDFVSALPdkldhecaeggENLSVGQRQLV 1330
Cdd:cd03292 78 RKIGVVFQDFRLLPDrnvyenvafALEVTGVP-PREIRKRVPAALELVGLSHKHRALP-----------AELSGGEQQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1331 CLARALLRKTKILVLDEATAAVDLETDDLIqSTIRTQFED--CTVLTIAHRLNTIMDYT-RVIVLDKGEI 1397
Cdd:cd03292 146 AIARAIVNSPTILIADEPTGNLDPDTTWEI-MNLLKKINKagTTVVVATHAKELVDTTRhRVIALERGKL 214
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1196-1406 |
1.89e-18 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 86.63 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1196 EDLDF------VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINE-----SAEGEIIIDGINI--AKIGLHDLRFKI 1262
Cdd:COG1117 15 RNLNVyygdkqALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDlipgaRVEGEILLDGEDIydPDVDVVELRRRV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1263 TIIPQDPVLFSGS--------LRMNLDPFSQYSDEEVWTSLELAHLKDFVSalpDKLDhecaEGGENLSVGQRQLVCLAR 1334
Cdd:COG1117 95 GMVFQKPNPFPKSiydnvaygLRLHGIKSKSELDEIVEESLRKAALWDEVK---DRLK----KSALGLSGGQQQRLCIAR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549096 1335 ALLRKTKILVLDEATAAVD-LETD---DLIQStIRtqfEDCTVLTIAHRLNT---IMDYTrvIVLDKGEIQEYGAPSDL 1406
Cdd:COG1117 168 ALAVEPEVLLMDEPTSALDpISTAkieELILE-LK---KDYTIVIVTHNMQQaarVSDYT--AFFYLGELVEFGPTEQI 240
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1185-1412 |
1.99e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 87.09 E-value: 1.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDLD-FVLRHINVTINGGEKVGIVGRTGAGKSS---LTLGLFrinESAEGEIIIDGINIAKIGLHDLRF 1260
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGLL---EAESGQIIIDGDLLTEENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1261 KITIIPQDP-VLFSGSLRMNLDPFS--------QYSDEEVWTSLELAHLKDFVSALPDKLdhecaeggenlSVGQRQLVC 1331
Cdd:PRK13650 82 KIGMVFQNPdNQFVGATVEDDVAFGlenkgiphEEMKERVNEALELVGMQDFKEREPARL-----------SGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1332 LARALLRKTKILVLDEATAAVDLETD-DLIQS--TIRTQFeDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDL-- 1406
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRlELIKTikGIRDDY-QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELfs 229
|
250
....*....|
gi 2462549096 1407 ----LQQRGL 1412
Cdd:PRK13650 230 rgndLLQLGL 239
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
612-738 |
2.01e-18 |
|
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: 84.02 E-value: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 612 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG--VN-----------------LSGGQKQRVSLAR 672
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGkeVSfasprdarragiamvyqLSVGERQMVEIAR 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549096 673 AVYSNADIYLFDDPLSAVDAHVGKHIFEnVIgpkGMLKN--KTRILVTHSMSYLPQV-DVIIVMSGGKI 738
Cdd:cd03216 96 ALARNARLLILDEPTAALTPAEVERLFK-VI---RRLRAqgVAVIFISHRLDEVFEIaDRVTVLRDGRV 160
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1208-1407 |
2.41e-18 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 87.86 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1208 TINGGEKVGIVGRTGAGKSslTLG--LFRINESAEGEIIIDGINIAKIG---LHDLRFKITIIPQDPvlfSGSL--RMNL 1280
Cdd:COG4608 40 DIRRGETLGLVGESGCGKS--TLGrlLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP---YASLnpRMTV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1281 -----DPFsqysdeEVWTSLELAHLKDFVSAL-------PDKLD---HEcaeggenLSVGQRQLVCLARALLRKTKILVL 1345
Cdd:COG4608 115 gdiiaEPL------RIHGLASKAERRERVAELlelvglrPEHADrypHE-------FSGGQRQRIGIARALALNPKLIVC 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462549096 1346 DEATAAVDLEtddlIQSTIRTQFED------CTVLTIAHRLNT---IMDytRVIVLDKGEIQEYGaPSDLL 1407
Cdd:COG4608 182 DEPVSALDVS----IQAQVLNLLEDlqdelgLTYLFISHDLSVvrhISD--RVAVMYLGKIVEIA-PRDEL 245
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1202-1395 |
2.76e-18 |
|
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: 85.08 E-value: 2.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1202 LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDL----RFKITIIPQDPVLFSGSLR 1277
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1278 MNLDPFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE-T 1356
Cdd:cd03290 97 ENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2462549096 1357 DDLIQSTIRTQFED--CTVLTIAHRLNTIMDYTRVIVLDKG 1395
Cdd:cd03290 177 DHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1201-1397 |
3.38e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 86.29 E-value: 3.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLtL----GLFRINEsaeGEIIIDGINIAKIGLHDlRFK-ITIIPQDPVL---- 1271
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTL-LnaiaGSLPPDS---GSILIDGKDVTKLPEYK-RAKyIGRVFQDPMMgtap 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1272 ---------------FSGSLRMNLdpfsqysdeevwTSLELAHLKDFVSA----LPDKLDHECaeggENLSVGQRQLVCL 1332
Cdd:COG1101 96 smtieenlalayrrgKRRGLRRGL------------TKKRRELFRELLATlglgLENRLDTKV----GLLSGGQRQALSL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549096 1333 ARALLRKTKILVLDEATAAVD-------LE-TDDLIQStirtqfEDCTVLTIAHRLNTIMDY-TRVIVLDKGEI 1397
Cdd:COG1101 160 LMATLTKPKLLLLDEHTAALDpktaalvLElTEKIVEE------NNLTTLMVTHNMEQALDYgNRLIMMHEGRI 227
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
602-742 |
3.62e-18 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 84.88 E-value: 3.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 602 FTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVAIKGVN--------------------- 659
Cdd:cd03259 6 LSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLR-LIAGLERPdSGEILIDGRDvtgvpperrnigmvfqdyalf 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 ----------------------------------------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 693
Cdd:cd03259 85 phltvaeniafglklrgvpkaeirarvrellelvglegllnrypheLSGGQQQRVALARALAREPSLLLLDEPLSALDAK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462549096 694 VGKHIFENVigpKGMLKN--KTRILVTHSMS-YLPQVDVIIVMSGGKISEMG 742
Cdd:cd03259 165 LREELREEL---KELQRElgITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
595-756 |
3.90e-18 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 85.08 E-value: 3.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTWaRSDPPTLNGITFSIPEGALVAVVGQVGCGKSSL---LSALLAEMdkvEGHVAIKGVN------------ 659
Cdd:COG1122 1 IELENLSFSY-PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLlrlLNGLLKPT---SGEVLVDGKDitkknlrelrrk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 ----------------------------------------------------------LSGGQKQRVSLARAVYSNADIY 681
Cdd:COG1122 77 vglvfqnpddqlfaptveedvafgpenlglpreeirerveealelvglehladrppheLSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 682 LFDDPLSAVDAHVGKHIFEnvigpkgMLK-----NKTRILVTHSMSYLPQV-DVIIVMSGGKISEMGSYQELLARDGAFA 755
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLE-------LLKrlnkeGKTVIIVTHDLDLVAELaDRVIVLDDGRIVADGTPREVFSDYELLE 229
|
.
gi 2462549096 756 E 756
Cdd:COG1122 230 E 230
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
594-750 |
5.91e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 87.05 E-value: 5.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 594 SITVRNATFTWarSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVAIKG--VN----------- 659
Cdd:COG3839 3 SLELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLR-MIAGLEDPtSGEILIGGrdVTdlppkdrniam 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 ------------------------------------------------------LSGGQKQRVSLARAVYSNADIYLFDD 685
Cdd:COG3839 80 vfqsyalyphmtvyeniafplklrkvpkaeidrrvreaaellgledlldrkpkqLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 686 PLSAVDAHvgkhifenvigpkgmLKNKTR--------------ILVTH------SMSylpqvDVIIVMSGGKISEMGSYQ 745
Cdd:COG3839 160 PLSNLDAK---------------LRVEMRaeikrlhrrlgtttIYVTHdqveamTLA-----DRIAVMNDGRIQQVGTPE 219
|
....*
gi 2462549096 746 ELLAR 750
Cdd:COG3839 220 ELYDR 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1184-1414 |
7.88e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 85.42 E-value: 7.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1184 RVEFRNYCLryrEDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIG-LHDLRFKI 1262
Cdd:PRK13644 3 RLENVSYSY---PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1263 TIIPQDP-VLFSGslRMNLDPFSQYSDEEVWTSLELAHLKDfvSALPD-KLDHECAEGGENLSVGQRQLVCLARALLRKT 1340
Cdd:PRK13644 80 GIVFQNPeTQFVG--RTVEEDLAFGPENLCLPPIEIRKRVD--RALAEiGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549096 1341 KILVLDEATAAVDLETDDLIQSTIRTQFEDC-TVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRGLFY 1414
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEKGkTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQT 230
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
594-750 |
7.92e-18 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 86.74 E-value: 7.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 594 SITVRNATFTWArsDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLS--------------------------------- 640
Cdd:COG1118 2 SIEVRNISKRFG--SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRiiagletpdsgrivlngrdlftnlpprerrvgf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 641 -----ALLAEMDkVEGHVA------------IKGV-------------------NLSGGQKQRVSLARAVYSNADIYLFD 684
Cdd:COG1118 80 vfqhyALFPHMT-VAENIAfglrvrppskaeIRARveellelvqlegladrypsQLSGGQRQRVALARALAVEPEVLLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549096 685 DPLSAVDAHVGK-------HIFENVigpkgmlkNKTRILVTHSmsylpQVDV------IIVMSGGKISEMGSYQELLAR 750
Cdd:COG1118 159 EPFGALDAKVRKelrrwlrRLHDEL--------GGTTVFVTHD-----QEEAleladrVVVMNQGRIEQVGTPDEVYDR 224
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
594-743 |
9.09e-18 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 83.70 E-value: 9.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 594 SITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGV--------------- 658
Cdd:cd03244 2 DIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVdiskiglhdlrsris 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 659 ---------------------------------------------------------NLSGGQKQRVSLARAVYSNADIY 681
Cdd:cd03244 82 iipqdpvlfsgtirsnldpfgeysdeelwqalervglkefveslpggldtvveeggeNLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462549096 682 LFDDPLSAVDAHVGKHIFEnVIgpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGS 743
Cdd:cd03244 162 VLDEATASVDPETDALIQK-TI--REAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1185-1407 |
9.50e-18 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 83.92 E-value: 9.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREdldFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAkiGLHDLRFKITI 1264
Cdd:cd03299 1 LKVENLSKDWKE---FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1265 IPQDPVLF---------SGSLRMNLDPFSQYSDE--EVWTSLELAHLkdfvsalpdkLDHEcaegGENLSVGQRQLVCLA 1333
Cdd:cd03299 76 VPQNYALFphmtvykniAYGLKKRKVDKKEIERKvlEIAEMLGIDHL----------LNRK----PETLSGGEQQRVAIA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549096 1334 RALLRKTKILVLDEATAAVDLETDDLIQS---TIRTQFeDCTVLTIAHRLNTI-MDYTRVIVLDKGEIQEYGAPSDLL 1407
Cdd:cd03299 142 RALVVNPKILLLDEPFSALDVRTKEKLREelkKIRKEF-GVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
653-756 |
9.72e-18 |
|
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: 89.03 E-value: 9.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 653 VAIKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGpkgmLKNKTRILVTHSMSYLPQVDVIIV 732
Cdd:TIGR01193 605 LSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN----LQDKTIIFVAHRLSVAKQSDKIIV 680
|
90 100
....*....|....*....|....
gi 2462549096 733 MSGGKISEMGSYQELLARDGAFAE 756
Cdd:TIGR01193 681 LDHGKIIEQGSHDELLDRNGFYAS 704
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
595-740 |
1.48e-17 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 83.99 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTWARSDPPT--LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVAIKGV------------- 658
Cdd:COG1116 8 LELRGVSKRFPTGGGGVtaLDDVSLTVAAGEFVALVGPSGCGKSTLLR-LIAGLEKPtSGEVLVDGKpvtgpgpdrgvvf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 659 -------------N--------------------------------------LSGGQKQRVSLARAVYSNADIYLFDDPL 687
Cdd:COG1116 87 qepallpwltvldNvalglelrgvpkaerrerarellelvglagfedayphqLSGGMRQRVAIARALANDPEVLLMDEPF 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549096 688 SAVDAHVgkhifenvigpKGML----------KNKTRILVTHSMS---YLpqVDVIIVMSG--GKISE 740
Cdd:COG1116 167 GALDALT-----------RERLqdellrlwqeTGKTVLFVTHDVDeavFL--ADRVVVLSArpGRIVE 221
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1184-1399 |
1.55e-17 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 83.99 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1184 RVEFRNYCLRYREDLD--FVLRHINVTINGGEKVGIVGRTGAGKSSLtlglFRI----NESAEGEIIIDGINIAKIGLhd 1257
Cdd:COG1116 7 ALELRGVSKRFPTGGGgvTALDDVSLTVAAGEFVALVGPSGCGKSTL----LRLiaglEKPTSGEVLVDGKPVTGPGP-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1258 lrfKITIIPQDPVLF----------SGsLRMNLDPFSQYsDEEVWTSLELAHLKDFVSALPdkldHEcaeggenLSVGQR 1327
Cdd:COG1116 81 ---DRGVVFQEPALLpwltvldnvaLG-LELRGVPKAER-RERARELLELVGLAGFEDAYP----HQ-------LSGGMR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1328 QLVCLARALLRKTKILVLDEATAAVDLET-----DDLIQstIRTQfEDCTVLTIAH------RLNtimdyTRVIVLDK-- 1394
Cdd:COG1116 145 QRVAIARALANDPEVLLMDEPFGALDALTrerlqDELLR--LWQE-TGKTVLFVTHdvdeavFLA-----DRVVVLSArp 216
|
....*
gi 2462549096 1395 GEIQE 1399
Cdd:COG1116 217 GRIVE 221
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
566-760 |
2.22e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 87.71 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 566 RLRIFLSHEELEPDSIERRPVKDGGG-TNSITVRNATFTWARSdPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLA 644
Cdd:PRK13657 305 KLEEFFEVEDAVPDVRDPPGAIDLGRvKGAVEFDDVSFSYDNS-RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQR 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 645 EMDKVEGHVAIKGVN----------------------------------------------------------------- 659
Cdd:PRK13657 384 VFDPQSGRILIDGTDirtvtraslrrniavvfqdaglfnrsiednirvgrpdatdeemraaaeraqahdfierkpdgydt 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 --------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG---KHIFENVigpkgmLKNKTRILVTHSMSYLPQVD 728
Cdd:PRK13657 464 vvgergrqLSGGERQRLAIARALLKDPPILILDEATSALDVETEakvKAALDEL------MKGRTTFIIAHRLSTVRNAD 537
|
250 260 270
....*....|....*....|....*....|..
gi 2462549096 729 VIIVMSGGKISEMGSYQELLARDGAFAEFLRT 760
Cdd:PRK13657 538 RILVFDNGRVVESGSFDELVARGGRFAALLRA 569
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
594-733 |
2.38e-17 |
|
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: 87.34 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 594 SITVRNATFTWARSDPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN-------------- 659
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPladadadswrdqia 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 -----------------------------------------------------------LSGGQKQRVSLARAVYSNADI 680
Cdd:TIGR02857 400 wvpqhpflfagtiaenirlarpdasdaeirealeragldefvaalpqgldtpigeggagLSGGQAQRLALARAFLRDAPL 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462549096 681 YLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRILVTHSMSYLPQVDVIIVM 733
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEAL---RALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1185-1379 |
3.11e-17 |
|
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: 80.66 E-value: 3.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDlDFVLRHINVTINGGEKVGIVGRTGAGKSSLtlglFRInesaegeiiIDGI------NIAKIGLHDL 1258
Cdd:cd03223 1 IELENLSLATPDG-RVLLKDLSFEIKPGDRLLITGPSGTGKSSL----FRA---------LAGLwpwgsgRIGMPEGEDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1259 RFkitiIPQDPVLFSGSLRmnldpfsqysdEEV---WtslelahlkdfvsalpdkldhecaegGENLSVGQRQLVCLARA 1335
Cdd:cd03223 67 LF----LPQRPYLPLGTLR-----------EQLiypW--------------------------DDVLSGGEQQRLAFARL 105
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462549096 1336 LLRKTKILVLDEATAAVDLETDDLIQSTIRTQFedCTVLTIAHR 1379
Cdd:cd03223 106 LLHKPKFVFLDEATSALDEESEDRLYQLLKELG--ITVISVGHR 147
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
868-1088 |
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 2462549096 868 FLSIFLFMCNHVSALASNYWLSLWTDDPIVNGTQEHTKVRL--SVYGALGISQGIAVFGYSMAVSIGGILASRCLHVDLL 945
Cdd:cd18544 2 ILALLLLLLATALELLGPLLIKRAIDDYIVPGQGDLQGLLLlaLLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 946 HSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVIL-----LATpIAAIIIPPLGLIYFF 1020
Cdd:cd18544 82 SHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFllnwrLAL-ISLLVLPLLLLATYL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549096 1021 VQRFYVASSRQLKrlESVSRspVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVAN 1088
Cdd:cd18544 161 FRKKSRKAYREVR--EKLSR--LNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLF 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
592-750 |
3.49e-17 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 84.76 E-value: 3.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 592 TNSITVRNATFTWArsDPPTLNGITFSIPEGALVAVVGQVGCGKSSLL---------------------SALLAE----- 645
Cdd:COG3842 3 MPALELENVSKRYG--DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLrmiagfetpdsgrilldgrdvTGLPPEkrnvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 646 -----------MDkVEGHVA----IKGVN---------------------------LSGGQKQRVSLARAVYSNADIYLF 683
Cdd:COG3842 81 mvfqdyalfphLT-VAENVAfglrMRGVPkaeirarvaellelvglegladryphqLSGGQQQRVALARALAPEPRVLLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549096 684 DDPLSAVDAHVGKHIFENVigpKGMLK--NKTRILVTH------SMSylpqvDVIIVMSGGKISEMGSYQELLAR 750
Cdd:COG3842 160 DEPLSALDAKLREEMREEL---RRLQRelGITFIYVTHdqeealALA-----DRIAVMNDGRIEQVGTPEEIYER 226
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
595-752 |
3.63e-17 |
|
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: 82.60 E-value: 3.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTWarSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN--------------- 659
Cdd:COG4555 2 IEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDvrkeprearrqigvl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 -----------------------------------------------------LSGGQKQRVSLARAVYSNADIYLFDDP 686
Cdd:COG4555 80 pderglydrltvreniryfaelyglfdeelkkrieeliellgleefldrrvgeLSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549096 687 LSAVDAhVGKHIFENVIgpKGMLK-NKTRILVTHSMSYLPQV-DVIIVMSGGKISEMGSYQELLARDG 752
Cdd:COG4555 160 TNGLDV-MARRLLREIL--RALKKeGKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1185-1408 |
3.79e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 82.45 E-value: 3.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDLdfVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINI--AKIGLHDLRFKI 1262
Cdd:PRK09493 2 IEFKNVSKHFGPTQ--VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1263 TIIPQDPVLFS----------GSLRMNldpfsQYSDEEvwtSLELAH-LKDFVsALPDKLDHECAEggenLSVGQRQLVC 1331
Cdd:PRK09493 80 GMVFQQFYLFPhltalenvmfGPLRVR-----GASKEE---AEKQAReLLAKV-GLAERAHHYPSE----LSGGQQQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549096 1332 LARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFED-CTVLTIAHRLNTIMDY-TRVIVLDKGEIQEYGAPSDLLQ 1408
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIK 225
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1201-1397 |
4.30e-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: 81.42 E-value: 4.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINI--AKIGLHDLRFKITIIPQDPVLFSgslRM 1278
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLFP---HL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1279 N------LDP---FSQYSDEEVWTSLELahLKDFvsALPDKLDHECAEggenLSVGQRQLVCLARALLRKTKILVLDEAT 1349
Cdd:cd03262 92 TvlenitLAPikvKGMSKAEAEERALEL--LEKV--GLADKADAYPAQ----LSGGQQQRVAIARALAMNPKVMLFDEPT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462549096 1350 AAVDLETDDLIQSTIRTQFED-CTVLTIAHRlntiMDY-----TRVIVLDKGEI 1397
Cdd:cd03262 164 SALDPELVGEVLDVMKDLAEEgMTMVVVTHE----MGFarevaDRVIFMDDGRI 213
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
595-759 |
4.99e-17 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 82.86 E-value: 4.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSL---LSALL---------AEMDK-------------- 648
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLaklLNGLLlptsgkvtvDGLDTldeenlweirkkvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 649 --------------VEGHVAI----KGV---------------------------NLSGGQKQRVSLARAVYSNADIYLF 683
Cdd:TIGR04520 81 mvfqnpdnqfvgatVEDDVAFglenLGVpreemrkrvdealklvgmedfrdrephLLSGGQKQRVAIAGVLAMRPDIIIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 684 DDPLSAVDahvgkhifenvigPKG-------MLK-----NKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARd 751
Cdd:TIGR04520 161 DEATSMLD-------------PKGrkevletIRKlnkeeGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQ- 226
|
....*...
gi 2462549096 752 gafAEFLR 759
Cdd:TIGR04520 227 ---VELLK 231
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
597-738 |
7.25e-17 |
|
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: 81.04 E-value: 7.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 597 VRNATFTWarSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN----------------- 659
Cdd:cd03235 2 VEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPlekerkrigyvpqrrsi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 -----------------------------------------------------LSGGQKQRVSLARAVYSNADIYLFDDP 686
Cdd:cd03235 80 drdfpisvrdvvlmglyghkglfrrlskadkakvdealervglseladrqigeLSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462549096 687 LSAVDAHVGKHIFENVIGPKGmlKNKTRILVTHSM-SYLPQVDVIIVMSGGKI 738
Cdd:cd03235 160 FAGVDPKTQEDIYELLRELRR--EGMTILVVTHDLgLVLEYFDRVLLLNRTVV 210
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
595-738 |
7.70e-17 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 80.98 E-value: 7.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTWARSDPPT--LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK------------------------ 648
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtaLEDISLSVEEGEFVALVGPSGCGKSTLLR-IIAGLERptsgevlvdgepvtgpgpdrgyvf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 649 ----------VEGHVA----IKGVN---------------------------LSGGQKQRVSLARAVYSNADIYLFDDPL 687
Cdd:cd03293 80 qqdallpwltVLDNVAlgleLQGVPkaeareraeellelvglsgfenayphqLSGGMRQRVALARALAVDPDVLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549096 688 SAVDAHVGKHIFENVIgpkGMLK--NKTRILVTHSMS---YLPqvDVIIVMSG--GKI 738
Cdd:cd03293 160 SALDALTREQLQEELL---DIWRetGKTVLLVTHDIDeavFLA--DRVVVLSArpGRI 212
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1201-1397 |
9.20e-17 |
|
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: 81.62 E-value: 9.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSL----TlGLFRINEsaeGEIIIDGINIAKIGLHDL------R-FKIT-IIPQD 1268
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLfnliT-GFYRPTS---GRILFDGRDITGLPPHRIarlgiaRtFQNPrLFPEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1269 PVL----------FSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSaLPDKLDHECAeggeNLSVGQRQLVCLARALLR 1338
Cdd:COG0411 95 TVLenvlvaaharLGRGLLAALLRLPRARREEREARERAEELLERVG-LADRADEPAG----NLSYGQQRRLEIARALAT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462549096 1339 KTKILVLDEATAAVDL-ETDDLIQsTIRT--QFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEI 1397
Cdd:COG0411 170 EPKLLLLDEPAAGLNPeETEELAE-LIRRlrDERGITILLIEHDMDLVMGLAdRIVVLDFGRV 231
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
595-759 |
1.03e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 81.96 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSS---LLSALL---------------------------- 643
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTiskILTGLLkpqsgeikidgitiskenlkeirkkigi 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 644 -----------------------------AEMDKVEGHVAIK-GV---------NLSGGQKQRVSLARAVYSNADIYLFD 684
Cdd:PRK13632 88 ifqnpdnqfigatveddiafglenkkvppKKMKDIIDDLAKKvGMedyldkepqNLSGGQKQRVAIASVLALNPEIIIFD 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549096 685 DPLSAVDAHvGKHIFENVIGPKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDgafaEFLR 759
Cdd:PRK13632 168 ESTSMLDPK-GKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK----EILE 237
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
579-756 |
1.28e-16 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 85.26 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 579 DSIERRPVKDGGGTnsITVRNATFTWarsDP--PTLNGITFSIPEGALVAVVGQVGCGKSSLlSALL------------- 643
Cdd:COG5265 344 DAPDAPPLVVGGGE--VRFENVSFGY---DPerPILKGVSFEVPAGKTVAIVGPSGAGKSTL-ARLLfrfydvtsgrili 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 644 -----------------------------------------AEMDKVEGhvAIK----------------------GVNL 660
Cdd:COG5265 418 dgqdirdvtqaslraaigivpqdtvlfndtiayniaygrpdASEEEVEA--AARaaqihdfieslpdgydtrvgerGLKL 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 661 SGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISE 740
Cdd:COG5265 496 SGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAAL---REVARGRTTLVIAHRLSTIVDADEILVLEAGRIVE 572
|
250
....*....|....*.
gi 2462549096 741 MGSYQELLARDGAFAE 756
Cdd:COG5265 573 RGTHAELLAQGGLYAQ 588
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
595-750 |
1.75e-16 |
|
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: 80.62 E-value: 1.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRN--ATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG--------------- 657
Cdd:COG1124 2 LEVRNlsVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGrpvtrrrrkafrrrv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 658 ----------VN---------------------------------------------LSGGQKQRVSLARAVYSNADIYL 682
Cdd:COG1124 82 qmvfqdpyasLHprhtvdrilaeplrihglpdreeriaelleqvglppsfldryphqLSGGQRQRVAIARALILEPELLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549096 683 FDDPLSAVDAHVGKHIFEnvigpkgMLK------NKTRILVTHSM---SYLpqVDVIIVMSGGKISEMGSYQELLAR 750
Cdd:COG1124 162 LDEPTSALDVSVQAEILN-------LLKdlreerGLTYLFVSHDLavvAHL--CDRVAVMQNGRIVEELTVADLLAG 229
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1201-1405 |
2.45e-16 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 79.79 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSslTL-----GLFRINEsaeGEIIIDGINIAKIGLHDLR-------FKITIIPQD 1268
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKT--TLfnlisGFLRPTS---GSVLFDGEDITGLPPHEIArlgigrtFQIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1269 ---------PVLFSGSLRMNLDPFSQYSDEEVWTSLELAhlkDFVsALPDKLDHECAeggeNLSVGQRQLVCLARALLRK 1339
Cdd:cd03219 90 ltvlenvmvAAQARTGSGLLLARARREEREARERAEELL---ERV-GLADLADRPAG----ELSYGQQRRLEIARALATD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549096 1340 TKILVLDEATAAVDL-ETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEIQEYGAPSD 1405
Cdd:cd03219 162 PKLLLLDEPAAGLNPeETEELAELIRELRERGITVLLVEHDMDVVMSLaDRVTVLDQGRVIAEGTPDE 229
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
595-751 |
6.16e-16 |
|
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: 78.70 E-value: 6.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFtwARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN--------------- 659
Cdd:cd03261 1 IELRGLTK--SFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisglseaelyrlrrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 ----------------------------------------------------------LSGGQKQRVSLARAVYSNADIY 681
Cdd:cd03261 79 mgmlfqsgalfdsltvfenvafplrehtrlseeeireivlekleavglrgaedlypaeLSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462549096 682 LFDDPLSAVDAhVGKHIFENVIGPKGMLKNKTRILVTHSMSYLPQV-DVIIVMSGGKISEMGSYQELLARD 751
Cdd:cd03261 159 LYDEPTAGLDP-IASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIaDRIAVLYDGKIVAEGTPEELRASD 228
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
594-743 |
9.62e-16 |
|
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: 77.45 E-value: 9.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 594 SITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGV--------------- 658
Cdd:cd03369 6 EIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIdistipledlrsslt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 659 ---------------------------------------NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIF 699
Cdd:cd03369 86 iipqdptlfsgtirsnldpfdeysdeeiygalrvsegglNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQ 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462549096 700 ENVigpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGS 743
Cdd:cd03369 166 KTI---REEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
569-750 |
1.00e-15 |
|
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: 81.87 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 569 IFLSHEELE--PDSIERRPVKDGGGTNS---ITVRNATFTWARSDPPT---LNGITFSIPEGALVAVVGQVGCGKSSLLS 640
Cdd:COG1123 230 ILAAPQALAavPRLGAARGRAAPAAAAAeplLEVRNLSKRYPVRGKGGvraVDDVSLTLRRGETLGLVGESGSGKSTLAR 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 641 ALLAEMDKVEGHVAIKGVN------------------------------------------------------------- 659
Cdd:COG1123 310 LLLGLLRPTSGSILFDGKDltklsrrslrelrrrvqmvfqdpysslnprmtvgdiiaeplrlhgllsraerrervaelle 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 ---------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEnvigpkgMLK------NKTRILVT 718
Cdd:COG1123 390 rvglppdladrypheLSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILN-------LLRdlqrelGLTYLFIS 462
|
250 260 270
....*....|....*....|....*....|...
gi 2462549096 719 HSMSYLPQV-DVIIVMSGGKISEMGSYQELLAR 750
Cdd:COG1123 463 HDLAVVRYIaDRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1187-1415 |
1.04e-15 |
|
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: 79.13 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1187 FRNYCLRYREdldfVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGiniakiglhdlrfKITIIP 1266
Cdd:cd03291 42 FSNLCLVGAP----VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1267 QDPVLFSGSLRMNLDPFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLD 1346
Cdd:cd03291 105 QFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLD 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549096 1347 EATAAVDLETDDLIqstirtqFEDC--------TVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRGLFYS 1415
Cdd:cd03291 185 SPFGYLDVFTEKEI-------FESCvcklmankTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSS 254
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
894-1156 |
1.15e-15 |
|
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: 79.14 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 894 DPIVNGTQEHTKVRLSVY-GALGISQGIAVFGYSMAVSIGGILASRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKEL 972
Cdd:cd18557 24 DTIIKGGDLDVLNELALIlLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 973 DTVDSMIPEVIKMFMGSLFNVIGaCIVILLA-----TPIAAIIIPPLGLIYFFVQRFYVASSRQLkrLESVSRSPvySHF 1047
Cdd:cd18557 104 SVLQSAVTDNLSQLLRNILQVIG-GLIILFIlswklTLVLLLVIPLLLIASKIYGRYIRKLSKEV--QDALAKAG--QVA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1048 NETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVAN---RWLAVRLECVGNCIVLFAALFAVISRHsLSAGLVGL 1124
Cdd:cd18557 179 EESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANalfQGITSLLIYLSLLLVLWYGGYLVLSGQ-LTVGELTS 257
|
250 260 270
....*....|....*....|....*....|..
gi 2462549096 1125 SVSYSLQVTTYLNWLVRMSSEMETNIVAVERL 1156
Cdd:cd18557 258 FILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1201-1406 |
1.22e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 81.60 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSslTL-----GLFRINEsaeGEIIIDGINIAKIGLHD-LRFKITIIPQDPVL--- 1271
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKS--TLmkilsGVYQPDS---GEILLDGEPVRFRSPRDaQAAGIAIIHQELNLvpn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1272 -------FSGSLRMN---LDPFSQYSD-EEVwtsleLAHLKdfVSALPDKLdhecaegGENLSVGQRQLVCLARALLRKT 1340
Cdd:COG1129 94 lsvaeniFLGREPRRgglIDWRAMRRRaREL-----LARLG--LDIDPDTP-------VGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549096 1341 KILVLDEATAAVDL-ETDDLIQsTIRT-QFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDL 1406
Cdd:COG1129 160 RVLILDEPTASLTErEVERLFR-IIRRlKAQGVAIIYISHRLDEVFEIAdRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
595-742 |
1.33e-15 |
|
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: 77.55 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRN--ATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN------------- 659
Cdd:cd03257 2 LEVKNlsVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDllklsrrlrkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 ----------------------------------------------------------------LSGGQKQRVSLARAVY 675
Cdd:cd03257 82 keiqmvfqdpmsslnprmtigeqiaeplrihgklskkearkeavllllvgvglpeevlnrypheLSGGQRQRVAIARALA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549096 676 SNADIYLFDDPLSAVDAHVGKHIFEnvigpkgMLK------NKTRILVTHSMSYLPQV-DVIIVMSGGKISEMG 742
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILD-------LLKklqeelGLTLLFITHDLGVVAKIaDRVAVMYAGKIVEEG 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1202-1401 |
1.35e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 78.28 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1202 LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINE-----SAEGEIIIDGINI--AKIGLHDLRFKITIIPQDPVLFSG 1274
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1275 S--------LRMNLDPFSQYSDEEVWTSLELAHLKDFVSalpDKLdHECAEGgenLSVGQRQLVCLARALLRKTKILVLD 1346
Cdd:PRK14239 101 SiyenvvygLRLKGIKDKQVLDEAVEKSLKGASIWDEVK---DRL-HDSALG---LSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549096 1347 EATAAVDLETDDLIQSTIRTQFEDCTVLTIAHRL---NTIMDYTrVIVLDkGEIQEYG 1401
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMqqaSRISDRT-GFFLD-GDLIEYN 229
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1202-1396 |
2.08e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.84 E-value: 2.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1202 LRHINVTINGGEKVGIVGRTGAGKSslTL-----GLFRINEsaeGEIIIDG--INIAkiGLHD-LRFKITIIPQDPVLFs 1273
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKS--TLmkilyGLYQPDS---GEILIDGkpVRIR--SPRDaIALGIGMVHQHFMLV- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1274 gslrmnlDPFSQYsdEEVWTSLE--------LAHLKDFVSAL---------PDKLDHEcaeggenLSVGQRQLVCLARAL 1336
Cdd:COG3845 93 -------PNLTVA--ENIVLGLEptkggrldRKAARARIRELserygldvdPDAKVED-------LSVGEQQRVEILKAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549096 1337 LRKTKILVLDEATaAV--DLETDDLIQsTIRtQF--EDCTVLTIAHRLNTIMDYT-RVIVLDKGE 1396
Cdd:COG3845 157 YRGARILILDEPT-AVltPQEADELFE-ILR-RLaaEGKSIIFITHKLREVMAIAdRVTVLRRGK 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1201-1410 |
2.37e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.88 E-value: 2.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSltlgLFRI----NESAEGEIIIDGiniakiglhdlRFKITIIPQDPVLFSG-S 1275
Cdd:COG0488 13 LLDDVSLSINPGDRIGLVGRNGAGKST----LLKIlageLEPDSGEVSIPK-----------GLRIGYLPQEPPLDDDlT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1276 LRMNLdpfsQYSDEEVWTSL----ELAHLKDFVSALPDKLD---HECAEGGE--------------------------NL 1322
Cdd:COG0488 78 VLDTV----LDGDAELRALEaeleELEAKLAEPDEDLERLAelqEEFEALGGweaearaeeilsglgfpeedldrpvsEL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1323 SVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTqfEDCTVLTIAH-R--LNTIMdyTRVIVLDKGEIQE 1399
Cdd:COG0488 154 SGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKN--YPGTVLVVSHdRyfLDRVA--TRILELDRGKLTL 229
|
250
....*....|..
gi 2462549096 1400 Y-GAPSDLLQQR 1410
Cdd:COG0488 230 YpGNYSAYLEQR 241
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1185-1412 |
2.98e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 77.85 E-value: 2.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDLDfVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITI 1264
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1265 IPQDP--VLFS---------GSLRMNLDPfsQYSDEEVWTSLELAHLKDFvsalPDKLDHecaeggeNLSVGQRQLVCLA 1333
Cdd:PRK13647 84 VFQDPddQVFSstvwddvafGPVNMGLDK--DEVERRVEEALKAVRMWDF----RDKPPY-------HLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1334 RALLRKTKILVLDEATAAVDLETDDLIQSTI-RTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPS-----DL 1406
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILdRLHNQGKTVIVATHDVDLAAEWAdQVIVLKEGRVLAEGDKSlltdeDI 230
|
....*.
gi 2462549096 1407 LQQRGL 1412
Cdd:PRK13647 231 VEQAGL 236
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1201-1409 |
3.72e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 77.12 E-value: 3.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLtLGLFrineSAE-----GEIIIDGINIAKIGLHDLRFKITIIPQDPVL-FSG 1274
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTL-LRAL----SGElspdsGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1275 S----LRMNLDPFSQYSDE------EVWTSLELAHLKD-FVSALpdkldhecaEGGEnlsvgqRQLVCLARALLR----- 1338
Cdd:PRK13548 92 TveevVAMGRAPHGLSRAEddalvaAALAQVDLAHLAGrDYPQL---------SGGE------QQRVQLARVLAQlwepd 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549096 1339 -KTKILVLDEATAAVDL----ETDDLIQStiRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLLQQ 1409
Cdd:PRK13548 157 gPPRWLLLDEPTSALDLahqhHVLRLARQ--LAHERGLAVIVVLHDLNLAARYAdRIVLLHQGRLVADGTPAEVLTP 231
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1198-1407 |
3.80e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 79.31 E-value: 3.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1198 LDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIG---LHDLRFK--------ITIIP 1266
Cdd:PRK10070 40 LSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaeLREVRRKkiamvfqsFALMP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1267 QDPVLFSGSLRMNLDPF-SQYSDEEVWTSLELAHLKDFVSALPDKldhecaeggenLSVGQRQLVCLARALLRKTKILVL 1345
Cdd:PRK10070 120 HMTVLDNTAFGMELAGInAEERREKALDALRQVGLENYAHSYPDE-----------LSGGMRQRVGLARALAINPDILLM 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549096 1346 DEATAAVD--LET---DDLIQSTIRTQFedcTVLTIAHRLNTIMDY-TRVIVLDKGEIQEYGAPSDLL 1407
Cdd:PRK10070 189 DEAFSALDplIRTemqDELVKLQAKHQR---TIVFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1201-1407 |
3.98e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 76.88 E-value: 3.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINE-----SAEGEIIIDGINIAKIGLHDLRFKITIIPQDP------ 1269
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnpipnl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1270 -VLFSGSLRMNLDPFSQYSDE---EVWTSLELAHLKDFVSalpDKLDhecAEGGEnLSVGQRQLVCLARALLRKTKILVL 1345
Cdd:PRK14247 98 sIFENVALGLKLNRLVKSKKElqeRVRWALEKAQLWDEVK---DRLD---APAGK-LSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549096 1346 DEATAAVDLETDDLIQSTIRTQFEDCTVLTIAH---RLNTIMDYtrVIVLDKGEIQEYGAPSDLL 1407
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqQAARISDY--VAFLYKGQIVEWGPTREVF 233
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1201-1406 |
8.07e-15 |
|
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: 79.08 E-value: 8.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLtLGLFRINESAE---GEII--------------------------------- 1244
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMDQYEptsGRIIyhvalcekcgyverpskvgepcpvcggtlepee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1245 IDGINIAKIGLHDLRFKITIIPQDPVLFSGSLR-----MNLDPFSQYS-DEEVWTSLELAHLKdfvsalpdKLDHECAEG 1318
Cdd:TIGR03269 94 VDFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTvldnvLEALEEIGYEgKEAVGRAVDLIEMV--------QLSHRITHI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1319 GENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIR--TQFEDCTVLTIAHRLNTIMDYT-RVIVLDKG 1395
Cdd:TIGR03269 166 ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEeaVKASGISMVLTSHWPEVIEDLSdKAIWLENG 245
|
250
....*....|.
gi 2462549096 1396 EIQEYGAPSDL 1406
Cdd:TIGR03269 246 EIKEEGTPDEV 256
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
612-747 |
9.14e-15 |
|
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: 75.29 E-value: 9.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 612 LNGITFSIPEGALVAVVGQVGCGKSSLLSAL-----LAEMDKVEGHVAIKGVN--------------------------- 659
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDiydldvdvlelrrrvgmvfqkpnpfpg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 ----------------------------------------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAh 693
Cdd:cd03260 96 siydnvayglrlhgiklkeelderveealrkaalwdevkdrlhalgLSGGQQQRLCLARALANEPEVLLLDEPTSALDP- 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549096 694 VGKHIFENVIgpKGMLKNKTRILVTHSMsylPQV----DVIIVMSGGKISEMGSYQEL 747
Cdd:cd03260 175 ISTAKIEELI--AELKKEYTIVIVTHNM---QQAarvaDRTAFLLNGRLVEFGPTEQI 227
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1192-1365 |
1.09e-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: 74.32 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1192 LRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSL--TL-GLFRineSAEGEIIIDGINIAKIglhdlrfkiTIIPQD 1268
Cdd:TIGR01189 6 LACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLlrILaGLLR---PDSGEVRWNGTPLAEQ---------RDEPHE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1269 PVLFSG---------SLRMNLD---PFSQYSDEEVWTSLELAHLKDFvSALPdkldheCAEggenLSVGQRQLVCLARAL 1336
Cdd:TIGR01189 74 NILYLGhlpglkpelSALENLHfwaAIHGGAQRTIEDALAAVGLTGF-EDLP------AAQ----LSAGQQRRLALARLW 142
|
170 180
....*....|....*....|....*....
gi 2462549096 1337 LRKTKILVLDEATAAVDLETDDLIQSTIR 1365
Cdd:TIGR01189 143 LSRRPLWILDEPTTALDKAGVALLAGLLR 171
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
940-1347 |
1.09e-14 |
|
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: 78.69 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 940 LHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVD---SMIPEVIKMFMgslfnVIGACIVIL--LATPIAAIIIPPL 1014
Cdd:COG4615 83 LRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISqafVRLPELLQSVA-----LVLGCLAYLawLSPPLFLLTLVLL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1015 GLIyFFVQRFYVASSRQLKRLESVSRSPVYSHFNetllgvSVIRAFEE----QER--FIHQSDLKV------DENQKAYY 1082
Cdd:COG4615 158 GLG-VAGYRLLVRRARRHLRRAREAEDRLFKHFR------ALLEGFKElklnRRRrrAFFDEDLQPtaeryrDLRIRADT 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1083 PSIVANRWlavrlecvGNCIvLFAALFAVIsrhslsAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNI----------VA 1152
Cdd:COG4615 231 IFALANNW--------GNLL-FFALIGLIL------FLLPALGWADPAVLSGFVLVLLFLRGPLSQLVgalptlsranVA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1153 VERLKEYSETEKEAPWQIQETAPPSSWPQVGRVEFRNYCLRYREDLD---FVLRHINVTINGGEKVGIVGRTGAGKSSLT 1229
Cdd:COG4615 296 LRKIEELELALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGdegFTLGPIDLTIRRGELVFIVGGNGSGKSTLA 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1230 ---LGLFRineSAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGslrmNLDPFSQYSDEEVwtsleLAHLKDFvsa 1306
Cdd:COG4615 376 kllTGLYR---PESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDR----LLGLDGEADPARA-----RELLERL--- 440
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2462549096 1307 lpdKLDHECA-EGGE----NLSVGQRQLVCLARALLRKTKILVLDE 1347
Cdd:COG4615 441 ---ELDHKVSvEDGRfsttDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1185-1409 |
1.20e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 75.88 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDLDfVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--INIAKIGLHDLRFKI 1262
Cdd:PRK13639 2 LETRDLKYSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1263 TIIPQDP--VLFS---------GSLRMNLdpfsqySDEEVWTSLELAHLKDFVSALPDKLDHecaeggeNLSVGQRQLVC 1331
Cdd:PRK13639 81 GIVFQNPddQLFAptveedvafGPLNLGL------SKEEVEKRVKEALKAVGMEGFENKPPH-------HLSGGQKKRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1332 LARALLRKTKILVLDEATAAVD-LETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLLQQ 1409
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDpMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYAdKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1185-1407 |
1.25e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 75.90 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDLDF-VLRHINVTINGGEKVGIVGRTGAGKSS---LTLGLFrinESAEGEIIIDGINIAKIGLHDLRF 1260
Cdd:PRK13642 5 LEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTtarLIDGLF---EEFEGKVKIDGELLTAENVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1261 KITIIPQDP-VLFSGSLRMNLDPFSQYSD----EEVWTSLELAHLKdfvsalPDKLDHECAEGGEnLSVGQRQLVCLARA 1335
Cdd:PRK13642 82 KIGMVFQNPdNQFVGATVEDDVAFGMENQgiprEEMIKRVDEALLA------VNMLDFKTREPAR-LSGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549096 1336 LLRKTKILVLDEATAAVDLETDDLIQSTIRtQFED---CTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLL 1407
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIH-EIKEkyqLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
325-551 |
1.48e-14 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 76.05 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 325 FLMSFFFKAIHDLMMFSGPQILKLLIKFVndTKAPDWQGYFYTVLLFVTAC-LQTLVLHQYFHICFVSGMRIKTAVIGAV 403
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDV--IPAGDLSLLLWIALLLLLLAlLRALLSYLRRYLAARLGQRVVFDLRRDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 404 YRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATY-INMIWSAPLQVILALYLLWLNLGPSVLAGVAVMVLMVPVNAV 482
Cdd:cd07346 79 FRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSgLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRY 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462549096 483 MAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWE----LAFKDKVLAIRQEELKVLKKSAYLSAVGTF 551
Cdd:cd07346 159 FRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEereiERFREANRDLRDANLRAARLSALFSPLIGL 231
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
595-747 |
1.54e-14 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 74.46 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL------------------LAEMDKVEGHVAI- 655
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLtgelrptsgtayingysiRTDRKAARQSLGYc 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 656 ----------------------KGV---------------------------NLSGGQKQRVSLARAVYSNADIYLFDDP 686
Cdd:cd03263 81 pqfdalfdeltvrehlrfyarlKGLpkseikeevelllrvlgltdkankrarTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549096 687 LSAVDaHVGKHIFENVIgpKGMLKNKTRILVTHSM---SYLpqVDVIIVMSGGKISEMGSYQEL 747
Cdd:cd03263 161 TSGLD-PASRRAIWDLI--LEVRKGRSIILTTHSMdeaEAL--CDRIAIMSDGKLRCIGSPQEL 219
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
595-755 |
1.60e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 78.61 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTW-ARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALL------------------------------ 643
Cdd:TIGR00958 479 IEFQDVSFSYpNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQnlyqptggqvlldgvplvqydhhylhrqva 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 644 -----------------------AEMDKV--------------------EGHVAIKGVNLSGGQKQRVSLARAVYSNADI 680
Cdd:TIGR00958 559 lvgqepvlfsgsvreniaygltdTPDEEImaaakaanahdfimefpngyDTEVGEKGSQLSGGQKQRIAIARALVRKPRV 638
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549096 681 YLFDDPLSAVDAHVgkhifENVIGPKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFA 755
Cdd:TIGR00958 639 LILDEATSALDAEC-----EQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYK 708
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
601-750 |
1.79e-14 |
|
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: 74.54 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 601 TFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVAIKGV--------------------- 658
Cdd:cd03258 10 VFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIR-CINGLERpTSGSVLVDGTdltllsgkelrkarrrigmif 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 659 ---------------------------------------------------NLSGGQKQRVSLARAVYSNADIYLFDDPL 687
Cdd:cd03258 89 qhfnllssrtvfenvalpleiagvpkaeieervlellelvgledkadaypaQLSGGQKQRVGIARALANNPKVLLCDEAT 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 688 SAVDAHVGKHIFEnvigpkgMLK--NK----TRILVTHSMSYLPQV-DVIIVMSGGKISEMGSYQELLAR 750
Cdd:cd03258 169 SALDPETTQSILA-------LLRdiNRelglTIVLITHEMEVVKRIcDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1201-1407 |
2.15e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 75.11 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKI---GLHDLRFKITIIPQDPV------- 1270
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDSIsavnprk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1271 ----LFSGSLR--MNLDPfsqySDEEVWTSlELAHLKDFVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILV 1344
Cdd:PRK10419 107 tvreIIREPLRhlLSLDK----AERLARAS-EMLRAVDLDDSVLDKRPPQ-------LSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462549096 1345 LDEATAAVDLetddLIQSTI-------RTQFeDCTVLTIAHRLNTIMDY-TRVIVLDKGEIQEYGAPSDLL 1407
Cdd:PRK10419 175 LDEAVSNLDL----VLQAGVirllkklQQQF-GTACLFITHDLRLVERFcQRVMVMDNGQIVETQPVGDKL 240
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1201-1407 |
2.24e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.80 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLtlgLFRINES---AEGEIIIDGINIAKIGLHDLRFKITIIPQDPVL---FSG 1274
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTL---LRAINGTltpTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsfeFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1275 S--LRMNLDP----FSQYSDEEVwTSLELAHLKDFVSALPDKldhecaeGGENLSVGQRQLVCLARALLRKTKILVLDEA 1348
Cdd:PRK09536 95 RqvVEMGRTPhrsrFDTWTETDR-AAVERAMERTGVAQFADR-------PVTSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549096 1349 TAAVDL----ETDDLIQSTIRtqfEDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLL 1407
Cdd:PRK09536 167 TASLDInhqvRTLELVRRLVD---DGKTAVAAIHDLDLAARYCdELVLLADGRVRAAGPPADVL 227
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1183-1406 |
2.57e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 76.27 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1183 GRVEFRNYCLRYREDldFVLRHINVTINGGEKVGIVGRTGAGKSSLtL----GLFRINEsaeGEIIIDGINIAKIGLHDl 1258
Cdd:COG3839 2 ASLELENVSKSYGGV--EALKDIDLDIEDGEFLVLLGPSGCGKSTL-LrmiaGLEDPTS---GEILIGGRDVTDLPPKD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1259 RfKITIIPQDPVLF----------SGsLRM-NLDPfsqysDE------EVWTSLELAHLKDfvsALPDkldhecaeggeN 1321
Cdd:COG3839 75 R-NIAMVFQSYALYphmtvyeniaFP-LKLrKVPK-----AEidrrvrEAAELLGLEDLLD---RKPK-----------Q 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1322 LSVGQRQLVCLARALLRKTKILVLDEATAAVD----LETddliqstiRTQfedctvltIA---HRLNTIMDY-------- 1386
Cdd:COG3839 134 LSGGQRQRVALGRALVREPKVFLLDEPLSNLDaklrVEM--------RAE--------IKrlhRRLGTTTIYvthdqvea 197
|
250 260
....*....|....*....|....
gi 2462549096 1387 ----TRVIVLDKGEIQEYGAPSDL 1406
Cdd:COG3839 198 mtlaDRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1185-1406 |
2.71e-14 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 73.81 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYreDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHdlRFKITI 1264
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1265 IPQDPVLF---------SGSLRMNLDPfSQYSDEEVWTSLELAHLKDFVSALPDKLdhecaeggenlSVGQRQLVCLARA 1335
Cdd:cd03300 77 VFQNYALFphltvfeniAFGLRLKKLP-KAEIKERVAEALDLVQLEGYANRKPSQL-----------SGGQQQRVAIARA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1336 LLRKTKILVLDEATAAVD--------LETDDLIQSTirtqfeDCTVLTIAHRLN---TIMDytRVIVLDKGEIQEYGAPS 1404
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDlklrkdmqLELKRLQKEL------GITFVFVTHDQEealTMSD--RIAVMNKGKIQQIGTPE 216
|
..
gi 2462549096 1405 DL 1406
Cdd:cd03300 217 EI 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
595-750 |
3.11e-14 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 73.87 E-value: 3.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTWaRSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMDkvEGHVAIKGVN------------- 659
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMInrLIEPT--SGEIFIDGEDireqdpvelrrki 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 ----------------------------------------------------------LSGGQKQRVSLARAVYSNADIY 681
Cdd:cd03295 78 gyviqqiglfphmtveenialvpkllkwpkekireradellalvgldpaefadrypheLSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 682 LFDDPLSAVDAHVGKHIFENVIGPKGMLkNKTRILVTHSM-SYLPQVDVIIVMSGGKISEMGSYQELLAR 750
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQEL-GKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
861-1156 |
3.12e-14 |
|
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: 74.78 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 861 AIGLFISFLSIFLFMcnhvsalaSNYWLSLWT-DDPIVNGTQEHTKVRLSVYGALGISQGIAVFGYSMAVSIGGILASRC 939
Cdd:cd18542 2 LLAILALLLATALNL--------LIPLLIRRIiDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 940 LHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGAcIVILLA-----TPIAAIIIPPL 1014
Cdd:cd18542 74 LRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGA-LIIMFSinwklTLISLAIIPFI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1015 GLI-YFF---VQRFYVASSRQLKRLESVsrspvyshFNETLLGVSVIRAF----EEQERFIHQSDLKVDENQKA------ 1080
Cdd:cd18542 153 ALFsYVFfkkVRPAFEEIREQEGELNTV--------LQENLTGVRVVKAFaredYEIEKFDKENEEYRDLNIKLakllak 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1081 YYPSIVAnrwlavrLECVGNCIVLFAALFAVIsRHSLSAG-LVGLSvSYslqvTTYLNWLVRMS----SEMETNIVAVER 1155
Cdd:cd18542 225 YWPLMDF-------LSGLQIVLVLWVGGYLVI-NGEITLGeLVAFI-SY----LWMLIWPVRQLgrliNDMSRASASAER 291
|
.
gi 2462549096 1156 L 1156
Cdd:cd18542 292 I 292
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1204-1397 |
3.79e-14 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 72.91 E-value: 3.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1204 HINVTINGGEKVGIVGRTGAGKSSLtLGLFRINESAE-GEIIIDGINIAKIGLHDLrfKITIIPQDPVLFSG-------- 1274
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTL-LNLIAGFETPQsGRVLINGVDVTAAPPADR--PVSMLFQENNLFAHltveqnvg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1275 ---SLRMNLDPFSQysdEEVWTSLELAHLKDFVSALPDKldhecaeggenLSVGQRQLVCLARALLRKTKILVLDEATAA 1351
Cdd:cd03298 93 lglSPGLKLTAEDR---QAIEVALARVGLAGLEKRLPGE-----------LSGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462549096 1352 VD----LETDDLIqSTIRTQfEDCTVLTIAHRLNTIMD-YTRVIVLDKGEI 1397
Cdd:cd03298 159 LDpalrAEMLDLV-LDLHAE-TKMTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1185-1409 |
5.93e-14 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 75.13 E-value: 5.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDldFVLRHINVTINGGEKVGIVGRTGAGKSSLtL----GLFRINEsaeGEIIIDGINIAKIGLHDlRf 1260
Cdd:COG3842 6 LELENVSKRYGDV--TALDDVSLSIEPGEFVALLGPSGCGKTTL-LrmiaGFETPDS---GRILLDGRDVTGLPPEK-R- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1261 KITIIPQDPVLFS----------GsLRM-NLDPfsQYSDEEVWTSLELAHLKDFVSALPdkldHEcaeggenLSVGQRQL 1329
Cdd:COG3842 78 NVGMVFQDYALFPhltvaenvafG-LRMrGVPK--AEIRARVAELLELVGLEGLADRYP----HQ-------LSGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1330 VCLARALLRKTKILVLDEATAAVDLETddliqsTIRTQFEdctVLTIAHRLN--TIM------------DytRVIVLDKG 1395
Cdd:COG3842 144 VALARALAPEPRVLLLDEPLSALDAKL------REEMREE---LRRLQRELGitFIYvthdqeealalaD--RIAVMNDG 212
|
250
....*....|....
gi 2462549096 1396 EIQEYGAPSDLLQQ 1409
Cdd:COG3842 213 RIEQVGTPEEIYER 226
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1201-1401 |
6.29e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 72.31 E-value: 6.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRF---------KITIIPQdpVL 1271
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYlpeerglypKMKVIDQ--LV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1272 FSGSLR-MNLDPFSQYSDEevW-TSLELAHLKDfvsalpDKLdhecaeggENLSVGQRQLVCLARALLRKTKILVLDEAT 1349
Cdd:cd03269 93 YLAQLKgLKKEEARRRIDE--WlERLELSEYAN------KRV--------EELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462549096 1350 AAVDLETDDLIQSTIRTQFED-CTVLTIAHRLNTIMDY-TRVIVLDKGEIQEYG 1401
Cdd:cd03269 157 SGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1201-1416 |
8.47e-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: 76.87 E-value: 8.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGiniakiglhdlrfKITIIPQDPVLFSGSLRMNL 1280
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1281 dPFSQYSDEEVWTSLELA-HLKDFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD-D 1358
Cdd:TIGR01271 508 -IFGLSYDEYRYTSVIKAcQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEkE 586
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549096 1359 LIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSDLLQQRGLFYSM 1416
Cdd:TIGR01271 587 IFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSL 644
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
612-750 |
1.55e-13 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 71.63 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 612 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN-------------------------------- 659
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDvardpaevrrrigyvpqepalypdltvrenlr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 ------------------------------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGKHIFENVI 703
Cdd:COG1131 96 ffarlyglprkeareridellelfgltdaadrkvgtLSGGMKQRLGLALALLHDPELLILDEPTSGLDP-EARRELWELL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2462549096 704 gpKGMLK-NKTRILVTHSMSYLPQV-DVIIVMSGGKISEMGSYQELLAR 750
Cdd:COG1131 175 --RELAAeGKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
594-747 |
1.75e-13 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 71.60 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 594 SITVRNATFTWARSdpPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVAIKG--------------- 657
Cdd:cd03296 2 SIEVRNVSKRFGDF--VALDDVSLDIPSGELVALLGPSGSGKTTLLR-LIAGLERPdSGTILFGGedatdvpvqernvgf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 658 --------------------------------------VN------------------LSGGQKQRVSLARAVYSNADIY 681
Cdd:cd03296 79 vfqhyalfrhmtvfdnvafglrvkprserppeaeirakVHellklvqldwladrypaqLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462549096 682 LFDDPLSAVDAHVGKHIfenvigpKGMLK------NKTRILVTHSMSYLPQV-DVIIVMSGGKISEMGSYQEL 747
Cdd:cd03296 159 LLDEPFGALDAKVRKEL-------RRWLRrlhdelHVTTVFVTHDQEEALEVaDRVVVMNKGRIEQVGTPDEV 224
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1185-1422 |
2.08e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 72.43 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDLD----FVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIG-LHDLR 1259
Cdd:PRK13633 5 IKCKNVSYKYESNEEstekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1260 FKITIIPQDP------------VLFsGSLRMNLDPfsqysdEEVWTSLELAHLKDFVSALPDKLDHEcaeggenLSVGQR 1327
Cdd:PRK13633 85 NKAGMVFQNPdnqivativeedVAF-GPENLGIPP------EEIRERVDESLKKVGMYEYRRHAPHL-------LSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1328 QLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIR--TQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGAPSD 1405
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKelNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKE 230
|
250
....*....|....*..
gi 2462549096 1406 LLQQrglfYSMAKDAGL 1422
Cdd:PRK13633 231 IFKE----VEMMKKIGL 243
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1202-1409 |
2.66e-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: 71.91 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1202 LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLR----------F-KITIIPQDPV 1270
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRelrrkkismvFqSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1271 LFSGSLRMNLDPFSQYSDEEVWT-SLELAHLKDFVSALPDKLdhecaeggenlSVGQRQLVCLARALLRKTKILVLDEAT 1349
Cdd:cd03294 120 LENVAFGLEVQGVPRAEREERAAeALELVGLEGWEHKYPDEL-----------SGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462549096 1350 AAVDletddliqSTIRTQFEDC----------TVLTIAHRLNTIM---DytRVIVLDKGEIQEYGAPSDLLQQ 1409
Cdd:cd03294 189 SALD--------PLIRREMQDEllrlqaelqkTIVFITHDLDEALrlgD--RIAIMKDGRLVQVGTPEEILTN 251
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
612-738 |
2.73e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 71.63 E-value: 2.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 612 LNGITFSIPEGALVAVVGQVGCGKSSLL-----------------SALLAE--------------------MDKV----- 649
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLrllagletpsagellagTAPLAEaredtrlmfqdarllpwkkvIDNVglglk 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 650 -----EGHVAIKGVNL-----------SGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG---KHIFENVIGPKGMlk 710
Cdd:PRK11247 108 gqwrdAALQALAAVGLadranewpaalSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRiemQDLIESLWQQHGF-- 185
|
170 180
....*....|....*....|....*....
gi 2462549096 711 nkTRILVTHSMSYLPQV-DVIIVMSGGKI 738
Cdd:PRK11247 186 --TVLLVTHDVSEAVAMaDRVLLIEEGKI 212
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
864-1071 |
2.87e-13 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 72.07 E-value: 2.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 864 LFISFLSIFLfmcnhVSALASnywLSLWTDDPIVNGTQEHTKVRLSVYGALGI-----SQGIAVFG--YSMAVSIGGILA 936
Cdd:cd18552 1 LALAILGMIL-----VAATTA---ALAWLLKPLLDDIFVEKDLEALLLVPLAIiglflLRGLASYLqtYLMAYVGQRVVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 937 SrcLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLA----TPIAAIIIP 1012
Cdd:cd18552 73 D--LRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLdwklTLIALVVLP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549096 1013 PLGL-IYFFVQRFYVASSRQLKRLESVSrspvySHFNETLLGVSVIRAF----EEQERFIHQSD 1071
Cdd:cd18552 151 LAALpIRRIGKRLRKISRRSQESMGDLT-----SVLQETLSGIRVVKAFgaedYEIKRFRKANE 209
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1196-1409 |
2.87e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 70.77 E-value: 2.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1196 EDLDFVLRHI----NVTINGGEKVGIVGRTGAGKSSLtLGL---FRINESaeGEIIIDGINIAKiglhdlrfkiTIIPQD 1268
Cdd:PRK10771 5 TDITWLYHHLpmrfDLTVERGERVAILGPSGAGKSTL-LNLiagFLTPAS--GSLTLNGQDHTT----------TPPSRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1269 PV--------LFSG-SLRMN----LDPFSQYSDEEVWTSLELAH---LKDFVSALPDKLdhecaeggenlSVGQRQLVCL 1332
Cdd:PRK10771 72 PVsmlfqennLFSHlTVAQNiglgLNPGLKLNAAQREKLHAIARqmgIEDLLARLPGQL-----------SGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1333 ARALLRKTKILVLDEATAAVD----LETDDLIQSTIRTQfeDCTVLTIAHRLNTIMDY-TRVIVLDKGEIQEYGAPSDLL 1407
Cdd:PRK10771 141 ARCLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQER--QLTLLMVSHSLEDAARIaPRSLVVADGRIAWDGPTDELL 218
|
..
gi 2462549096 1408 QQ 1409
Cdd:PRK10771 219 SG 220
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1201-1408 |
2.95e-13 |
|
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: 71.03 E-value: 2.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSL---TLGLFRINEsaeGEIIIDGINIAKIGLHD-LRFKITIIPQDPVLFSG-S 1275
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTfymIVGLVKPDS---GKILLDGQDITKLPMHKrARLGIGYLPQEASIFRKlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1276 LRMNLDPF--SQYSDEEVWTSLELAHLKDFvsalpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1353
Cdd:cd03218 92 VEENILAVleIRGLSKKEREEKLEELLEEF------HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549096 1354 LETDDLIQSTIRTQFE-DCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLLQ 1408
Cdd:cd03218 166 PIAVQDIQKIIKILKDrGIGVLITDHNVRETLSITdRAYIIYEGKVLAEGTPEEIAA 222
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1201-1401 |
2.96e-13 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 70.64 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGiNIAKIglhdLRFKITIIPQ----DPVLFSGSL 1276
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVSSL----LGLGGGFNPEltgrENIYLNGRL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1277 rMNLDPfsQYSDEEVWTSLELAHLKDFVSaLPDKldhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET 1356
Cdd:cd03220 112 -LGLSR--KEIDEKIDEIIEFSELGDFID-LPVK----------TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2462549096 1357 DDLIQSTIRTQFEDC-TVLTIAHRLNTIMDY-TRVIVLDKGEIQEYG 1401
Cdd:cd03220 178 QEKCQRRLRELLKQGkTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1201-1406 |
3.17e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.93 E-value: 3.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIG-LHDLRFKITIIPQDPVLFSG-SLRM 1278
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQLGIYLVPQEPLLFPNlSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1279 NLD---PFSQYSDEEvwtslelahLKDFVSALPDKLDHECAEGgeNLSVGQRQLVCLARALLRKTKILVLDEATAAVD-L 1354
Cdd:PRK15439 106 NILfglPKRQASMQK---------MKQLLAALGCQLDLDSSAG--SLEVADRQIVEILRGLMRDSRILILDEPTASLTpA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462549096 1355 ETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDL 1406
Cdd:PRK15439 175 ETERLFSRIRELLAQGVGIVFISHKLPEIRQLAdRISVMRDGTIALSGKTADL 227
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1185-1415 |
3.28e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 72.95 E-value: 3.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYreDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHdlRFKITI 1264
Cdd:PRK11607 20 LEIRNLTKSF--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY--QRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1265 IPQDPVLF---------SGSLRMNLDPFSQYSDEeVWTSLELAHLKDFVSALPdkldHEcaeggenLSVGQRQLVCLARA 1335
Cdd:PRK11607 96 MFQSYALFphmtveqniAFGLKQDKLPKAEIASR-VNEMLGLVHMQEFAKRKP----HQ-------LSGGQRQRVALARS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1336 LLRKTKILVLDEATAAVDLETDDLIQSTIRTQFE--DCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLLQQRGL 1412
Cdd:PRK11607 164 LAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILErvGVTCVMVTHDQEEAMTMAgRIAIMNRGKFVQIGEPEEIYEHPTT 243
|
...
gi 2462549096 1413 FYS 1415
Cdd:PRK11607 244 RYS 246
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1185-1412 |
3.28e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 71.76 E-value: 3.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDLDfVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITI 1264
Cdd:PRK13652 4 IETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1265 IPQDP--VLFS---------GSLRMNLDPFS-QYSDEEVWTSLELAHLKDFVSalpdkldhecaeggENLSVGQRQLVCL 1332
Cdd:PRK13652 83 VFQNPddQIFSptveqdiafGPINLGLDEETvAHRVSSALHMLGLEELRDRVP--------------HHLSGGEKKRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1333 ARALLRKTKILVLDEATAAVDLE-TDDLIQSTIRTQFE-DCTVLTIAHRLNTI---MDYtrVIVLDKGEIQEYGAPSDLL 1407
Cdd:PRK13652 149 AGVIAMEPQVLVLDEPTAGLDPQgVKELIDFLNDLPETyGMTVIFSTHQLDLVpemADY--IYVMDKGRIVAYGTVEEIF 226
|
....*
gi 2462549096 1408 QQRGL 1412
Cdd:PRK13652 227 LQPDL 231
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1151-1353 |
3.29e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 74.24 E-value: 3.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1151 VAVERLKEYSETEKEAPWQIqeTAPPSSWPqvgRVEFRNYCLRYrEDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTL 1230
Cdd:PRK10522 294 VAFNKLNKLALAPYKAEFPR--PQAFPDWQ---TLELRNVTFAY-QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAM 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1231 GLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSgslRMnLDPFSQYSDEEV---WtsleLAHLKdfvsaL 1307
Cdd:PRK10522 368 LLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFD---QL-LGPEGKPANPALvekW----LERLK-----M 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1308 PDKLDHecaEGGE----NLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1353
Cdd:PRK10522 435 AHKLEL---EDGRisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQD 481
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
594-742 |
3.39e-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: 69.89 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 594 SITVRNATFT----WARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMDKVEGHVAIKGVN-------- 659
Cdd:cd03213 3 TLSFRNLTVTvkssPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPldkrsfrk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 -----------------------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEnvigpkgMLK 710
Cdd:cd03213 83 iigyvpqddilhptltvretlmfaaklrgLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS-------LLR 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462549096 711 -----NKTRILVTHSMSYL--PQVDVIIVMSGGKISEMG 742
Cdd:cd03213 156 rladtGRTIICSIHQPSSEifELFDKLLLLSQGRVIYFG 194
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
612-688 |
3.57e-13 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 68.44 E-value: 3.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 612 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGV--------------------------------- 658
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQdltdderkslrkeigyvfqdpqlfprltvrenl 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 659 ----------------------------------------NLSGGQKQRVSLARAVYSNADIYLFDDPLS 688
Cdd:pfam00005 81 rlglllkglskrekdaraeealeklglgdladrpvgerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
595-748 |
4.44e-13 |
|
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: 70.84 E-value: 4.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFtwARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN--------------- 659
Cdd:COG1120 2 LEAENLSV--GYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDlaslsrrelarriay 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 ----------------------------------------------------------LSGGQKQRVSLARAVYSNADIY 681
Cdd:COG1120 80 vpqeppapfgltvrelvalgryphlglfgrpsaedreaveealertglehladrpvdeLSGGERQRVLIARALAQEPPLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 682 LFDDPLSAVDAHvgkHIFEnvigpkgML---------KNKTRILVTHsmsYLPQV----DVIIVMSGGKISEMGSYQELL 748
Cdd:COG1120 160 LLDEPTSHLDLA---HQLE-------VLellrrlareRGRTVVMVLH---DLNLAaryaDRLVLLKDGRIVAQGPPEEVL 226
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1201-1408 |
4.50e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 70.69 E-value: 4.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHD-LRFKITIIPQDPVLFSG-SLRM 1278
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQEASIFRRlSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1279 NLDPFSQYSD-----------EEVWTSLELAHLKDFVsalpdkldhecaegGENLSVGQRQLVCLARALLRKTKILVLDE 1347
Cdd:PRK10895 98 NLMAVLQIRDdlsaeqredraNELMEEFHIEHLRDSM--------------GQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462549096 1348 ATAAVD-LETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEIQEYGAPSDLLQ 1408
Cdd:PRK10895 164 PFAGVDpISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVcERAYIVSQGHLIAHGTPTEILQ 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1185-1387 |
4.83e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 70.84 E-value: 4.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYreDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINEsAEGEIIIDG--------INIAKIGLH 1256
Cdd:PRK14258 8 IKVNNLSFYY--DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGrveffnqnIYERRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1257 DLRFKITIIPQDPVLFSGSLRMNLdpfsQYSDEEV-W-TSLEL-----AHLKDfvSALPDKLDHECAEGGENLSVGQRQL 1329
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNV----AYGVKIVgWrPKLEIddiveSALKD--ADLWDEIKHKIHKSALDLSGGQQQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462549096 1330 VCLARALLRKTKILVLDEATAAVD----LETDDLIQS-TIRTQFEDCTVLTIAHRLNTIMDYT 1387
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSlRLRSELTMVIVSHNLHQVSRLSDFT 221
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
612-750 |
5.22e-13 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 70.41 E-value: 5.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 612 LNGITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMDkvEGHVAIKGVN------------------------------ 659
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCInlLEEPD--SGTITVDGEDltdskkdinklrrkvgmvfqqfnlfphltv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 ------------------------------------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVD----AH 693
Cdd:COG1126 95 lenvtlapikvkkmskaeaeeramellervgladkadaypaqLSGGQQQRVAIARALAMEPKVMLFDEPTSALDpelvGE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462549096 694 VgkhifENVIgpK-----GMlknkTRILVTHSMSYLPQV-DVIIVMSGGKISEMGSYQELLAR 750
Cdd:COG1126 175 V-----LDVM--RdlakeGM----TMVVVTHEMGFAREVaDRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
595-740 |
6.87e-13 |
|
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: 69.77 E-value: 6.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTWARSDPPT--LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVAIKGVN------------ 659
Cdd:COG4181 9 IELRGLTKTVGTGAGELtiLKGISLEVEAGESVAIVGASGSGKSTLLG-LLAGLDRPtSGTVRLAGQDlfaldedararl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 -----------------------------------------------------------LSGGQKQRVSLARAVYSNADI 680
Cdd:COG4181 88 rarhvgfvfqsfqllptltalenvmlplelagrrdarararallervglghrldhypaqLSGGEQQRVALARAFATEPAI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549096 681 YLFDDPLSAVDAHVGKHI----FEnvigpkgmlKNKTR----ILVTHSMSYLPQVDVIIVMSGGKISE 740
Cdd:COG4181 168 LFADEPTGNLDAATGEQIidllFE---------LNRERgttlVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
612-738 |
7.15e-13 |
|
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: 69.10 E-value: 7.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 612 LNGITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMDkvEGHVAIKGVN------------------------------ 659
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCInlLEEPD--SGTIIIDGLKltddkkninelrqkvgmvfqqfnlfphltv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 ------------------------------------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKH 697
Cdd:cd03262 94 lenitlapikvkgmskaeaeeralellekvgladkadaypaqLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462549096 698 IFENV--IGPKGMlknkTRILVTHSMSYLPQV-DVIIVMSGGKI 738
Cdd:cd03262 174 VLDVMkdLAEEGM----TMVVVTHEMGFAREVaDRVIFMDDGRI 213
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1201-1412 |
7.44e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 70.04 E-value: 7.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSG-SLR-- 1277
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRel 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1278 --------MNL-DPFSQYSDEEVWTSLELAHlkdfVSALPDKLdhecaegGENLSVGQRQLVCLARALLRKTKILVLDEA 1348
Cdd:PRK11231 97 vaygrspwLSLwGRLSAEDNARVNQAMEQTR----INHLADRR-------LTDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549096 1349 TAAVDL----ETDDLIQstiRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLLQQRGL 1412
Cdd:PRK11231 166 TTYLDInhqvELMRLMR---ELNTQGKTVVTVLHDLNQASRYCdHLVVLANGHVMAQGTPEEVMTPGLL 231
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1201-1401 |
9.36e-13 |
|
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: 68.76 E-value: 9.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGeKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIaKIGLHDLRFKITIIPQDpvlFSGSLRMNL 1280
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV-LKQPQKLRRRIGYLPQE---FGVYPNFTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1281 DPFSQY-----------SDEEVWTSLELAHLKDFVSALPDKLdhecaeggenlSVGQRQLVCLARALLRKTKILVLDEAT 1349
Cdd:cd03264 90 REFLDYiawlkgipskeVKARVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462549096 1350 AAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNTIMD-YTRVIVLDKGEIQEYG 1401
Cdd:cd03264 159 AGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
595-750 |
1.18e-12 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 70.88 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTWARSDPPT--LNGITFSIPEGALVAVVGQVGCGKSSLL---SAL--------------LAEMDK------- 648
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIrciNLLerptsgsvlvdgvdLTALSErelraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 649 -----------------VEGHVA----IKGV---------------------------NLSGGQKQRVSLARAVYSNADI 680
Cdd:COG1135 82 rkigmifqhfnllssrtVAENVAlpleIAGVpkaeirkrvaellelvglsdkadaypsQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 681 YLFDDPLSAVDAHVGKHIFEnvigpkgMLK--NK----TRILVTHSMsylpqvDVI--I-----VMSGGKISEMGSYQEL 747
Cdd:COG1135 162 LLCDEATSALDPETTRSILD-------LLKdiNRelglTIVLITHEM------DVVrrIcdrvaVLENGRIVEQGPVLDV 228
|
...
gi 2462549096 748 LAR 750
Cdd:COG1135 229 FAN 231
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1185-1406 |
1.25e-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: 69.29 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYRedlDFV-LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAK-------IGL- 1255
Cdd:cd03296 3 IEVRNVSKRFG---DFVaLDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDvpvqernVGFv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1256 --HDLRFK-ITIIpqDPVLFSgsLRM---NLDPFSQYSDEEVWTSLELAHLKDFVSALPdkldhecaeggENLSVGQRQL 1329
Cdd:cd03296 80 fqHYALFRhMTVF--DNVAFG--LRVkprSERPPEAEIRAKVHELLKLVQLDWLADRYP-----------AQLSGGQRQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1330 VCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCTVLTI--AHRLNTIMDYT-RVIVLDKGEIQEYGAPSDL 1406
Cdd:cd03296 145 VALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVfvTHDQEEALEVAdRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
645-747 |
1.46e-12 |
|
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: 68.80 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 645 EMDKVEGHVAIKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVigpKGMLKN--KTRILVTH--- 719
Cdd:cd03300 116 DLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLEL---KRLQKElgITFVFVTHdqe 192
|
90 100 110
....*....|....*....|....*....|.
gi 2462549096 720 ---SMSylpqvDVIIVMSGGKISEMGSYQEL 747
Cdd:cd03300 193 ealTMS-----DRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1201-1397 |
1.56e-12 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 68.55 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLhDLRFKITIIPQDPVLFSG-SLRMN 1279
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPA-EARRRLGFVSDSTGLYDRlTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1280 LDPFSQYSdeevwtSLELAHLKDFVSALPDKLD--HECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD 1357
Cdd:cd03266 99 LEYFAGLY------GLKGDELTARLEELADRLGmeELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMAT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462549096 1358 DLIQSTIRTQFED-CTVLTIAHRLNTIMDYT-RVIVLDKGEI 1397
Cdd:cd03266 173 RALREFIRQLRALgKCILFSTHIMQEVERLCdRVVVLHRGRV 214
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1201-1407 |
1.59e-12 |
|
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: 68.86 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDL-RFKITIIPQDPVLFSG-SLRM 1278
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSlTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1279 NLD--PFSQYSDEEVWTSLELAH-----LKDFVSALpdkldhecaeGGeNLSVGQRQLVCLARALLRKTKILVLDEATAA 1351
Cdd:COG0410 98 NLLlgAYARRDRAEVRADLERVYelfprLKERRRQR----------AG-TLSGGEQQMLAIGRALMSRPKLLLLDEPSLG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462549096 1352 -----VDlETDDLIQsTIRTqfEDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLL 1407
Cdd:COG0410 167 lapliVE-EIFEIIR-RLNR--EGVTILLVEQNARFALEIAdRAYVLERGRIVLEGTAAELL 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
660-749 |
2.13e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 68.62 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH-VGKHIfeNVIgpKGMLKNK-TRILVTHSMSYLPQV-DVIIVMSGG 736
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPElVGEVL--NTI--RQLAQEKrTMVIVTHEMSFARDVaDRAIFMDQG 220
|
90
....*....|...
gi 2462549096 737 KISEMGSYQELLA 749
Cdd:PRK11264 221 RIVEQGPAKALFA 233
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1185-1409 |
2.37e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 70.13 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDLdfVLRHINVTINGGEKVGIVGRTGAGKSS---LTLGLfriNESAEGEIIIDGINIAK--IGLHDlr 1259
Cdd:PRK11432 7 VVLKNITKRFGSNT--VIDNLNLTIKQGTMVTLLGPSGCGKTTvlrLVAGL---EKPTEGQIFIDGEDVTHrsIQQRD-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1260 fkITIIPQDPVLFSG---------SLRMNLDPFSQYSdEEVWTSLELAHLKDFVSALPDKLdhecaeggenlSVGQRQLV 1330
Cdd:PRK11432 80 --ICMVFQSYALFPHmslgenvgyGLKMLGVPKEERK-QRVKEALELVDLAGFEDRYVDQI-----------SGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1331 CLARALLRKTKILVLDEATAAVDLETDDLIQSTIR---TQFeDCTVLTIAHrlntimDYTR-------VIVLDKGEIQEY 1400
Cdd:PRK11432 146 ALARALILKPKVLLFDEPLSNLDANLRRSMREKIRelqQQF-NITSLYVTH------DQSEafavsdtVIVMNKGKIMQI 218
|
....*....
gi 2462549096 1401 GAPSDLLQQ 1409
Cdd:PRK11432 219 GSPQELYRQ 227
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
559-720 |
2.80e-12 |
|
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: 71.24 E-value: 2.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 559 LASVSLKRLRIFLSH-EELEPDSIERRPVKD------GGGTNSITVRNATFTWArSDPPTLNGITFSIPEGALVAVVGQV 631
Cdd:TIGR02868 292 AAAQQLTRVRAAAERiVEVLDAAGPVAEGSApaagavGLGKPTLELRDLSAGYP-GAPPVLDGVSLDLPPGERVAILGPS 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 632 GCGKSSLLSALLAEMDKVEGHVAIKGVN---------------------------------------------------- 659
Cdd:TIGR02868 371 GSGKSTLLATLAGLLDPLQGEVTLDGVPvssldqdevrrrvsvcaqdahlfdttvrenlrlarpdatdeelwaalervgl 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 ---------------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPkgmLKNKTRILVT 718
Cdd:TIGR02868 451 adwlralpdgldtvlgeggarLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAA---LSGRTVVLIT 527
|
..
gi 2462549096 719 HS 720
Cdd:TIGR02868 528 HH 529
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1167-1401 |
3.04e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.89 E-value: 3.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1167 PWQIQETAPPSSWPQVGRVEF--RNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESaEGEII 1244
Cdd:PRK15134 265 PVPLPEPASPLLDVEQLQVAFpiRKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-QGEIW 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1245 IDGINIAKIG---LHDLRFKITIIPQDPvlfSGSL--RMNLDPFSQYSDEEVWTSLELAHLKDFVSALPDK--LDHEC-- 1315
Cdd:PRK15134 344 FDGQPLHNLNrrqLLPVRHRIQVVFQDP---NSSLnpRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEvgLDPETrh 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1316 ---AEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRT--QFEDCTVLTIAHRLNTIMDYT-RV 1389
Cdd:PRK15134 421 rypAE----FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSlqQKHQLAYLFISHDLHVVRALChQV 496
|
250
....*....|..
gi 2462549096 1390 IVLDKGEIQEYG 1401
Cdd:PRK15134 497 IVLRQGEVVEQG 508
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1201-1407 |
3.47e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 68.47 E-value: 3.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL 1280
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1281 DPFSQYSDEEVWTSLELAHLKDFVSAL-PDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD-- 1357
Cdd:PRK10253 102 VARGRYPHQPLFTRWRKEDEEAVTKAMqATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQid 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462549096 1358 --DLIQSTIRTQfeDCTVLTIAHRLNTIMDY-TRVIVLDKGEIQEYGAPSDLL 1407
Cdd:PRK10253 182 llELLSELNREK--GYTLAAVLHDLNQACRYaSHLIALREGKIVAQGAPKEIV 232
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1202-1353 |
4.73e-12 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 66.74 E-value: 4.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1202 LRHINVTINGGEKVGIVGRTGAGKSSL---TLGLFRINESAEGEIIIDGINIAKIGLHDLRfkITIIPQDPVLFS----- 1273
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLlaaIAGTLSPAFSASGEVLLNGRRLTALPAEQRR--IGILFQDDLLFPhlsvg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1274 GSLRMNLDPFSQYSD--EEVWTSLELAHLKDFVSALPDKLdhecaeggenlSVGQRQLVCLARALLRKTKILVLDEATAA 1351
Cdd:COG4136 95 ENLAFALPPTIGRAQrrARVEQALEEAGLAGFADRDPATL-----------SGGQRARVALLRALLAEPRALLLDEPFSK 163
|
..
gi 2462549096 1352 VD 1353
Cdd:COG4136 164 LD 165
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
595-756 |
4.98e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 68.12 E-value: 4.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSL---LSALLAEMD---KVEG----------------- 651
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLaklLNGLLLPEAgtiTVGGmvlseetvwdvrrqvgm 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 652 ------------------------------------HVAIKGVN-----------LSGGQKQRVSLARAVYSNADIYLFD 684
Cdd:PRK13635 86 vfqnpdnqfvgatvqddvafglenigvpreemvervDQALRQVGmedflnrephrLSGGQKQRVAIAGVLALQPDIIILD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549096 685 DPLSAVDAhVGKhifENVIGPKGMLKNKTRILV---THSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAE 756
Cdd:PRK13635 166 EATSMLDP-RGR---REVLETVRQLKEQKGITVlsiTHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGHMLQE 236
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
595-738 |
5.56e-12 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 66.38 E-value: 5.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNatFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN--------------- 659
Cdd:COG4619 1 LELEG--LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPlsampppewrrqvay 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 ----------------------------------------------------LSGGQKQRVSLARAVYSNADIYLFDDPL 687
Cdd:COG4619 79 vpqepalwggtvrdnlpfpfqlrerkfdreralellerlglppdildkpverLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462549096 688 SAVDAHvGKHIFENVIgpKGMLKNKTR--ILVTHSMSYLPQV-DVIIVMSGGKI 738
Cdd:COG4619 159 SALDPE-NTRRVEELL--REYLAEEGRavLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
612-747 |
6.90e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 68.59 E-value: 6.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 612 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVAIKG--------------------------------- 657
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLR-LVAGLEKpTEGQIFIDGedvthrsiqqrdicmvfqsyalfphmslgenvg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 658 -----------------------VNL-----------SGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVI 703
Cdd:PRK11432 101 yglkmlgvpkeerkqrvkealelVDLagfedryvdqiSGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462549096 704 GPKGMLkNKTRILVTHSMSYLPQV-DVIIVMSGGKISEMGSYQEL 747
Cdd:PRK11432 181 ELQQQF-NITSLYVTHDQSEAFAVsDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1201-1409 |
7.72e-12 |
|
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: 66.01 E-value: 7.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSL--TLGLFRINESAEGEIIIDGINIAKIGLHDlRFK--ITIIPQDPVLFSGsl 1276
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLakTIMGHPKYEVTEGEILFKGEDITDLPPEE-RARlgIFLAFQYPPEIPG-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1277 rmnldpfsqysdeevwtslelAHLKDFVSALpdkldhecaegGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET 1356
Cdd:cd03217 92 ---------------------VKNADFLRYV-----------NEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549096 1357 DDLIQSTIRT-QFEDCTVLTIAHRLNtIMDY---TRVIVLDKGEIQEYGaPSDLLQQ 1409
Cdd:cd03217 140 LRLVAEVINKlREEGKSVLIITHYQR-LLDYikpDRVHVLYDGRIVKSG-DKELALE 194
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1194-1399 |
8.97e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 66.28 E-value: 8.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1194 YREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFS 1273
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1274 GSLRMNLD-PF---SQYSDEEVWtsleLAHLKDFvsALPDK-LDHECAEggenLSVGQRQLVCLARALLRKTKILVLDEA 1348
Cdd:PRK10247 95 DTVYDNLIfPWqirNQQPDPAIF----LDDLERF--ALPDTiLTKNIAE----LSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549096 1349 TAAVD----LETDDLIQSTIRTQfeDCTVLTIAHRLNTIMDYTRVIVLDK--GEIQE 1399
Cdd:PRK10247 165 TSALDesnkHNVNEIIHRYVREQ--NIAVLWVTHDKDEINHADKVITLQPhaGEMQE 219
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1201-1401 |
1.45e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 66.19 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSL--TLGLFRINESAEgeiiidgINIAkiglhDLRFKITIIPQDPVLFSgsLRM 1278
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLlrVLNLLEMPRSGT-------LNIA-----GNHFDFSKTPSDKAIRE--LRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1279 NLD-PFSQY----------------------SDEEVWTS----LELAHLKDFVSALPdkldhecaeggENLSVGQRQLVC 1331
Cdd:PRK11124 83 NVGmVFQQYnlwphltvqqnlieapcrvlglSKDQALARaeklLERLRLKPYADRFP-----------LHLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462549096 1332 LARALLRKTKILVLDEATAAVDLETDDLIQSTIRT-QFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEIQEYG 1401
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDPEITAQIVSIIRElAETGITQVIVTHEVEVARKTaSRVVYMENGHIVEQG 223
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1199-1423 |
1.53e-11 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 67.82 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1199 DFVLRhINVTINGGEKVGIVGRTGAGKSSLtL----GLFRineSAEGEIIIDG---------INIA----KIGLhdlrfk 1261
Cdd:COG4148 13 GFTLD-VDFTLPGRGVTALFGPSGSGKTTL-LraiaGLER---PDSGRIRLGGevlqdsargIFLPphrrRIGY------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1262 itiIPQDPVLFSG-SLRMNLD--------PFSQYSDEEVWTSLELAHLkdfvsalpdkLDHecaeGGENLSVGQRQLVCL 1332
Cdd:COG4148 82 ---VFQEARLFPHlSVRGNLLygrkraprAERRISFDEVVELLGIGHL----------LDR----RPATLSGGERQRVAI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1333 ARALLRKTKILVLDEATAAVDLETDDLIQ---STIRTQFeDCTVLTIAHRLNTIM---DytRVIVLDKGEIQEYGAPSDL 1406
Cdd:COG4148 145 GRALLSSPRLLLMDEPLAALDLARKAEILpylERLRDEL-DIPILYVSHSLDEVArlaD--HVVLLEQGRVVASGPLAEV 221
|
250
....*....|....*...
gi 2462549096 1407 LQQRGLF-YSMAKDAGLV 1423
Cdd:COG4148 222 LSRPDLLpLAGGEEAGSV 239
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
598-738 |
1.73e-11 |
|
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: 65.57 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 598 RNATFTW-ARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALL--------------------------------- 643
Cdd:cd03248 15 QNVTFAYpTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLEnfyqpqggqvlldgkpisqyehkylhskvslvg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 644 --------------------AEMDKV-------EGHVAI-------------KGVNLSGGQKQRVSLARAVYSNADIYLF 683
Cdd:cd03248 95 qepvlfarslqdniayglqsCSFECVkeaaqkaHAHSFIselasgydtevgeKGSQLSGGQKQRVAIARALIRNPQVLIL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462549096 684 DDPLSAVDAHvGKHIFENVIgpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKI 738
Cdd:cd03248 175 DEATSALDAE-SEQQVQQAL--YDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1201-1397 |
1.87e-11 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 64.38 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHD-LRFKITIIPQDPvlfsgsLRMN 1279
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVPEDR------KREG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1280 LdpFSQYSdeeVWTSLELAHLkdfvsalpdkldhecaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDL 1359
Cdd:cd03215 89 L--VLDLS---VAENIALSSL---------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462549096 1360 IQSTIRTQFED-CTVLTIAHRLNTIM---DytRVIVLDKGEI 1397
Cdd:cd03215 143 IYRLIRELADAgKAVLLISSELDELLglcD--RILVMYEGRI 182
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
644-742 |
1.96e-11 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 64.97 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 644 AEMDKVEGHVAIKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGkhiFENVIGPKGMLKN--KTRILVTHSm 721
Cdd:cd03301 115 AELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLR---VQMRAELKRLQQRlgTTTIYVTHD- 190
|
90 100
....*....|....*....|....*..
gi 2462549096 722 sylpQV------DVIIVMSGGKISEMG 742
Cdd:cd03301 191 ----QVeamtmaDRIAVMNDGQIQQIG 213
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1185-1407 |
2.21e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 65.97 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNY--CLRYREDLdFVLRHINV------TINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGiniakiglH 1256
Cdd:PRK15112 5 LEVRNLskTFRYRTGW-FRRQTVEAvkplsfTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD--------H 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1257 DLRF--------KITIIPQDPV-----------LFSGSLRMNLDPFSQYSDEEVWTSL-ELAHLKDFVSALPdkldheca 1316
Cdd:PRK15112 76 PLHFgdysyrsqRIRMIFQDPStslnprqrisqILDFPLRLNTDLEPEQREKQIIETLrQVGLLPDHASYYP-------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1317 eggENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLetddliqsTIRTQFEDCTV-LTIAHRLNTI--------MDYT 1387
Cdd:PRK15112 148 ---HMLAPGQKQRLGLARALILRPKVIIADEALASLDM--------SMRSQLINLMLeLQEKQGISYIyvtqhlgmMKHI 216
|
250 260
....*....|....*....|..
gi 2462549096 1388 --RVIVLDKGEIQEYGAPSDLL 1407
Cdd:PRK15112 217 sdQVLVMHQGEVVERGSTADVL 238
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
658-749 |
2.27e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 65.76 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 658 VNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEnvIGPKGMLKNKTRILVTHSMSYLPQVDV-IIVMSGG 736
Cdd:PRK10619 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR--IMQQLAEEGKTMVVVTHEMGFARHVSShVIFLHQG 228
|
90
....*....|...
gi 2462549096 737 KISEMGSYQELLA 749
Cdd:PRK10619 229 KIEEEGAPEQLFG 241
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
590-747 |
2.37e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 65.93 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 590 GGTNSITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV---------------- 653
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitddnfeklr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 654 -------------------------------------------AIKGVN-----------LSGGQKQRVSLARAVYSNAD 679
Cdd:PRK13648 83 khigivfqnpdnqfvgsivkydvafglenhavpydemhrrvseALKQVDmleradyepnaLSGGQKQRVAIAGVLALNPS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549096 680 IYLFDDPLSAVDAHVGKHIFENVIGPKGMlKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQEL 747
Cdd:PRK13648 163 VIILDEATSMLDPDARQNLLDLVRKVKSE-HNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
611-738 |
2.77e-11 |
|
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: 64.59 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 611 TLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN------------------------------- 659
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPikakerrksigyvmqdvdyqlftdsvreell 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 --------------------------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH----VGKHIFEnvI 703
Cdd:cd03226 95 lglkeldagneqaetvlkdldlyalkerhplsLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKnmerVGELIRE--L 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 2462549096 704 GPKGmlknKTRILVTHSMSYLPQV-DVIIVMSGGKI 738
Cdd:cd03226 173 AAQG----KAVIVITHDYEFLAKVcDRVLLLANGAI 204
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1201-1392 |
2.80e-11 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 64.18 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII-DGINIAKIGLH---DLRFKITIIpqDPV---LFS 1273
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRaGGARVAYVPQRsevPDSLPLTVR--DLVamgRWA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1274 --GSLRmnldPFSQYSDEEVWTSLELAHLKDFVSAlpdKLDhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEATAA 1351
Cdd:NF040873 85 rrGLWR----RLTRDDRAAVDDALERVGLADLAGR---QLG--------ELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462549096 1352 VDLETDDLIQSTIRTQFED-CTVLTIAHRLNTIMDYTRVIVL 1392
Cdd:NF040873 150 LDAESRERIIALLAEEHARgATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1164-1401 |
3.88e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 66.27 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1164 KEAPWQiqetaPPSSWPQVGRVEFRNYclryredldfvlrhinvtinGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEI 1243
Cdd:PRK15079 24 KQWFWQ-----PPKTLKAVDGVTLRLY--------------------EGETLGVVGESGCGKSTFARAIIGLVKATDGEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1244 IIDGINIAKIG---LHDLRFKITIIPQDPvLFSGSLRMNL-----DPFSQY----SDEEVWTSLELAHLKdfVSALPDKL 1311
Cdd:PRK15079 79 AWLGKDLLGMKddeWRAVRSDIQMIFQDP-LASLNPRMTIgeiiaEPLRTYhpklSRQEVKDRVKAMMLK--VGLLPNLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1312 D---HEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLEtddlIQSTI-----RTQFE-DCTVLTIAHRLNT 1382
Cdd:PRK15079 156 NrypHE-------FSGGQCQRIGIARALILEPKLIICDEPVSALDVS----IQAQVvnllqQLQREmGLSLIFIAHDLAV 224
|
250 260
....*....|....*....|..
gi 2462549096 1383 ---IMDytRVIVLDKGEIQEYG 1401
Cdd:PRK15079 225 vkhISD--RVLVMYLGHAVELG 244
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1202-1409 |
4.10e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 65.57 E-value: 4.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1202 LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINI-AKIG---LHDLRFKITIIPQDP--VLFSGS 1275
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKdkyIRPVRKRIGMVFQFPesQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1276 L-----------RMNLDPFSQYSDEEVwtsLELAHLKDFVSALPDKldhecaeggenLSVGQRQLVCLARALLRKTKILV 1344
Cdd:PRK13646 103 VereiifgpknfKMNLDEVKNYAHRLL---MDLGFSRDVMSQSPFQ-----------MSGGQMRKIAIVSILAMNPDIIV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549096 1345 LDEATAAVDLETDDLIQSTIRT-QFEDC-TVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLLQQ 1409
Cdd:PRK13646 169 LDEPTAGLDPQSKRQVMRLLKSlQTDENkTIILVSHDMNEVARYAdEVIVMKEGSIVSQTSPKELFKD 236
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
595-692 |
4.39e-11 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 64.88 E-value: 4.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRN--ATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLS-------------------------------- 640
Cdd:COG4525 4 LTVRHvsVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNliagflapssgeitldgvpvtgpgadrgvvfq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 641 --ALLAEMDKVEgHVA----IKGVN---------------------------LSGGQKQRVSLARAVYSNADIYLFDDPL 687
Cdd:COG4525 84 kdALLPWLNVLD-NVAfglrLRGVPkaerraraeellalvgladfarrriwqLSGGMRQRVGIARALAADPRFLLMDEPF 162
|
....*
gi 2462549096 688 SAVDA 692
Cdd:COG4525 163 GALDA 167
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1202-1405 |
4.54e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 65.29 E-value: 4.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1202 LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLrfkITIIPQD-------PVLFSG 1274
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSeevdwsfPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1275 SLRMnldpfSQYSDEEvWTSLELAHLKDFVS---ALPDKLDHECAEGGEnLSVGQRQLVCLARALLRKTKILVLDEATAA 1351
Cdd:PRK15056 100 VVMM-----GRYGHMG-WLRRAKKRDRQIVTaalARVDMVEFRHRQIGE-LSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462549096 1352 VDLETDDLIQSTIRT-QFEDCTVLTIAHRLNTIMDYTRVIVLDKGEIQEYGaPSD 1405
Cdd:PRK15056 173 VDVKTEARIISLLRElRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG-PTE 226
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
864-1155 |
4.58e-11 |
|
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: 65.50 E-value: 4.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 864 LFISFLSIFLFMcnhVSALASNYWLSLWTDDpIVNGTQEHTKVRLS-VYGALGISQGIAVFG--------YSMAVSIGGI 934
Cdd:cd18547 1 LILVIILAIIST---LLSVLGPYLLGKAIDL-IIEGLGGGGGVDFSgLLRILLLLLGLYLLSalfsylqnRLMARVSQRT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 935 LASrcLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGAcIVILLAT--PIAAIIIP 1012
Cdd:cd18547 77 VYD--LRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGT-LIMMLYIspLLTLIVLV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1013 PLGLIYFFV-------QRFYVASSRQLKRLEsvsrspvySHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSI 1085
Cdd:cd18547 154 TVPLSLLVTkfiakrsQKYFRKQQKALGELN--------GYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQ 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462549096 1086 VANRWL--AVRLecVGN----CIVLFAALFAVisRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVER 1155
Cdd:cd18547 226 FYSGLLmpIMNF--INNlgyvLVAVVGGLLVI--NGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAER 297
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1201-1409 |
5.28e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 64.61 E-value: 5.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSgSLRMNL 1280
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVADKNQLRLLRT-RLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1281 DPFSQYSDEEVWTS----------LELAHLKDFVSALPDKLDHECAEGGE---NLSVGQRQLVCLARALLRKTKILVLDE 1347
Cdd:PRK10619 99 QHFNLWSHMTVLENvmeapiqvlgLSKQEARERAVKYLAKVGIDERAQGKypvHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549096 1348 ATAAVDLE-TDDLIQSTIRTQFEDCTVLTIAHRlntiMDYTR-----VIVLDKGEIQEYGAPSDLLQQ 1409
Cdd:PRK10619 179 PTSALDPElVGEVLRIMQQLAEEGKTMVVVTHE----MGFARhvsshVIFLHQGKIEEEGAPEQLFGN 242
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
660-759 |
5.92e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 64.34 E-value: 5.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVgKHIFENV---IGPKGMlknkTRILVTHSMSYLPQVDV-IIVMSG 735
Cdd:PRK09493 137 LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPEL-RHEVLKVmqdLAEEGM----TMVIVTHEIGFAEKVASrLIFIDK 211
|
90 100
....*....|....*....|....*.
gi 2462549096 736 GKISEMGSYQELLAR--DGAFAEFLR 759
Cdd:PRK09493 212 GRIAEDGDPQVLIKNppSQRLQEFLQ 237
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1200-1397 |
6.12e-11 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 63.34 E-value: 6.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1200 FVLRHINVTINGGEKVGIVGRTGAGKSSL--TLGLFRINESAEGEIIIDGINiakIGLHDLRFKITIIPQDPVLFsGSL- 1276
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLlnALAGRRTGLGVSGEVLINGRP---LDKRSFRKIIGYVPQDDILH-PTLt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1277 -RMNLDpFSqysdeevwtslelAHLKdfvsalpdkldhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1355
Cdd:cd03213 99 vRETLM-FA-------------AKLR-------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462549096 1356 TDDLIQSTIRtQFED--CTVLTIAHRLNTIMDYT--RVIVLDKGEI 1397
Cdd:cd03213 146 SALQVMSLLR-RLADtgRTIICSIHQPSSEIFELfdKLLLLSQGRV 190
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
595-703 |
7.53e-11 |
|
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: 63.27 E-value: 7.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFtwARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN--------------- 659
Cdd:COG4133 3 LEAENLSC--RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPirdaredyrrrlayl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 ---------------------------------------------------LSGGQKQRVSLARAVYSNADIYLFDDPLS 688
Cdd:COG4133 81 ghadglkpeltvrenlrfwaalyglradreaidealeavglagladlpvrqLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170
....*....|....*
gi 2462549096 689 AVDAHvGKHIFENVI 703
Cdd:COG4133 161 ALDAA-GVALLAELI 174
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
646-746 |
8.48e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 65.35 E-value: 8.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 646 MDKVEGHVAIKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHifenvigpkgM---LK------NKTRIL 716
Cdd:PRK09452 131 MVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQ----------MqneLKalqrklGITFVF 200
|
90 100 110
....*....|....*....|....*....|....*.
gi 2462549096 717 VTH------SMSylpqvDVIIVMSGGKISEMGSYQE 746
Cdd:PRK09452 201 VTHdqeealTMS-----DRIVVMRDGRIEQDGTPRE 231
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1191-1401 |
8.53e-11 |
|
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: 63.08 E-value: 8.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1191 CLRYREDLDFVLRHINVTINGgEKVGIVGRTGAGKSSL---TLGLFRINEsaeGEIIIDGINI----AKIGLHDLRFKIT 1263
Cdd:cd03297 3 CVDIEKRLPDFTLKIDFDLNE-EVTGIFGASGAGKSTLlrcIAGLEKPDG---GTIVLNGTVLfdsrKKINLPPQQRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1264 IIPQDPVLFSG-SLRMNL--------DPFSQYSDEEVWTSLELAHLKDfvsALPDKLdhecaeggenlSVGQRQLVCLAR 1334
Cdd:cd03297 79 LVFQQYALFPHlNVRENLafglkrkrNREDRISVDELLDLLGLDHLLN---RYPAQL-----------SGGEKQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1335 ALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFED--CTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYG 1401
Cdd:cd03297 145 ALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNlnIPVIFVTHDLSEAEYLAdRIVVMEDGRLQYIG 214
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1201-1397 |
8.78e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 63.93 E-value: 8.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIdginiAKIGLHDLRFKITIIPQDPVLF-------- 1272
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLA-----GTAPLAEAREDTRLMFQDARLLpwkkvidn 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1273 -----SGSLRmnldpfsqysdEEVWTSLELAHLKDFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDE 1347
Cdd:PRK11247 102 vglglKGQWR-----------DAALQALAAVGLADRANEWP-----------AALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549096 1348 ATAAVD----LETDDLIQSTIRTQ-FedcTVLTIAHRLN---TIMDytRVIVLDKGEI 1397
Cdd:PRK11247 160 PLGALDaltrIEMQDLIESLWQQHgF---TVLLVTHDVSeavAMAD--RVLLIEEGKI 212
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1201-1409 |
9.23e-11 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 65.17 E-value: 9.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLtL----GLfrinESA-EGEIIIDGiNIAKIGLHDLRFKITIIPQDPVLFS-- 1273
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTL-LriiaGL----ETPdSGRIVLNG-RDLFTNLPPRERRVGFVFQHYALFPhm 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1274 --------GsLRMnLDPFSQYSDEEVWTSLELAHLKDFVSALPDkldhecaeggeNLSVGQRQLVCLARALLRKTKILVL 1345
Cdd:COG1118 91 tvaeniafG-LRV-RPPSKAEIRARVEELLELVQLEGLADRYPS-----------QLSGGQRQRVALARALAVEPEVLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549096 1346 DEATAAVDletddliqSTIRTQFE----------DCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLLQQ 1409
Cdd:COG1118 158 DEPFGALD--------AKVRKELRrwlrrlhdelGGTTVFVTHDQEEALELAdRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1212-1401 |
9.26e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.42 E-value: 9.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1212 GEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIG---LHDLRFKITIIPQDPVlfsgslrMNLDPFSQ--Y 1286
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPY-------ASLDPRQTvgD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1287 SDEE---VWTSLE-------LAHLKDFVSALPD---KLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1353
Cdd:PRK10261 423 SIMEplrVHGLLPgkaaaarVAWLLERVGLLPEhawRYPHE-------FSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462549096 1354 LET-DDLIQSTIRTQFE-DCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYG 1401
Cdd:PRK10261 496 VSIrGQIINLLLDLQRDfGIAYLFISHDMAVVERIShRVAVMYLGQIVEIG 546
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1201-1409 |
9.39e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 63.56 E-value: 9.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSL--TLGlfRINESAEGEIIIDGiNIAKI-----GLH-DL--RfkitiipqDPV 1270
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLlkLIA--GILEPTSGRVEVNG-RVSALlelgaGFHpELtgR--------ENI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1271 LFSGSLrMNLDPfSQYSD--EEVwtsLELAHLKDFVSaLPDKldhecaeggeNLSVGQRqlvclAR-----ALLRKTKIL 1343
Cdd:COG1134 110 YLNGRL-LGLSR-KEIDEkfDEI---VEFAELGDFID-QPVK----------TYSSGMR-----ARlafavATAVDPDIL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462549096 1344 VLDEATAAVDLE----TDDLIQSTIRtqfEDCTVLTIAHRLNTIMDY-TRVIVLDKGEIQEYGAPSDLLQQ 1409
Cdd:COG1134 169 LVDEVLAVGDAAfqkkCLARIRELRE---SGRTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
659-750 |
9.78e-11 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 65.12 E-value: 9.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 659 NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI---FENvigpkgmLKNKTRI---LVTHSMsylPQV----D 728
Cdd:COG4148 133 TLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEIlpyLER-------LRDELDIpilYVSHSL---DEVarlaD 202
|
90 100
....*....|....*....|..
gi 2462549096 729 VIIVMSGGKISEMGSYQELLAR 750
Cdd:COG4148 203 HVVLLEQGRVVASGPLAEVLSR 224
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
595-738 |
1.02e-10 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 63.54 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTWArSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN--------------- 659
Cdd:COG3638 3 LELRNLSKRYP-GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDvtalrgralrrlrrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 -----------------------------------------------------------------LSGGQKQRVSLARAV 674
Cdd:COG3638 82 igmifqqfnlvprlsvltnvlagrlgrtstwrsllglfppedreralealervgladkayqradqLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549096 675 YSNADIYLFDDPLSAVDAHVGKHIFEnvigpkgMLK------NKTRILVTHsmsylpQVDV-------IIVMSGGKI 738
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTARQVMD-------LLRriaredGITVVVNLH------QVDLarryadrIIGLRDGRV 225
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1201-1387 |
1.25e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.59 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSL---TLGLFrinESAEGEIIidginiakiglHDLRFKITIIPQ----DPVL-F 1272
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLvrvVLGLV---APDEGVIK-----------RNGKLRIGYVPQklylDTTLpL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1273 SGSLRMNLDPFSQYSD-EEVWTSLELAHLKDFVSalpdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAA 1351
Cdd:PRK09544 85 TVNRFLRLRPGTKKEDiLPALKRVQAGHLIDAPM--------------QKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2462549096 1352 VD----LETDDLIQStIRTQFeDCTVLTIAHRLNTIMDYT 1387
Cdd:PRK09544 151 VDvngqVALYDLIDQ-LRREL-DCAVLMVSHDLHLVMAKT 188
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
660-758 |
1.37e-10 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 63.12 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhvgkHIFENVIgpkGMLK------NKTRILVTHSMS-YLPQVDVIIV 732
Cdd:cd03299 130 LSGGEQQRVAIARALVVNPKILLLDEPFSALDV----RTKEKLR---EELKkirkefGVTVLHVTHDFEeAWALADKVAI 202
|
90 100
....*....|....*....|....*...
gi 2462549096 733 MSGGKISEMGSYQELLAR--DGAFAEFL 758
Cdd:cd03299 203 MLNGKLIQVGKPEEVFKKpkNEFVAEFL 230
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1203-1393 |
1.47e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.13 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1203 RHINVTINGGEKVGIVGRTGAGKSSL--TL-GLFRineSAEGEIIIDGINIAKIG---LHDLrfkitiipqdpvLFSG-- 1274
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLlrILaGLAR---PDAGEVLWQGEPIRRQRdeyHQDL------------LYLGhq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1275 -----------SLRMNLDPFSQYSDEEVWTSLELAHLKDFvsalpdkLDHECAeggeNLSVGQRQLVCLARALLRKTKIL 1343
Cdd:PRK13538 83 pgikteltaleNLRFYQRLHGPGDDEALWEALAQVGLAGF-------EDVPVR----QLSAGQQRRVALARLWLTRAPLW 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462549096 1344 VLDEATAAVDLETDDLIQSTIRTQFED--CTVLTIAHRLNTIMDYTRVIVLD 1393
Cdd:PRK13538 152 ILDEPFTAIDKQGVARLEALLAQHAEQggMVILTTHQDLPVASDKVRKLRLG 203
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
911-1082 |
1.50e-10 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 64.03 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 911 YGALGISQGIAVFGYSMAVSIGGILASRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSL 990
Cdd:cd18577 53 FVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 991 FNVIGACIV----------ILLATpiaaiiIPPLGLIYFFVQRFYV-ASSRQLKRLESVSrspvySHFNETLLGVSVIRA 1059
Cdd:cd18577 133 STFIAGFIIafiyswkltlVLLAT------LPLIAIVGGIMGKLLSkYTKKEQEAYAKAG-----SIAEEALSSIRTVKA 201
|
170 180
....*....|....*....|...
gi 2462549096 1060 FEEQERFIHQSDLKVDENQKAYY 1082
Cdd:cd18577 202 FGGEEKEIKRYSKALEKARKAGI 224
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
660-747 |
1.56e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 64.72 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPKGMLKNkTRILVTHSMSYLPQV-DVIIVMSGGKI 738
Cdd:PRK10851 137 LSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKF-TSVFVTHDQEEAMEVaDRVVVMSQGNI 215
|
....*....
gi 2462549096 739 SEMGSYQEL 747
Cdd:PRK10851 216 EQAGTPDQV 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1152-1400 |
1.61e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 65.47 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1152 AVERLKEYSETEKEAPWQIQETAPPSSWPQVgrVEFRNYCLRYREDLdfVLRHINVTINGGEKVGIVGRTGAGKSSltlg 1231
Cdd:COG0488 285 ALEKLEREEPPRRDKTVEIRFPPPERLGKKV--LELEGLSKSYGDKT--LLDDLSLRIDRGDRIGLIGPNGAGKST---- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1232 LFRI----NESAEGEIIIdGINIakiglhdlrfKITIIPQDPVLFSGSLRMnLDPFSQYSDEevWTSLEL-AHLKDFvsa 1306
Cdd:COG0488 357 LLKLlageLEPDSGTVKL-GETV----------KIGYFDQHQEELDPDKTV-LDELRDGAPG--GTEQEVrGYLGRF--- 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1307 L--PDKLDHECaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETddliqstiRTQFEDC------TVLTIAH 1378
Cdd:COG0488 420 LfsGDDAFKPV----GVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET--------LEALEEAlddfpgTVLLVSH 487
|
250 260
....*....|....*....|....*
gi 2462549096 1379 -R--LNTIMDytRVIVLDKGEIQEY 1400
Cdd:COG0488 488 dRyfLDRVAT--RILEFEDGGVREY 510
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1192-1412 |
1.73e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 63.49 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1192 LRYREDLdfVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--INIAKIGLHDLRFKITIIPQDP 1269
Cdd:PRK13638 9 FRYQDEP--VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1270 vlfsgslrmNLDPFSQYSDEEVWTSL--------ELAHLKDFVSALPDKlDHECAEGGENLSVGQRQLVCLARALLRKTK 1341
Cdd:PRK13638 87 ---------EQQIFYTDIDSDIAFSLrnlgvpeaEITRRVDEALTLVDA-QHFRHQPIQCLSHGQKKRVAIAGALVLQAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549096 1342 ILVLDEATAAVDLE-TDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAP------SDLLQQRGL 1412
Cdd:PRK13638 157 YLLLDEPTAGLDPAgRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISdAVYVLRQGQILTHGAPgevfacTEAMEQAGL 235
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1201-1407 |
1.75e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 63.14 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGI------NIAKIGLHDLRFKITIIPQDPVLFSG 1274
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1275 -SLRMNLD-PFSQY---SDEEVWTSLELAHLK-DFVSALPDKLDHECAEggenLSVGQRQLVCLARALLRKTKILVLDEA 1348
Cdd:PRK14246 105 lSIYDNIAyPLKSHgikEKREIKKIVEECLRKvGLWKEVYDRLNSPASQ----LSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462549096 1349 TAAVDLETDDLIQSTIRTQFEDCTVLTIAH---RLNTIMDYtrVIVLDKGEIQEYGAPSDLL 1407
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEIAIVIVSHnpqQVARVADY--VAFLYNGELVEWGSSNEIF 240
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1155-1409 |
1.85e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 64.08 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1155 RLKEYSETEKEAPWQIQETAPPSSWPQVGRVEFRNYCLRYREDLdfVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFR 1234
Cdd:PRK13536 12 RRLELSPIERKHQGISEAKASIPGSMSTVAIDLAGVSKSYGDKA--VVNGLSFTVASGECFGLLGPNGAGKSTIARMILG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1235 INESAEGEIIIDGINI-AKIGLhdLRFKITIIPQ-DPVLFSGSLRMNLDPFSQY------SDEEVWTSL-ELAHLKDfvs 1305
Cdd:PRK13536 90 MTSPDAGKITVLGVPVpARARL--ARARIGVVPQfDNLDLEFTVRENLLVFGRYfgmstrEIEAVIPSLlEFARLES--- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1306 alpdKLDHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQF-EDCTVLTIAHrlntIM 1384
Cdd:PRK13536 165 ----KADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTH----FM 232
|
250 260 270
....*....|....*....|....*....|
gi 2462549096 1385 DYT-----RVIVLDKGEIQEYGAPSDLLQQ 1409
Cdd:PRK13536 233 EEAerlcdRLCVLEAGRKIAEGRPHALIDE 262
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
591-751 |
1.89e-10 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 62.69 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 591 GTNSITVRNATFtwARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN----------- 659
Cdd:COG1127 2 SEPMIEVRNLTK--SFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDitglsekelye 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 --------------------------------------------------------------LSGGQKQRVSLARAVYSN 677
Cdd:COG1127 80 lrrrigmlfqggalfdsltvfenvafplrehtdlseaeirelvleklelvglpgaadkmpseLSGGMRKRVALARALALD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 678 ADIYLFDDPLSAVDAhVGKHIFENVIgpkgmLK-----NKTRILVTHSMSYLPQV-DVIIVMSGGKISEMGSYQELLARD 751
Cdd:COG1127 160 PEILLYDEPTAGLDP-ITSAVIDELI-----RElrdelGLTSVVVTHDLDSAFAIaDRVAVLADGKIIAEGTPEELLASD 233
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1201-1407 |
2.03e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 62.85 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSL--TLGLFRINESAE---GEIIIDG---INIAKIGLHDLRFKITIIPQDpvlf 1272
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLlrCINLLEQPEAGTirvGDITIDTarsLSQQKGLIRQLRQHVGFVFQN---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1273 sgslrMNLDPFSqysdeevwTSLE---------LAHLKDFVSALPDKLDHECA-EGGEN-----LSVGQRQLVCLARALL 1337
Cdd:PRK11264 94 -----FNLFPHR--------TVLEniiegpvivKGEPKEEATARARELLAKVGlAGKETsyprrLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462549096 1338 RKTKILVLDEATAAVDLETDDLIQSTIRTQFEDC-TVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLL 1407
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARDVAdRAIFMDQGRIVEQGPAKALF 232
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1205-1409 |
2.16e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 63.98 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1205 INVTINGGEKVGIVGRTGAGKSSLT---LGLFRINESAEGEIIIDG---INIAKIGLHDLRF-KITIIPQDPVlfsgslr 1277
Cdd:PRK09473 35 LNFSLRAGETLGIVGESGSGKSQTAfalMGLLAANGRIGGSATFNGreiLNLPEKELNKLRAeQISMIFQDPM------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1278 MNLDPFSQYSDE--EVwtsLELAHLKDFVSALPDK---LD---------------HEcaeggenLSVGQRQLVCLARALL 1337
Cdd:PRK09473 108 TSLNPYMRVGEQlmEV---LMLHKGMSKAEAFEESvrmLDavkmpearkrmkmypHE-------FSGGMRQRVMIAMALL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1338 RKTKILVLDEATAAVDLEtddlIQSTIRTQFED------CTVLTIAHRLNT---IMDytRVIVLDKGEIQEYGAPSDLLQ 1408
Cdd:PRK09473 178 CRPKLLIADEPTTALDVT----VQAQIMTLLNElkrefnTAIIMITHDLGVvagICD--KVLVMYAGRTMEYGNARDVFY 251
|
.
gi 2462549096 1409 Q 1409
Cdd:PRK09473 252 Q 252
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
864-1122 |
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 2462549096 864 LFISFLSIFLFMcnhVSALASNYWLSLWTDDPIVNGTQEHTKVRLSVYGALGISQGIAVFG--YSMAVSIGGILASrcLH 941
Cdd:cd18545 2 LLLALLLMLLST---AASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLriYLMAKVGQRILYD--LR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 942 VDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGAcIVILLA-----TPIAAIIIPPLGL 1016
Cdd:cd18545 77 QDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGI-VIIMFSlnvrlALVTLAVLPLLVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1017 IYFFVQRFyvasSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANR--WLAVR 1094
Cdd:cd18545 156 VVFLLRRR----ARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNAlfWPLVE 231
|
250 260
....*....|....*....|....*....
gi 2462549096 1095 L-ECVGNCIVLFAALFAVISrHSLSAGLV 1122
Cdd:cd18545 232 LiSALGTALVYWYGGKLVLG-GAITVGVL 259
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1186-1409 |
2.31e-10 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 65.09 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1186 EFRNYCLRYREDLDF--VLRHINVTINGGEKVGIVGRTGAGKS--SL-TLGLF-RINESAEGEIIIDGINIAKIGLHDLR 1259
Cdd:COG4172 8 SVEDLSVAFGQGGGTveAVKGVSFDIAAGETLALVGESGSGKSvtALsILRLLpDPAAHPSGSILFDGQDLLGLSERELR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1260 ----FKITIIPQDPvlfsgslrMN-LDPfsqysdeeVWT-------SLELaHLKdfVSA---------------LPD--- 1309
Cdd:COG4172 88 rirgNRIAMIFQEP--------MTsLNP--------LHTigkqiaeVLRL-HRG--LSGaaararalellervgIPDper 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1310 KLD---HEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLetddliqsTIRTQF----------EDCTVLTI 1376
Cdd:COG4172 149 RLDaypHQ-------LSGGQRQRVMIAMALANEPDLLIADEPTTALDV--------TVQAQIldllkdlqreLGMALLLI 213
|
250 260 270
....*....|....*....|....*....|....
gi 2462549096 1377 AHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLLQQ 1409
Cdd:COG4172 214 THDLGVVRRFAdRVAVMRQGEIVEQGPTAELFAA 247
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1202-1384 |
2.51e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.57 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1202 LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRI--NESAEGEIIIDGINIAKIGLHDLRFK-ITIIPQDPVL------- 1271
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQASNIRDTERAgIAIIHQELALvkelsvl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1272 ---FSGSL-----RMNLDpfSQYSDEEVWtsleLAHLKdfvsalpdkLDHECAEGGENLSVGQRQLVCLARALLRKTKIL 1343
Cdd:PRK13549 101 eniFLGNEitpggIMDYD--AMYLRAQKL----LAQLK---------LDINPATPVGNLGLGQQQLVEIAKALNKQARLL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2462549096 1344 VLDEATAAV-DLETDDLIqSTIRT-QFEDCTVLTIAHRLNTIM 1384
Cdd:PRK13549 166 ILDEPTASLtESETAVLL-DIIRDlKAHGIACIYISHKLNEVK 207
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1199-1366 |
2.81e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.43 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1199 DFVLRHINVTINGGEKVGIVGRTGAGKSSL--TL-GLFRInesAEGEIIIDGiniAKIGLHDLRFKITII-PQD---PVL 1271
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLlrLIaGLLPP---AAGTIKLDG---GDIDDPDVAEACHYLgHRNamkPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1272 fsgSLRMNLDpF-------SQYSDEEVWTSLELAHLKDfvsaLPdkldhecaegGENLSVGQRQLVCLARALLRKTKILV 1344
Cdd:PRK13539 89 ---TVAENLE-FwaaflggEELDIAAALEAVGLAPLAH----LP----------FGYLSAGQKRRVALARLLVSNRPIWI 150
|
170 180
....*....|....*....|..
gi 2462549096 1345 LDEATAAVDLETDDLIQSTIRT 1366
Cdd:PRK13539 151 LDEPTAALDAAAVALFAELIRA 172
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
593-747 |
3.19e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 62.90 E-value: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 593 NSITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSS---LLSALLAEMDKVEGHVAIKGV----------- 658
Cdd:PRK13640 4 NIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGItltaktvwdir 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 659 -----------------------------------------------------------NLSGGQKQRVSLARAVYSNAD 679
Cdd:PRK13640 84 ekvgivfqnpdnqfvgatvgddvafglenravprpemikivrdvladvgmldyidsepaNLSGGQKQRVAIAGILAVEPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549096 680 IYLFDDPLSAVDAHVGKHIFENVIGPKGMlKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQEL 747
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKLKKK-NNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
660-738 |
3.47e-10 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 61.54 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVgKHIFENVIgpKGMLK--NKTRILVTHSMSYLPQV-DVIIVMSGG 736
Cdd:cd03297 132 LSGGEKQRVALARALAAQPELLLLDEPFSALDRAL-RLQLLPEL--KQIKKnlNIPVIFVTHDLSEAEYLaDRIVVMEDG 208
|
..
gi 2462549096 737 KI 738
Cdd:cd03297 209 RL 210
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1202-1387 |
3.68e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 62.49 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1202 LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINE-----SAEGEIIIDGINI--AKIGLHDLRFKITIIPQDPVLFSG 1274
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1275 SLRMNL------DPFSQYSDEEVWTSLELAHLKDFVSalpDKLDhecaEGGENLSVGQRQLVCLARALLRKTKILVLDEA 1348
Cdd:PRK14243 106 SIYDNIaygariNGYKGDMDELVERSLRQAALWDEVK---DKLK----QSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462549096 1349 TAAVDLETDDLIQSTIRTQFEDCTVLTIAHRLNT---IMDYT 1387
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQYTIIIVTHNMQQaarVSDMT 220
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
872-1155 |
4.02e-10 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 62.56 E-value: 4.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 872 FLFMCnhVSALAS---NYWLSLWTDDPIVNGTQEHTKVRLSVYGALGISQGIAVF--GYSMAVsIGGILASRcLHVDLLH 946
Cdd:cd18572 2 FVFLV--VAALSElaiPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGlrGGCFSY-AGTRLVRR-LRRDLFR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 947 SILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATP----IAAIIIPPLGLIYFFVQ 1022
Cdd:cd18572 78 SLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWrltlLAFITVPVIALITKVYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1023 RFYvassRQLKRLESVSRSPVYSHFNETLLGVSVIRAF--EEQE--RFIHQSDLKVDENQK---AYypsiVANRWLAVRL 1095
Cdd:cd18572 158 RYY----RKLSKEIQDALAEANQVAEEALSNIRTVRSFatEEREarRYERALDKALKLSVRqalAY----AGYVAVNTLL 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1096 ECVGNCIVLFAALFAVISrHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVER 1155
Cdd:cd18572 230 QNGTQVLVLFYGGHLVLS-GRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEK 288
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1185-1401 |
4.32e-10 |
|
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: 61.12 E-value: 4.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDLdfVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDlRfKITI 1264
Cdd:cd03301 1 VELENVTKRFGNVT--ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-R-DIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1265 IPQDPVLF---------SGSLRMNLDPFSQYSD--EEVWTSLELAHLkdfvsalpdkLDHECAEggenLSVGQRQLVCLA 1333
Cdd:cd03301 77 VFQNYALYphmtvydniAFGLKLRKVPKDEIDErvREVAELLQIEHL----------LDRKPKQ----LSGGQRQRVALG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1334 RALLRKTKILVLDEATAAVDLetddLIQSTIRTQFEdctvlTIAHRLNTIMDY------------TRVIVLDKGEIQEYG 1401
Cdd:cd03301 143 RAIVREPKVFLMDEPLSNLDA----KLRVQMRAELK-----RLQQRLGTTTIYvthdqveamtmaDRIAVMNDGQIQQIG 213
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1201-1401 |
4.40e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 61.78 E-value: 4.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLTLG---LFRINESA--EGEIIIDGINI--AKIGLHDLRFKITIIPQDPVLF- 1272
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrLLELNEEArvEGEVRLFGRNIysPDVDPIEVRREVGMVFQYPNPFp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1273 ------SGSLRMNLDPFSQySDEEVWTSLELAHLKdfvSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLD 1346
Cdd:PRK14267 99 hltiydNVAIGVKLNGLVK-SKKELDERVEWALKK---AALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549096 1347 EATAAVDLETDDLIQSTIRTQFEDCTVLTIAH---RLNTIMDYTRVIVLdkGEIQEYG 1401
Cdd:PRK14267 175 EPTANIDPVGTAKIEELLFELKKEYTIVLVTHspaQAARVSDYVAFLYL--GKLIEVG 230
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1201-1405 |
4.53e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 63.43 E-value: 4.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLtLGLFRINESA-EGEIIIDGINIAKIGLHDlRFKITIIPQ----------DP 1269
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTV-LRLIAGFETPdSGRIMLDGQDITHVPAEN-RHVNTVFQSyalfphmtvfEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1270 VLFSgsLRMNLDPFSQYsDEEVWTSLELAHLKDFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEAT 1349
Cdd:PRK09452 107 VAFG--LRMQKTPAAEI-TPRVMEALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPKVLLLDESL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462549096 1350 AAVDLETDDLIQSTIRT-QFE-DCTVLTIAHRLN---TIMDytRVIVLDKGEIQEYGAPSD 1405
Cdd:PRK09452 173 SALDYKLRKQMQNELKAlQRKlGITFVFVTHDQEealTMSD--RIVVMRDGRIEQDGTPRE 231
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
612-750 |
4.61e-10 |
|
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: 62.76 E-value: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 612 LNGITFSIPEGALVAVVGQVGCGKSSLLSA---LLAEMDKVEGHVAIKGVN----------------------------- 659
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAilgLLPPPGITSGEILFDGEDllklsekelrkirgreiqmifqdpmtsln 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 --------------------------------------------------LSGGQKQRVSLARAVYSNADIYLFDDPLSA 689
Cdd:COG0444 101 pvmtvgdqiaeplrihgglskaeareraiellervglpdperrldrypheLSGGMRQRVMIARALALEPKLLIADEPTTA 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549096 690 VDAHVGKHIFEnvigpkgMLK------NKTRILVTHSMSYLPQV-DVIIVMSGGKISEMGSYQELLAR 750
Cdd:COG0444 181 LDVTIQAQILN-------LLKdlqrelGLAILFITHDLGVVAEIaDRVAVMYAGRIVEEGPVEELFEN 241
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
619-766 |
4.76e-10 |
|
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: 60.28 E-value: 4.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 619 IPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG---------VNLSGGQKQRVSLARAVYSNADIYLFDDPLSA 689
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGitpvykpqyIDLSGGELQRVAIAAALLRNATFYLFDEPSAY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 690 VDAHVGKHIfENVIGPKGMLKNKTRILVTHSMSYLPQV-DVIIVMSGgkisEMGSYQELLARDG---AFAEFLRTYASTE 765
Cdd:cd03222 102 LDIEQRLNA-ARAIRRLSEEGKKTALVVEHDLAVLDYLsDRIHVFEG----EPGVYGIASQPKGtreGINRFLRGYLITF 176
|
.
gi 2462549096 766 Q 766
Cdd:cd03222 177 R 177
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1201-1408 |
6.57e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 61.73 E-value: 6.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQD-PVLFSGSLRM- 1278
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQlPAAEGMTVREl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1279 ----------NLDPFSQYSDEEVWTSLELAHLKDFVSALPDkldhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEA 1348
Cdd:PRK10575 106 vaigrypwhgALGRFGAADREKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWIAMLVAQDSRCLLLDEP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549096 1349 TAAVDL----ETDDLIQSTirTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLLQ 1408
Cdd:PRK10575 175 TSALDIahqvDVLALVHRL--SQERGLTVIAVLHDINMAARYCdYLVALRGGEMIAQGTPAELMR 237
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
594-746 |
6.64e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 61.99 E-value: 6.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 594 SITVRNATFTWARSDP---PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN----------- 659
Cdd:PRK13637 2 SIKIENLTHIYMEGTPfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDitdkkvklsdi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 ---------------------------------------------------------------LSGGQKQRVSLARAVYS 676
Cdd:PRK13637 82 rkkvglvfqypeyqlfeetiekdiafgpinlglseeeienrvkramnivgldyedykdkspfeLSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462549096 677 NADIYLFDDPLSAVDAHVGKHIFENVigpKGMLK--NKTRILVTHSMSYLPQ-VDVIIVMSGGKISEMGSYQE 746
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKI---KELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1201-1398 |
6.80e-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: 61.19 E-value: 6.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGI--------NIAKIGLHdLRFKITIIPQDPVLf 1272
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvpwkrrkkFLRRIGVV-FGQKTQLWWDLPVI- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1273 sGSLRMNLDPFSqysdeevwtsLELAHLKDFVSALPDKLD--HECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATA 1350
Cdd:cd03267 114 -DSFYLLAAIYD----------LPPARFKKRLDELSELLDleELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462549096 1351 AVDLETDDLIQSTIRTQFED--CTVLTIAHRLNTIMDY-TRVIVLDKGEIQ 1398
Cdd:cd03267 183 GLDVVAQENIRNFLKEYNRErgTTVLLTSHYMKDIEALaRRVLVIDKGRLL 233
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
659-750 |
7.43e-10 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 62.51 E-value: 7.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 659 NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEnvigpkgMLK--NK----TRILVTHSMSYLPQV-DVII 731
Cdd:PRK11153 140 QLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILE-------LLKdiNRelglTIVLITHEMDVVKRIcDRVA 212
|
90
....*....|....*....
gi 2462549096 732 VMSGGKISEMGSYQELLAR 750
Cdd:PRK11153 213 VIDAGRLVEQGTVSEVFSH 231
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
594-750 |
7.84e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 62.55 E-value: 7.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 594 SITVRNATFTWArSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVAIKG--VN----------- 659
Cdd:PRK11650 3 GLKLQAVRKSYD-GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLR-MVAGLERItSGEIWIGGrvVNelepadrdiam 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 ------------------------------------------------------LSGGQKQRVSLARAVYSNADIYLFDD 685
Cdd:PRK11650 81 vfqnyalyphmsvrenmayglkirgmpkaeieervaeaarileleplldrkpreLSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 686 PLSAVDAHVGKHifenvigpkgM---LK------NKTRILVTHSmsylpQV------DVIIVMSGGKISEMGSYQELLAR 750
Cdd:PRK11650 161 PLSNLDAKLRVQ----------MrleIQrlhrrlKTTSLYVTHD-----QVeamtlaDRVVVMNGGVAEQIGTPVEVYEK 225
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1202-1408 |
8.14e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 61.57 E-value: 8.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1202 LRHINVTINGGEKVGIVGRTGAGKSSL----------TLGLFRINEsaegEIIIDGINIAKigLHDLRFKITIIPQDP-- 1269
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLlqhlngllqpTSGTVTIGE----RVITAGKKNKK--LKPLRKKVGIVFQFPeh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1270 VLFSGSLR-------MNLDpfsqYSDEEvwtSLELA-HLKDFVSALPDKLDHECAEggenLSVGQRQLVCLARALLRKTK 1341
Cdd:PRK13634 97 QLFEETVEkdicfgpMNFG----VSEED---AKQKArEMIELVGLPEELLARSPFE----LSGGQMRRVAIAGVLAMEPE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462549096 1342 ILVLDEATAAVD----LETDDLIQSTIRTQfeDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLLQ 1408
Cdd:PRK13634 166 VLVLDEPTAGLDpkgrKEMMEMFYKLHKEK--GLTTVLVTHSMEDAARYAdQIVVMHKGTVFLQGTPREIFA 235
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
660-759 |
1.02e-09 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 61.12 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPKGMLKnKTRILVTHSMSYLPQV-DVIIVMSGGKI 738
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQ-KTIVFITHDLDEALRLgDRIAIMKDGRL 239
|
90 100
....*....|....*....|...
gi 2462549096 739 SEMGSYQELLAR--DGAFAEFLR 759
Cdd:cd03294 240 VQVGTPEEILTNpaNDYVREFFR 262
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
651-750 |
1.07e-09 |
|
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: 62.05 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 651 GHVAIKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI---FENvigpkgmLKNKTRI---LVTHSMSY 723
Cdd:TIGR02142 122 GHLLGRLPGrLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIlpyLER-------LHAEFGIpilYVSHSLQE 194
|
90 100
....*....|....*....|....*...
gi 2462549096 724 LPQV-DVIIVMSGGKISEMGSYQELLAR 750
Cdd:TIGR02142 195 VLRLaDRVVVLEDGRVAAAGPIAEVWAS 222
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1201-1408 |
1.14e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.00 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLtLGLF--RINESAE-------GEIIIDGINIAKIGLHDLRFKITIIPQ--DP 1269
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTL-LKALagDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQaaQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1270 VL-FSGSLRMNLDPF---------SQYSDEEVWTSLELAHlkdfvsalPDKLDhecAEGGENLSVGQRQLVCLARAL--- 1336
Cdd:PRK13547 95 AFaFSAREIVLLGRYpharragalTHRDGEIAWQALALAG--------ATALV---GRDVTTLSGGELARVQFARVLaql 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1337 ------LRKTKILVLDEATAAVDLETDDLIQSTIRTQFED--CTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLL 1407
Cdd:PRK13547 164 wpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwnLGVLAIVHDPNLAARHAdRIAMLADGAIVAHGAPADVL 243
|
.
gi 2462549096 1408 Q 1408
Cdd:PRK13547 244 T 244
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
893-1146 |
1.19e-09 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 60.96 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 893 DDPIVNGTQEHTKVRLSVYGALGISQGIAVFGYSMAVSIGGILASRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKEL 972
Cdd:cd18543 27 DGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 973 DTVD---SMIPevikMFMGSLFNVIGACIVILLATP----IAAIIIPPLGLI-YFFVQRFYVASSRQLKRLESVSrspvy 1044
Cdd:cd18543 107 SLVQrflAFGP----FLLGNLLTLVVGLVVMLVLSPplalVALASLPPLVLVaRRFRRRYFPASRRAQDQAGDLA----- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1045 SHFNETLLGVSVIRAF----EEQERFIHQSD-LKVDENQKAyypSIVANRWLAVR-LECVGNCIVLFAALFAVIsRHSLS 1118
Cdd:cd18543 178 TVVEESVTGIRVVKAFgrerRELDRFEAAARrLRATRLRAA---RLRARFWPLLEaLPELGLAAVLALGGWLVA-NGSLT 253
|
250 260
....*....|....*....|....*....
gi 2462549096 1119 AG-LVGLSvSYSlqvtTYLNWLVRMSSEM 1146
Cdd:cd18543 254 LGtLVAFS-AYL----TMLVWPVRMLGWL 277
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1185-1408 |
1.22e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 61.36 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDLdfVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHdLRFKITI 1264
Cdd:PRK13537 8 IDFRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH-ARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1265 IPQ----DPVLfsgSLRMNLDPFSQY-------SDEEVWTSLELAHLKDfvsalpdKLDHECAEggenLSVGQRQLVCLA 1333
Cdd:PRK13537 85 VPQfdnlDPDF---TVRENLLVFGRYfglsaaaARALVPPLLEFAKLEN-------KADAKVGE----LSGGMKRRLTLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1334 RALLRKTKILVLDEATAAVDLETDDLIQSTIRTQF-EDCTVLTIAH------RLntimdYTRVIVLDKGEIQEYGAPSDL 1406
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHfmeeaeRL-----CDRLCVIEEGRKIAEGAPHAL 225
|
..
gi 2462549096 1407 LQ 1408
Cdd:PRK13537 226 IE 227
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
612-742 |
1.61e-09 |
|
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: 58.49 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 612 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGH-----------VAIK--------GVN----------LSG 662
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLIsflpkfsrnklIFIDqlqflidvGLGyltlgqklstLSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 663 GQKQRVSLARAVYSNAD--IYLFDDPLSAVDaHVGKHIFENVIGPKGMLKNkTRILVTHSMSYLPQVDVIIVM------S 734
Cdd:cd03238 91 GELQRVKLASELFSEPPgtLFILDEPSTGLH-QQDINQLLEVIKGLIDLGN-TVILIEHNLDVLSSADWIIDFgpgsgkS 168
|
....*...
gi 2462549096 735 GGKISEMG 742
Cdd:cd03238 169 GGKVVFSG 176
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1185-1409 |
1.77e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.52 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDLDFVLR---HINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIG----LHD 1257
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASRalfDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1258 LRFKITIIPQDP--VLFSGSL-------RMNLDPFSQYSDEEVWTSLELAHL-KDFVSALPDKldhecaeggenLSVGQR 1327
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVlkdvafgPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFE-----------LSGGQM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1328 QLVCLARALLRKTKILVLDEATAAVD----LETDDLIQSTIRTqfeDCTVLTIAHRLNTIMDYTR-VIVLDKGEIQEYGA 1402
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDpkarIEMMQLFESIHQS---GQTVVLVTHLMDDVADYADyVYLLEKGHIISCGT 227
|
....*..
gi 2462549096 1403 PSDLLQQ 1409
Cdd:PRK13643 228 PSDVFQE 234
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
660-759 |
2.02e-09 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 59.64 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFE--NVIGPKGMlknkTRILVTHSMSYLPQV-DVIIVMSGG 736
Cdd:COG4161 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEiiRELSQTGI----TQVIVTHEVEFARKVaSQVVYMEKG 217
|
90 100
....*....|....*....|....*
gi 2462549096 737 KISEMGSyQELLA--RDGAFAEFLR 759
Cdd:COG4161 218 RIIEQGD-ASHFTqpQTEAFAHYLS 241
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1185-1356 |
2.09e-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: 59.37 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRY---REDLDfVLRHINVTINGGEKVGIVGRTGAGKSSLtLGLFRINESA-EGEIIIDGINIAKI---GLHD 1257
Cdd:COG4181 9 IELRGLTKTVgtgAGELT-ILKGISLEVEAGESVAIVGASGSGKSTL-LGLLAGLDRPtSGTVRLAGQDLFALdedARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1258 LRF-KITIIPQDPVLFsGSLRMnLdpfsqysdEEVWTSLELAHLKD-FVSA--------LPDKLDHECAEggenLSVGQR 1327
Cdd:COG4181 87 LRArHVGFVFQSFQLL-PTLTA-L--------ENVMLPLELAGRRDaRARArallervgLGHRLDHYPAQ----LSGGEQ 152
|
170 180
....*....|....*....|....*....
gi 2462549096 1328 QLVCLARALLRKTKILVLDEATAAVDLET 1356
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAAT 181
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
584-752 |
2.16e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 62.04 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 584 RPVKDGggtnSITVRNATFTWaRSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL--------------------- 642
Cdd:PRK10790 334 RPLQSG----RIDIDNVSFAY-RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLmgyypltegeirldgrplssl 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 643 ----------------------------------------------LAEM-----DKVEGHVAIKGVNLSGGQKQRVSLA 671
Cdd:PRK10790 409 shsvlrqgvamvqqdpvvladtflanvtlgrdiseeqvwqaletvqLAELarslpDGLYTPLGEQGNNLSVGQKQLLALA 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 672 RAVYSNADIYLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARD 751
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDSGTEQAIQQAL---AAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQ 565
|
.
gi 2462549096 752 G 752
Cdd:PRK10790 566 G 566
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
595-738 |
2.40e-09 |
|
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: 59.50 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTWARSDPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMDKVEGHV------------------- 653
Cdd:cd03256 1 IEVENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLngLVEPTSGSVLIdgtdinklkgkalrqlrrq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 654 ---------------AIKGVN--------------------------------------------LSGGQKQRVSLARAV 674
Cdd:cd03256 80 igmifqqfnlierlsVLENVLsgrlgrrstwrslfglfpkeekqralaalervglldkayqradqLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549096 675 YSNADIYLFDDPLSAVD---AHVGKHIFENvigpKGMLKNKTRILVTHsmsylpQVDV-------IIVMSGGKI 738
Cdd:cd03256 160 MQQPKLILADEPVASLDpasSRQVMDLLKR----INREEGITVIVSLH------QVDLareyadrIVGLKDGRI 223
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
660-749 |
2.45e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 59.85 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFeNVigpkgMLKNKTR-----ILVTHSMSYLPQV-DVIIVM 733
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQII-NL-----MLELQEKlgisyIYVSQHLGIVKHIsDKVLVM 223
|
90
....*....|....*.
gi 2462549096 734 SGGKISEMGSYQELLA 749
Cdd:COG4167 224 HQGEVVEYGKTAEVFA 239
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1208-1385 |
2.97e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 60.36 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1208 TINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIA---KIGLHDLRFKITIIPQDPVlfsGSlrmnLDPFS 1284
Cdd:PRK11308 37 TLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadPEAQKLLRQKIQIVFQNPY---GS----LNPRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1285 QYSD--EE---VWTSLELAHLKDFVSALPDK--LDHECAEGGENL-SVGQRQLVCLARALLRKTKILVLDEATAAVDLet 1356
Cdd:PRK11308 110 KVGQilEEpllINTSLSAAERREKALAMMAKvgLRPEHYDRYPHMfSGGQRQRIAIARALMLDPDVVVADEPVSALDV-- 187
|
170 180
....*....|....*....|....*....
gi 2462549096 1357 ddliqsTIRTQFedctvltiahrLNTIMD 1385
Cdd:PRK11308 188 ------SVQAQV-----------LNLMMD 199
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
607-738 |
4.27e-09 |
|
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: 57.44 E-value: 4.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 607 SDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGV---------------------------- 658
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpvtrrsprdairagiayvpedrkreglv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 659 -------N------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDahVG--KHIFENVIGPKGmlKNKTRILVThsmSY 723
Cdd:cd03215 91 ldlsvaeNialsslLSGGNQQKVVLARWLARDPRVLILDEPTRGVD--VGakAEIYRLIRELAD--AGKAVLLIS---SE 163
|
170
....*....|....*....
gi 2462549096 724 LPQV----DVIIVMSGGKI 738
Cdd:cd03215 164 LDELlglcDRILVMYEGRI 182
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
592-750 |
4.93e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 58.97 E-value: 4.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 592 TNSITVRNATFTW-ARSDPPTLNGITFSIPEGALVAVVGQVGCGKSS-------LLSA----------LLAEMD------ 647
Cdd:PRK13650 2 SNIIEVKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTtvrlidgLLEAesgqiiidgdLLTEENvwdirh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 648 ----------------KVEGHVAI----KGV---------------------------NLSGGQKQRVSLARAVYSNADI 680
Cdd:PRK13650 82 kigmvfqnpdnqfvgaTVEDDVAFglenKGIpheemkervnealelvgmqdfkerepaRLSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 681 YLFDDPLSAVDahvgkhifenvigPKGMLK------------NKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELL 748
Cdd:PRK13650 162 IILDEATSMLD-------------PEGRLEliktikgirddyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELF 228
|
..
gi 2462549096 749 AR 750
Cdd:PRK13650 229 SR 230
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
594-747 |
5.03e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 60.04 E-value: 5.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 594 SITVRNATFTWArsDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLS--------------------------------- 640
Cdd:PRK11000 3 SVTLRNVTKAYG--DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRmiagleditsgdlfigekrmndvppaergvgmv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 641 ----AL---------------LAEMDKVE-----GHVAI----------KGVNLSGGQKQRVSLARAVYSNADIYLFDDP 686
Cdd:PRK11000 81 fqsyALyphlsvaenmsfglkLAGAKKEEinqrvNQVAEvlqlahlldrKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549096 687 LSAVDA--HVGKHIfenVIGPKGMLKNKTRILVTHSmsylpQV------DVIIVMSGGKISEMGSYQEL 747
Cdd:PRK11000 161 LSNLDAalRVQMRI---EISRLHKRLGRTMIYVTHD-----QVeamtlaDKIVVLDAGRVAQVGKPLEL 221
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
560-750 |
5.23e-09 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 60.58 E-value: 5.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 560 ASVSLKRL-RIFLSHEELEPDSIERRPVKDGGGTNSITVRNATFTWARSDPP---TLNGITFSIPEGALVAVVGQVGCGK 635
Cdd:COG4615 292 ANVALRKIeELELALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGDegfTLGPIDLTIRRGELVFIVGGNGSGK 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 636 SSLL---------------------------------SA-------------------------LLAEMdKVEGHVAIKG 657
Cdd:COG4615 372 STLAklltglyrpesgeilldgqpvtadnreayrqlfSAvfsdfhlfdrllgldgeadparareLLERL-ELDHKVSVED 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 658 -----VNLSGGQKQRVSLARAVYSNADIYLFD------DPlsavdahVGKHIFENVIGPkgMLK--NKTRILVTHSMSYL 724
Cdd:COG4615 451 grfstTDLSQGQRKRLALLVALLEDRPILVFDewaadqDP-------EFRRVFYTELLP--ELKarGKTVIAISHDDRYF 521
|
250 260
....*....|....*....|....*.
gi 2462549096 725 PQVDVIIVMSGGKISEMGSYQELLAR 750
Cdd:COG4615 522 DLADRVLKMDYGKLVELTGPAALAAS 547
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1201-1407 |
5.32e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 59.33 E-value: 5.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLT--LGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDP----VLFSG 1274
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIehLNALLLPDTGTIEWIFKDEKNKKKTKEKEKVLEKLVIQKTrfkkIKKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1275 SLRMNLD---PFSQY--------------------SDEEvwtSLELAhlKDFVSALpdKLDHECAEGGE-NLSVGQRQLV 1330
Cdd:PRK13651 102 EIRRRVGvvfQFAEYqlfeqtiekdiifgpvsmgvSKEE---AKKRA--AKYIELV--GLDESYLQRSPfELSGGQKRRV 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549096 1331 CLARALLRKTKILVLDEATAAVDLE-TDDLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLL 1407
Cdd:PRK13651 175 ALAGILAMEPDFLVFDEPTAGLDPQgVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTkRTIFFKDGKIIKDGDTYDIL 253
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
894-1140 |
5.71e-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: 58.96 E-value: 5.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 894 DPIVNGTQEHTKVRLSVYGALGISQGIAVFGYSMAVSIGGilASRclHV------DLLHSILRSPMSFFERTPSGNLVNR 967
Cdd:cd18541 27 DALTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFG--ASR--RIeydlrnDLFAHLLTLSPSFYQKNRTGDLMAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 968 FSKELDTVDSMIPEVIKMFMGSLFnVIGACIVILLAT--PIAAIIIPPLGLIYFFVQRFyvasSRQL-KRLESVSRSpvY 1044
Cdd:cd18541 103 ATNDLNAVRMALGPGILYLVDALF-LGVLVLVMMFTIspKLTLIALLPLPLLALLVYRL----GKKIhKRFRKVQEA--F 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1045 SHFN----ETLLGVSVIRAF----EEQERFIHQSDLKVDENQK------AYYPSIVanrwLAVRLecvGNCIVLFAALFA 1110
Cdd:cd18541 176 SDLSdrvqESFSGIRVIKAFvqeeAEIERFDKLNEEYVEKNLRlarvdaLFFPLIG----LLIGL---SFLIVLWYGGRL 248
|
250 260 270
....*....|....*....|....*....|.
gi 2462549096 1111 VIsRHSLSAG-LVglsvsyslQVTTYLNWLV 1140
Cdd:cd18541 249 VI-RGTITLGdLV--------AFNSYLGMLI 270
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
595-674 |
6.52e-09 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 58.59 E-value: 6.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTwaRSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVNLSGGQKQRVSLARAV 674
Cdd:COG4559 2 LEAENLSVR--LGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAV 79
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1199-1406 |
7.03e-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: 57.76 E-value: 7.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1199 DFV-LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKiGLHDLRFKITIIPQDPVLFSG-SL 1276
Cdd:cd03265 12 DFEaVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDElTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1277 RMNLDPFSQ---YSDEEvWTSlELAHLKDFVsALPDKLDHECAeggeNLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1353
Cdd:cd03265 91 WENLYIHARlygVPGAE-RRE-RIDELLDFV-GLLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549096 1354 LETDDLIQSTIRTQFE--DCTVLTIAHRL---NTIMDytRVIVLDKGEIQEYGAPSDL 1406
Cdd:cd03265 164 PQTRAHVWEYIEKLKEefGMTILLTTHYMeeaEQLCD--RVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1201-1392 |
7.73e-09 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 57.12 E-value: 7.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL 1280
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1281 DPFSQY-SDEEVWTSLELAHLKDFVsalpdklDHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDL 1359
Cdd:cd03231 95 RFWHADhSDEQVEEALARVGLNGFE-------DRPVAQ----LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180 190
....*....|....*....|....*....|....*
gi 2462549096 1360 IQSTIRTQFED--CTVLTIAHRLNTIMDYTRVIVL 1392
Cdd:cd03231 164 FAEAMAGHCARggMVVLTTHQDLGLSEAGARELDL 198
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1202-1397 |
7.73e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 58.49 E-value: 7.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1202 LRHINVTINGGEKVGIVGRTGAGKSSLTL---GLFRINESAEGEIIIDGINIAKIG--LHDLR----------------F 1260
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsGLITGDKSAGSHIELLGRTVQREGrlARDIRksrantgyifqqfnlvN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1261 KITIIPQDPVLFSGSL---RMNLDPFSQYSDEEVWTSLELAHLKDFVsalpdkldHECAEggeNLSVGQRQLVCLARALL 1337
Cdd:PRK09984 100 RLSVLENVLIGALGSTpfwRTCFSWFTREQKQRALQALTRVGMVHFA--------HQRVS---TLSGGQQQRVAIARALM 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462549096 1338 RKTKILVLDEATAAVDLETDDLIQSTIR--TQFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEI 1397
Cdd:PRK09984 169 QQAKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDYALRYcERIVALRQGHV 231
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
612-721 |
8.20e-09 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 58.12 E-value: 8.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 612 LNGITFSIPEGALVAVVGQVGCGKSSLLSAL-----LAEMDKVEGHVAIKGVN--------------------------- 659
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndLIPGARVEGEILLDGEDiydpdvdvvelrrrvgmvfqkpnpfpk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 ------------------------------------------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 691
Cdd:COG1117 107 siydnvayglrlhgikskseldeiveeslrkaalwdevkdrlkksalgLSGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
170 180 190
....*....|....*....|....*....|.
gi 2462549096 692 AHVGKHIfENVIgpkGMLKNK-TRILVTHSM 721
Cdd:COG1117 187 PISTAKI-EELI---LELKKDyTIVIVTHNM 213
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1201-1380 |
9.34e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 58.18 E-value: 9.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEG-----EIIIDGINIAKI-GLHDLRFKITIIPQDPVLFSG 1274
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1275 SLRMNLDP---FSQYSDEEVWTSLELAHLKDFvsALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAA 1351
Cdd:PRK14271 116 SIMDNVLAgvrAHKLVPRKEFRGVAQARLTEV--GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180
....*....|....*....|....*....
gi 2462549096 1352 VDLETDDLIQSTIRTQFEDCTVLTIAHRL 1380
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADRLTVIIVTHNL 222
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
647-721 |
1.07e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 57.86 E-value: 1.07e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462549096 647 DKVEGHVAIKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGpkgmLKNK-TRILVTHSM 721
Cdd:PRK14239 136 DEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLG----LKDDyTMLLVTRSM 207
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1201-1353 |
1.13e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 59.26 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--INI--------AKIGL-------------HD 1257
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIrsprdairAGIAYvpedrkgeglvldLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1258 LRFKITIipqdPVLFSGSLRMNLDPfsqysdeevwtSLELAHLKDFVSAL---PDKLDHECAeggeNLSVGQRQLVCLAR 1334
Cdd:COG1129 347 IRENITL----ASLDRLSRGGLLDR-----------RRERALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAK 407
|
170
....*....|....*....
gi 2462549096 1335 ALLRKTKILVLDEATAAVD 1353
Cdd:COG1129 408 WLATDPKVLILDEPTRGID 426
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1201-1396 |
1.13e-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: 55.15 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLtlglfrinesaegeiiidginiakiglhdlrfkITIIPQDPVLFSGSLRmnl 1280
Cdd:cd03221 15 LLKDISLTINPGDRIGLVGRNGAGKSTL---------------------------------LKLIAGELEPDEGIVT--- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1281 dpfsqysdeevWTS-LELAHLkdfvsalpdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDL 1359
Cdd:cd03221 59 -----------WGStVKIGYF-------------------EQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEA 108
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2462549096 1360 IQSTIRTQfeDCTVLTIAH-R--LNTIMdyTRVIVLDKGE 1396
Cdd:cd03221 109 LEEALKEY--PGTVILVSHdRyfLDQVA--TKIIELEDGK 144
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1201-1397 |
1.72e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 58.97 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHDL----RFKITIIPQDPVLFSG-S 1275
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLSHlT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1276 LRMNLDPFSQYSDEEVWTSLELAHLKDFVSALPDKLDHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1355
Cdd:PRK10535 103 AAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQ----LSGGQQQRVSIARALMNGGQVILADEPTGALDSH 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462549096 1356 TDDLIQSTIRtQFED--CTVLTIAHRLNTIMDYTRVIVLDKGEI 1397
Cdd:PRK10535 179 SGEEVMAILH-QLRDrgHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1205-1409 |
1.78e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 58.66 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1205 INVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII----DGINIAKIGLhDLRFKIT-----------IIPQDP 1269
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGP-DGRGRAKryigilhqeydLYPHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1270 VLFSGSLRMNLD-PFSQYSDEEVWTSLELAHLKDFVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEA 1348
Cdd:TIGR03269 382 VLDNLTEAIGLElPDELARMKAVITLKMVGFDEEKAEEILDKYPDE-------LSEGERHRVALAQVLIKEPRIVILDEP 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549096 1349 TAAVDLETDDLIQSTI---RTQFEDcTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLLQQ 1409
Cdd:TIGR03269 455 TGTMDPITKVDVTHSIlkaREEMEQ-TFIIVSHDMDFVLDVCdRAALMRDGKIVKIGDPEEIVEE 518
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1203-1397 |
1.86e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.91 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1203 RHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHD-LRFKITIIPQD---PVLF-SGSLR 1277
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEDrqsSGLYlDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1278 MNLDPFSqYSDEEVW--TSLELAHLKDFVSALPDKLDHECAEGGeNLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1355
Cdd:PRK15439 360 WNVCALT-HNRRGFWikPARENAVLERYRRALNIKFNHAEQAAR-TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462549096 1356 TDDLIQSTIRTQFEDCT-VLTIAHRLNTIMDYT-RVIVLDKGEI 1397
Cdd:PRK15439 438 ARNDIYQLIRSIAAQNVaVLFISSDLEEIEQMAdRVLVMHQGEI 481
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
660-747 |
2.47e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 57.55 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPKGmlKNKTRILVTHSMSYLPQV-DVIIVMSGGKI 738
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKA--NNKTVFVITHTMEHVLEVaDEVIVMDKGKI 254
|
....*....
gi 2462549096 739 SEMGSYQEL 747
Cdd:PRK13631 255 LKTGTPYEI 263
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
593-747 |
3.05e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 56.63 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 593 NSITVRNATFTWARSD----PPTLNGITFSIPEGALVAVVGQVGCGKSSL---LSALLA---------EMDK-------- 648
Cdd:PRK13633 3 EMIKCKNVSYKYESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALLIpsegkvyvdGLDTsdeenlwd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 649 --------------------VEGHVA--------------------IKGVN-----------LSGGQKQRVSLARAVYSN 677
Cdd:PRK13633 83 irnkagmvfqnpdnqivatiVEEDVAfgpenlgippeeirervdesLKKVGmyeyrrhaphlLSGGQKQRVAIAGILAMR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 678 ADIYLFDDPLSAVDAhVGKHIFENVIGPKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQEL 747
Cdd:PRK13633 163 PECIIFDEPTAMLDP-SGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1188-1360 |
3.18e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 55.98 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1188 RNYCLRYRED--LDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKI---GLHDLR-FK 1261
Cdd:PRK11629 9 DNLCKRYQEGsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaAKAELRnQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1262 ITIIPQ------D---------PVLFSGSLRMNldpfSQYSDEEVWTSLELAHlkdfvsalpdKLDHECAEggenLSVGQ 1326
Cdd:PRK11629 89 LGFIYQfhhllpDftalenvamPLLIGKKKPAE----INSRALEMLAAVGLEH----------RANHRPSE----LSGGE 150
|
170 180 190
....*....|....*....|....*....|....
gi 2462549096 1327 RQLVCLARALLRKTKILVLDEATAAVDLETDDLI 1360
Cdd:PRK11629 151 RQRVAIARALVNNPRLVLADEPTGNLDARNADSI 184
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
622-719 |
3.20e-08 |
|
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: 54.30 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 622 GALVAVVGQVGCGKSSLLSALLAEMDKVEGHV---------------------AIKGVNLSGGQKQRVSLARAVYSNADI 680
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGViyidgedileevldqllliivGGKKASGSGELRLRLALALARKLKPDV 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2462549096 681 YLFDDPLSAVDAHVGKHIFENVIGPKGMLKNKTR----ILVTH 719
Cdd:smart00382 82 LILDEITSLLDAEQEALLLLLEELRLLLLLKSEKnltvILTTN 124
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
660-759 |
3.73e-08 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 55.96 E-value: 3.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH-VGKhifenVIGPKGMLKN--KTRILVTHSMSYLPQV-DVIIVMSG 735
Cdd:COG4598 155 LSGGQQQRAAIARALAMEPEVMLFDEPTSALDPElVGE-----VLKVMRDLAEegRTMLVVTHEMGFARDVsSHVVFLHQ 229
|
90 100
....*....|....*....|....*.
gi 2462549096 736 GKISEMGSYQELLA--RDGAFAEFLR 759
Cdd:COG4598 230 GRIEEQGPPAEVFGnpKSERLRQFLS 255
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1185-1409 |
3.97e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 56.29 E-value: 3.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1185 VEFRNYCLRYREDLDF---VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIG----LHD 1257
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1258 LRFKITIIPQDP--VLFSGSLRMNL----DPFSQYSDEEVWTSLELAHLKDFVSALPDKLDHEcaeggenLSVGQRQLVC 1331
Cdd:PRK13649 83 IRKKVGLVFQFPesQLFEETVLKDVafgpQNFGVSQEEAEALAREKLALVGISESLFEKNPFE-------LSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1332 LARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFED-CTVLTIAHRLNTIMDY-TRVIVLDKGEIQEYGAPSDLLQQ 1409
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVANYaDFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1202-1395 |
5.20e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.10 E-value: 5.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1202 LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGlHDLRFK--ITIIPQD-PVLFSGSLRM 1278
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD-HKLAAQlgIGIIYQElSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1279 NLdPFSQYSDEEVW--TSLELAHLKDFVSALPDKLD--HECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAV-D 1353
Cdd:PRK09700 100 NL-YIGRHLTKKVCgvNIIDWREMRVRAAMMLLRVGlkVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtN 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2462549096 1354 LETDDLIQSTIRTQFEDCTVLTIAHRLNTIMDY-TRVIVLDKG 1395
Cdd:PRK09700 179 KEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRIcDRYTVMKDG 221
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1201-1353 |
5.33e-08 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 55.13 E-value: 5.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIID----GINIAKIG---LHDLRfKITI--------- 1264
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASpreILALR-RRTIgyvsqflrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1265 IPQDP---VLFSGSLRMNLDPFSQYSDEEVWtsleLAHLKdfvsaLPDKLDHecaeggenL-----SVGQRQLVCLARAL 1336
Cdd:COG4778 105 IPRVSaldVVAEPLLERGVDREEARARAREL----LARLN-----LPERLWD--------LppatfSGGEQQRVNIARGF 167
|
170
....*....|....*..
gi 2462549096 1337 LRKTKILVLDEATAAVD 1353
Cdd:COG4778 168 IADPPLLLLDEPTASLD 184
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1201-1406 |
5.40e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 56.63 E-value: 5.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLtlglFRI----NESAEGEIIIDGINIAKigLHDLRFKITIIPQDPVLF---- 1272
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTL----LRIiaglEHQTSGHIRFHGTDVSR--LHARDRKVGFVFQHYALFrhmt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1273 -----SGSLRM---NLDPFSQYSDEEVWTSLELAHLKDFVSALPDKLdhecaeggenlSVGQRQLVCLARALLRKTKILV 1344
Cdd:PRK10851 91 vfdniAFGLTVlprRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQL-----------SGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549096 1345 LDEATAAVDLETDDLIQSTIRTQFEDC--TVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDL 1406
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHDQEEAMEVAdRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
921-1155 |
6.06e-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: 55.98 E-value: 6.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 921 AVFGYSMAVsIGGILASRcLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVI 1000
Cdd:cd18563 61 ILRGRLLAR-LGERITAD-LRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1001 L-----LAtpiAAIIIP-PL--GLIYFFVQRFYVASSRQLKRlesvsRSPVYSHFNETLLGVSVIRAF----EEQERFIH 1068
Cdd:cd18563 139 FslnwkLA---LLVLIPvPLvvWGSYFFWKKIRRLFHRQWRR-----WSRLNSVLNDTLPGIRVVKAFgqekREIKRFDE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1069 QSDLKVDENQKA------YYPSIVAnrwlavrLECVGNCIVLFAALFAVISRHsLSAGLVGLSVSYSLQVTTYLNWLVRM 1142
Cdd:cd18563 211 ANQELLDANIRAeklwatFFPLLTF-------LTSLGTLIVWYFGGRQVLSGT-MTLGTLVAFLSYLGMFYGPLQWLSRL 282
|
250
....*....|...
gi 2462549096 1143 SSEMETNIVAVER 1155
Cdd:cd18563 283 NNWITRALTSAER 295
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1196-1379 |
6.23e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 57.45 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1196 EDLDFVLRHinvtingGEKVGIVGRTGAGKSSLtlglFRInesaEGEII-IDGINIAKiglhDLRFKITIIPQDPVLFSG 1274
Cdd:TIGR00954 469 ESLSFEVPS-------GNNLLICGPNGCGKSSL----FRI----LGELWpVYGGRLTK----PAKGKLFYVPQRPYMTLG 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1275 SLR------MNLDPFSQ--YSDEEVWTSLELAHLKDFV------SALPDKLDHecaeggenLSVGQRQLVCLARALLRKT 1340
Cdd:TIGR00954 530 TLRdqiiypDSSEDMKRrgLSDKDLEQILDNVQLTHILereggwSAVQDWMDV--------LSGGEKQRIAMARLFYHKP 601
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462549096 1341 KILVLDEATAAVDLETDDLIqstirtqFEDC-----TVLTIAHR 1379
Cdd:TIGR00954 602 QFAILDECTSAVSVDVEGYM-------YRLCrefgiTLFSVSHR 638
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
606-738 |
6.71e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 54.58 E-value: 6.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 606 RSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL---LAEMDKVEGHVAIKGVN----------------------- 659
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPykefaekypgeiiyvseedvhfp 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 ----------------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEnvigpkgMLKNKTRILV 717
Cdd:cd03233 97 tltvretldfalrckgnefvrgISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILK-------CIRTMADVLK 169
|
170 180
....*....|....*....|....*....
gi 2462549096 718 THSMSYLPQ--------VDVIIVMSGGKI 738
Cdd:cd03233 170 TTTFVSLYQasdeiydlFDKVLVLYEGRQ 198
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
612-742 |
7.21e-08 |
|
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: 54.85 E-value: 7.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 612 LNGITFSIPEGALVAVVGQVGCGKSSLL--------------------SALLA--------------------------- 644
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLrllagiyppdsgtvtvrgrvSSLLGlgggfnpeltgreniylngrllglsrk 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 645 EMDKVEGHVA------------IKgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH----VGKHIFEnvigpkgM 708
Cdd:cd03220 118 EIDEKIDEIIefselgdfidlpVK--TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfqekCQRRLRE-------L 188
|
170 180 190
....*....|....*....|....*....|....*.
gi 2462549096 709 LKN-KTRILVTHSMSYLPQV-DVIIVMSGGKISEMG 742
Cdd:cd03220 189 LKQgKTVILVSHDPSSIKRLcDRALVLEKGKIRFDG 224
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
913-1156 |
7.65e-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: 55.60 E-value: 7.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 913 ALGISQGIAVFG--YSMAvSIGGILASRcLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSL 990
Cdd:cd18564 62 GIALLRGLASYAgtYLTA-LVGQRVVLD-LRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 991 FNVIGACIVIL-----LATpIAAIIIPplgLIYFFVQRFY---VASSRQLKRLESVsrspVYSHFNETLLGVSVIRAF-- 1060
Cdd:cd18564 140 LTLVGMLGVMFwldwqLAL-IALAVAP---LLLLAARRFSrriKEASREQRRREGA----LASVAQESLSAIRVVQAFgr 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1061 --EEQERFIHQSDLKVDENQKAYYPSIVANRWLAVrLECVGNCIVLFAALFAVIsRHSLSAGlvGLSVsyslqVTTYLNW 1138
Cdd:cd18564 212 eeHEERRFARENRKSLRAGLRAARLQALLSPVVDV-LVAVGTALVLWFGAWLVL-AGRLTPG--DLLV-----FLAYLKN 282
|
250 260
....*....|....*....|....*
gi 2462549096 1139 L---VRMSSEMETNI----VAVERL 1156
Cdd:cd18564 283 LykpVRDLAKLTGRIakasASAERV 307
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
615-758 |
7.73e-08 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 54.76 E-value: 7.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 615 ITFSIPEGALVAVVGQVGCGKSSLLSAL---------------------------------------------------- 642
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIagflppdsgrilwngqdltalppaerpvsmlfqennlfphltvaqniglglr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 643 ----LAEMDKVEGHVAIKGVN-----------LSGGQKQRVSLARAVYSNADIYLFDDPLSAvdahvgkhifenvIGP-- 705
Cdd:COG3840 98 pglkLTAEQRAQVEQALERVGlaglldrlpgqLSGGQRQRVALARCLVRKRPILLLDEPFSA-------------LDPal 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 706 -KGMLK---------NKTRILVTHSmsylPQ-----VDVIIVMSGGKISEMGSYQELLARDG--AFAEFL 758
Cdd:COG3840 165 rQEMLDlvdelcrerGLTVLMVTHD----PEdaariADRVLLVADGRIAADGPTAALLDGEPppALAAYL 230
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
660-758 |
8.01e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 55.02 E-value: 8.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVD----AHVGKHIFEnvIGPKGMlknkTRILVTHsmsylpQVDV------ 729
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeitAQIVSIIRE--LAETGI----TQVIVTH------EVEVarktas 209
|
90 100 110
....*....|....*....|....*....|.
gi 2462549096 730 -IIVMSGGKISEMGSYQELLA-RDGAFAEFL 758
Cdd:PRK11124 210 rVVYMENGHIVEQGDASCFTQpQTEAFKNYL 240
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
595-672 |
8.91e-08 |
|
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: 54.34 E-value: 8.91e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549096 595 ITVRNATFTWArSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVNLSGGQKQRVSLAR 672
Cdd:cd03292 1 IEFINVTKTYP-NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
595-740 |
1.06e-07 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 54.29 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTWARsDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVN--------------- 659
Cdd:COG2884 2 IRFENVSKRYPG-GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrlkrreipylrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 ---------------------------------------------------------LSGGQKQRVSLARAVYSNADIYL 682
Cdd:COG2884 81 igvvfqdfrllpdrtvyenvalplrvtgksrkeirrrvrevldlvglsdkakalpheLSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549096 683 FDDPLSAVDAHVGKHIFEnvigpkgMLK--NK---TRILVTHSMSYLPQVDV-IIVMSGGKISE 740
Cdd:COG2884 161 ADEPTGNLDPETSWEIME-------LLEeiNRrgtTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
637-772 |
1.08e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 54.79 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 637 SLLSALLaeMDKVEGHVAIKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRIL 716
Cdd:PRK14243 131 SLRQAAL--WDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELM---HELKEQYTIII 205
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549096 717 VTHSMSYLPQVDVIIVMSGGKISEMGSyqellaRDGAFAEFLRTYA--STEQEQDAEE 772
Cdd:PRK14243 206 VTHNMQQAARVSDMTAFFNVELTEGGG------RYGYLVEFDRTEKifNSPQQQATRD 257
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
612-750 |
1.10e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 54.70 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 612 LNGITFSIPEGALVAVVGQVGCGKSSLL--------------------SALL---------------------------A 644
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLkliagileptsgrvevngrvSALLelgagfhpeltgreniylngrllglsrK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 645 EMDKVEGHVA------------IKgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH----VGKHIFEnvigpkgM 708
Cdd:COG1134 122 EIDEKFDEIVefaelgdfidqpVK--TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRE-------L 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2462549096 709 LKN-KTRILVTHSMSYLPQV-DVIIVMSGGKISEMGS-------YQELLAR 750
Cdd:COG1134 193 RESgRTVIFVSHSMGAVRRLcDRAIWLEKGRLVMDGDpeeviaaYEALLAG 243
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
612-743 |
1.21e-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: 53.68 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 612 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMD-KV-EGHVAIKGVNL----------------------------- 660
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyEVtEGEILFKGEDItdlppeerarlgiflafqyppeipgvkna 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 661 ----------SGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIfENVIgpKGML-KNKTRILVTHSMSYLPQV-- 727
Cdd:cd03217 96 dflryvnegfSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLV-AEVI--NKLReEGKSVLIITHYQRLLDYIkp 172
|
170
....*....|....*.
gi 2462549096 728 DVIIVMSGGKISEMGS 743
Cdd:cd03217 173 DRVHVLYDGRIVKSGD 188
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
660-738 |
1.32e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 56.27 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGkhifENVIGPKGMLKNK--TRILVTHSMSYLPQVDVIIVMSGGK 737
Cdd:PRK10535 145 LSGGQQQRVSIARALMNGGQVILADEPTGALDSHSG----EEVMAILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDGE 220
|
.
gi 2462549096 738 I 738
Cdd:PRK10535 221 I 221
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1197-1353 |
1.64e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.71 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1197 DLDFVLRHinvtingGEKVGIVGRTGAGKSSLTLGLFRINESA-EGEIIIDG--INIaKIGLHDLRFKITIIPQD----- 1268
Cdd:PRK13549 280 DVSFSLRR-------GEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGkpVKI-RNPQQAIAQGIAMVPEDrkrdg 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1269 --PVLFSG--SLRMNLDPFSQYS--DEevwtSLELAHLKDFVSALPDKLDHECAEGGeNLSVGQRQLVCLARALLRKTKI 1342
Cdd:PRK13549 352 ivPVMGVGknITLAALDRFTGGSriDD----AAELKTILESIQRLKVKTASPELAIA-RLSGGNQQKAVLAKCLLLNPKI 426
|
170
....*....|.
gi 2462549096 1343 LVLDEATAAVD 1353
Cdd:PRK13549 427 LILDEPTRGID 437
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
660-749 |
1.70e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 54.22 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVigPKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKIS 739
Cdd:PRK13644 137 LSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERI--KKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIV 214
|
90
....*....|
gi 2462549096 740 EMGSYQELLA 749
Cdd:PRK13644 215 LEGEPENVLS 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
612-750 |
1.87e-07 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 55.46 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 612 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAeMDKVEGHVAIKGVNL------------------------------- 660
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDLdglsrralrplrrrmqvvfqdpfgslsprmt 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 661 ----------------------------------------------SGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHV 694
Cdd:COG4172 381 vgqiiaeglrvhgpglsaaerrarvaealeevgldpaarhryphefSGGQRQRIAIARALILEPKLLVLDEPTSALDVSV 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462549096 695 GKHIFEnvigpkgMLKnktRILVTHSMSYL-----PQV-----DVIIVMSGGKISEMGSYQELLAR 750
Cdd:COG4172 461 QAQILD-------LLR---DLQREHGLAYLfishdLAVvralaHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
592-768 |
2.34e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 54.12 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 592 TNSITVRNATFTWaRSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGV------------- 658
Cdd:PRK15056 4 QAGIVVNDVTVTW-RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlvay 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 659 -----------------------------------------------------------NLSGGQKQRVSLARAVYSNAD 679
Cdd:PRK15056 83 vpqseevdwsfpvlvedvvmmgryghmgwlrrakkrdrqivtaalarvdmvefrhrqigELSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 680 IYLFDDPLSAVDAHVGKHIfenvIGPKGMLKN--KTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDG---AF 754
Cdd:PRK15056 163 VILLDEPFTGVDVKTEARI----ISLLRELRDegKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFTAENlelAF 238
|
250
....*....|....
gi 2462549096 755 AEFLRTYASTEQEQ 768
Cdd:PRK15056 239 SGVLRHVALNGSEE 252
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
594-674 |
2.37e-07 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 53.62 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 594 SITVRNATFtwARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVNLSGGQKQRVSLARA 673
Cdd:PRK13548 2 MLEARNLSV--RLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA 79
|
.
gi 2462549096 674 V 674
Cdd:PRK13548 80 V 80
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
910-1120 |
2.43e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 54.03 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 910 VYGALGISQGIAVFGYSMAVsigGILASRCLH---VDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMF 986
Cdd:cd18546 44 AYLAVVLAGWVAQRAQTRLT---GRTGERLLYdlrLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 987 MGSLFNVIGACIVILLATP----IAAIIIPPLGLIYFFVQRfyvASSRQLKRL-ESVSRspVYSHFNETLLGVSVIRAF- 1060
Cdd:cd18546 121 VVSLLTLVGIAVVLLVLDPrlalVALAALPPLALATRWFRR---RSSRAYRRArERIAA--VNADLQETLAGIRVVQAFr 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549096 1061 ---EEQERFIHQSDLKVDENQKA------YYPSIvanRWLAVrlecVGNCIVLFAALFAVIsRHSLSAG 1120
Cdd:cd18546 196 rerRNAERFAELSDDYRDARLRAqrlvaiYFPGV---ELLGN----LATAAVLLVGAWRVA-AGTLTVG 256
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
595-756 |
2.61e-07 |
|
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: 53.70 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLaEMDKVEGHVAIKGVN--------------- 659
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGVSwnsvplqkwrkafgv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 ---------------------------------------------------------LSGGQKQRVSLARAVYSNADIYL 682
Cdd:cd03289 82 ipqkvfifsgtfrknldpygkwsdeeiwkvaeevglksvieqfpgqldfvlvdggcvLSHGHKQLMCLARSVLSKAKILL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549096 683 FDDPLSAVDAhVGKHIFENVIgpKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAE 756
Cdd:cd03289 162 LDEPSAHLDP-ITYQVIRKTL--KQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQ 232
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
615-750 |
2.71e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 53.87 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 615 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIK-------------------------------------- 656
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGervitagkknkklkplrkkvgivfqfpehqlfeetvek 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 657 ---------GV----------------------------NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI- 698
Cdd:PRK13634 106 dicfgpmnfGVseedakqkaremielvglpeellarspfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMm 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2462549096 699 --FENVIGPKGMlknkTRILVTHSMSYLPQ-VDVIIVMSGGKISEMGSYQELLAR 750
Cdd:PRK13634 186 emFYKLHKEKGL----TTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFAD 236
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1201-1347 |
2.73e-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: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINI-----AKIglhdLRFKITIIPQDPVLFSgs 1275
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItdwqtAKI----MREAVAIVPEGRRVFS-- 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462549096 1276 lRM----NLDPFSQYSDEEVWTSlelaHLKDFVSALPDKLDHECAEGGeNLSVGQRQLVCLARALLRKTKILVLDE 1347
Cdd:PRK11614 94 -RMtveeNLAMGGFFAERDQFQE----RIKWVYELFPRLHERRIQRAG-TMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
940-1086 |
2.81e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 53.69 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 940 LHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATPI-AAIIIPPLGLIY 1018
Cdd:cd18778 75 LRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKlALLTLIPIPFLA 154
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549096 1019 FFVqRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAF----EEQERFIHQSDLKVDENQKA------YYPSIV 1086
Cdd:cd18778 155 LGA-WLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFgreeEEAKRFEALSRRYRKAQLRAmklwaiFHPLME 231
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
943-1120 |
2.82e-07 |
|
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: 53.98 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 943 DLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACI-----------VILLATPIAAIII 1011
Cdd:cd18551 74 RLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVlmflldwvltlVTLAVVPLAFLII 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1012 PPLGliyffvQRFYVASSRQLKRLESVSrspvySHFNETLLGVSVIRAF--EEQErfihqSDLKVDENQKAYYPSIVANR 1089
Cdd:cd18551 154 LPLG------RRIRKASKRAQDALGELS-----AALERALSAIRTVKASnaEERE-----TKRGGEAAERLYRAGLKAAK 217
|
170 180 190
....*....|....*....|....*....|....*...
gi 2462549096 1090 WLAVrLECVGNcIVLFAALFAVI-------SRHSLSAG 1120
Cdd:cd18551 218 IEAL-IGPLMG-LAVQLALLVVLgvggarvASGALTVG 253
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1208-1401 |
2.94e-07 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 53.18 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1208 TINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAkiglhdlrFKI-TIIPQDPVLFSGSLRMNLDPF--S 1284
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS--------YKPqYIKADYEGTVRDLLSSITKDFytH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1285 QYSDEEVWTSLELAHLKDfvSALPDkldhecaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTI 1364
Cdd:cd03237 93 PYFKTEIAKPLQIEQILD--REVPE------------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462549096 1365 RTQFE--DCTVLTIAHrlNTIM-DYT--RVIVLDkGEIQEYG 1401
Cdd:cd03237 159 RRFAEnnEKTAFVVEH--DIIMiDYLadRLIVFE-GEPSVNG 197
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1188-1402 |
2.99e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.86 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1188 RNYCLRYREDLDFV--LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEI-------------IIDGINIAK 1252
Cdd:PRK10261 16 ENLNIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIELSEQSA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1253 IGLHDLR-------FKITIIPQDPVLFSG-----SLRMNLDPFSQYSDEEVWTSLELAHLKDFVSALpDKLDHEcaegge 1320
Cdd:PRK10261 96 AQMRHVRgadmamiFQEPMTSLNPVFTVGeqiaeSIRLHQGASREEAMVEAKRMLDQVRIPEAQTIL-SRYPHQ------ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1321 nLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQFEDCT--VLTIAHRLNTIMDYT-RVIVLDKGEI 1397
Cdd:PRK10261 169 -LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIAdRVLVMYQGEA 247
|
....*
gi 2462549096 1398 QEYGA 1402
Cdd:PRK10261 248 VETGS 252
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
612-748 |
3.74e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 52.92 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 612 LNGITFSIPEGALVAVVGQVGCGKSSLLSAL-----LAEMDKVEGHVAIKGV---------------------------- 658
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrlleLNEEARVEGEVRLFGRniyspdvdpievrrevgmvfqypnpfph 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 659 -------------------------------------------------NLSGGQKQRVSLARAVYSNADIYLFDDPLSA 689
Cdd:PRK14267 100 ltiydnvaigvklnglvkskkeldervewalkkaalwdevkdrlndypsNLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 690 VDAHVGKHIFENVIGPKgmlKNKTRILVTHSMSYLPQV-DVIIVMSGGKISEMGSYQELL 748
Cdd:PRK14267 180 IDPVGTAKIEELLFELK---KEYTIVLVTHSPAQAARVsDYVAFLYLGKLIEVGPTRKVF 236
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1202-1409 |
4.34e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 53.55 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1202 LRHINVTINGGEKVGIVGRTGAGKSS----LTlGLfrINESAeGEIIIDGINIAKiGLHDLRFKITIIpqdpvlfsgslr 1277
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTtikmLT-GI--LVPTS-GEVRVLGYVPFK-RRKEFARRIGVV------------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1278 mnldpFSQYS----DEEVWTSLELahLKDfVSALPDK-----LDhECAEG---GE-------NLSVGQRQLVCLARALLR 1338
Cdd:COG4586 101 -----FGQRSqlwwDLPAIDSFRL--LKA-IYRIPDAeykkrLD-ELVELldlGElldtpvrQLSLGQRMRCELAAALLH 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549096 1339 KTKILVLDEATAAVDLETDDLIQSTIRT--QFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEIQEYGAPSDLLQQ 1409
Cdd:COG4586 172 RPKILFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIEALcDRVIVIDHGRIIYDGSLEELKER 245
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
634-771 |
4.55e-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: 54.42 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 634 GKSSLLSAL-LAEMDKVEGHVAIKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIgpKGMLKNK 712
Cdd:TIGR03269 142 GKEAVGRAVdLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALE--EAVKASG 219
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549096 713 TRILVThsmSYLPQV-----DVIIVMSGGKISEMGSYQELLARdgafaeFLRTYASTEQEQDAE 771
Cdd:TIGR03269 220 ISMVLT---SHWPEViedlsDKAIWLENGEIKEEGTPDEVVAV------FMEGVSEVEKECEVE 274
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
657-760 |
5.76e-07 |
|
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: 52.60 E-value: 5.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 657 GVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVgkhifENVIGPKGMLKNKTRILVT--HSMSYLPQVDVIIVMS 734
Cdd:cd03288 154 GENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT-----ENILQKVVMTAFADRTVVTiaHRVSTILDADLVLVLS 228
|
90 100
....*....|....*....|....*..
gi 2462549096 735 GGKISEMGSYQELLAR-DGAFAEFLRT 760
Cdd:cd03288 229 RGILVECDTPENLLAQeDGVFASLVRT 255
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
595-774 |
6.48e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 52.79 E-value: 6.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTWAR-SDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG---------------- 657
Cdd:PRK13642 5 LEVENLVFKYEKeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGelltaenvwnlrrkig 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 658 -------------------------------------------VN-----------LSGGQKQRVSLARAVYSNADIYLF 683
Cdd:PRK13642 85 mvfqnpdnqfvgatveddvafgmenqgipreemikrvdeallaVNmldfktreparLSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 684 DDPLSAVDAhVGKHIFENVIGPKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKISEMGSYQELLARDGAFAEF-LRTYA 762
Cdd:PRK13642 165 DESTSMLDP-TGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDMVEIgLDVPF 243
|
250
....*....|..
gi 2462549096 763 STEQEQDAEENG 774
Cdd:PRK13642 244 SSNLMKDLRKNG 255
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
610-692 |
7.49e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 52.01 E-value: 7.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 610 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLA------------EMDKVEGHVAIKGV------------------- 658
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLN-LIAgfvpyqhgsitlDGKPVEGPGAERGVvfqnegllpwrnvqdnvaf 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549096 659 ----------------------------------NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 692
Cdd:PRK11248 94 glqlagvekmqrleiahqmlkkvglegaekryiwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1202-1383 |
8.23e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.38 E-value: 8.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1202 LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGiniakiglHDLRFK---------ITIIPQD---- 1268
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG--------QEMRFAsttaalaagVAIIYQElhlv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1269 P---V---LFSGSLrmnldP----FSQYSDEEVWTSLELAHLKDFVSalPD-KLDHecaeggenLSVGQRQLVCLARALL 1337
Cdd:PRK11288 92 PemtVaenLYLGQL-----PhkggIVNRRLLNYEAREQLEHLGVDID--PDtPLKY--------LSIGQRQMVEIAKALA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2462549096 1338 RKTKILVLDEATAAVDL-ETDDLIQSTIRTQFEDCTVLTIAHRLNTI 1383
Cdd:PRK11288 157 RNARVIAFDEPTSSLSArEIEQLFRVIRELRAEGRVILYVSHRMEEI 203
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
660-750 |
1.13e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 51.93 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFENVIGPKGMLKNKTRILVTHSMSYLPQV-DVIIVMSGGKI 738
Cdd:PRK13645 151 LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK-GEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIaDEVIVMHEGKV 229
|
90
....*....|....*...
gi 2462549096 739 SEMG------SYQELLAR 750
Cdd:PRK13645 230 ISIGspfeifSNQELLTK 247
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
604-691 |
1.14e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 52.40 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 604 WARSDPPTL---NGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVNLSG-GQKQRvslaRAVYSnaD 679
Cdd:PRK15079 26 WFWQPPKTLkavDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGmKDDEW----RAVRS--D 99
|
90
....*....|...
gi 2462549096 680 IYL-FDDPLSAVD 691
Cdd:PRK15079 100 IQMiFQDPLASLN 112
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
643-747 |
1.27e-06 |
|
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: 51.14 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 643 LAEMDKV--EGHVAIKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD---AHVGKHIFENVIGPKGmlknKTRILV 717
Cdd:TIGR02315 127 LSALERVglADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDpktSKQVMDYLKRINKEDG----ITVIIN 202
|
90 100 110
....*....|....*....|....*....|.
gi 2462549096 718 THSMSYLPQ-VDVIIVMSGGKISEMGSYQEL 747
Cdd:TIGR02315 203 LHQVDLAKKyADRIVGLKAGEIVFDGAPSEL 233
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1199-1406 |
1.41e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1199 DFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDgINIAkiglhdlrFK---ITIIPQDPVlfSGS 1275
Cdd:PRK13409 352 DFSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKIS--------YKpqyIKPDYDGTV--EDL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1276 LRMNLDPF-SQYSDEEVWTSLELAHLkdfvsalpdkLDHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1354
Cdd:PRK13409 421 LRSITDDLgSSYYKSEIIKPLQLERL----------LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549096 1355 ETDDLIQSTIRTQFE--DCTVLTIAHRLnTIMDY--TRVIVLDkGEIQEYG---APSDL 1406
Cdd:PRK13409 487 EQRLAVAKAIRRIAEerEATALVVDHDI-YMIDYisDRLMVFE-GEPGKHGhasGPMDM 543
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
643-748 |
1.67e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 51.76 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 643 LAEMDKVEGHVAIKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVigpKGML-KNKTRILVTHSM 721
Cdd:PRK13536 156 LLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERL---RSLLaRGKTILLTTHFM 232
|
90 100
....*....|....*....|....*....
gi 2462549096 722 SYLPQV-DVIIVMSGG-KISEmGSYQELL 748
Cdd:PRK13536 233 EEAERLcDRLCVLEAGrKIAE-GRPHALI 260
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
660-761 |
1.76e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 51.96 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPKGMlKNKTRILVTHSMSYLPQV-DVIIVMSGGKI 738
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAK-HQRTIVFISHDLDEAMRIgDRIAIMQNGEV 243
|
90 100
....*....|....*....|...
gi 2462549096 739 SEMGSYQELLarDGAFAEFLRTY 761
Cdd:PRK10070 244 VQVGTPDEIL--NNPANDYVRTF 264
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
659-754 |
1.86e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 51.63 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 659 NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEnvIGPKGMLKNKTRILVTHSM-SYLPQVDVIIVMSGGK 737
Cdd:PRK13651 165 ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLNKQGKTIILVTHDLdNVLEWTKRTIFFKDGK 242
|
90
....*....|....*..
gi 2462549096 738 ISEMGSYQELLaRDGAF 754
Cdd:PRK13651 243 IIKDGDTYDIL-SDNKF 258
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
908-1120 |
2.13e-06 |
|
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: 51.01 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 908 LSVYGAlgisQGIAVFGY-SMAVSIGGILASRcLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMF 986
Cdd:cd18574 49 LGLYLL----QSLLTFAYiSLLSVVGERVAAR-LRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 987 MGSLFNVIGACIVILLATP----IAAIIIPPLGLIYFFVQRFYVASSRQLKRLESVSRspvySHFNETLLGVSVIRAF-- 1060
Cdd:cd18574 124 LRSVTQTVGCVVSLYLISPkltlLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKAT----GVADEALGNIRTVRAFam 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462549096 1061 --EEQERFIhqsdlkvDENQKAyypsIVANRWLAVRLEC-------VGNCIVLfAALFA---VISRHSLSAG 1120
Cdd:cd18574 200 edRELELYE-------EEVEKA----AKLNEKLGLGIGIfqglsnlALNGIVL-GVLYYggsLVSRGELTAG 259
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
612-747 |
2.30e-06 |
|
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: 50.54 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 612 LNGITFSIPEGALVAVVGQVGCGKSSLLS--------------------------------------------------- 640
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNlisglaqptsggvilegkqitepgpdrmvvfqnysllpwltvrenialavd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 641 ALLAEMDK------VEGHVAIKGV---------NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVgkhifenvigp 705
Cdd:TIGR01184 81 RVLPDLSKserraiVEEHIALVGLteaadkrpgQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT----------- 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462549096 706 KGMLKNK----------TRILVTHSM-SYLPQVDVIIVMSGGKISEMGSYQEL 747
Cdd:TIGR01184 150 RGNLQEElmqiweehrvTVLMVTHDVdEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
659-766 |
2.68e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.93 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 659 NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFE--NVIGPKGMlknkTRILVTHSMsylPQV----DVIIV 732
Cdd:PRK10762 395 LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQliNQFKAEGL----SIILVSSEM---PEVlgmsDRILV 467
|
90 100 110
....*....|....*....|....*....|....
gi 2462549096 733 MSGGKISemgsyqellardgafAEFLRTYASTEQ 766
Cdd:PRK10762 468 MHEGRIS---------------GEFTREQATQEK 486
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
919-1142 |
2.82e-06 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 50.86 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 919 GIAVFGYSMAVsIGGILASRC-------LHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLF 991
Cdd:cd18548 47 LLALLGLIAGI-LAGYFAAKAsqgfgrdLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 992 NVIGACIVILLATP----IAAIIIPPLGLIYFFVQRF-YVASSRQLKRLESVSRSpvyshFNETLLGVSVIRAF----EE 1062
Cdd:cd18548 126 MLIGAIIMAFRINPklalILLVAIPILALVVFLIMKKaIPLFKKVQKKLDRLNRV-----VRENLTGIRVIRAFnredYE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1063 QERFIhqsdlkvDENQKAYYPSIVANRWLAVR---LECVGN----CIVLFAALFavISRHSLSAG-LVGLsVSYSLQVTT 1134
Cdd:cd18548 201 EERFD-------KANDDLTDTSLKAGRLMALLnplMMLIMNlaivAILWFGGHL--INAGSLQVGdLVAF-INYLMQILM 270
|
....*...
gi 2462549096 1135 YLNWLVRM 1142
Cdd:cd18548 271 SLMMLSMV 278
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1322-1403 |
3.10e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 51.00 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1322 LSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD-DLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQE 1399
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEhEMMQLILDAKANNKTVFVITHTMEHVLEVAdEVIVMDKGKILK 256
|
....
gi 2462549096 1400 YGAP 1403
Cdd:PRK13631 257 TGTP 260
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1189-1413 |
3.10e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 50.78 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1189 NYCLRYREDLDFVLRHIN---VTINGGEKVGIVGRTGAGKSS---LTLGLFrINESAE---GEIIIDGiNIAKIG-LHDL 1258
Cdd:PRK13645 11 NVSYTYAKKTPFEFKALNntsLTFKKNKVTCVIGTTGSGKSTmiqLTNGLI-ISETGQtivGDYAIPA-NLKKIKeVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1259 RFKITIIPQDP--VLFSGSLRMNL--DPFSQYSD-EEVWTslELAHLKDFVSALPDKLDHECAEggenLSVGQRQLVCLA 1333
Cdd:PRK13645 89 RKEIGLVFQFPeyQLFQETIEKDIafGPVNLGENkQEAYK--KVPELLKLVQLPEDYVKRSPFE----LSGGQKRRVALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1334 RALLRKTKILVLDEATAAVDLE-TDDLIQSTIRTQFEDCT-VLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLLQQR 1410
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKgEEDFINLFERLNKEYKKrIIMVTHNMDQVLRIAdEVIVMHEGKVISIGSPFEIFSNQ 242
|
...
gi 2462549096 1411 GLF 1413
Cdd:PRK13645 243 ELL 245
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
612-750 |
3.93e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 50.73 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 612 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVNL------------------------------- 660
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkadpeaqkllrqkiqivfqnpygslnprkk 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 661 ---------------------------------------------SGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVG 695
Cdd:PRK11308 111 vgqileepllintslsaaerrekalammakvglrpehydryphmfSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQ 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 696 KHIFeNVIgpkgM-LK---NKTRILVTHSMSYLPQV-DVIIVMSGGKISEMGSYQELLAR 750
Cdd:PRK11308 191 AQVL-NLM----MdLQqelGLSYVFISHDLSVVEHIaDEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
612-742 |
4.31e-06 |
|
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: 49.11 E-value: 4.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 612 LNGITFSIPEGaLVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG---------------------------------- 657
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklrrrigylpqefgvypnftvrefld 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 658 -----------------------VNL-----------SGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGKHIFENVI 703
Cdd:cd03264 95 yiawlkgipskevkarvdevlelVNLgdrakkkigslSGGMRRRVGIAQALVGDPSILIVDEPTAGLDP-EERIRFRNLL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462549096 704 GPKGmlKNKTRILVTHSMSylpqvDV------IIVMSGGKISEMG 742
Cdd:cd03264 174 SELG--EDRIVILSTHIVE-----DVeslcnqVAVLNKGKLVFEG 211
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
647-787 |
4.41e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 50.09 E-value: 4.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 647 DKVEGHVAIKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVigpKGMLKNKTRILVTHSMSYLPQ 726
Cdd:PRK14271 151 DAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFI---RSLADRLTVIIVTHNLAQAAR 227
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462549096 727 V-DVIIVMSGGKISEMGSYQELlardgafaeflrtYASTEQEQDAEEngVTGVSGPGKEAKQ 787
Cdd:PRK14271 228 IsDRAALFFDGRLVEEGPTEQL-------------FSSPKHAETARY--VAGLSGDVKDAKR 274
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
919-1064 |
5.01e-06 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 50.21 E-value: 5.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 919 GIAVFG--YSMAVSIGGILASrcLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGA 996
Cdd:cd18573 55 AAANFGrvYLLRIAGERIVAR--LRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGG 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549096 997 CIVILLATP----IAAIIIPPLGLIYFFVQRFYVASSRQLkrLESVSRSpvySHF-NETLLGVSVIRAF--EEQE 1064
Cdd:cd18573 133 IGMMLYISPkltlVMLLVVPPIAVGAVFYGRYVRKLSKQV--QDALADA---TKVaEERLSNIRTVRAFaaERKE 202
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
647-750 |
5.39e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 49.53 E-value: 5.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 647 DKVEGHVAIKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPKgmlKNKTRILVTHsmsYLPQ 726
Cdd:PRK14247 134 DEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELK---KDMTIVLVTH---FPQQ 207
|
90 100
....*....|....*....|....*...
gi 2462549096 727 V----DVIIVMSGGKISEMGSYQELLAR 750
Cdd:PRK14247 208 AarisDYVAFLYKGQIVEWGPTREVFTN 235
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
608-767 |
6.15e-06 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 49.24 E-value: 6.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 608 DPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL--------------------------------------------- 642
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFarlltpqsgtvflgdkpismlssrqlarrlallpqhhltpegitv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 643 -----------------LAEMDK--VE--------GHVAIKGV-NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHv 694
Cdd:PRK11231 94 relvaygrspwlslwgrLSAEDNarVNqameqtriNHLADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDIN- 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549096 695 gkHIFEnVIGPKGMLKN--KTRILVTHSmsyLPQV----DVIIVMSGGKISEMGSYQELLArdgafAEFLRTYASTEQE 767
Cdd:PRK11231 173 --HQVE-LMRLMRELNTqgKTVVTVLHD---LNQAsrycDHLVVLANGHVMAQGTPEEVMT-----PGLLRTVFDVEAE 240
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
944-1059 |
6.67e-06 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 49.51 E-value: 6.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 944 LLHSILRSPMSFFERTPSGNLVNRFSkELDTV-DSMIPEVIKMFMGSLFNVIgACIVILLATP----IAAIIIPPLGLIY 1018
Cdd:cd18782 81 IIDHLLRLPLGFFDKRPVGELSTRIS-ELDTIrGFLTGTALTTLLDVLFSVI-YIAVLFSYSPlltlVVLATVPLQLLLT 158
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2462549096 1019 FFVQRFYvasSRQLKRLESvSRSPVYSHFNETLLGVSVIRA 1059
Cdd:cd18782 159 FLFGPIL---RRQIRRRAE-ASAKTQSYLVESLTGIQTVKA 195
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
913-1080 |
8.18e-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: 49.37 E-value: 8.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 913 ALGISQGIAVF--GYSMAVSiGGILASRcLHVDLLHSILRSPMSFFERTP--SGNLVNRFSKELDTVDSMIPEVIKMFMG 988
Cdd:cd18578 60 VLAIVAGIAYFlqGYLFGIA-GERLTRR-LRKLAFRAILRQDIAWFDDPEnsTGALTSRLSTDASDVRGLVGDRLGLILQ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 989 SLFNVIGACIVILLA----TPIAAIIIPPLGLIYFFVQRFYVASSRQLKR-LESVSRspvysHFNETLLGVSVIRAFEEQ 1063
Cdd:cd18578 138 AIVTLVAGLIIAFVYgwklALVGLATVPLLLLAGYLRMRLLSGFEEKNKKaYEESSK-----IASEAVSNIRTVASLTLE 212
|
170
....*....|....*..
gi 2462549096 1064 ERFIHQSDLKVDENQKA 1080
Cdd:cd18578 213 DYFLEKYEEALEEPLKK 229
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
893-1155 |
8.52e-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: 349984 [Multi-domain] Cd Length: 295 Bit Score: 49.40 E-value: 8.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 893 DDPIVNGTQEHTKVRLSVYGALGISQGIAVFGYSMAVSIGGILASRCLHVDLLHSILRSPMSFFERTPSGNLVNRFSKEL 972
Cdd:cd18540 30 DHFITPGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 973 DTVDSMIPEVIKMFMGSLFNVIGACIVILLATP----IAAIIIPPLGLIYFFVQRFYVASSRQLKRLESVsrspVYSHFN 1048
Cdd:cd18540 110 QRLGEIISWGLVDLVWGITYMIGILIVMLILNWklalIVLAVVPVLAVVSIYFQKKILKAYRKVRKINSR----ITGAFN 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1049 ETLLGVSVIRAF--EEQerfiHQSDLKVDeNQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSLSAGLV---G 1123
Cdd:cd18540 186 EGITGAKTTKTLvrEEK----NLREFKEL-TEEMRRASVRAARLSALFLPIVLFLGSIATALVLWYGGILVLAGAItigT 260
|
250 260 270
....*....|....*....|....*....|....
gi 2462549096 1124 LSV--SYSLQVTTYLNWLVRMSSEMETNIVAVER 1155
Cdd:cd18540 261 LVAfiSYATQFFEPIQQLARVLAELQSAQASAER 294
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
595-720 |
8.57e-06 |
|
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: 47.53 E-value: 8.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTwARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALlAEMDKV-EGHVAIKGVN-------------- 659
Cdd:cd03223 1 IELENLSLA-TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-AGLWPWgSGRIGMPEGEdllflpqrpylplg 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462549096 660 -------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEnvigpkgMLKNK--TRILVTHS 720
Cdd:cd03223 79 tlreqliypwddvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQ-------LLKELgiTVISVGHR 147
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
593-751 |
9.07e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 48.96 E-value: 9.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 593 NSITVRNATFTWaRSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLL------------------SALLAEMDK-VEGHV 653
Cdd:PRK13647 3 NIIEVEDLHFRY-KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLlhlngiylpqrgrvkvmgREVNAENEKwVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 654 ----------------------------------------AIKGVN-----------LSGGQKQRVSLARAVYSNADIYL 682
Cdd:PRK13647 82 glvfqdpddqvfsstvwddvafgpvnmgldkdeverrveeALKAVRmwdfrdkppyhLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462549096 683 FDDPLSAVDAHVGKHIFE--NVIGPKGmlknKTRILVTHSMSYLPQ-VDVIIVMSGGKISEMGSyQELLARD 751
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEilDRLHNQG----KTVIVATHDVDLAAEwADQVIVLKEGRVLAEGD-KSLLTDE 228
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1202-1397 |
9.21e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 48.33 E-value: 9.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1202 LRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGLHD---LRFKITIIPQDPVLFsgslrM 1278
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLL-----M 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1279 NLDPFSQYSDEEVWTSLELAHLKDFVSALPDK--LDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDlet 1356
Cdd:PRK10908 93 DRTVYDNVAIPLIIAGASGDDIRRRVSAALDKvgLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD--- 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2462549096 1357 DDLIQSTIRTqFED-----CTVLTIAHRLNTIMDYT-RVIVLDKGEI 1397
Cdd:PRK10908 170 DALSEGILRL-FEEfnrvgVTVLMATHDIGLISRRSyRMLTLSDGHL 215
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
651-703 |
9.28e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 48.33 E-value: 9.28e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2462549096 651 GHVA-IKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFENVI 703
Cdd:PRK13539 118 APLAhLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA-AVALFAELI 170
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
948-1156 |
9.91e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 49.05 E-value: 9.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 948 ILRSPMSFFERTPSGNLVNRFSkELDTVDSMIPE-VIKMFMGSLFnVIGACIVILLATPIAAIIIPPLGLIYFFvqrFYV 1026
Cdd:cd18555 85 LLKLPYSFFENRSSGDLLFRAN-SNVYIRQILSNqVISLIIDLLL-LVIYLIYMLYYSPLLTLIVLLLGLLIVL---LLL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1027 ASSRQLKRL---ESVSRSPVYSHFNETLLGVSVIRAF--EEQ------ERFIHQsdLKVDENqKAYYPSIVANrwLAVRL 1095
Cdd:cd18555 160 LTRKKIKKLnqeEIVAQTKVQSYLTETLYGIETIKSLgsEKNiykkweNLFKKQ--LKAFKK-KERLSNILNS--ISSSI 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462549096 1096 ECVGNCIVLFAALFAVISrHSLSAG-LVGLSvSYSLQVTTYLNWLVRMSSEMETNIVAVERL 1156
Cdd:cd18555 235 QFIAPLLILWIGAYLVIN-GELTLGeLIAFS-SLAGSFLTPIVSLINSYNQFILLKSYLERL 294
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
643-751 |
1.08e-05 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 49.03 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 643 LAEMDKVEGHVAIKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVigpKGML-KNKTRILVTHSM 721
Cdd:PRK13537 122 LLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERL---RSLLaRGKTILLTTHFM 198
|
90 100 110
....*....|....*....|....*....|..
gi 2462549096 722 SYLPQV--DVIIVMSGGKISEmGSYQELLARD 751
Cdd:PRK13537 199 EEAERLcdRLCVIEEGRKIAE-GAPHALIESE 229
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
646-742 |
1.15e-05 |
|
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: 47.87 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 646 MDKVEGHVAIKGV------NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPKGMLKNkTRILVTH 719
Cdd:cd03298 109 IEVALARVGLAGLekrlpgELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKM-TVLMVTH 187
|
90 100
....*....|....*....|....
gi 2462549096 720 SMSYLPQV-DVIIVMSGGKISEMG 742
Cdd:cd03298 188 QPEDAKRLaQRVVFLDNGRIAAQG 211
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1212-1396 |
1.16e-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: 46.60 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1212 GEKVGIVGRTGAGKSSLTLGLFR-INESAEGEIIIDGINIAKIGLHDLRFKITiipqdpvlfsgslrmnldpfsqysdee 1290
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQLLLIIV--------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1291 vwtslelahlkdfvsalpdkldhecAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIRTQF-- 1368
Cdd:smart00382 55 -------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLll 109
|
170 180 190
....*....|....*....|....*....|....*....
gi 2462549096 1369 -----EDCTVLTIAHRLNTIMD------YTRVIVLDKGE 1396
Cdd:smart00382 110 llkseKNLTVILTTNDEKDLGPallrrrFDRRIVLLLIL 148
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1208-1412 |
1.19e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 48.39 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1208 TINGGEKVGIVGRTGAGKSSL---TLGLFrineSAEGEIIIDGINIAKIGLHDL-RFKITIIPQDPVLFSgslrMnldpf 1283
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLlarMAGLL----PGSGSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPFA----M----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1284 sqysdeEVWTSLEL-----AHLKDFVSALPD-----KLDHECAEGGENLSVGQRQLVCLARALLR-------KTKILVLD 1346
Cdd:PRK03695 85 ------PVFQYLTLhqpdkTRTEAVASALNEvaealGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462549096 1347 EATAAVDLETDDLIQSTIRtqfEDC----TVLTIAHRLNTIMDY-TRVIVLDKGEIQEYGAPSDLLQQRGL 1412
Cdd:PRK03695 159 EPMNSLDVAQQAALDRLLS---ELCqqgiAVVMSSHDLNHTLRHaDRVWLLKQGKLLASGRRDEVLTPENL 226
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1172-1356 |
1.24e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 48.03 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1172 ETAPPSSwPQVGRVeFRNYCLRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDginia 1251
Cdd:COG2401 18 SSVLDLS-ERVAIV-LEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1252 kiglhdlrFKITIIPQDPVLfsgslrmnLDPFsqYSDEEVWTSLELAH---LKDFVSALpDKLDHecaeggenLSVGQRQ 1328
Cdd:COG2401 91 --------VPDNQFGREASL--------IDAI--GRKGDFKDAVELLNavgLSDAVLWL-RRFKE--------LSTGQKF 143
|
170 180
....*....|....*....|....*...
gi 2462549096 1329 LVCLARALLRKTKILVLDEATAAVDLET 1356
Cdd:COG2401 144 RFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
660-751 |
1.39e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 48.62 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEnvigpkgMLK------NKTRILVTHSMSYLPQ-VDVIIV 732
Cdd:PRK13646 146 MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMR-------LLKslqtdeNKTIILVSHDMNEVARyADEVIV 218
|
90
....*....|....*....
gi 2462549096 733 MSGGKISEMGSYQELLARD 751
Cdd:PRK13646 219 MKEGSIVSQTSPKELFKDK 237
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
595-754 |
1.56e-05 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 49.07 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTwaRSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG----------------- 657
Cdd:PRK09536 4 IDVSDLSVE--FGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraasrrvas 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 658 --------------------------------------------------------VNLSGGQKQRVSLARAVYSNADIY 681
Cdd:PRK09536 82 vpqdtslsfefdvrqvvemgrtphrsrfdtwtetdraaveramertgvaqfadrpvTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549096 682 LFDDPLSAVDAHVGKHIFENV--IGPKGmlknKTRILVTHSMSYLPQ-VDVIIVMSGGKISEMGSYQELLARD---GAF 754
Cdd:PRK09536 162 LLDEPTASLDINHQVRTLELVrrLVDDG----KTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLTADtlrAAF 236
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
594-727 |
1.62e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 48.11 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 594 SITVRNATFTWarSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMD---KVEGHV--------------- 653
Cdd:PRK14258 7 AIKVNNLSFYY--DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrMNELEsevRVEGRVeffnqniyerrvnln 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 654 ---------------------------------------------AIK---------------GVNLSGGQKQRVSLARA 673
Cdd:PRK14258 85 rlrrqvsmvhpkpnlfpmsvydnvaygvkivgwrpkleiddivesALKdadlwdeikhkihksALDLSGGQQQRLCIARA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2462549096 674 VYSNADIYLFDDPLSAVDAHVGKHIfENVIGPKGMLKNKTRILVTHSMsylPQV 727
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKV-ESLIQSLRLRSELTMVIVSHNL---HQV 214
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1322-1406 |
1.73e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 49.23 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1322 LSVGQRQLVCLARALLRKTKILVLDEATAAV-DLETDDLIqSTIRT-QFEDCTVLTIAHRLNTIMDYT-RVIVLDKGE-I 1397
Cdd:PRK10762 142 LSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLF-RVIRElKSQGRGIVYISHRLKEIFEICdDVTVFRDGQfI 220
|
....*....
gi 2462549096 1398 QEYgAPSDL 1406
Cdd:PRK10762 221 AER-EVADL 228
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
660-746 |
2.25e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 48.33 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA-----------HVGKHIfenvigpkgmlknKTRIL-VTHSMSYLPQV 727
Cdd:PRK11144 129 LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrellpyleRLAREI-------------NIPILyVSHSLDEILRL 195
|
90 100
....*....|....*....|
gi 2462549096 728 -DVIIVMSGGKISEMGSYQE 746
Cdd:PRK11144 196 aDRVVVLEQGKVKAFGPLEE 215
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1201-1407 |
2.37e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.55 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESA-----EGEIIIDGINIAKIGLHDLRF----KITIIPQDPVL 1271
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1272 fsgslrmNLDPFSQYSDE------------------EVWTSLELAHLKDFVSALPDkLDHEcaeggenLSVGQRQLVCLA 1333
Cdd:PRK15134 104 -------SLNPLHTLEKQlyevlslhrgmrreaargEILNCLDRVGIRQAAKRLTD-YPHQ-------LSGGERQRVMIA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462549096 1334 RALLRKTKILVLDEATAAVDLETDDLIQSTIR--TQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEIQEYGAPSDLL 1407
Cdd:PRK15134 169 MALLTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVRKLAdRVAVMQNGRCVEQNRAATLF 245
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
945-1156 |
2.71e-05 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 47.83 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 945 LHSILRSPMSFFERTPSGNLVNRFSkelDTvdSMIPEVIKMFMGSLF-NVIGACIV-ILLA------TPIAAIIIPPLGL 1016
Cdd:cd18570 82 FKHLLKLPLSFFETRKTGEIISRFN---DA--NKIREAISSTTISLFlDLLMVIISgIILFfynwklFLITLLIIPLYIL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1017 IYFFVQRFYvassRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPS---IVANRWLAV 1093
Cdd:cd18570 157 IILLFNKPF----KKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLgklSNLQSSIKG 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462549096 1094 RLECVGNCIVLFAALFAVISrHSLSAG-LVGLsvsYSLQV--TTYLNWLVRMSSEMETNIVAVERL 1156
Cdd:cd18570 233 LISLIGSLLILWIGSYLVIK-GQLSLGqLIAF---NALLGyfLGPIENLINLQPKIQEAKVAADRL 294
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
612-749 |
2.71e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 47.76 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 612 LNGITFSIPEGALVAVVGQVGCGKSSLL-------------------------SALLA---------------------- 644
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFlhfngilkptsgevlikgepikydkKSLLEvrktvgivfqnpddqlfaptve 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 645 ------------EMDKVEGHV--AIKGV-----------NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIF 699
Cdd:PRK13639 98 edvafgplnlglSKEEVEKRVkeALKAVgmegfenkpphHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIM 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2462549096 700 ENV--IGPKGMlknkTRILVTHSMSYLP-QVDVIIVMSGGKISEMGSYQELLA 749
Cdd:PRK13639 178 KLLydLNKEGI----TIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
659-751 |
3.89e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.04 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 659 NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVgKHIFENVIGPKGMLKNKTRILVTHSMSYLPQVDVIIVMSGGKI 738
Cdd:PRK10522 449 KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHF-RREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
|
90
....*....|....
gi 2462549096 739 SEM-GSYQELLARD 751
Cdd:PRK10522 528 SELtGEERDAASRD 541
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
603-686 |
4.10e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 47.75 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 603 TWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLL------------------------------------------- 639
Cdd:COG0488 5 SKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLkilagelepdsgevsipkglrigylpqeppldddltvldtvld 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 640 -----SALLAEMDKVEGHVA---------------------------IKGV----------------NLSGGQKQRVSLA 671
Cdd:COG0488 85 gdaelRALEAELEELEAKLAepdedlerlaelqeefealggweaearAEEIlsglgfpeedldrpvsELSGGWRRRVALA 164
|
170
....*....|....*
gi 2462549096 672 RAVYSNADIYLFDDP 686
Cdd:COG0488 165 RALLSEPDLLLLDEP 179
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1201-1360 |
5.22e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 46.31 E-value: 5.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKI---GLHDLRFK--------ITIIP--- 1266
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARAKLRAKhvgfvfqsFMLIPtln 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1267 -QDPVLFSGSLRMNLDPFSQYSDEEVWTSLELAhlkdfvsalpDKLDHECAEggenLSVGQRQLVCLARALLRKTKILVL 1345
Cdd:PRK10584 105 aLENVELPALLRGESSRQSRNGAKALLEQLGLG----------KRLDHLPAQ----LSGGEQQRVALARAFNGRPDVLFA 170
|
170
....*....|....*
gi 2462549096 1346 DEATAAVDLETDDLI 1360
Cdd:PRK10584 171 DEPTGNLDRQTGDKI 185
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
660-747 |
6.03e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 47.04 E-value: 6.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPKGMlKNKTRILVTHSMSYLPQV-DVIIVMSGGKI 738
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQK-ENMALVLITHDLALVAEAaHKIIVMYAGQV 232
|
....*....
gi 2462549096 739 SEMGSYQEL 747
Cdd:PRK11022 233 VETGKAHDI 241
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
659-768 |
6.34e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 47.32 E-value: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 659 NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDahVG-KHIFENVIGpkGMLKNKTRILVThSmSYLPQV----DVIIVM 733
Cdd:COG1129 394 NLSGGNQQKVVLAKWLATDPKVLILDEPTRGID--VGaKAEIYRLIR--ELAAEGKAVIVI-S-SELPELlglsDRILVM 467
|
90 100 110
....*....|....*....|....*....|....*
gi 2462549096 734 SGGKISEMgsyqelLARDGAFAEFLRTYASTEQEQ 768
Cdd:COG1129 468 REGRIVGE------LDREEATEEAIMAAATGGAAA 496
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
916-1065 |
6.60e-05 |
|
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: 46.32 E-value: 6.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 916 ISQGIAVFGYSMAVSIGG--ILASrcLHVDLLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNV 993
Cdd:cd18576 47 LLQAVFSFFRIYLFARVGerVVAD--LRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTL 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549096 994 IGACIVILLATP----IAAIIIPPLGLIYFFVQRFYVASSRQlkRLESVSRSPVysHFNETLLGVSVIRAF--EEQER 1065
Cdd:cd18576 125 IGGVVLLFFISWkltlLMLATVPVVVLVAVLFGRRIRKLSKK--VQDELAEANT--IVEETLQGIRVVKAFtrEDYEI 198
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1201-1406 |
6.75e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 46.76 E-value: 6.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLtL----GLFRInesAEGEIIIDG--IN--------IAKI------------- 1253
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTL-LrmvaGLERI---TSGEIWIGGrvVNelepadrdIAMVfqnyalyphmsvr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1254 -----GLhdlrfKITIIPQDPVlfsgSLRMnldpfsqysdEEVWTSLELAHLkdfvsalpdkLDHECAEggenLSVGQRQ 1328
Cdd:PRK11650 95 enmayGL-----KIRGMPKAEI----EERV----------AEAARILELEPL----------LDRKPRE----LSGGQRQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1329 LVCLARALLRKTKILVLDEATAAVD--------LETDDLiQSTIRT--------QFEdctVLTIAHRLntimdytrvIVL 1392
Cdd:PRK11650 142 RVAMGRAIVREPAVFLFDEPLSNLDaklrvqmrLEIQRL-HRRLKTtslyvthdQVE---AMTLADRV---------VVM 208
|
250
....*....|....
gi 2462549096 1393 DKGEIQEYGAPSDL 1406
Cdd:PRK11650 209 NGGVAEQIGTPVEV 222
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
612-722 |
7.14e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 45.96 E-value: 7.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 612 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVAIKG--------------------------------- 657
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLH-LLGGLDTpTSGDVIFNGqpmsklssaakaelrnqklgfiyqfhhllpdft 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 658 ----------------------------------------VNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKH 697
Cdd:PRK11629 104 alenvamplligkkkpaeinsralemlaavglehranhrpSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
|
170 180
....*....|....*....|....*
gi 2462549096 698 IFEnVIGPKGMLKNKTRILVTHSMS 722
Cdd:PRK11629 184 IFQ-LLGELNRLQGTAFLVVTHDLQ 207
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
656-746 |
7.58e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 45.86 E-value: 7.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 656 KGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFENVIGPKGMLKNKTRILVTHSMSYLPQVDVIIVMS 734
Cdd:PRK10247 133 KNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDES-NKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQ 211
|
90
....*....|..
gi 2462549096 735 ggkiSEMGSYQE 746
Cdd:PRK10247 212 ----PHAGEMQE 219
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1204-1395 |
7.59e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 46.14 E-value: 7.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1204 HINVTINGGEKVGIVGRTGAGKSS----LTlGLFRineSAEGEIIIDGIN--------IAKIGL-----HDLRFK-ITII 1265
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTvfncLT-GFYK---PTGGTILLRGQHieglpghqIARMGVvrtfqHVRLFReMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1266 PQDPV---------LFSGSLRMnldPFSQYSDEE------VWtsLELAHLKDFVSAlpdkldhecaEGGeNLSVGQRQLV 1330
Cdd:PRK11300 99 ENLLVaqhqqlktgLFSGLLKT---PAFRRAESEaldraaTW--LERVGLLEHANR----------QAG-NLAYGQQRRL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549096 1331 CLARALLRKTKILVLDEATAAVD-LETDDLIQ--STIRTQFeDCTVLTIAHRLNTIMDYT-RVIVLDKG 1395
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNpKETKELDEliAELRNEH-NVTVLLIEHDMKLVMGISdRIYVVNQG 230
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
659-735 |
7.66e-05 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 45.86 E-value: 7.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 659 NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD-------AHVGKHIFENvigpkgmlKNKTRILVTHSM---SYLpqVD 728
Cdd:cd03237 115 ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDveqrlmaSKVIRRFAEN--------NEKTAFVVEHDIimiDYL--AD 184
|
....*..
gi 2462549096 729 VIIVMSG 735
Cdd:cd03237 185 RLIVFEG 191
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
615-657 |
8.18e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 46.13 E-value: 8.18e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2462549096 615 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG 657
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDG 68
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
660-750 |
8.45e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 45.85 E-value: 8.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIF---ENVI---GPkGMLknktriLVTHSMSYLPQV-DVIIV 732
Cdd:PRK10418 141 MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILdllESIVqkrAL-GML------LVTHDMGVVARLaDDVAV 213
|
90
....*....|....*...
gi 2462549096 733 MSGGKISEMGSYQELLAR 750
Cdd:PRK10418 214 MSHGRIVEQGDVETLFNA 231
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
660-748 |
8.74e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 45.81 E-value: 8.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGKHIFENVIGPkgmLKNK-TRILVTHSMSYLPQV-DVIIVMSGGK 737
Cdd:PRK14246 154 LSGGQQQRLTIARALALKPKVLLMDEPTSMIDI-VNSQAIEKLITE---LKNEiAIVIVSHNPQQVARVaDYVAFLYNGE 229
|
90
....*....|.
gi 2462549096 738 ISEMGSYQELL 748
Cdd:PRK14246 230 LVEWGSSNEIF 240
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
564-686 |
9.10e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 46.98 E-value: 9.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 564 LKRLriflshEELEPDSIERR--------PVKDGGGTNSITVRNATFTWArsDPPTLNGITFSIPEGALVAVVGQVGCGK 635
Cdd:COG0488 283 IKAL------EKLEREEPPRRdktveirfPPPERLGKKVLELEGLSKSYG--DKTLLDDLSLRIDRGDRIGLIGPNGAGK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 636 SSLLSALLAEMDKVEGHVAIkGVN-------------------------------------------------------L 660
Cdd:COG0488 355 STLLKLLAGELEPDSGTVKL-GETvkigyfdqhqeeldpdktvldelrdgapggteqevrgylgrflfsgddafkpvgvL 433
|
170 180
....*....|....*....|....*.
gi 2462549096 661 SGGQKQRVSLARAVYSNADIYLFDDP 686
Cdd:COG0488 434 SGGEKARLALAKLLLSPPNVLLLDEP 459
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
612-719 |
9.75e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 45.33 E-value: 9.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 612 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEG-------------------HVAIKG--------------- 657
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVagcvdvpdnqfgreaslidAIGRKGdfkdavellnavgls 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549096 658 ---------VNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD---AHVGKHIFENVIGPKGmlknKTRILVTH 719
Cdd:COG2401 126 davlwlrrfKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtAKRVARNLQKLARRAG----ITLVVATH 195
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
659-739 |
9.99e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 46.73 E-value: 9.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 659 NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDahvgkhIFE-----NVIgpKGMLKNKTRILVTHSMS---YLpqVDVI 730
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLD------IRQrlnvaRLI--RELAEGKYVLVVEHDLAvldYL--ADNV 281
|
90
....*....|....
gi 2462549096 731 IVMSG-----GKIS 739
Cdd:PRK13409 282 HIAYGepgayGVVS 295
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1322-1416 |
1.27e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.48 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1322 LSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTIrTQFEDcTVLTIAH-RL---NTIMdyTRVIVLDKGEI 1397
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELL-DSYQG-TVLLVSHdRQfvdNTVT--ECWIFEGNGKI 516
|
90 100
....*....|....*....|
gi 2462549096 1398 QEY-GAPSDLLQQRGLFYSM 1416
Cdd:PRK11147 517 GRYvGGYHDARQQQAQYLAL 536
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
579-747 |
1.28e-04 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 45.98 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 579 DSIERRPVKDGGG-TNSITVRNATFTWarSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKG 657
Cdd:PRK11607 3 DAIPRPQAKTRKAlTPLLEIRNLTKSF--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 658 VN-------------------------------------------------------------------LSGGQKQRVSL 670
Cdd:PRK11607 81 VDlshvppyqrpinmmfqsyalfphmtveqniafglkqdklpkaeiasrvnemlglvhmqefakrkphqLSGGQRQRVAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 671 ARAVYSNADIYLFDDPLSAVDAHVGKH-------IFENVigpkgmlkNKTRILVTHSM-SYLPQVDVIIVMSGGKISEMG 742
Cdd:PRK11607 161 ARSLAKRPKLLLLDEPMGALDKKLRDRmqlevvdILERV--------GVTCVMVTHDQeEAMTMAGRIAIMNRGKFVQIG 232
|
....*
gi 2462549096 743 SYQEL 747
Cdd:PRK11607 233 EPEEI 237
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1321-1384 |
1.38e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.32 E-value: 1.38e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462549096 1321 NLSVGQRQLVCLARALLRKTKILVLDEATAAVDlETD-----DLIQStIRTQfeDCTVLTIAHRLNTIM 1384
Cdd:NF040905 139 DIGVGKQQLVEIAKALSKDVKLLILDEPTAALN-EEDsaallDLLLE-LKAQ--GITSIIISHKLNEIR 203
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
603-692 |
1.52e-04 |
|
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: 44.27 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 603 TWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV-------------------------AIKG 657
Cdd:TIGR01189 7 ACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVrwngtplaeqrdephenilylghlpGLKP 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549096 658 ----------------------------VNLSG-----------GQKQRVSLARAVYSNADIYLFDDPLSAVDA 692
Cdd:TIGR01189 87 elsalenlhfwaaihggaqrtiedalaaVGLTGfedlpaaqlsaGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
660-774 |
1.56e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 46.24 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPKGMLkNKTRILVTHSMSYLPQV-DVIIVMSGGKI 738
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQEL-NMGLLFITHNLSIVRKLaDRVAVMQNGRC 235
|
90 100 110
....*....|....*....|....*....|....*.
gi 2462549096 739 SEMGSYQELLARDgafaeflrTYASTEQEQDAEENG 774
Cdd:PRK15134 236 VEQNRAATLFSAP--------THPYTQKLLNSEPSG 263
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
624-691 |
1.66e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 44.57 E-value: 1.66e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462549096 624 LVAVVGQVGCgkSSLLSALLAEmdkveghvaikgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 691
Cdd:PRK10771 110 LHAIARQMGI--EDLLARLPGQ--------------LSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
612-692 |
2.01e-04 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 44.68 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 612 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVNLSG-GQKQRVSLARAVYsnadiYLFDDPLSAV 690
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlNRAQRKAFRRDIQ-----MVFQDSISAV 102
|
..
gi 2462549096 691 DA 692
Cdd:PRK10419 103 NP 104
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1217-1364 |
2.11e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.09 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1217 IVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIAKIGL-------HDLRFKITIIPQDpvlfsgslrmNLDPFSqysde 1289
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKpyctyigHNLGLKLEMTVFE----------NLKFWS----- 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549096 1290 EVWTSLELAHLKDFVSALPDKLDHECAeggeNLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDDLIQSTI 1364
Cdd:PRK13541 96 EIYNSAETLYAAIHYFKLHDLLDEKCY----SLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
921-1085 |
2.14e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 44.86 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 921 AVFGYSMAVSIGGiLASRCLH---VDLLHSILRSPMSFFERTPSGNL-------VNRFSKELDTvdsMIPEVIKMFMGSL 990
Cdd:cd18565 68 SLFQYLSGVLWRR-FAQRVQHdlrTDTYDHVQRLDMAFFEDRQTGDLmsvlnndVNQLERFLDD---GANSIIRVVVTVL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 991 fnVIGAcIVILLATPIAAIIIPPLGLIYFFVQRFyvasSRQLKRLESVSRSPV---YSHFNETLLGVSVIRAF----EEQ 1063
Cdd:cd18565 144 --GIGA-ILFYLNWQLALVALLPVPLIIAGTYWF----QRRIEPRYRAVREAVgdlNARLENNLSGIAVIKAFtaedFER 216
|
170 180
....*....|....*....|....*...
gi 2462549096 1064 ERFIHQSDLKVDENQKA------YYPSI 1085
Cdd:cd18565 217 ERVADASEEYRDANWRAirlraaFFPVI 244
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
660-748 |
2.53e-04 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 45.42 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVigpKGM-LKNKTRILVTHSMSY--LPQVDVIIVMSGG 736
Cdd:TIGR00955 167 LSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVL---KGLaQKGKTIICTIHQPSSelFELFDKIILMAEG 243
|
90
....*....|..
gi 2462549096 737 KISEMGSYQELL 748
Cdd:TIGR00955 244 RVAYLGSPDQAV 255
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
618-719 |
2.93e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.12 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 618 SIPEGALVAVVGQVGCGKSSLLSA----LLAEMDKVEGHVAIK-GVN--------------LSGGQKQRVSLARAV---- 674
Cdd:cd03227 17 TFGEGSLTIITGPNGSGKSTILDAiglaLGGAQSATRRRSGVKaGCIvaavsaeliftrlqLSGGEKELSALALILalas 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2462549096 675 YSNADIYLFDDPLSAVDAHVGkHIFENVIgpKGMLKNKTR-ILVTH 719
Cdd:cd03227 97 LKPRPLYILDEIDRGLDPRDG-QALAEAI--LEHLVKGAQvIVITH 139
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
652-770 |
3.22e-04 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 44.23 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 652 HVAIKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVigpKGMLKNK--TRILVTHSMSY-LPQV 727
Cdd:PRK09984 144 HFAHQRVStLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTL---RDINQNDgiTVVVTLHQVDYaLRYC 220
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2462549096 728 DVIIVMSGGKISEMGSYQELlaRDGAFAEFLRTYASTEQEQDA 770
Cdd:PRK09984 221 ERIVALRQGHVFYDGSSQQF--DNERFDHLYRSINRVEENAKA 261
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1205-1401 |
3.52e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 44.48 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1205 INVTINGGEKVGIVGRTGAGKSSLtlglfrINESA------EGEIIIDGiniaKIgLHDLRFKITIIP---------QDP 1269
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSL------INAISgltrpqKGRIVLNG----RV-LFDAEKGICLPPekrrigyvfQDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1270 VLF-----SGSLRMNLDPFSQYSDEEVWTSLELAHLkdfVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKILV 1344
Cdd:PRK11144 86 RLFphykvRGNLRYGMAKSMVAQFDKIVALLGIEPL---LDRYP-----------GSLSGGEKQRVAIGRALLTAPELLL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1345 LDEATAAVD----------LETddLIQsTIRTqfedcTVLTIAHRLNTIM---DytRVIVLDKGEIQEYG 1401
Cdd:PRK11144 152 MDEPLASLDlprkrellpyLER--LAR-EINI-----PILYVSHSLDEILrlaD--RVVVLEQGKVKAFG 211
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
940-1059 |
3.59e-04 |
|
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: 44.11 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 940 LHVDLLHSILRSPMSFFERTPSGNLVNRFsKELDTV-DSMIPEVIKMFMGSLFNVIGACIVILLATPIAAIiipPLGLIY 1018
Cdd:cd18566 77 LSNAAFEHLLSLPLSFFEREPSGAHLERL-NSLEQIrEFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLV---PLVLLG 152
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2462549096 1019 FFVQRFYVASSRQLKRLESVSRSPV--YSHFNETLLGVSVIRA 1059
Cdd:cd18566 153 LFVLVAILLGPILRRALKERSRADErrQNFLIETLTGIHTIKA 195
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
944-1134 |
3.77e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 43.99 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 944 LLHSILRSPMSFFERTPSGNLVNRFSkELDTVDSMIpevIKMFMGSLFN---VIGACIVILLATPIAAIIIPPLGLIYFF 1020
Cdd:cd18567 81 LFRHLLRLPLSYFEKRHLGDIVSRFG-SLDEIQQTL---TTGFVEALLDglmAILTLVMMFLYSPKLALIVLAAVALYAL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1021 VQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAF-EEQERFIHQSDLKVDE-NQkayypSIVANRWLAVR---- 1094
Cdd:cd18567 157 LRLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFgREAEREARWLNLLVDAiNA-----DIRLQRLQILFsaan 231
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2462549096 1095 --LECVGNCIVLFAALFAVISRHsLSAG-LVGLsVSYSLQVTT 1134
Cdd:cd18567 232 glLFGLENILVIYLGALLVLDGE-FTVGmLFAF-LAYKDQFSS 272
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
948-1156 |
4.24e-04 |
|
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: 44.09 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 948 ILRSPMSFFERTPSGNLVNRFsKELDTVDSMI-PEVIKMFMGSLFNVIgaCIVILLA-----TPIAAIIIPPLGLIyffv 1021
Cdd:cd18568 85 LLSLPLSFFASRKVGDIITRF-QENQKIRRFLtRSALTTILDLLMVFI--YLGLMFYynlqlTLIVLAFIPLYVLL---- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1022 qrfYVASSRQLKRLES---VSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVanrwLAVRLECV 1098
Cdd:cd18568 158 ---TLLSSPKLKRNSReifQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQK----LSIVLQLI 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462549096 1099 -------GNCIVLFAALFAVISrHSLSAG-LVGLSVSYSLqVTTYLNWLVRMSSEMETNIVAVERL 1156
Cdd:cd18568 231 sslinhlGTIAVLWYGAYLVIS-GQLTIGqLVAFNMLFGS-VINPLLALVGLWDELQETRISVERL 294
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
955-1156 |
4.37e-04 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 43.95 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 955 FFERTPSGNLVNRFSKELD-TVDSMIPEVIKMFMGSLFNVIGACIVILL---ATPIAAIIIPplglIYFFVQRFYVASSR 1030
Cdd:cd18554 96 YYANNRSGEIISRVINDVEqTKDFITTGLMNIWLDMITIIIAICIMLVLnpkLTFVSLVIFP----FYILAVKYFFGRLR 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1031 QLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDlkvDENQKAYYPSIVANRWLAVRLECV------GNCIVL 1104
Cdd:cd18554 172 KLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFD---KRNGHFLTRALKHTRWNAKTFSAVntitdlAPLLVI 248
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462549096 1105 FAALFAVISrHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERL 1156
Cdd:cd18554 249 GFAAYLVIE-GNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
659-749 |
4.88e-04 |
|
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: 43.19 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 659 NLSGGQKQRVSLARAVYSNADIYLFDDP---LSAVDAHVGKHIFENvIGPKGMlknkTRILVTHSMSYLPQV-DVIIVMS 734
Cdd:cd03219 143 ELSYGQQRRLEIARALATDPKLLLLDEPaagLNPEETEELAELIRE-LRERGI----TVLLVEHDMDVVMSLaDRVTVLD 217
|
90
....*....|....*
gi 2462549096 735 GGKISEMGSYQELLA 749
Cdd:cd03219 218 QGRVIAEGTPDEVRN 232
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
659-691 |
5.10e-04 |
|
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: 43.51 E-value: 5.10e-04
10 20 30
....*....|....*....|....*....|...
gi 2462549096 659 NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 691
Cdd:cd03236 139 QLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1180-1408 |
5.85e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 43.15 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1180 PQVgrVEFRNYCLRYREDLdfvLRHINVTINGGEKVGIVGRTGAGKSSLTLGLFRI-----NESAeGEIIIDGINIAkig 1254
Cdd:PRK10418 2 PQQ--IELRNIALQAAQPL---VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIlpagvRQTA-GRVLLDGKPVA--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1255 LHDLR-FKITIIPQDPvlfsgslRMNLDPFSQYSDEEVWTSLELAHLKDfVSALPDKLDhecAEGGEN-----------L 1322
Cdd:PRK10418 73 PCALRgRKIATIMQNP-------RSAFNPLHTMHTHARETCLALGKPAD-DATLTAALE---AVGLENaarvlklypfeM 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1323 SVGQRQLVCLARALLRKTKILVLDEATAAVDLETD----DLIQSTIRTQfeDCTVLTIAHRLNTIMDYT-RVIVLDKGEI 1397
Cdd:PRK10418 142 SGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQarilDLLESIVQKR--ALGMLLVTHDMGVVARLAdDVAVMSHGRI 219
|
250
....*....|.
gi 2462549096 1398 QEYGAPSDLLQ 1408
Cdd:PRK10418 220 VEQGDVETLFN 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
661-747 |
6.02e-04 |
|
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: 42.74 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 661 SGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVigpKGMLK--NKTRILVTHSMSYLPQV-DVIIVMSGGK 737
Cdd:cd03265 133 SGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYI---EKLKEefGMTILLTTHYMEEAEQLcDRVAIIDHGR 209
|
90
....*....|
gi 2462549096 738 ISEMGSYQEL 747
Cdd:cd03265 210 IIAEGTPEEL 219
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
614-693 |
6.22e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 42.48 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 614 GITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV-------------------------AIKG----------- 657
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVlwqgepirrqrdeyhqdllylghqpGIKTeltalenlrfy 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462549096 658 ------------------VNLSG-----------GQKQRVSLARAVYSNADIYLFDDPLSAVDAH 693
Cdd:PRK13538 99 qrlhgpgddealwealaqVGLAGfedvpvrqlsaGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
660-749 |
7.63e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 43.24 E-value: 7.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFeNVigpkgMLKNKTR-----ILVTHSMSYLPQV-DVIIVM 733
Cdd:PRK15112 150 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLI-NL-----MLELQEKqgisyIYVTQHLGMMKHIsDQVLVM 223
|
90
....*....|....*.
gi 2462549096 734 SGGKISEMGSYQELLA 749
Cdd:PRK15112 224 HQGEVVERGSTADVLA 239
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1205-1353 |
8.24e-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: 44.23 E-value: 8.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1205 INVTINGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGINIaKIGLHDLRFKITIIPQDPVLFSG-SLRMNLDPF 1283
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAEHILFY 1027
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462549096 1284 SQY---SDEEVWTSLElAHLKDfvsalpDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1353
Cdd:TIGR01257 1028 AQLkgrSWEEAQLEME-AMLED------TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
656-691 |
9.34e-04 |
|
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: 42.53 E-value: 9.34e-04
10 20 30
....*....|....*....|....*....|....*.
gi 2462549096 656 KGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 691
Cdd:cd03218 130 KASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1201-1378 |
1.03e-03 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 42.38 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1201 VLRHINVTINGGEKVGIVGRTGAGKSSLtLGLFR-INESAEGEIIIDGINIAKIGlhdlrfkitiiPQDPVLFSGSlrmN 1279
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTL-LNLIAgFVPYQHGSITLDGKPVEGPG-----------AERGVVFQNE---G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1280 LDPFSQYSDEeVWTSLELAHL-----KDFVSALPDKLDHECAEGGE--NLSVGQRQLVCLARALLRKTKILVLDEATAAV 1352
Cdd:PRK11248 81 LLPWRNVQDN-VAFGLQLAGVekmqrLEIAHQMLKKVGLEGAEKRYiwQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180
....*....|....*....|....*...
gi 2462549096 1353 DLETDDLIQSTIRTQFEDC--TVLTIAH 1378
Cdd:PRK11248 160 DAFTREQMQTLLLKLWQETgkQVLLITH 187
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
591-715 |
1.22e-03 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 42.44 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 591 GTNSITVRNATFTwaRSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGVNLSGGQKQRVSL 670
Cdd:PRK11831 4 VANLVDMRGVSFT--RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYT 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2462549096 671 ARAVYSnadiYLFDDPLSAVDAHVgkhiFENVIGPkgmLKNKTRI 715
Cdd:PRK11831 82 VRKRMS----MLFQSGALFTDMNV----FDNVAYP---LREHTQL 115
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
603-692 |
1.23e-03 |
|
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: 41.71 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 603 TWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV-------------------------AIKG 657
Cdd:cd03231 7 TCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVllnggpldfqrdsiargllylghapGIKT 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462549096 658 V-------------------------------------NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 692
Cdd:cd03231 87 TlsvlenlrfwhadhsdeqveealarvglngfedrpvaQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
659-735 |
1.27e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.26 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 659 NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD-------AHVGKHIFENvigpkgmlKNKTRILVTH---SMSYLpqVD 728
Cdd:PRK13409 453 DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavAKAIRRIAEE--------REATALVVDHdiyMIDYI--SD 522
|
....*..
gi 2462549096 729 VIIVMSG 735
Cdd:PRK13409 523 RLMVFEG 529
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
595-751 |
1.51e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 42.10 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATFTWaRSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGV---------------- 658
Cdd:PRK13652 4 IETRDLCYSY-SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfvgl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 659 ------------------------------------------------------NLSGGQKQRVSLARAVYSNADIYLFD 684
Cdd:PRK13652 83 vfqnpddqifsptveqdiafgpinlgldeetvahrvssalhmlgleelrdrvphHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462549096 685 DPLSAVDAHVGKHIFE---NVIGPKGMlknkTRILVTHSMSYLPQV-DVIIVMSGGKISEMGSYQELLARD 751
Cdd:PRK13652 163 EPTAGLDPQGVKELIDflnDLPETYGM----TVIFSTHQLDLVPEMaDYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
660-749 |
1.59e-03 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 42.87 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPKGMLkNKTRILVTHSMSYLPQV-DVIIVMSGGKI 738
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEM-EQTFIIVSHDMDFVLDVcDRAALMRDGKI 506
|
90
....*....|.
gi 2462549096 739 SEMGSYQELLA 749
Cdd:TIGR03269 507 VKIGDPEEIVE 517
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
659-691 |
1.66e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 42.85 E-value: 1.66e-03
10 20 30
....*....|....*....|....*....|...
gi 2462549096 659 NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 691
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
660-749 |
1.69e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 42.12 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEnvigpkgMLKN-----KTRILVTHSMSYLPQ-VDVIIVM 733
Cdd:PRK13641 146 LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQ-------LFKDyqkagHTVILVTHNMDDVAEyADDVLVL 218
|
90
....*....|....*.
gi 2462549096 734 SGGKISEMGSYQELLA 749
Cdd:PRK13641 219 EHGKLIKHASPKEIFS 234
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
660-742 |
2.14e-03 |
|
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: 41.20 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGPKGMlkNKTRILVTHSMSYLPQV-DVIIVMSGGKI 738
Cdd:cd03266 137 FSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL--GKCILFSTHIMQEVERLcDRVVVLHRGRV 214
|
....
gi 2462549096 739 SEMG 742
Cdd:cd03266 215 VYEG 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
660-719 |
2.34e-03 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 41.30 E-value: 2.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIfENVIGPKGMLKNKTRILVTH 719
Cdd:PRK10584 147 LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI-ADLLFSLNREHGTTLILVTH 205
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
660-747 |
2.72e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 42.15 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVigpkGMLKNKTR---ILVTHSMSYLPQV-DVIIVMSG 735
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLI----KVLQKEMSmgvIFITHDMGVVAEIaDRVLVMYQ 244
|
90
....*....|..
gi 2462549096 736 GKISEMGSYQEL 747
Cdd:PRK10261 245 GEAVETGSVEQI 256
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
639-691 |
3.14e-03 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 40.78 E-value: 3.14e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2462549096 639 LSALLAEMDKveGHVA-IKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 691
Cdd:COG1137 117 LEELLEEFGI--THLRkSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
944-1025 |
3.32e-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: 41.14 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 944 LLHSILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVIL-LA---TPIAAIIIPplglIYF 1019
Cdd:cd18784 75 LFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFkLSwqlSLVTLIGLP----LIA 150
|
....*.
gi 2462549096 1020 FVQRFY 1025
Cdd:cd18784 151 IVSKVY 156
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
595-748 |
3.49e-03 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 40.84 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 595 ITVRNATftWARSDPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEG----------------------- 651
Cdd:COG1119 4 LELRNVT--VRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvrlfgerrggedvwelrkrig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 652 -----------------HVAIKGV------------------------------------NLSGGQKQRVSLARAVYSNA 678
Cdd:COG1119 82 lvspalqlrfprdetvlDVVLSGFfdsiglyreptdeqrerarellellglahladrpfgTLSQGEQRRVLIARALVKDP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462549096 679 DIYLFDDPLSAVDAHvGKHIFENVIGPKGMLKNKTRILVTHSMSYLPQ-VDVIIVMSGGKISEMGSYQELL 748
Cdd:COG1119 162 ELLILDEPTAGLDLG-ARELLLALLDKLAAEGAPTLVLVTHHVEEIPPgITHVLLLKDGRVVAAGPKEEVL 231
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
612-738 |
3.51e-03 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 40.34 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 612 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAI------------------------------------ 655
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFdgkpldiaarnrigylpeerglypkmkvidqlvyla 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 656 --KGVN---------------------------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGKHIFENVIGPk 706
Cdd:cd03269 96 qlKGLKkeearrridewlerlelseyankrveeLSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP-VNVELLKDVIRE- 173
|
170 180 190
....*....|....*....|....*....|....*
gi 2462549096 707 gmLK--NKTRILVTHSMSYLPQV-DVIIVMSGGKI 738
Cdd:cd03269 174 --LAraGKTVILSTHQMELVEELcDRVLLLNKGRA 206
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
948-1156 |
3.59e-03 |
|
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: 40.93 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 948 ILRSPMSFFERTPSGNLVNRFSKELDTVDSMIPEVIKMFMGSLFNVIGACIVILLATP----IAAIIIP-PLGLIYFFVQ 1022
Cdd:cd18575 79 LLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPkltlLVLLVIPlVVLPIILFGR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1023 RFYVASSRQLKRLESVSrspvySHFNETLLGVSVIRAF--EEQERFIHQSDLkvdenQKAYypsIVANRWLAVRLECVGN 1100
Cdd:cd18575 159 RVRRLSRASQDRLADLS-----AFAEETLSAIKTVQAFtrEDAERQRFATAV-----EAAF---AAALRRIRARALLTAL 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462549096 1101 CIVL-FAALFAVI-------SRHSLSAGLVGLSVSYSLQVTTYLNWLVRMSSEMETNIVAVERL 1156
Cdd:cd18575 226 VIFLvFGAIVFVLwlgahdvLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
552-661 |
3.65e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 41.69 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 552 TWVCTPFLASVSLKRLRIFLSHEELEPDSIERRPVKDGGGTNSI-TVRNATftwaRSDPPTLNGITFSIPEGALVAVVGQ 630
Cdd:PRK09700 222 SSVCSGMVSDVSNDDIVRLMVGRELQNRFNAMKENVSNLAHETVfEVRNVT----SRDRKKVRDISFSVCRGEILGFAGL 297
|
90 100 110
....*....|....*....|....*....|.
gi 2462549096 631 VGCGKSSLLSALLAEMDKVEGHVAIKGVNLS 661
Cdd:PRK09700 298 VGSGRTELMNCLFGVDKRAGGEIRLNGKDIS 328
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
647-738 |
3.85e-03 |
|
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: 40.33 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 647 DKVEGHVAIKGvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEnvigpkgMLK-----NKTRILVTHSm 721
Cdd:cd03234 133 LTRIGGNLVKG--ISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVS-------TLSqlarrNRIVILTIHQ- 202
|
90 100
....*....|....*....|...
gi 2462549096 722 sylPQVDV------IIVMSGGKI 738
Cdd:cd03234 203 ---PRSDLfrlfdrILLLSSGEI 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
660-750 |
3.93e-03 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 41.59 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 660 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEnvigpkgMLKNKTR------ILVTHSMSYLPQV-DVIIV 732
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILD-------LLKDLQRelgmalLLITHDLGVVRRFaDRVAV 229
|
90
....*....|....*...
gi 2462549096 733 MSGGKISEMGSYQELLAR 750
Cdd:COG4172 230 MRQGEIVEQGPTAELFAA 247
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
657-691 |
4.29e-03 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 40.65 E-value: 4.29e-03
10 20 30
....*....|....*....|....*....|....*
gi 2462549096 657 GVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 691
Cdd:PRK10895 135 GQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
659-735 |
4.73e-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: 41.31 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 659 NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD-------AHVGKHIFENvigpkgmlKNKTRILVTHSMSYLPQV-DVI 730
Cdd:COG1245 455 DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavAKAIRRFAEN--------RGKTAMVVDHDIYLIDYIsDRL 526
|
....*
gi 2462549096 731 IVMSG 735
Cdd:COG1245 527 MVFEG 531
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
659-727 |
5.64e-03 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 41.07 E-value: 5.64e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462549096 659 NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhvgkhifENVIGPKGMLKN--KTRILVTHSMSYLPQV 727
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA-------ESVAWLERHLQEypGTVVAVTHDRYFLDNV 224
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1192-1241 |
5.78e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.92 E-value: 5.78e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2462549096 1192 LRYREDLDFVLRHINVTINGGEKVGIVGRTGAGKSSLtLGLFRINESAEG 1241
Cdd:PRK10636 7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTL-LALLKNEISADG 55
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
658-739 |
6.05e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 41.05 E-value: 6.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 658 VNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDahVG-KHIFENVI---GPKGMlknkTRILVThsmSYLPQV----DV 729
Cdd:PRK11288 395 MNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID--VGaKHEIYNVIyelAAQGV----AVLFVS---SDLPEVlgvaDR 465
|
90
....*....|
gi 2462549096 730 IIVMSGGKIS 739
Cdd:PRK11288 466 IVVMREGRIA 475
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
612-644 |
6.61e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.88 E-value: 6.61e-03
10 20 30
....*....|....*....|....*....|...
gi 2462549096 612 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLA 644
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLS-LIA 48
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
661-749 |
8.10e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 40.46 E-value: 8.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 661 SGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFENVIGpkgmLKNKTR---ILVTHSM----SYLPQVdviIVM 733
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKS----LQQKHQlayLFISHDLhvvrALCHQV---IVL 499
|
90
....*....|....*.
gi 2462549096 734 SGGKISEMGSYQELLA 749
Cdd:PRK15134 500 RQGEVVEQGDCERVFA 515
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
615-700 |
8.65e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 40.61 E-value: 8.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462549096 615 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVAIKGV---NLSGGQKQrvSLARavysnaDI-YLFDDPLSAV 690
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQ--ALRR------DIqFIFQDPYASL 414
|
90
....*....|..
gi 2462549096 691 DAH--VGKHIFE 700
Cdd:PRK10261 415 DPRqtVGDSIME 426
|
|
| |
